PROTEIN	SOURCE	LENGTH	UniProt	PDB_wild	MUTATED_CHAIN	CLASS	PFAM	CATH	EC_NUMBER	MUTATION_UNIPROT	MUTATION_PDB	SEC_STR	RSA	T	pH	BUFFER_NAME	BUFFER_CONC	ION_NAME	ION_CONC	ADDITIVES	MEASURE_KIN	METHOD_KIN	ln(kf)_H2O	dln(kf)_H2O	ln(ku)_H2O	dln(ku)_H2O	dGKIN_H2O	ddGKIN_H2O	ln(kf)_DEN	dln(kf)_DEN	ln(ku)_DEN	dln(ku)_DEN	mf	mu	CM_KIN	beta-T	PhiF_H2O	BACKGROUND_MUT_UNIPROT	BACKGROUND_MUT_PDB	AUTHOR_KIN	REFERENCE_KIN	YEAR_KIN	PMID_KIN	STATE	REVERSIBILITY	REVIEW_DATE
yrosine-protein kinase transforming protein Src	Rous sarcoma virus subgroup A	104.0	P00524	1sha	A	Alpha Beta	PF00017	1shaA00 (3.30.505.10)	2.7.10.2	N/A	WT	N/A	N/A	25.0	7.0	imidizole	0.02	N/A	N/A	0.1 mM TCEP	stopped-flow	urea	8.74	N/A	-3.48	N/A	29.53	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T22A	T21A	Beta	19.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.3	-1.18	-6.94	1.52	N/A	N/A	N/A	N/A	-3.36	N/A	N/A	2.28	N/A	N/A	0.44	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205419	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T22S	T21S	Beta	19.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.46	-1.34	-7.37	1.09	N/A	N/A	N/A	N/A	-3.67	N/A	N/A	2.35	N/A	N/A	0.55	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205420	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I77A	I76A	Beta	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-2.39	-3.27	-5.3	3.16	N/A	N/A	N/A	N/A	-0.73	N/A	N/A	2.82	N/A	N/A	0.51	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205443	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V99A	V98A	Beta	10.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.25	-1.13	-5.94	2.52	N/A	N/A	N/A	N/A	-2.31	N/A	N/A	2.3	N/A	N/A	0.31	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205447	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V102A	V101A	Beta	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.94	-2.82	-6.64	1.82	N/A	N/A	N/A	N/A	-2.99	N/A	N/A	2.33	N/A	N/A	0.61	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205448	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	L107A	L106A	Beta	20.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.44	-1.32	-5.86	2.6	N/A	N/A	N/A	N/A	-2.43	N/A	N/A	2.18	N/A	N/A	0.34	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205449	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V24A	V23A	Beta	5.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.87	-2.75	-6.19	2.27	N/A	N/A	N/A	N/A	-2.56	N/A	N/A	2.28	N/A	N/A	0.55	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205422	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V25A	V24A	Beta	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.48	-2.36	-5.43	3.03	N/A	N/A	N/A	N/A	-1.64	N/A	N/A	2.4	N/A	N/A	0.44	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205423	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T28A	T27A	Beta	24.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.39	-1.27	-6.4	2.06	N/A	N/A	N/A	N/A	-2.56	N/A	N/A	2.45	N/A	N/A	0.38	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205424	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	WT	WT	N/A	N/A	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.88	N/A	-8.46	N/A	N/A	N/A	N/A	N/A	-4.97	N/A	N/A	2.21	N/A	N/A	N/A	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205415	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T76V	T75V	Beta	14.1	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.08	-0.96	-8.05	0.41	N/A	N/A	N/A	N/A	-4.47	N/A	N/A	2.28	N/A	N/A	0.7	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205441	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I77V	I76V	Beta	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.16	-0.72	-7.9	0.56	N/A	N/A	N/A	N/A	-4.24	N/A	N/A	2.33	N/A	N/A	0.56	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205442	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T28V	T27V	Beta	24.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	1.0	0.12	-8.73	-0.27	N/A	N/A	N/A	N/A	-5.03	N/A	N/A	2.35	N/A	N/A	0.31	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205426	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	F37A	F36A	Beta	31.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	1.35	0.47	-2.01	6.45	N/A	N/A	N/A	N/A	0.13	N/A	N/A	1.36	N/A	N/A	-0.08	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205427	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	L51A	L50A	Coil	0.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.12	-2.0	-6.12	2.34	N/A	N/A	N/A	N/A	-2.34	N/A	N/A	2.4	N/A	N/A	0.46	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V56A	V55A	Coil	22.5	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.44	-0.44	-5.3	3.16	N/A	N/A	N/A	N/A	-1.67	N/A	N/A	2.3	N/A	N/A	0.12	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205429	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I57T	I56T	Coil	15.4	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.36	-0.52	-5.92	2.54	N/A	N/A	N/A	N/A	-2.16	N/A	N/A	2.38	N/A	N/A	0.17	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205431	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I57D	I56D	Coil	15.4	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.46	-0.42	-3.54	4.92	N/A	N/A	N/A	N/A	-0.6	N/A	N/A	1.88	N/A	N/A	0.08	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205432	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	R58A	R57A	Helix	52.8	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.31	-0.57	-7.66	0.8	N/A	N/A	N/A	N/A	-4.05	N/A	N/A	2.3	N/A	N/A	0.42	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205433	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	R58G	R57G	Helix	52.8	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.53	-0.35	-4.94	3.52	N/A	N/A	N/A	N/A	-1.65	N/A	N/A	2.08	N/A	N/A	0.09	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205434	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	E61A	E60A	Helix	13.9	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.42	-0.46	-5.32	3.14	N/A	N/A	N/A	N/A	-1.89	N/A	N/A	2.18	N/A	N/A	0.13	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205435	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	E61G	E60G	Helix	13.9	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.57	-0.31	-3.97	4.49	N/A	N/A	N/A	N/A	-0.79	N/A	N/A	2.03	N/A	N/A	0.06	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205436	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V3A	V2A	Beta	21.1	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.38	-2.26	-6.62	1.84	N/A	N/A	N/A	N/A	-2.47	N/A	N/A	2.63	N/A	N/A	0.55	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205416	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V5A	V4A	Beta	23.2	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.95	-1.83	-5.6	2.86	N/A	N/A	N/A	N/A	-1.54	N/A	N/A	2.58	N/A	N/A	0.39	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205417	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I8V	I7V	Beta	50.3	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.64	-0.24	-7.15	1.31	N/A	N/A	N/A	N/A	-3.55	N/A	N/A	2.28	N/A	N/A	0.16	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205418	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T28S	T27S	Beta	24.6	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.72	-1.6	-7.54	0.92	N/A	N/A	N/A	N/A	-3.44	N/A	N/A	2.6	N/A	N/A	0.63	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205425	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.6	N/A	-8.1	N/A	24.03	N/A	N/A	N/A	N/A	N/A	-5.07	2.2	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.,	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205414	2005.0	15689503	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T22V	T21V	Beta	19.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	1.76	0.88	-9.03	-0.57	N/A	N/A	N/A	N/A	-5.56	N/A	N/A	2.21	N/A	N/A	0.61	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205421	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I92V	I91V	Beta	5.9	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.37	-0.51	-8.33	0.13	N/A	N/A	N/A	N/A	-4.54	N/A	N/A	2.4	N/A	N/A	0.8	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205444	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I92A	I91A	Beta	5.9	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.88	0.0	-5.86	2.6	N/A	N/A	N/A	N/A	-2.47	N/A	N/A	2.16	N/A	N/A	0.0	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205445	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	L98A	L97A	Beta	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.05	-0.93	-3.38	5.08	N/A	N/A	N/A	N/A	-0.32	N/A	N/A	1.93	N/A	N/A	0.16	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205446	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	I57A	I56A	Coil	15.4	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.02	-0.9	-5.17	3.29	N/A	N/A	N/A	N/A	-1.58	N/A	N/A	2.28	N/A	N/A	0.21	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205430	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	E62A	E61A	Helix	38.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	0.75	-0.13	-7.17	1.29	N/A	N/A	N/A	N/A	-3.59	N/A	N/A	2.28	N/A	N/A	0.09	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205437	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	E62G	E61G	Helix	38.7	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.16	-1.04	-5.29	3.17	N/A	N/A	N/A	N/A	-1.59	N/A	N/A	2.35	N/A	N/A	0.25	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205438	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	V64A	V63A	Helix	0.0	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-1.56	-2.44	-5.88	2.58	N/A	N/A	N/A	N/A	-2.5	N/A	N/A	2.16	N/A	N/A	0.49	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205439	1999.0	10438631	2	yes	2023-06-04 01:00:00
FKBP12	Homo sapiens	107.0	P62942	1fkb	A	Alpha Beta	PF00254	1fkbA00 (3.10.50.40)	5.2.1.8	T76A	T75A	Beta	14.1	25.0	7.5	Tris	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	-0.65	-1.53	-5.51	2.95	N/A	N/A	N/A	N/A	-1.55	N/A	N/A	2.5	N/A	N/A	0.34	N/A	N/A	Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205440	1999.0	10438631	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.02	N/A	-3.88	N/A	14.62	N/A	N/A	N/A	N/A	N/A	-3.46	1.17	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205420	2005.0	15689503	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	WT	WT	N/A	N/A	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.02	N/A	-9.51	N/A	30.92	N/A	N/A	N/A	N/A	N/A	-4.28	3.99	3.73	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205420	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	I8V	I8V	Beta	0.6	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.81	-0.21	-7.14	2.37	24.56	-6.36	N/A	N/A	N/A	N/A	-4.22	3.54	3.17	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205421	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V12A	V12A	Coil	11.3	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.88	-0.14	-6.36	3.15	22.8	-8.12	N/A	N/A	N/A	N/A	-4.17	3.31	3.06	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205422	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	L13A	L13A	Coil	36.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.79	-0.23	-7.14	2.37	24.56	-6.36	N/A	N/A	N/A	N/A	-4.22	3.54	3.15	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205423	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	Y18A	Y18A	Helix	28.8	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.76	-0.26	-9.83	-0.32	31.17	0.25	N/A	N/A	N/A	N/A	-3.99	3.99	3.91	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205424	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	F21A	F21A	Helix	9.6	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.86	-0.16	-7.3	2.21	25.1	-5.82	N/A	N/A	N/A	N/A	-4.11	3.31	3.39	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205425	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	Y26A	Y26A	Beta	2.7	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.93	-1.09	-2.76	6.75	11.63	-19.29	N/A	N/A	N/A	N/A	-3.71	2.57	1.85	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205426	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V30A	V30A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.75	-1.27	-5.94	3.57	19.04	-11.88	N/A	N/A	N/A	N/A	-4.56	3.77	2.3	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205427	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	I39V	I39V	Helix	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.35	-0.67	-7.83	1.68	25.1	-5.82	N/A	N/A	N/A	N/A	-4.51	3.82	3.03	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V43A	V43A	Helix	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.91	-1.11	-5.83	3.68	19.16	-11.8	N/A	N/A	N/A	N/A	-5.19	3.37	2.24	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205429	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V49A	V49A	Coil	15.5	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.65	-0.37	-5.07	4.44	19.08	-11.84	N/A	N/A	N/A	N/A	-4.79	3.54	2.29	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205430	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V51A	V51A	Beta	4.2	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.51	-0.51	-4.54	4.97	17.36	-13.56	N/A	N/A	N/A	N/A	-4.34	2.85	2.41	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205431	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V54A	V54A	Beta	11.3	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.86	-0.16	-3.36	6.15	15.31	-15.61	N/A	N/A	N/A	N/A	-5.02	2.57	2.03	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205432	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	L57A	L57A	Beta	51.2	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.74	-0.28	-7.88	1.63	26.28	-4.64	N/A	N/A	N/A	N/A	-4.05	3.65	3.42	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205433	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	I80A	I80A	Beta	12.4	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.23	-0.79	-5.57	3.94	19.25	-11.67	N/A	N/A	N/A	N/A	-4.51	3.25	2.49	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205434	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V81A	V81A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.24	-1.78	-6.49	3.02	19.12	-11.8	N/A	N/A	N/A	N/A	-4.62	3.25	2.44	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205435	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	V83A	V83A	Beta	4.9	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.91	-1.11	-5.34	4.17	17.95	-12.97	N/A	N/A	N/A	N/A	-4.17	3.71	2.3	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205436	2004.0	15136744	2	yes	2023-06-04 01:00:00
L23	Thermus thermophilus	96.0	Q9RA57	1n88	A	Alpha Beta	PF00276	1n88A00 (3.30.70.330)	N/A	I89A	I89A	Coil	1.8	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.81	-0.21	-5.73	3.78	21.09	-9.83	N/A	N/A	N/A	N/A	-4.05	3.25	2.88	N/A	N/A	N/A	N/A	Hedberg, L., Oliveberg, M.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205437	2004.0	15136744	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)/1divA02 (3.10.430.100)	N/A	WT	WT	N/A	N/A	25.0	7.0	Tris	0.02	N/A	N/A	N/A	stopped-flow	urea	6.55	N/A	0.08	N/A	16.03	N/A	N/A	N/A	N/A	N/A	-1.84	0.71	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L141A	L141A	Beta	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	0.57	-2.7	-4.67	3.18	12.97	-14.6	N/A	N/A	N/A	N/A	-3.89	1.55	N/A	N/A	0.46	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	V143A	V143A	Beta	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.02	-1.25	-3.51	4.34	13.68	-13.89	N/A	N/A	N/A	N/A	-3.77	1.13	N/A	N/A	0.22	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	H144Q	H144Q	Beta	21.2	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.38	0.11	-6.5	1.35	22.68	-4.89	N/A	N/A	N/A	N/A	-3.14	1.38	N/A	N/A	-0.07	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	V145A	V145A	Beta	1.4	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.65	-0.62	-5.22	2.63	19.5	-8.07	N/A	N/A	N/A	N/A	-3.35	1.38	N/A	N/A	0.19	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	K96G	K96G	Helix	51.2	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.5	0.23	-6.21	1.64	24.1	-3.47	N/A	N/A	N/A	N/A	-3.05	1.13	N/A	N/A	N/A	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	K96A	K96A	Helix	51.2	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.47	0.2	-10.03	-2.18	33.47	5.9	N/A	N/A	N/A	N/A	-2.93	1.88	N/A	N/A	0.08	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	E100G	E100G	Helix	59.8	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.67	-0.6	-4.42	3.43	17.61	-9.96	N/A	N/A	N/A	N/A	-2.89	0.96	N/A	N/A	0.15	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	E100A	E100A	Helix	59.8	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.3	0.03	-6.32	1.53	23.85	-3.72	N/A	N/A	N/A	N/A	-3.05	1.13	N/A	N/A	-0.02	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)/1divA02 (3.10.430.100)	N/A	WT	WT	N/A	N/A	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.76	N/A	-0.11	N/A	17.02	N/A	N/A	N/A	N/A	N/A	-1.88	0.84	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.054	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	M1G	M1G	Coil	38.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.66	-1.1	2.19	2.3	8.58	-8.44	N/A	N/A	N/A	N/A	-2.38	0.92	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.055	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	M1A	M1A	Coil	38.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.94	-0.82	1.43	1.54	11.18	-5.84	N/A	N/A	N/A	N/A	-2.13	0.84	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.056	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V3I	V3I	Beta	0.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.92	0.16	0.84	0.95	15.06	-1.96	N/A	N/A	N/A	N/A	-1.8	1.05	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.057	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V3L	V3L	Beta	0.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.58	0.82	4.21	4.32	8.35	-8.67	N/A	N/A	N/A	N/A	-2.38	1.05	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.058	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V3A	V3A	Beta	0.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.05	-1.71	2.4	2.51	6.57	-10.45	N/A	N/A	N/A	N/A	-2.47	1.21	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.059	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	I4V	I4V	Beta	3.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.42	-0.34	0.2	0.31	15.43	-1.59	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.060	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	I4A	I4A	Beta	3.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.35	-1.41	1.9	2.01	8.55	-8.47	N/A	N/A	N/A	N/A	-2.55	0.84	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.061	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	L6I	L6I	Coil	37.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.66	-0.1	0.06	0.17	16.37	-0.65	N/A	N/A	N/A	N/A	-1.92	0.88	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.062	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	L6V	L6V	Coil	37.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.45	-0.31	0.62	0.73	14.46	-2.56	N/A	N/A	N/A	N/A	-1.97	0.79	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.063	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	L6A	L6A	Coil	37.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.74	-1.02	3.25	3.36	6.17	-10.85	N/A	N/A	N/A	N/A	-2.59	1.09	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.064	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V21I	V21I	Coil	7.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.09	0.33	1.41	1.52	14.06	-2.96	N/A	N/A	N/A	N/A	-2.05	0.67	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.065	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V21L	V21L	Coil	7.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.92	0.16	2.34	2.45	11.35	-5.67	N/A	N/A	N/A	N/A	-2.26	0.71	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.066	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	V21A	V21A	Coil	7.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.74	-1.02	1.92	2.03	9.47	-7.55	N/A	N/A	N/A	N/A	-2.22	1.26	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.067	2005.0	16246369	2	yes	2023-06-04 01:00:00
NTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)	N/A	L30A	L30A	Coil	4.3	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.16	-0.6	3.27	3.38	7.16	-9.86	N/A	N/A	N/A	N/A	-2.22	1.21	N/A	N/A	N/A	N/A	N/A	Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.	Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693–705. https://doi.org/10.1016/j.jmb.2005.08.069	2005.0	16246369	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA01 (3.40.5.10)/1divA02 (3.10.430.100)	N/A	WT	WT	N/A	N/A	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.27	N/A	-7.85	N/A	27.57	N/A	N/A	N/A	N/A	N/A	-3.1	1.38	N/A	N/A	N/A	N/A	N/A	Li, Y., Gupta, R., Cho, J.-H., Raleigh, D.P.	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L72A	L72A	Helix	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	1.42	-1.85	-3.51	4.34	12.68	-14.89	N/A	N/A	N/A	N/A	-3.68	1.92	N/A	N/A	0.31	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	I79A	I79A	Beta	5.3	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.53	-0.74	-2.66	5.19	12.76	-14.81	N/A	N/A	N/A	N/A	-3.43	1.46	N/A	N/A	0.13	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	I93A	I93A	Beta	7.7	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.83	-0.44	-2.66	5.19	13.6	-13.97	N/A	N/A	N/A	N/A	-2.97	1.59	N/A	N/A	0.08	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	I98A	I98A	Helix	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.64	-0.63	-0.51	7.34	7.82	-19.75	N/A	N/A	N/A	N/A	-3.89	1.3	N/A	N/A	0.08	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L102A	L102A	Helix	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.51	-0.76	-3.91	3.94	16.15	-11.42	N/A	N/A	N/A	N/A	-3.18	1.21	N/A	N/A	0.17	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	H106Q	H106Q	Helix	34.8	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.12	-0.15	-3.91	3.94	17.53	-10.04	N/A	N/A	N/A	N/A	-3.22	1.05	N/A	N/A	0.04	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L108A	L108A	Coil	14.6	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.17	-0.1	-3.51	4.34	16.9	-10.67	N/A	N/A	N/A	N/A	-3.39	1.26	N/A	N/A	0.02	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L110A	L110A	Coil	11.6	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.01	-0.26	-2.81	5.04	14.52	-13.05	N/A	N/A	N/A	N/A	-3.47	1.38	N/A	N/A	0.05	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	I115A	I115A	Beta	3.6	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.08	-0.19	-1.71	6.14	11.88	-15.69	N/A	N/A	N/A	N/A	-3.39	1.21	N/A	N/A	0.03	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L117A	L117A	Coil	22.6	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	3.07	-0.2	-7.42	0.43	25.98	-1.59	N/A	N/A	N/A	N/A	-3.22	1.59	N/A	N/A	0.31	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	I121A	I121A	Beta	9.5	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.95	-0.32	-2.66	5.19	13.89	-13.68	N/A	N/A	N/A	N/A	-3.14	1.38	N/A	N/A	0.06	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	V129A	V129A	Beta	1.4	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	2.56	-0.71	-5.78	2.07	20.67	-6.9	N/A	N/A	N/A	N/A	-3.68	1.26	N/A	N/A	0.26	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	V131A	V131A	Beta	0.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	1.35	-1.92	-7.42	0.43	21.71	-5.86	N/A	N/A	N/A	N/A	-3.43	1.76	N/A	N/A	0.82	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	L133A	L133A	Beta	11.6	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	0.11	-3.16	-6.03	1.82	15.23	-12.34	N/A	N/A	N/A	N/A	-3.47	1.72	N/A	N/A	0.63	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	H134Q	H134Q	Beta	19.0	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	1.13	-2.14	-6.12	1.73	18.45	-9.12	N/A	N/A	N/A	N/A	-3.47	1.63	N/A	N/A	0.55	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
CTL9	Geobacillus stearothermophilus	149.0	P02417	1div	A	Alpha Beta	PF01281/PF03948	1divA02 (3.10.430.100)	N/A	V137A	V137A	Beta	3.5	25.0	8.0	Phosphate	0.02	N/A	N/A	N/A	stopped-flow	urea	1.33	-1.94	-6.57	1.28	19.58	-7.99	N/A	N/A	N/A	N/A	-3.22	2.01	N/A	N/A	0.6	N/A	N/A	N/A	Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013–1021. https://doi.org/10.1021/bi061516j	2007.0	17240985	2	yes	2023-06-04 01:00:00
Src SH3	Gallus gallus	64.0	P00523	1rlq	C	Mainly Beta	PF00018	1rlqC00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.36	N/A	-1.27	N/A	13.95	N/A	N/A	N/A	N/A	N/A	-4.19	1.7	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.1	N/A	-3.25	N/A	18.21	N/A	N/A	N/A	N/A	N/A	-6.38	2.08	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	WT	WT	N/A	N/A	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.1	N/A	N/A	N/A	N/A	N/A	3.08	N/A	-2.21	N/A	-6.28	2.09	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3701	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	V41A	V18A	Beta	23.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.7	-1.4	N/A	N/A	N/A	N/A	1.78	-1.3	-1.31	0.9	-5.86	2.55	N/A	N/A	0.67	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3702	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T42A	T19A	Beta	63.4	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.28	-0.82	N/A	N/A	N/A	N/A	2.21	-0.87	-0.09	2.12	-6.69	2.47	N/A	N/A	0.3	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3703	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I43A	I20A	Beta	1.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.22	-2.88	N/A	N/A	N/A	N/A	0.1	-2.98	2.97	5.18	-6.69	3.22	N/A	N/A	0.34	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3704	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I43V	I20V	Beta	1.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.33	-0.77	N/A	N/A	N/A	N/A	2.33	-0.75	-1.77	0.44	-6.28	2.34	N/A	N/A	0.82	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3705	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K44A	K21A	Beta	37.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.0	-1.1	N/A	N/A	N/A	N/A	2.07	-1.01	-1.61	0.6	-5.86	2.09	N/A	N/A	0.7	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3707	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A45G	A22G	Beta	0.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.34	-1.76	N/A	N/A	N/A	N/A	1.05	-2.03	-0.53	1.68	-7.95	2.26	N/A	N/A	0.43	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3708	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	N46A	N23A	Beta	14.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.95	-0.15	N/A	N/A	N/A	N/A	2.74	-0.34	0.11	2.32	-7.53	2.34	N/A	N/A	0.05	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3709	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	L47A	L24A	Beta	1.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.45	-1.65	N/A	N/A	N/A	N/A	1.14	-1.94	0.19	2.4	-7.95	2.26	N/A	N/A	0.31	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3710	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I48A	I25A	Beta	21.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.69	-1.41	N/A	N/A	N/A	N/A	1.59	-1.49	-1.56	0.65	-6.69	2.01	N/A	N/A	0.59	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3711	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I48V	I25V	Beta	21.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.01	-0.09	N/A	N/A	N/A	N/A	2.95	-0.13	-1.56	0.65	-6.69	2.05	N/A	N/A	0.11	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3712	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F49A	F26A	Coil	11.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.46	-0.64	N/A	N/A	N/A	N/A	2.17	-0.91	1.23	3.44	-7.95	2.34	N/A	N/A	0.12	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3714	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F49L	F26L	Coil	11.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.14	0.04	N/A	N/A	N/A	N/A	3.14	0.06	-1.43	0.78	-6.28	2.18	N/A	N/A	-0.03	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3715	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A50P	A27P	Coil	56.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.42	0.32	N/A	N/A	N/A	N/A	3.41	0.33	-1.77	0.44	-6.28	2.34	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3717	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A50V	A27V	Coil	56.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.0	-1.1	N/A	N/A	N/A	N/A	1.82	-1.26	-1.35	0.86	-7.11	2.47	N/A	N/A	0.78	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3718	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	N51A	N28A	Coil	73.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.0	-2.1	N/A	N/A	N/A	N/A	0.84	-2.24	-1.51	0.7	-7.11	2.3	N/A	N/A	0.67	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3719	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	G52A	G29A	Coil	70.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.96	-2.14	N/A	N/A	N/A	N/A	0.74	-2.34	-1.9	0.31	-7.53	2.43	N/A	N/A	0.86	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3720	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	G52V	G29V	Coil	70.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.45	-2.65	N/A	N/A	N/A	N/A	0.22	-2.86	-0.8	1.41	-7.53	2.43	N/A	N/A	0.61	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3721	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	N51A/G52A	N28A/G29A	Coil/Coil	73.9/70.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.05	-3.05	N/A	N/A	N/A	N/A	-0.26	-3.34	-1.27	0.94	-7.95	2.18	N/A	N/A	0.65	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3724	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	S53A	S30A	Coil	46.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	0.1	N/A	N/A	N/A	N/A	3.11	0.03	-1.9	0.31	-6.69	2.13	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3725	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T54A	T31A	Coil	63.4	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.28	-0.82	N/A	N/A	N/A	N/A	2.22	-0.86	-1.05	1.16	-6.69	2.26	N/A	N/A	0.42	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3726	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T56A	T33A	Beta	47.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.79	-0.31	N/A	N/A	N/A	N/A	2.72	-0.36	-1.11	1.1	-6.69	2.43	N/A	N/A	0.17	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3727	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A57G	A34G	Beta	2.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.95	-1.15	N/A	N/A	N/A	N/A	1.8	-1.28	-0.08	2.13	-7.11	2.43	N/A	N/A	0.31	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3728	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A57V	A34V	Beta	2.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.48	1.38	N/A	N/A	N/A	N/A	4.65	1.57	-2.41	-0.2	-5.02	2.26	N/A	N/A	0.54	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3729	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	E58A	E35A	Beta	69.1	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.03	-1.07	N/A	N/A	N/A	N/A	2.08	-1.0	-1.97	0.24	-5.86	18.95	N/A	N/A	1.08	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3730	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F59A	F36A	Beta	8.1	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	0.82	-3.28	N/A	N/A	N/A	N/A	-0.36	-3.44	2.68	4.89	-7.11	3.39	N/A	N/A	0.45	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3731	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F59L	F36L	Beta	8.1	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.75	-1.35	N/A	N/A	N/A	N/A	1.49	-1.59	1.55	3.76	-7.53	2.89	N/A	N/A	0.25	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3732	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K60A	K37A	Beta	56.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.25	-0.85	N/A	N/A	N/A	N/A	2.22	-0.86	-1.27	0.94	-6.28	2.13	N/A	N/A	0.57	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3734	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	G61A	G38A	Beta	27.4	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.38	-0.72	N/A	N/A	N/A	N/A	2.22	-0.86	-0.17	2.04	-7.11	2.43	N/A	N/A	0.2	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3735	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T62A	T39A	Coil	55.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.32	-0.78	N/A	N/A	N/A	N/A	2.33	-0.75	-1.31	0.9	-5.86	2.22	N/A	N/A	0.37	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3736	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F63G	F40G	Coil	39.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.06	-1.04	N/A	N/A	N/A	N/A	1.74	-1.34	1.05	3.26	-7.95	2.64	N/A	N/A	0.2	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3737	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F63L	F40L	Coil	39.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.95	-0.15	N/A	N/A	N/A	N/A	3.01	-0.07	-1.56	0.65	-5.86	2.26	N/A	N/A	0.24	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3738	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K65G	K42G	Helix	56.6	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.85	-0.25	N/A	N/A	N/A	N/A	2.93	-0.15	-2.21	0.0	-5.44	2.09	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3740	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A66G	A43G	Helix	3.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.23	-0.87	N/A	N/A	N/A	N/A	2.12	-0.96	0.59	2.8	-6.69	2.18	N/A	N/A	0.2	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3741	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T67A	T44A	Helix	21.1	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.85	-0.25	N/A	N/A	N/A	N/A	2.89	-0.19	-0.48	1.73	-5.86	2.55	N/A	N/A	0.14	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3742	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	S68A	S45A	Helix	50.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.47	0.37	N/A	N/A	N/A	N/A	3.48	0.4	-2.41	-0.2	-6.28	2.3	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3743	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	S68G	S45G	Helix	50.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.05	-0.05	N/A	N/A	N/A	N/A	2.92	-0.16	-1.11	1.1	-7.11	2.3	N/A	N/A	0.04	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3744	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	E69G	E46G	Helix	49.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.88	-0.22	N/A	N/A	N/A	N/A	2.82	-0.26	-0.84	1.37	-6.28	2.38	N/A	N/A	0.11	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3746	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	E69I	E46I	Helix	49.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.01	-0.09	N/A	N/A	N/A	N/A	3.01	-0.07	-0.54	1.67	-6.28	2.64	N/A	N/A	0.05	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3747	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A70G	A47G	Helix	0.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.2	-0.9	N/A	N/A	N/A	N/A	1.84	-1.24	1.13	3.34	-8.37	2.51	N/A	N/A	0.17	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3748	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	Y71A	Y48A	Helix	48.2	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.28	0.18	N/A	N/A	N/A	N/A	2.86	-0.22	1.66	3.87	-8.79	2.51	N/A	N/A	-0.04	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3749	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A72G	A49G	Helix	55.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.52	-0.58	N/A	N/A	N/A	N/A	2.5	-0.58	-0.73	1.48	-6.28	2.09	N/A	N/A	0.25	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3750	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	Y73A	Y50A	Helix	45.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.94	-1.16	N/A	N/A	N/A	N/A	1.89	-1.19	0.62	2.83	-6.28	2.55	N/A	N/A	0.27	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3751	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A74G	A51G	Helix	0.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.71	-0.39	N/A	N/A	N/A	N/A	2.48	-0.6	2.62	4.83	-7.53	2.89	N/A	N/A	0.07	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3752	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	D75A	D52A	Helix	55.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.86	0.76	N/A	N/A	N/A	N/A	3.75	0.67	0.04	2.25	-6.69	2.26	N/A	N/A	-0.42	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3753	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	D75G	D52G	Helix	55.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.4	0.3	N/A	N/A	N/A	N/A	3.23	0.15	1.02	3.23	-7.11	2.34	N/A	N/A	-0.08	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3754	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T76G	T53G	Coil	80.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.69	0.59	N/A	N/A	N/A	N/A	3.63	0.55	-1.51	0.7	-6.28	2.51	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3756	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	L77A	L54A	Coil	28.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.78	-0.32	N/A	N/A	N/A	N/A	2.6	-0.48	1.03	3.24	-7.11	2.18	N/A	N/A	0.08	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3757	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	E69G/A72G/T76G	E46G/A49G/T53G	Helix/Helix/Coil	49.5/55.7/80.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.22	-0.88	N/A	N/A	N/A	N/A	2.0	-1.08	1.94	4.15	-7.53	2.8	N/A	N/A	0.18	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3758	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K78A	K55A	Coil	44.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.23	0.13	N/A	N/A	N/A	N/A	3.28	0.2	-2.3	-0.09	-5.86	1.97	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3759	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K79A	K56A	Coil	82.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.11	0.01	N/A	N/A	N/A	N/A	3.14	0.06	-2.21	0.0	-5.86	2.26	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3760	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	N81A	N58A	Coil	25.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.06	-0.04	N/A	N/A	N/A	N/A	3.03	-0.05	-1.51	0.7	-6.28	2.05	N/A	N/A	0.08	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3761	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	G82A	G59A	Coil	59.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.5	0.4	N/A	N/A	N/A	N/A	3.36	0.28	1.21	3.42	-7.11	1.88	N/A	N/A	-0.1	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3762	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	E83A	E60A	Coil	57.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.11	0.01	N/A	N/A	N/A	N/A	3.09	0.01	-1.97	0.24	-6.28	2.26	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3763	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T85A	T62A	Beta	62.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.31	-0.79	N/A	N/A	N/A	N/A	2.36	-0.72	-0.73	1.48	-5.86	2.8	N/A	N/A	0.48	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3764	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	V86A	V63A	Beta	33.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.55	-0.55	N/A	N/A	N/A	N/A	2.54	-0.54	-1.24	0.97	-6.28	2.26	N/A	N/A	0.35	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3765	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	D87A	D64A	Coil	52.1	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.43	0.33	N/A	N/A	N/A	N/A	3.39	0.31	-1.97	0.24	-6.28	2.18	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3766	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	V88A	V65A	Coil	71.8	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.84	-0.26	N/A	N/A	N/A	N/A	2.79	-0.29	-1.08	1.13	-6.28	2.22	N/A	N/A	0.13	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3767	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	A89G	A66G	Beta	44.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.08	-0.02	N/A	N/A	N/A	N/A	3.16	0.08	-1.05	1.16	-5.44	2.26	N/A	N/A	0.04	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3768	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K91A	K68A	Coil	83.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	0.1	N/A	N/A	N/A	N/A	3.15	0.07	-2.04	0.17	-6.28	2.18	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3769	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	G92A	G69A	Coil	33.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.57	-0.53	N/A	N/A	N/A	N/A	2.36	-0.72	0.5	2.71	-7.53	2.64	N/A	N/A	0.18	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3770	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	Y93A	Y70A	Coil	2.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.93	-0.17	N/A	N/A	N/A	N/A	2.71	-0.37	-0.03	2.18	-7.53	2.09	N/A	N/A	0.06	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3771	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	Y93L	Y70L	Coil	2.3	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.62	-0.48	N/A	N/A	N/A	N/A	2.69	-0.39	-1.77	0.44	-5.86	1.97	N/A	N/A	N/A	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3772	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	T94A	T71A	Beta	19.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.88	-0.22	N/A	N/A	N/A	N/A	2.71	-0.37	0.18	2.39	-7.11	2.22	N/A	N/A	0.07	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3774	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	L95A	L72A	Beta	3.7	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.4	-1.7	N/A	N/A	N/A	N/A	1.37	-1.71	2.3	4.51	-6.28	2.89	N/A	N/A	0.26	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3775	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	N96A	N73A	Beta	28.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.75	-0.35	N/A	N/A	N/A	N/A	2.63	-0.45	-0.06	2.15	-6.69	2.09	N/A	N/A	0.12	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3776	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I97A	I74A	Beta	0.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.24	-1.86	N/A	N/A	N/A	N/A	1.69	-1.39	4.8	7.01	-3.35	3.35	N/A	N/A	0.23	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3777	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	I97V	I74V	Beta	0.0	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.62	-0.48	N/A	N/A	N/A	N/A	2.54	-0.54	-0.6	1.61	-6.69	2.47	N/A	N/A	0.17	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3778	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	K98A	K75A	Beta	45.9	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.97	-0.13	N/A	N/A	N/A	N/A	2.93	-0.15	-1.43	0.78	-6.28	2.09	N/A	N/A	0.18	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3780	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F99L	F76L	Beta	0.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.03	-0.07	N/A	N/A	N/A	N/A	2.92	-0.16	2.9	5.11	-6.69	2.55	N/A	N/A	0.01	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3781	2000.0	10801362	2	yes	2023-06-04 01:00:00
Protein LG	Finegoldia magna (Peptostreptococcus magnus)	78.0	Q53291	2ptl	A	Alpha Beta	PF02246	2ptlA00 (3.10.20.10)	N/A	F99V	F76V	Beta	0.5	22.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	0.1	N/A	N/A	N/A	N/A	3.18	0.1	4.41	6.62	-6.28	3.1	N/A	N/A	-0.02	N/A	N/A	Kim, D.E., Fisher, C., Baker, D.	A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971–984. https://doi.org/10.1006/jmbi.2000.3782	2000.0	10801362	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	151.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.88	N/A	-4.34	N/A	22.84	N/A	N/A	N/A	N/A	N/A	-4.92	1.68	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.41	N/A	-0.67	N/A	-5.23	2.03	N/A	0.72	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107D	E107D	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.45	0.04	-1.39	-0.72	-5.62	1.68	N/A	0.77	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107Q	E107Q	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.83	-0.58	-0.12	0.55	-5.52	2.16	N/A	0.72	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107T	E107T	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.92	-0.49	-0.01	0.66	-6.52	1.81	N/A	0.78	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107H	E107H	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.5	-0.91	0.03	0.7	-5.87	1.91	N/A	0.75	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107K	E107K	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.33	-1.08	-0.01	0.66	-5.18	2.16	N/A	0.71	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A	E107A	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.66	-0.75	0.41	1.08	-5.7	1.68	N/A	0.77	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107S	E107S	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.38	-1.03	0.47	1.14	-5.25	2.28	N/A	0.7	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107V	E107V	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.14	-1.27	0.83	1.5	-5.05	1.78	N/A	0.74	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107P	E107P	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.04	-1.37	1.16	1.83	-5.65	1.73	N/A	0.77	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107G	E107G	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.49	-0.92	1.79	2.46	-5.18	1.93	N/A	0.73	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107R	E107R	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.53	-1.88	1.76	2.43	-4.91	1.21	N/A	0.8	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107I	E107I	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.7	-1.71	2.42	3.09	-5.28	1.96	N/A	0.73	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107L	E107L	Coil	10.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.74	-1.67	2.69	3.36	-5.4	2.08	N/A	0.72	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124K	S124K	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.89	-1.52	-1.31	-0.64	-5.72	2.11	N/A	0.73	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124R	S124R	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.67	-1.74	-1.47	-0.8	-5.77	1.78	N/A	0.76	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124L	S124L	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.05	-1.36	-0.97	-0.3	-4.73	2.03	N/A	0.7	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124A	S124A	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.77	-1.64	-1.14	-0.47	-5.35	1.88	N/A	0.74	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124H	S124H	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.77	-1.64	-1.02	-0.35	-5.33	1.93	N/A	0.73	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124V	S124V	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.81	-1.6	-0.89	-0.22	-4.71	1.93	N/A	0.71	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124I	S124I	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.97	-1.44	-0.25	0.42	-4.48	2.18	N/A	0.67	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124N	S124N	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.9	-1.51	0.21	0.88	-4.71	2.65	N/A	0.64	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124T	S124T	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.88	-2.53	-0.06	0.61	-5.3	1.76	N/A	0.75	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124D	S124D	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.72	-1.69	1.03	1.7	-5.35	1.68	N/A	0.76	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124G	S124G	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.31	-2.1	0.79	1.46	-4.58	2.01	N/A	0.7	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124F	S124F	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.38	-1.03	1.97	2.64	-3.99	2.21	N/A	0.65	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	S124Y	S124Y	Beta	0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.57	-1.84	1.36	2.03	-4.91	2.13	N/A	0.7	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A/S124L	E107A/S124L	Coil/Beta	10.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.56	-0.85	-0.42	0.25	-4.96	2.01	N/A	0.71	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A/S124D	E107A/S124D	Coil/Beta	10.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.73	0.32	1.13	1.8	-5.62	1.98	N/A	0.74	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A/S124K	E107A/S124K	Coil/Beta	10.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.74	-2.67	-1.47	-0.8	-4.78	1.91	N/A	0.71	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A/S124A	E107A/S124A	Coil/Beta	10.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.1	-2.31	-0.49	0.18	-4.96	1.88	N/A	0.72	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E107A/S124R	E107A/S124R	Coil/Beta	10.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.59	-2.82	-0.92	-0.25	-4.56	1.78	N/A	0.72	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T127A	T127A	Coil	56.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.0	-3.41	0.53	1.2	-5.62	1.83	N/A	0.75	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	G128A	G128A	Coil	31.0	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.79	-2.62	-0.45	0.22	-5.72	1.76	N/A	0.77	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T127A/S124K	T127A/S124K	Coil/Beta	56.3/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	-0.97	-4.38	0.31	0.98	-4.58	1.64	N/A	0.74	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	62.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	G128A/S124K	G128A/S124K	Coil/Beta	31.0/0.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	-0.71	-4.12	-0.71	-0.04	-6.62	1.59	N/A	0.81	N/A	N/A	N/A	Northey JGB, Maxwell KL, Davidson AR	Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X	2002.0	12079394	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.41	N/A	-0.67	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-8.83	3.43	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb748	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87S	F87S	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.7	-0.71	1.95	2.62	N/A	-8.2	N/A	N/A	N/A	N/A	-7.49	1.88	N/A	N/A	0.21	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb749	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87A	F87A	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.78	-0.63	0.96	1.63	N/A	-5.61	N/A	N/A	N/A	N/A	-7.95	4.06	N/A	N/A	0.28	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb750	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87V	F87V	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.17	-0.24	-0.13	0.54	N/A	-1.97	N/A	N/A	N/A	N/A	-8.58	3.18	N/A	N/A	0.3	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb751	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87L	F87L	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.97	-0.44	2.25	2.92	N/A	-8.33	N/A	N/A	N/A	N/A	-8.37	3.64	N/A	N/A	0.13	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb752	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A89S	A89S	Beta	2.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.1	-0.31	1.16	1.83	N/A	-5.27	N/A	N/A	N/A	N/A	-7.91	4.31	N/A	N/A	0.14	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb753	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A89G	A89G	Beta	2.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.92	-0.49	1.48	2.15	N/A	-6.53	N/A	N/A	N/A	N/A	-8.37	2.8	N/A	N/A	0.18	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb754	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A89L/F103L	A89L/F103L	Beta/Beta	2.8/2.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.95	0.54	4.52	5.19	N/A	-11.55	N/A	N/A	N/A	N/A	-6.28	2.72	N/A	N/A	-0.11	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb755	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L101V	L101V	Coil	4.9	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.23	-0.18	1.9	2.57	N/A	-6.82	N/A	N/A	N/A	N/A	-8.95	3.89	N/A	N/A	0.06	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb756	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L101I	L101I	Coil	4.9	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.49	0.08	0.59	1.26	N/A	-2.89	N/A	N/A	N/A	N/A	-8.66	4.14	N/A	N/A	-0.07	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb757	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L101F	L101F	Coil	4.9	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.72	0.31	1.67	2.34	N/A	-5.02	N/A	N/A	N/A	N/A	-8.62	4.14	N/A	N/A	-0.15	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb758	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F103S	F103S	Beta	2.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.73	-0.68	3.77	4.44	N/A	-12.68	N/A	N/A	N/A	N/A	-6.95	2.01	N/A	N/A	0.13	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb759	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F103A	F103A	Beta	2.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.49	-0.92	2.49	3.16	N/A	-10.08	N/A	N/A	N/A	N/A	-7.24	2.93	N/A	N/A	0.22	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb760	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F103V	F103V	Beta	2.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.49	0.08	2.58	3.25	N/A	-7.87	N/A	N/A	N/A	N/A	-7.74	4.39	N/A	N/A	-0.03	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb761	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F103L	F103L	Beta	2.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.43	0.02	1.22	1.89	N/A	-4.64	N/A	N/A	N/A	N/A	-7.41	3.56	N/A	N/A	-0.01	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb762	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F109V	F109V	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.86	-0.55	2.33	3.0	N/A	-8.83	N/A	N/A	N/A	N/A	-6.57	4.18	N/A	N/A	0.15	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb763	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F109I	F109I	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.48	0.07	2.77	3.44	N/A	-8.33	N/A	N/A	N/A	N/A	-6.86	3.81	N/A	N/A	-0.02	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb764	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F109L	F109L	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.64	0.23	0.83	1.5	N/A	-3.18	N/A	N/A	N/A	N/A	-7.91	3.89	N/A	N/A	-0.18	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb765	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111S	I111S	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	-0.21	-3.62	0.88	1.55	N/A	-12.72	N/A	N/A	N/A	N/A	-5.69	2.76	N/A	N/A	0.7	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb766	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111A	I111A	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	0.22	-3.19	0.59	1.26	N/A	-11.05	N/A	N/A	N/A	N/A	-7.95	3.77	N/A	N/A	0.71	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb767	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111V	I111V	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.02	-0.39	-0.82	-0.15	N/A	-0.67	N/A	N/A	N/A	N/A	-9.58	3.18	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb768	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111L	I111L	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.97	-0.44	0.59	1.26	N/A	-4.23	N/A	N/A	N/A	N/A	-8.74	3.97	N/A	N/A	0.25	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb769	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111F	I111F	Beta	17.8	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.61	-1.8	2.13	2.8	N/A	-11.34	N/A	N/A	N/A	N/A	-8.2	3.93	N/A	N/A	0.39	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb770	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122S	A122S	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	0.83	-2.58	1.06	1.73	N/A	-10.63	N/A	N/A	N/A	N/A	-9.67	3.68	N/A	N/A	0.6	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb771	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122G	A122G	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.46	-1.95	-0.36	0.31	N/A	-5.65	N/A	N/A	N/A	N/A	-8.95	3.56	N/A	N/A	0.86	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb772	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122V	A122V	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	5.49	2.08	1.1	1.77	N/A	0.75	N/A	N/A	N/A	N/A	-8.41	4.56	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb773	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122L	A122L	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.87	-1.54	1.84	2.51	N/A	-10.0	N/A	N/A	N/A	N/A	-8.66	3.56	N/A	N/A	0.38	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb774	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122F	A122F	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.63	0.22	3.27	3.94	N/A	-9.2	N/A	N/A	N/A	N/A	-7.57	2.64	N/A	N/A	-0.06	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb775	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I133A	I133A	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.44	-1.97	2.62	3.29	N/A	-13.05	N/A	N/A	N/A	N/A	-3.35	3.64	N/A	N/A	0.37	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb776	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I133V	I133V	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.17	-0.24	-0.87	-0.2	N/A	-0.17	N/A	N/A	N/A	N/A	-8.91	2.76	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb777	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I133L	I133L	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.87	-0.54	0.1	0.77	N/A	-3.14	N/A	N/A	N/A	N/A	-8.54	3.26	N/A	N/A	0.42	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb778	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I133F	I133F	Beta	0.0	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.28	-0.13	5.08	5.75	N/A	-14.52	N/A	N/A	N/A	N/A	-7.45	3.39	N/A	N/A	0.02	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb779	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	V138A	V138A	Beta	9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.37	-0.04	2.89	3.56	N/A	-8.91	N/A	N/A	N/A	N/A	-8.16	4.02	N/A	N/A	0.01	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb780	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	V138I	V138I	Beta	9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.96	0.55	-0.42	0.25	N/A	0.71	N/A	N/A	N/A	N/A	-9.08	4.14	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb781	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	V138L	V138L	Beta	9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	3.99	0.58	0.11	0.78	N/A	-0.5	N/A	N/A	N/A	N/A	-8.7	4.31	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb782	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	V138F	V138F	Beta	9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	4.43	1.02	1.59	2.26	N/A	-3.05	N/A	N/A	N/A	N/A	-8.45	4.27	N/A	N/A	-0.82	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb783	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122G/V138I	A122G/V138I	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.63	-1.78	-0.4	0.27	N/A	-5.06	N/A	N/A	N/A	N/A	-8.95	3.43	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb784	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122V/V138I	A122V/V138I	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	6.06	2.65	0.99	1.66	N/A	2.26	N/A	N/A	N/A	N/A	-8.49	4.77	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb785	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122G/V138L	A122G/V138L	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	1.72	-1.69	-0.78	-0.11	N/A	-3.93	N/A	N/A	N/A	N/A	-9.12	3.1	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb786	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122V/V138L	A122V/V138L	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	5.81	2.4	1.59	2.26	N/A	0.29	N/A	N/A	N/A	N/A	-8.12	4.6	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb787	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122G/V138F	A122G/V138F	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	2.37	-1.04	0.57	1.24	N/A	-5.65	N/A	N/A	N/A	N/A	-10.25	3.68	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb788	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122V/V138F	A122V/V138F	Beta/Beta	0.0/9.2	25.0	8.0	Tris	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	6.38	2.97	4.59	5.26	N/A	-5.69	N/A	N/A	N/A	N/A	-8.58	3.35	N/A	N/A	N/A	N/A	N/A	Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.	Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126–130. https://doi.org/10.1038/nsb789	2002.0	11786916	2	yes	2023-06-04 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.92	N/A	-0.94	N/A	-4.41	2.18	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136A	N136A	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.18	0.26	-0.89	0.05	-4.83	2.25	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136I	N136I	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.78	0.86	0.35	1.29	-4.73	2.3	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136F	N136F	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.53	0.61	0.41	1.35	-4.93	2.21	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136K	N136K	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.19	0.27	-0.11	0.83	-5.28	2.28	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136D	N136D	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.65	-0.27	-0.97	-0.03	-4.91	1.81	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136S	N136S	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.18	0.26	-0.97	-0.03	-5.05	2.08	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136L	N136L	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.25	0.33	0.49	1.43	-4.93	1.96	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136V	N136V	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.32	0.4	0.56	1.5	-5.2	2.13	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136P	N136P	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.62	0.7	1.66	2.6	-4.98	1.56	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136Y	N136Y	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.62	0.7	0.1	1.04	-4.91	2.3	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136H	N136H	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.37	0.45	-0.05	0.89	-5.18	2.23	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136E	N136E	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.09	0.17	-0.67	0.27	-4.93	1.98	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136T	N136T	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.98	0.06	-0.03	0.91	-4.96	2.5	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136R	N136R	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.21	0.29	0.04	0.98	-5.08	2.4	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136Q	N136Q	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.25	0.33	0.05	0.99	-4.98	2.23	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136M	N136M	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.31	0.39	0.31	1.25	-4.68	2.45	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136W	N136W	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.99	1.07	-1.27	-0.33	-4.83	2.45	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136G	N136G	Helix	78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.97	0.05	-0.07	0.87	-4.96	2.16	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L86A	L86A	Beta	34.1	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.92	0.0	1.05	1.99	-4.98	2.16	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87A	F87A	Beta	17.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.73	-0.19	0.03	0.97	-4.61	2.4	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	R123I	R123I	Beta	48.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.42	0.5	-0.4	0.54	-4.39	2.53	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T130I	T130I	Beta	45.8	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.85	0.93	-0.97	-0.03	-4.61	2.28	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L86A/N136A	L86A/N136A	Beta/Helix	34.1/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.33	0.41	1.28	2.22	-4.63	2.18	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L86A/N136I	L86A/N136I	Beta/Helix	34.1/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.31	0.39	2.46	3.4	-4.16	2.03	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87A/N136A	F87A/N136A	Beta/Helix	17.8/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.04	0.12	0.97	1.91	-5.05	1.46	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87A/N136I	F87A/N136I	Beta/Helix	17.8/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.12	0.2	2.19	3.13	-4.71	1.68	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	R123I/N136I	R123I/N136I	Beta/Helix	48.8/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.6	0.68	0.71	1.65	-4.51	2.4	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T130I/N136I	T130I/N136I	Beta/Helix	45.8/78.3	25.0	8.0	Tris-HCl	0.01	N/A	N/A	0.2 mM EDTA	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	5.21	1.29	0.66	1.6	-4.48	2.48	N/A	N/A	N/A	N/A	N/A	Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS	Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999–10004. https://doi.org/10.1073/pnas.0801874105	2008.0	18626019	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	WT	WT	N/A	N/A	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.03	N/A	-0.87	N/A	-5.2	2.16	N/A	0.7	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F87V	F87V	Beta	17.8	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.81	-0.22	-0.11	0.76	-4.71	1.54	N/A	0.75	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E88V	E88V	N/A	N/A	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.38	0.35	-1.43	-0.56	-5.05	2.45	N/A	0.67	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A89S	A89S	Beta	2.8	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.93	-0.1	1.36	2.23	-5.55	1.88	N/A	0.75	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T97R	T97R	Coil	50.7	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.99	-0.04	-1.02	-0.15	-5.15	2.28	N/A	0.69	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F103A	F103A	Beta	2.0	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.18	-0.85	2.22	3.09	-3.72	1.91	N/A	0.66	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	F109V	F109V	Beta	0.0	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.4	-0.63	2.36	3.23	-5.2	1.98	N/A	0.72	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	I111A	I111A	Beta	17.8	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.1	-2.93	0.47	1.34	-5.7	2.23	N/A	0.75	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	L112Y	L112Y	Beta	55.5	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.14	-0.89	-0.24	0.63	-5.43	1.98	N/A	0.73	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E121A	E121A	Beta	31.4	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.22	-0.81	-0.29	0.58	-4.78	1.91	N/A	0.72	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	A122G	A122G	Beta	0.0	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.81	-2.22	-0.48	0.39	-4.83	2.21	N/A	0.69	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	R123N	R123N	Beta	48.8	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.19	-2.84	-0.29	0.58	-5.2	1.96	N/A	0.73	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T126N	T126N	Coil	71.1	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.11	-0.92	-0.62	0.25	-5.18	2.01	N/A	0.72	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	E129A	E129A	Coil	55.7	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.71	-0.32	-0.54	0.33	-5.5	2.25	N/A	0.71	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	T130A	T130A	Beta	45.8	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.89	-1.14	-0.54	0.33	-5.57	2.01	N/A	0.73	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	N136V	N136V	Helix	78.3	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.33	0.3	0.56	1.43	-5.2	2.4	N/A	0.68	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
Fyn SH3	Homo sapiens	59.0	P06241	1shf	A	Mainly Beta	PF00018	1shfA00 (2.30.30.40)	2.7.10.2	V138L	V138L	Beta	9.2	25.0	7.0	Sodium Phosphate	0.01	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.37	0.34	0.1	0.97	-5.03	2.43	N/A	0.67	N/A	N/A	N/A	Lin SL, Zarrine-Afsar A, Davidson AR	The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52	2009.0	19241379	2	yes	2023-06-11 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (3.10.20.10)	N/A	WT	WT	N/A	N/A	25.0	7.0	HEPES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.96	N/A	-3.86	N/A	26.81	N/A	N/A	N/A	N/A	N/A	-9.74	4.8	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	WT	WT	N/A	N/A	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.4	5.4	-9.16	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9384	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	F6A	F5A	Helix	0.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.15	-1.25	-5.68	3.48	N/A	-10.93	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.74	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9385	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	A10G	A9G	Helix	6.6	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	-1.2	-6.76	2.4	N/A	-8.32	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.67	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9386	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	V13A	V12A	Helix	7.7	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.29	-1.11	-7.58	1.58	N/A	-6.21	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.59	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9387	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	L16A	L15A	Coil	0.6	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	3.24	-2.16	-4.89	4.27	N/A	-14.86	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.66	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9388	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	P20A	P19A	Coil	5.9	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.76	0.36	-7.17	1.99	N/A	-3.76	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.22	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9389	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	D22A	D21A	Helix	20.2	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.76	0.36	-8.09	1.07	N/A	-1.64	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.49	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9390	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	L26A	L25A	Helix	9.8	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.59	0.19	-5.33	3.83	N/A	-8.41	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.05	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9391	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	F27A	F26A	Helix	25.9	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.34	-0.06	-6.27	2.89	N/A	-6.82	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.98	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9392	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y29A	Y28A	Helix	27.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.64	1.24	-3.38	5.78	N/A	-10.49	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.27	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9393	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y29N	Y28N	Helix	27.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.9	0.5	-4.23	4.93	N/A	-10.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.11	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9394	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y29F	Y28F	Helix	27.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.93	0.53	-6.36	2.8	N/A	-5.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.23	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9395	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y32N	Y31N	Helix	28.8	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.42	0.02	-7.39	1.77	N/A	-4.04	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.01	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9396	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K33A	K32A	Helix	28.3	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.24	0.84	-5.44	3.72	N/A	-6.65	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.29	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9397	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K33E	K32E	Helix	28.3	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.29	-0.11	-6.63	2.53	N/A	-6.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.96	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9398	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K33R	K32R	Helix	28.3	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.85	-0.55	-5.72	3.44	N/A	-9.22	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.86	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9399	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Q34A	Q33A	Helix	1.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.44	2.04	-1.67	7.49	N/A	-12.59	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.37	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9400	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	A35G	A34G	Helix	8.5	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.78	0.38	-6.84	2.32	N/A	-4.48	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.19	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9401	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	T36A	T35A	Helix	34.5	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.23	0.83	-6.03	3.13	N/A	-5.31	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.36	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9402	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	I40A	I39A	Coil	4.1	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.51	0.11	-7.15	2.01	N/A	-4.39	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.05	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9403	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	P45A	P44A	Coil	35.3	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.38	-0.02	-6.98	2.18	N/A	-5.08	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.99	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9404	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K53M	K52M	Helix	35.1	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.93	0.53	-9.5	-0.34	N/A	2.01	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.39	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9405	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K55A	K54A	Helix	22.4	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.93	-0.47	-7.1	2.06	N/A	-5.85	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.81	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9406	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	K55M	K54M	Helix	22.4	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.07	-0.33	-9.11	0.05	N/A	-0.88	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9407	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	E68A	E67A	Helix	56.7	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.34	0.94	-6.79	2.37	N/A	-3.3	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.65	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9408	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	A70G	A69G	Helix	0.0	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.3	-0.1	-6.3	2.86	N/A	-6.84	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.96	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9409	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y74A	Y73A	Helix	3.2	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	2.97	-2.43	-3.47	5.69	N/A	-18.77	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.7	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9410	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	Y74F	Y73F	Helix	3.2	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.11	0.71	-8.52	0.64	N/A	0.16	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-10.9	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9411	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	I75A	I74A	Helix	10.7	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	-1.2	-7.95	1.21	N/A	-5.57	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.5	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9412	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	V78A	V77A	Helix	4.9	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	3.4	-2.0	-8.38	0.78	N/A	-6.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.28	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9413	1999.0	10360367	2	yes	2023-06-04 01:00:00
ACBP	Bos taurus	86.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (1.20.80.10)	N/A	L81A	L80A	Helix	2.4	5.0	5.3	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	2.46	-2.94	-3.87	5.29	N/A	-19.02	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.64	N/A	N/A	Kragelund, B.B., Osmark, P., Neergaard, T.B., Schiødt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.	The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594–601. https://doi.org/10.1038/9414	1999.0	10360367	2	yes	2023-06-04 01:00:00
bACBP	Bos taurus	79.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (3.10.20.10)	N/A	I28A	I27A	Helix	9.5	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	3.74	-1.66	-5.89	3.27	22.2	-11.6	N/A	N/A	N/A	N/A	-9.0	6.36	N/A	N/A	0.33	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20358	2005.0	15690348	2	yes	2023-06-04 01:00:00
bACBP	Bos taurus	79.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (3.10.20.10)	N/A	H31A	H30A	Helix	18.5	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.45	1.05	-3.93	5.23	24.0	-9.83	N/A	N/A	N/A	N/A	-8.96	4.16	N/A	N/A	-0.25	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20359	2005.0	15690348	2	yes	2023-06-04 01:00:00
bACBP	Bos taurus	79.0	P07107	2abd	A	Mainly Alpha	PF00887	2abdA00 (3.10.20.10)	N/A	Y32A	Y31A	Helix	28.8	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.51	0.11	-6.1	3.06	26.8	-7.0	N/A	N/A	N/A	N/A	-10.7	5.52	N/A	N/A	-0.04	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20360	2005.0	15690348	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	WT(F653W)	WT(F45W)	N/A	N/A	25.0	5.0	Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.33	N/A	-6.84	N/A	35.11	N/A	N/A	N/A	N/A	N/A	-5.66	3.43	N/A	N/A	N/A	F653W	F45W	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	WT(F653W)	WT(F45W)	N/A	N/A	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.85	N/A	-6.43	N/A	30.42	N/A	N/A	N/A	N/A	N/A	-6.57	3.37	N/A	N/A	N/A	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi025	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I611V	I3V	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.06	-0.34	-4.57	4.59	23.86	-6.56	N/A	N/A	N/A	N/A	-6.37	3.17	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi026	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I611A	I3A	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.78	-2.07	-2.85	6.31	16.43	-13.99	N/A	N/A	N/A	N/A	-7.18	3.37	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi027	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	V613A	V5A	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.51	-2.34	-3.65	5.51	17.74	-12.68	N/A	N/A	N/A	N/A	-6.27	2.87	N/A	N/A	0.6	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi028	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	T615A	T7A	Beta	14.8	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.39	-1.46	-5.66	3.5	24.9	-5.52	N/A	N/A	N/A	N/A	-7.16	3.2	N/A	N/A	0.6	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi029	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	T617A	T9A	Coil	87.3	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.69	-0.16	-4.3	4.86	24.75	-5.67	N/A	N/A	N/A	N/A	-6.89	3.0	N/A	N/A	N/A	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi030	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I621V	I13V	Beta	3.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.03	-0.82	-4.28	4.88	23.07	-7.35	N/A	N/A	N/A	N/A	-6.59	2.87	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi031	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I621A	I13A	Beta	3.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.4	-2.45	-2.03	7.13	13.45	-16.97	N/A	N/A	N/A	N/A	-7.18	2.45	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi032	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L623A	L15A	Beta	4.3	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.2	-2.65	-2.16	7.0	13.28	-17.14	N/A	N/A	N/A	N/A	-6.94	2.73	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi033	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	V625A	V17A	Coil	2.8	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.26	-1.59	-4.55	4.61	21.83	-8.59	N/A	N/A	N/A	N/A	-6.84	3.02	N/A	N/A	0.6	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi034	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	D629N	D21N	Coil	22.7	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.17	-1.68	-6.01	3.15	25.22	-5.2	N/A	N/A	N/A	N/A	-6.42	3.0	N/A	N/A	1.2	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi035	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	T630A	T22A	Beta	33.1	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.22	-1.63	-4.46	4.7	21.51	-8.91	N/A	N/A	N/A	N/A	-6.79	3.07	N/A	N/A	0.6	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi036	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I631V	I23V	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.18	-0.67	-5.54	3.62	26.56	-3.86	N/A	N/A	N/A	N/A	-6.79	3.07	N/A	N/A	0.9	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi037	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I631A	I23A	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.6	-1.25	-2.62	6.54	17.89	-12.53	N/A	N/A	N/A	N/A	-7.85	2.77	N/A	N/A	0.3	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi038	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I631G	I23G	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.06	-2.79	-2.41	6.75	13.55	-16.87	N/A	N/A	N/A	N/A	-5.8	2.82	N/A	N/A	0.5	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi039	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	V634A	V26A	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.61	-2.24	-2.44	6.72	14.99	-15.43	N/A	N/A	N/A	N/A	-7.33	3.47	N/A	N/A	0.4	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi040	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	K635A	K27A	Helix	6.3	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.15	0.3	-1.14	8.02	18.06	-12.36	N/A	N/A	N/A	N/A	-8.6	2.55	N/A	N/A	-0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi041	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	A636G	A28G	Helix	41.5	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.91	-0.94	-6.58	2.58	28.47	-1.95	N/A	N/A	N/A	N/A	-6.89	3.42	N/A	N/A	1.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi042	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I638V	I30V	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.78	-1.07	-4.71	4.45	23.51	-6.91	N/A	N/A	N/A	N/A	-6.71	2.97	N/A	N/A	0.5	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi043	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I638A	I30A	Helix	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.31	-1.54	-2.36	6.8	16.53	-13.89	N/A	N/A	N/A	N/A	-8.35	2.45	N/A	N/A	0.3	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi044	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	Q649A	Q41A	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.56	-0.29	-3.12	6.04	21.51	-8.91	N/A	N/A	N/A	N/A	-5.97	2.85	N/A	N/A	0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi045	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L651A	L43A	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.11	0.26	1.62	10.78	11.12	-19.3	N/A	N/A	N/A	N/A	-9.24	1.68	N/A	N/A	0.0	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi046	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L658A	L50A	Coil	2.4	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.85	0.0	-1.1	8.06	17.22	-13.2	N/A	N/A	N/A	N/A	-7.68	2.82	N/A	N/A	0.0	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi047	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L664A	L56A	Coil	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.6	-0.25	-0.16	9.0	14.27	-16.15	N/A	N/A	N/A	N/A	-8.87	3.1	N/A	N/A	0.0	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi048	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I669V	I61V	Coil	3.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.73	-0.12	-4.38	4.78	25.05	-5.37	N/A	N/A	N/A	N/A	-6.59	3.12	N/A	N/A	0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi049	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	I669A	I61A	Coil	3.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.23	-0.62	-0.6	8.56	14.44	-15.98	N/A	N/A	N/A	N/A	-5.48	3.25	N/A	N/A	0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi050	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L675A	L67A	Beta	0.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.45	-0.4	-1.74	7.42	17.81	-12.61	N/A	N/A	N/A	N/A	-7.09	3.27	N/A	N/A	0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi051	2005.0	15857839	2	yes	2023-06-04 01:00:00
Ubiquitin	Homo sapiens	76.0	P0CG48	1ubq	A	Alpha Beta	PF00240	1ubqA00 (3.10.20.90)	N/A	L677A	L69A	Beta	3.0	25.0	7.4	Tris-HCl	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.32	-0.53	-1.3	7.86	16.4	-14.02	N/A	N/A	N/A	N/A	-7.38	2.35	N/A	N/A	0.1	F653W	F45W	Went, H.M., Jackson, S.E.	Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229–237. https://doi.org/10.1093/protein/gzi052	2005.0	15857839	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.05	N/A	-4.83	N/A	14.57	N/A	N/A	N/A	N/A	N/A	-2.27	0.55	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	WT	WT	N/A	N/A	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	2.52	N/A	-2.53	N/A	12.5	N/A	N/A	N/A	N/A	N/A	-3.69	1.29	N/A	N/A	N/A	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14932	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D1011G	D48G	Coil	69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.34	3.03	-4.51	0.79	21.94	5.57	N/A	N/A	N/A	N/A	-2.08	1.06	N/A	N/A	1.1	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14897	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	L971S/D1011G	L8S/D48G	Beta/Coil	42.1/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.08	2.77	-3.24	2.06	18.14	-3.8	N/A	N/A	N/A	N/A	-2.06	1.06	N/A	N/A	0.16	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14898	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	A974G/D1011G	A11G/D48G	Beta/Coil	1.9/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.26	2.95	-0.63	4.67	12.13	-9.81	N/A	N/A	N/A	N/A	-2.3	0.97	N/A	N/A	0.0	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14899	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D977S	D14S	Coil	49.1	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.06	-0.25	-3.96	1.34	12.46	-3.91	N/A	N/A	N/A	N/A	-2.21	1.04	N/A	N/A	0.16	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14900	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V986A/D1011G	V23A/D48G	Coil/Coil	1.4/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.18	1.87	-2.3	3.0	13.58	-8.36	N/A	N/A	N/A	N/A	-1.88	1.29	N/A	N/A	0.32	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14901	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	T987A/D1011G	T24A/D48G	Coil/Coil	39.4/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.81	2.5	-3.22	2.08	17.41	-4.53	N/A	N/A	N/A	N/A	-2.06	1.06	N/A	N/A	0.29	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14902	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D992A/D1011G	D29A/D48G	Coil/Coil	33.1/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.89	2.58	-3.0	2.3	17.06	-4.88	N/A	N/A	N/A	N/A	-2.28	1.14	N/A	N/A	0.22	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14903	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	L996V/D1011G	L33V/D48G	Beta/Coil	6.1/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.85	3.54	-2.21	3.09	17.49	-4.45	N/A	N/A	N/A	N/A	-1.93	1.16	N/A	N/A	-0.2	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14904	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	S999N/D1011G	S36N/D48G	Coil/Coil	34.6/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.87	2.56	-3.22	2.08	17.57	-4.37	N/A	N/A	N/A	N/A	-2.28	0.89	N/A	N/A	0.25	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14905	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	K1006A/D1011G	K43A/D48G	Beta/Coil	31.2/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.91	2.6	-3.32	1.98	17.93	-4.01	N/A	N/A	N/A	N/A	-2.13	1.06	N/A	N/A	0.26	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14906	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1007A/D1011G	V44A/D48G	Beta/Coil	0.0/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.61	0.3	-1.51	3.79	7.74	-14.2	N/A	N/A	N/A	N/A	-2.63	1.04	N/A	N/A	0.48	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14907	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1009A/D1011G	V46A/D48G	Beta/Coil	12.0/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.42	1.11	-4.96	0.34	18.3	-3.64	N/A	N/A	N/A	N/A	-2.21	1.06	N/A	N/A	1.25	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14908	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	N1010G	N47G	Coil	93.6	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.69	0.38	-5.52	-0.22	17.86	1.49	N/A	N/A	N/A	N/A	-2.21	1.06	N/A	N/A	0.63	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14909	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	F1015A/D1011G	F52A/D48G	Beta/Coil	28.4/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.7	0.39	-2.66	2.64	10.81	-11.13	N/A	N/A	N/A	N/A	-2.48	0.84	N/A	N/A	0.58	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14910	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1016A/D1011G	V53A/D48G	Beta/Coil	0.0/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.08	0.77	-3.22	2.08	13.13	-8.81	N/A	N/A	N/A	N/A	-2.3	1.19	N/A	N/A	0.61	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14911	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	A1018G/D1011G	A55G/D48G	Helix/Coil	13.2/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.56	1.25	-3.0	2.3	13.76	-8.18	N/A	N/A	N/A	N/A	-2.38	1.04	N/A	N/A	0.53	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14912	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1021A/D1011G	V58A/D48G	Beta/Coil	8.5/69.3	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.71	2.4	-1.14	4.16	12.02	-9.92	N/A	N/A	N/A	N/A	-2.38	1.11	N/A	N/A	0.16	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14913	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D1011G	D48G	Coil	69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.91	1.39	-2.53	0.0	15.95	3.45	N/A	N/A	N/A	N/A	-2.97	1.24	N/A	N/A	1.0	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14933	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	L971S/D1011G	L8S/D48G	Beta/Coil	42.1/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.81	1.29	-1.27	1.26	12.59	-3.36	N/A	N/A	N/A	N/A	-3.39	1.19	N/A	N/A	0.07	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14934	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	A974G/D1011G	A11G/D48G	Beta/Coil	1.9/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.76	1.24	0.34	2.87	8.47	-7.48	N/A	N/A	N/A	N/A	-3.12	1.26	N/A	N/A	0.05	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14935	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D977S	D14S	Coil	49.1	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	2.44	-0.08	-2.66	-0.13	12.64	0.14	N/A	N/A	N/A	N/A	-2.97	1.39	N/A	N/A	0.16	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14936	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V986A/D1011G	V23A/D48G	Coil/Coil	1.4/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.18	0.66	-0.51	2.02	9.14	-6.81	N/A	N/A	N/A	N/A	-3.42	1.36	N/A	N/A	0.27	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14937	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	T987A/D1011G	T24A/D48G	Coil/Coil	39.4/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.5	0.98	-1.24	1.29	11.73	-4.22	N/A	N/A	N/A	N/A	-2.82	1.24	N/A	N/A	0.24	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14938	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	D992A/D1011G	D29A/D48G	Coil/Coil	33.1/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.61	1.09	-1.66	0.87	13.06	-2.89	N/A	N/A	N/A	N/A	-3.12	1.54	N/A	N/A	0.25	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14939	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	L996V/D1011G	L33V/D48G	Beta/Coil	6.1/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	4.44	1.92	-0.45	2.08	12.11	-3.84	N/A	N/A	N/A	N/A	-3.1	1.21	N/A	N/A	-0.3	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14940	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	S999N/D1011G	S36N/D48G	Coil/Coil	34.6/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.78	1.26	-1.61	0.92	13.36	-2.59	N/A	N/A	N/A	N/A	-2.92	1.24	N/A	N/A	0.12	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14941	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	K1006A/D1011G	K43A/D48G	Beta/Coil	31.2/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.64	1.12	-1.71	0.82	13.26	-2.69	N/A	N/A	N/A	N/A	-2.8	1.31	N/A	N/A	0.25	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14942	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1007A/D1011G	V44A/D48G	Beta/Coil	0.0/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	1.1	-1.42	0.12	2.65	2.42	-13.53	N/A	N/A	N/A	N/A	-2.97	1.24	N/A	N/A	0.52	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14943	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1009A/D1011G	V46A/D48G	Beta/Coil	12.0/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	2.17	-0.35	-2.66	-0.13	11.98	-3.97	N/A	N/A	N/A	N/A	-3.0	1.07	N/A	N/A	1.1	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14944	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	N1010G	N47G	Coil	93.6	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	2.89	0.37	-3.22	-0.69	15.14	2.64	N/A	N/A	N/A	N/A	-3.15	1.39	N/A	N/A	0.69	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14945	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	F1015A/D1011G	F52A/D48G	Beta/Coil	28.4/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	1.16	-1.36	-0.97	1.56	5.28	-10.67	N/A	N/A	N/A	N/A	-2.97	1.14	N/A	N/A	0.64	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14946	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1016A/D1011G	V53A/D48G	Beta/Coil	0.0/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	0.96	-1.56	-0.73	1.8	4.19	-11.76	N/A	N/A	N/A	N/A	-2.97	1.26	N/A	N/A	0.62	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14947	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	A1018G/D1011G	A55G/D48G	Helix/Coil	13.2/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	1.59	-0.93	-1.43	1.1	7.47	-8.48	N/A	N/A	N/A	N/A	-2.6	1.31	N/A	N/A	0.68	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14948	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	V1021A/D1011G	V58A/D48G	Beta/Coil	8.5/69.3	25.0	3.5	Glycine	0.05	N/A	N/A	N/A	stopped-flow	urea	3.14	0.62	0.22	2.75	7.24	-8.71	N/A	N/A	N/A	N/A	-3.07	1.46	N/A	N/A	0.22	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14949	1999.0	10542091	2	yes	2023-06-04 01:00:00
Spectrin SH3	Gallus gallus	62.0	P07751	1shg	A	Mainly Beta	PF00018	1shgA00 (2.30.30.40)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	1.31	N/A	-5.3	N/A	16.37	N/A	N/A	N/A	N/A	N/A	-2.18	1.07	N/A	N/A	N/A	N/A	N/A	Martínez, J.C., Serrano, L.	The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010–1016. https://doi.org/10.1038/14896	1999.0	10542091	2	yes	2023-06-04 01:00:00
Chemotaxis protein CheW	Thermotoga maritima	143.0	Q56311	1k0s	A	Mainly Beta	PF01584	1k0sA01 (2.30.30.40)/1k0sA02 (2.40.50.180)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	7.44	N/A	-12.05	N/A	48.29	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
UPF0337 protein YjbJ	Escherichia coli	69.0	P68206	1ryk	A	Mainly Alpha	PF05532	1rykA00 (1.10.1470.10)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	9.08	N/A	4.49	N/A	11.37	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
internalin B (SH3-like domain of virulence protein internalin B)	Listeria monocytogenes	71.0	P0DQD3	1m9s	A	Mainly Beta	PF13457	1m9sA03 (2.30.30.170)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	3.98	N/A	-1.66	N/A	13.99	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
Actin binding protein ABP1 SH3 domain	Saccharomyces cerevisiae	58.0	P15891	1jo8	A	Mainly Beta	PF00018	1jo8A00 (2.30.30.40)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	2.47	N/A	-2.72	N/A	10.22	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
Repressor protein cI	Escherichia phage lambda	78.0	P03034	3kz3	A	Mainly Alpha	PF01381	3kz3A00 (1.10.260.40)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	10.38	N/A	3.21	N/A	17.76	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	Yes	N/A	2023-06-09 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	A131G	A131G	Beta	14.2	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.79	-0.44	6.82	3.82	N/A	N/A	N/A	N/A	N/A	N/A	-2.05	0.42	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.019	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	V135A	V135A	Helix	2.1	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.93	-0.3	6.51	3.51	N/A	N/A	N/A	N/A	N/A	N/A	-1.92	0.71	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.020	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	Y138F	Y138F	Helix	18.9	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.45	-0.78	6.15	3.15	N/A	N/A	N/A	N/A	N/A	N/A	-1.92	1.05	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.021	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	A139G	A139G	Helix	0.9	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.97	-1.26	6.8	3.8	N/A	N/A	N/A	N/A	N/A	N/A	-2.01	0.75	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.022	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	E141A	E141A	Helix	70.1	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	10.04	-0.19	4.17	1.17	N/A	N/A	N/A	N/A	N/A	N/A	-2.34	1.0	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.023	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	V144A	V144A	Coil	4.2	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.73	-1.5	5.48	2.48	N/A	N/A	N/A	N/A	N/A	N/A	-2.47	0.88	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.024	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	D145N	D145N	Coil	42.9	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.55	-0.68	4.09	1.09	N/A	N/A	N/A	N/A	N/A	N/A	-2.09	1.05	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.025	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	D145A	D145A	Coil	42.9	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.81	-1.42	4.7	1.7	N/A	N/A	N/A	N/A	N/A	N/A	-2.05	1.05	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.026	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	I146V	I146V	Helix	8.3	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.2	-1.03	5.7	2.7	N/A	N/A	N/A	N/A	N/A	N/A	-1.92	0.75	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.027	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	L159A	L159A	Coil	35.4	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.56	-1.67	5.44	2.44	N/A	N/A	N/A	N/A	N/A	N/A	-2.68	0.84	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.030	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	D162N	D162N	Helix	17.8	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.07	-2.16	4.55	1.55	N/A	N/A	N/A	N/A	N/A	N/A	-2.8	0.96	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.031	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	I163V	I163V	Helix	0.0	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.54	-0.69	3.91	0.91	N/A	N/A	N/A	N/A	N/A	N/A	-2.34	1.0	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.032	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	D164N	D164N	Helix	52.1	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.24	-0.99	4.87	1.87	N/A	N/A	N/A	N/A	N/A	N/A	-2.09	0.96	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.033	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	D164A	D164A	Helix	52.1	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.81	-0.42	6.43	3.43	N/A	N/A	N/A	N/A	N/A	N/A	-2.3	0.84	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.034	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	A165G	A165G	Helix	48.1	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.9	-1.33	4.09	1.09	N/A	N/A	N/A	N/A	N/A	N/A	-2.43	1.09	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.035	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	V149A	V149A	Coil	4.9	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.37	-1.86	5.48	2.48	N/A	N/A	N/A	N/A	N/A	N/A	-2.47	1.0	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.028	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	V158A	V158A	Beta	0.7	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	7.94	-2.29	6.86	3.86	N/A	N/A	N/A	N/A	N/A	N/A	-3.93	0.38	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.029	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	L167A	L167A	Helix	48.2	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	8.99	-1.24	4.38	1.38	N/A	N/A	N/A	N/A	N/A	N/A	-2.51	1.09	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.036	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	WT(F166W)	WT	N/A	N/A	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	10.23	N/A	3.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-2.3	1.26	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.016	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	V129A	V129A	Coil	24.6	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	10.07	-0.16	5.35	2.35	N/A	N/A	N/A	N/A	N/A	N/A	-2.18	0.75	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.016	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	I130A	I130A	Coil	37.3	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.74	-0.49	5.99	2.99	N/A	N/A	N/A	N/A	N/A	N/A	-2.01	0.54	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.017	2006.0	16406408	2	yes	2023-06-04 01:00:00
E3BD (F166W)	Geobacillus stearothermophilus (Bacillus stearothermophilus)	45.0	P11961	1w4e	A	Few Secondary Structures	PF02817	1w4eA00 (4.10.320.10)	2.3.1.12	I130G	I130G	Coil	37.3	25.0	5.5	Sodium Acetate	0.02	N/A	N/A	N/A	T-jump or stopped-flow	GuHCl	9.78	-0.45	6.21	3.21	N/A	N/A	N/A	N/A	N/A	N/A	-1.92	0.59	N/A	N/A	N/A	F166W	N/A	Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.	The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.018	2006.0	16406408	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	WT	WT	N/A	N/A	25.0	7.0	Tris	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.58	N/A	-9.0	N/A	18.38	N/A	N/A	N/A	N/A	N/A	-1.27	4.12	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.,	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205421	2005.0	15689503	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	WT	WT	N/A	N/A	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.42	N/A	-9.64	N/A	20.6	N/A	N/A	N/A	N/A	N/A	-4.2	1.25	3.77	N/A	N/A	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14890	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	Y12F	Y12F	Beta	0.9	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-0.12	1.3	-9.35	0.29	N/A	2.5	N/A	N/A	N/A	N/A	-3.38	1.0	5.27	N/A	0.93	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14891	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	Y12I	Y12I	Beta	0.9	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-4.15	-2.73	-9.09	0.55	N/A	-8.25	N/A	N/A	N/A	N/A	-4.25	1.33	2.22	N/A	0.83	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14892	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V14A	V14A	Beta	0.0	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-3.02	-1.6	-6.93	2.71	N/A	-10.85	N/A	N/A	N/A	N/A	-3.83	1.3	1.91	N/A	0.37	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14893	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V18A	V18A	Coil	1.4	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.73	-0.31	-6.99	2.65	N/A	-7.4	N/A	N/A	N/A	N/A	-4.3	1.35	2.32	N/A	0.1	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14894	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V21A	V21A	Coil	7.7	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.54	-0.12	-9.1	0.54	N/A	-1.7	N/A	N/A	N/A	N/A	-4.33	1.18	3.43	N/A	0.18	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14895	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	F23L	F23L	Helix	1.5	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.65	-0.23	-7.43	2.21	N/A	-6.15	N/A	N/A	N/A	N/A	-4.3	1.35	2.56	N/A	0.09	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14896	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	Y26A	Y26A	Helix	45.9	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.68	-0.26	-9.32	0.32	N/A	-1.5	N/A	N/A	N/A	N/A	-3.38	1.3	4.1	N/A	>1	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14897	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	E30D	E30D	Helix	17.5	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.36	-0.94	-4.42	5.22	N/A	-15.45	N/A	N/A	N/A	N/A	N/A	1.5	N/A	N/A	0.15	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14898	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	A31G	A31G	Helix	0.0	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.26	-0.84	-8.48	1.16	N/A	-5.05	N/A	N/A	N/A	N/A	-4.25	1.43	2.74	N/A	0.42	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14899	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V37A	V37A	Beta	12.7	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.18	-0.76	-6.92	2.72	N/A	-8.75	N/A	N/A	N/A	N/A	-3.98	1.53	2.15	N/A	0.22	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14900	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V40A	V40A	Beta	0.0	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.86	-0.44	-6.97	2.67	N/A	-7.8	N/A	N/A	N/A	N/A	-4.28	1.2	2.33	N/A	0.14	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14902	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	T43A	T43A	Coil	20.4	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.78	-1.36	-7.35	2.29	N/A	-9.15	N/A	N/A	N/A	N/A	-4.38	1.1	2.09	N/A	0.37	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14903	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	G46A	G46A	Coil	36.9	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-3.55	-2.13	-8.13	1.51	N/A	-9.15	N/A	N/A	N/A	N/A	-4.05	1.08	2.24	N/A	0.58	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14904	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V48A	V48A	Beta	0.0	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-3.21	-1.79	-8.14	1.5	N/A	-8.25	N/A	N/A	N/A	N/A	-3.83	1.28	2.41	N/A	0.54	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14905	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	V52A	V52A	Beta	1.4	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.71	-1.29	-7.64	2.0	N/A	-8.25	N/A	N/A	N/A	N/A	-4.4	1.25	2.18	N/A	0.39	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14906	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	P55A	P55A	Beta	18.4	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.49	-1.07	-9.62	0.02	N/A	-2.75	N/A	N/A	N/A	N/A	-4.25	1.08	3.35	N/A	0.98	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14907	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	M62A	M62A	Helix	0.0	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.57	-1.15	-5.44	4.2	N/A	-13.0	N/A	N/A	N/A	N/A	N/A	1.55	N/A	N/A	0.21	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14908	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	W65F	W65F	Helix	7.5	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-2.22	-0.8	-8.11	1.53	N/A	-5.85	N/A	N/A	N/A	N/A	-4.3	1.3	2.63	N/A	0.34	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14909	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	L66V	L66V	Helix	0.6	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	N/A	N/A	-3.08	6.56	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.35	N/A	N/A	0.27	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14910	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	P72A	P72A	Coil	76.5	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.62	-0.2	-7.61	2.03	N/A	-5.6	N/A	N/A	N/A	N/A	-4.23	1.33	2.69	N/A	0.09	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14911	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	I76V	I76V	Beta	20.1	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.45	-0.03	-8.41	1.23	N/A	-3.2	N/A	N/A	N/A	N/A	-4.2	1.38	3.12	N/A	0.02	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14912	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	T79S	T79S	Beta	14.8	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.47	-0.05	-7.45	2.19	N/A	-5.6	N/A	N/A	N/A	N/A	-4.35	1.1	2.74	N/A	0.02	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14913	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	E84D	E84D	Beta	44.3	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.52	-0.1	-7.35	2.29	N/A	-6.0	N/A	N/A	N/A	N/A	-4.2	1.15	2.71	N/A	0.04	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14914	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	I87V	I87V	Beta	11.8	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.98	-0.56	-6.95	2.69	N/A	-8.15	N/A	N/A	N/A	N/A	-3.68	0.85	2.75	N/A	0.0	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14915	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	L90A	L90A	Coil	45.1	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	-1.67	-0.25	-6.44	3.2	N/A	-8.65	N/A	N/A	N/A	N/A	-4.15	1.03	2.31	N/A	0.07	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14916	1999.0	10542090	2	yes	2023-06-04 01:00:00
mAcP	Homo sapiens	98.0	P14621	AF-P14621	A	N/A	PF00708	N/A	3.6.1.7	F95L	F95L	Beta	7.1	28.0	5.5	Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	N/A	N/A	-7.91	1.73	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-1.13	N/A	N/A	0.76	N/A	N/A	Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.	Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005–1009. https://doi.org/10.1038/14917	1999.0	10542090	2	yes	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.75	N/A	-10.33	N/A	39.84	N/A	N/A	N/A	N/A	N/A	-5.7	4.2	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52A/V58A/F70L	L51A/V57A/F69L	Beta/Coil/Beta	23.8/40.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.47	-1.56	-5.06	3.98	18.66	N/A	N/A	N/A	N/A	N/A	-5.95	2.73	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52V/V58A/F70L	L51V/V57A/F69L	Beta/Coil/Beta	23.8/40.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.01	-1.02	-5.81	3.23	21.85	N/A	N/A	N/A	N/A	N/A	-5.57	2.95	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V54T	V53T	Coil	49.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.63	-0.4	-7.78	1.26	28.27	N/A	N/A	N/A	N/A	N/A	-5.48	2.92	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V54A	V53A	Coil	49.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.05	0.02	-8.21	0.83	30.38	N/A	N/A	N/A	N/A	N/A	-6.14	3.02	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V54G	V53G	Coil	49.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.36	-0.67	-6.05	2.99	23.31	N/A	N/A	N/A	N/A	N/A	-6.14	2.7	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T56V	T55V	Coil	42.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.79	-0.24	-7.83	1.21	28.79	N/A	N/A	N/A	N/A	N/A	-5.67	2.92	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V58A	V57A	Coil	40.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.73	-0.3	-7.22	1.82	27.13	N/A	N/A	N/A	N/A	N/A	-5.95	2.97	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V58A/F70L	V57A/F69L	Coil/Beta	40.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.9	-1.13	-6.31	2.73	22.82	N/A	N/A	N/A	N/A	N/A	-6.39	2.92	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V58A/F70A	V57A/F69A	Coil/Beta	40.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.02	-2.01	-4.12	4.92	15.21	N/A	N/A	N/A	N/A	N/A	-6.84	2.75	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T59A	T58A	Coil	66.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.97	-0.06	-8.39	0.65	30.62	N/A	N/A	N/A	N/A	N/A	-5.33	3.27	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T59D	T58D	Coil	66.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-9.3	-0.26	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.34	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T59A/E61A	T58A/E60A	Coil/Coil	66.9/54.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-7.99	1.05	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T59D/E61A	T58D/E60A	Coil/Coil	66.9/54.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-8.95	0.09	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.32	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E61A	E60A	Coil	54.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-8.1	0.94	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	R63A	R62A	Coil	53.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.95	-0.08	-8.25	0.79	30.23	N/A	N/A	N/A	N/A	N/A	-5.25	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	R63A/D65A	R62A/D64A	Coil/Coil	53.6/23.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.9	-0.13	-6.37	2.67	25.44	N/A	N/A	N/A	N/A	N/A	-6.32	2.9	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	D65A	D64A	Coil	23.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.51	-0.52	-8.08	0.96	28.72	N/A	N/A	N/A	N/A	N/A	-5.65	3.15	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V67A	V66A	Beta	0.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.31	-1.72	-3.08	5.96	13.35	N/A	N/A	N/A	N/A	N/A	-6.34	3.49	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L69A	L68A	Beta	0.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	0.61	-3.42	-6.05	2.99	16.5	N/A	N/A	N/A	N/A	N/A	-6.96	2.85	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	F70L	F69L	Beta	16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.03	-1.0	-7.13	1.91	25.17	N/A	N/A	N/A	N/A	N/A	-6.69	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	F70V	F69V	Beta	16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.03	-1.0	-6.26	2.78	23.02	N/A	N/A	N/A	N/A	N/A	-5.72	2.95	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	F70A	F69A	Beta	16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.08	-1.95	-5.12	3.92	17.84	N/A	N/A	N/A	N/A	N/A	-6.76	2.97	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V71A	V70A	Beta	5.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.2	-0.83	-7.2	1.84	25.77	N/A	N/A	N/A	N/A	N/A	-6.29	3.1	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	D72A	D71A	Coil	40.5	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.34	-0.69	-4.14	4.9	18.53	N/A	N/A	N/A	N/A	N/A	-6.81	2.38	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	D72N	D71N	Coil	40.5	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-8.93	0.11	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.12	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	N76D	N75D	Beta	30.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.65	-0.38	-7.92	1.12	28.67	N/A	N/A	N/A	N/A	N/A	-6.34	2.95	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	N76A	N75A	Beta	30.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.91	-0.12	-8.12	0.92	29.81	N/A	N/A	N/A	N/A	N/A	-5.92	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	A78G	A77G	Coil	40.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.68	-0.35	-6.46	2.58	25.12	N/A	N/A	N/A	N/A	N/A	-4.66	2.9	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V80T	V79T	Coil	28.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.71	-0.32	-8.42	0.62	30.05	N/A	N/A	N/A	N/A	N/A	-4.68	3.07	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V80A	V79A	Coil	28.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.11	0.08	-6.93	2.11	27.35	N/A	N/A	N/A	N/A	N/A	-5.72	3.27	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V80G	V79G	Coil	28.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.82	-0.21	-3.93	5.11	19.2	N/A	N/A	N/A	N/A	N/A	-5.2	3.32	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	P81A	P80A	Coil	2.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.94	-0.09	-7.43	1.61	28.17	N/A	N/A	N/A	N/A	N/A	-5.13	3.3	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V80M/M60L	V79M/M59L	Coil/Coil	28.9/100.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-4.03	5.01	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.54	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V83T	V82T	Beta	12.7	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.89	-0.14	-7.35	1.69	27.85	N/A	N/A	N/A	N/A	N/A	-4.93	3.15	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V83A	V82A	Beta	12.7	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.96	-0.07	-7.19	1.85	27.62	N/A	N/A	N/A	N/A	N/A	-5.3	3.37	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V83G	V82G	Beta	12.7	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.86	-0.17	-3.98	5.06	19.42	N/A	N/A	N/A	N/A	N/A	-5.57	3.44	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	WT	WT	N/A	N/A	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.03	N/A	-9.04	N/A	32.38	N/A	N/A	N/A	N/A	N/A	-4.51	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K22A	K21A	Coil	36.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.21	0.18	-7.83	1.21	29.83	N/A	N/A	N/A	N/A	N/A	-5.55	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K22A/E27A	K21A/E26A	Coil/Helix	36.1/46.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-7.36	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.1	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K22A/D43A	K21A/D42A	Coil/Helix	36.1/39.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	-6.74	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	3.2	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K22M	K21M	Coil	36.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.01	-0.02	-8.25	0.79	30.38	N/A	N/A	N/A	N/A	N/A	-4.71	3.3	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T23A	T22A	Coil	48.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.84	-0.19	-7.98	1.06	29.28	N/A	N/A	N/A	N/A	N/A	-4.61	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T23V	T22V	Coil	48.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.75	-0.28	-8.58	0.46	30.55	N/A	N/A	N/A	N/A	N/A	-4.19	3.2	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	T23G	T22G	Coil	48.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.94	-0.09	-7.68	1.36	28.79	N/A	N/A	N/A	N/A	N/A	-5.35	3.2	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	P26A	P25A	Helix	50.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.86	-0.17	-7.62	1.42	28.44	N/A	N/A	N/A	N/A	N/A	-5.1	3.96	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	P26A/A36G	P25A/A35G	Helix/Helix	50.0/0.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.95	-2.08	-6.65	2.39	21.31	N/A	N/A	N/A	N/A	N/A	-4.04	3.32	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E27A	E26A	Helix	46.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.72	-0.31	-8.59	0.45	30.5	N/A	N/A	N/A	N/A	N/A	-4.83	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L28A	L27A	Helix	2.4	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.36	-0.67	-4.42	4.62	19.28	N/A	N/A	N/A	N/A	N/A	-5.0	2.6	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K31A	K30A	Coil	47.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.59	-0.44	-9.39	-0.35	32.16	N/A	N/A	N/A	N/A	N/A	-4.01	3.15	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	S32G	S31G	Beta	33.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.65	-0.38	-8.42	0.62	29.9	N/A	N/A	N/A	N/A	N/A	-5.77	3.2	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	S32A	S31A	Beta	33.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.39	-0.64	-8.53	0.51	29.53	N/A	N/A	N/A	N/A	N/A	-5.08	3.2	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E34Q	E33Q	Helix	71.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.43	-0.6	-8.97	0.07	30.72	N/A	N/A	N/A	N/A	N/A	-5.1	3.27	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E34D	E33D	Helix	71.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.86	-0.17	-8.76	0.28	31.27	N/A	N/A	N/A	N/A	N/A	-6.0	3.3	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E34N	E33N	Helix	71.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.14	-0.89	-9.01	0.03	30.1	N/A	N/A	N/A	N/A	N/A	-5.65	3.42	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E35Q	E34Q	Helix	62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.62	-0.41	-8.71	0.33	30.55	N/A	N/A	N/A	N/A	N/A	-5.52	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E35D	E34D	Helix	62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.76	-0.27	-8.28	0.76	29.83	N/A	N/A	N/A	N/A	N/A	-5.38	3.39	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E35N	E34N	Helix	62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.07	-0.96	-7.95	1.09	27.3	N/A	N/A	N/A	N/A	N/A	-5.28	3.12	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E34A/E35A	E33A/E34A	Helix/Helix	71.6/62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.1	-0.93	-8.17	0.87	27.92	N/A	N/A	N/A	N/A	N/A	-4.19	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	S32G/E34A/E35A	S31G/E33A/E34A	Beta/Helix/Helix	33.8/71.6/62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.73	-1.3	-6.66	2.38	23.26	N/A	N/A	N/A	N/A	N/A	-4.56	2.92	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	S32A/E34A/E35A	S31A/E33A/E34A	Beta/Helix/Helix	33.8/71.6/62.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.9	-1.13	-7.03	2.01	24.6	N/A	N/A	N/A	N/A	N/A	-5.3	3.0	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	A36G	A35G	Helix	0.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.09	-1.94	-9.47	-0.43	28.64	N/A	N/A	N/A	N/A	N/A	-6.09	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K37A	K36A	Helix	48.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.81	-0.22	-7.83	1.21	28.84	N/A	N/A	N/A	N/A	N/A	-5.45	3.07	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K37G	K36G	Helix	48.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.56	-1.47	-6.13	2.91	21.53	N/A	N/A	N/A	N/A	N/A	-5.05	2.8	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K38A	K37A	Helix	47.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.9	-0.13	-8.89	0.15	31.69	N/A	N/A	N/A	N/A	N/A	-4.39	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K38G	K37G	Helix	47.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.88	-1.15	-8.35	0.69	27.82	N/A	N/A	N/A	N/A	N/A	-4.61	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	V39A	V38A	Helix	29.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.25	0.22	-7.8	1.24	29.85	N/A	N/A	N/A	N/A	N/A	-4.66	3.34	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I40V	I39V	Helix	0.0	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.16	-0.87	-8.02	1.02	27.7	N/A	N/A	N/A	N/A	N/A	-5.57	3.15	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L41A	L40A	Helix	47.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.48	-0.55	-7.44	1.6	27.06	N/A	N/A	N/A	N/A	N/A	-5.45	2.9	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L41G	L40G	Helix	47.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.23	-0.8	-7.19	1.85	25.82	N/A	N/A	N/A	N/A	N/A	-5.75	2.82	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	Q42A	Q41A	Helix	76.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.24	0.21	-8.98	0.06	32.75	N/A	N/A	N/A	N/A	N/A	-5.33	3.27	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	Q42G	Q41G	Helix	76.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.92	-0.11	-8.27	0.77	30.2	N/A	N/A	N/A	N/A	N/A	-5.62	3.15	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	D43A	D42A	Helix	39.3	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.43	0.4	-7.87	1.17	30.47	N/A	N/A	N/A	N/A	N/A	-5.35	3.42	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K44A	K43A	Coil	2.4	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.42	0.39	-7.9	1.14	30.52	N/A	N/A	N/A	N/A	N/A	-5.72	3.22	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	K44G	K43G	Coil	2.4	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.52	-0.51	-4.48	4.56	19.82	N/A	N/A	N/A	N/A	N/A	-6.12	3.39	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	P45A	P44A	Coil	77.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.44	-0.59	-6.43	2.61	24.45	N/A	N/A	N/A	N/A	N/A	-6.19	2.87	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	E46A	E45A	Coil	47.9	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.81	-0.22	-8.61	0.43	30.77	N/A	N/A	N/A	N/A	N/A	-5.45	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I49V	I48V	Beta	20.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.72	-0.31	-8.0	1.04	29.04	N/A	N/A	N/A	N/A	N/A	-5.75	3.27	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I49A	I48A	Beta	20.1	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.37	-1.66	-4.3	4.74	16.53	N/A	N/A	N/A	N/A	N/A	-6.76	2.73	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I50V	I49V	Beta	42.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.92	-0.11	-8.99	0.05	31.99	N/A	N/A	N/A	N/A	N/A	-5.52	3.02	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I50A	I49A	Beta	42.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.94	-1.09	-7.5	1.54	25.87	N/A	N/A	N/A	N/A	N/A	-7.18	3.1	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I50G	I49G	Beta	42.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.48	-1.55	-5.29	3.75	19.25	N/A	N/A	N/A	N/A	N/A	-7.14	3.17	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	I50T	I49T	Beta	42.6	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.25	-0.78	-8.19	0.85	28.34	N/A	N/A	N/A	N/A	N/A	-6.0	3.07	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52A	L51A	Beta	23.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.29	-0.74	-6.34	2.7	23.86	N/A	N/A	N/A	N/A	N/A	-7.46	3.1	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52I	L51I	Beta	23.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.17	0.14	-8.54	0.5	31.49	N/A	N/A	N/A	N/A	N/A	-5.3	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52V	L51V	Beta	23.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.07	0.04	-8.22	0.82	30.45	N/A	N/A	N/A	N/A	N/A	-5.33	3.25	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52V/F70L	L51V/F69L	Beta/Beta	23.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.18	-0.85	-6.17	2.87	23.17	N/A	N/A	N/A	N/A	N/A	-5.85	3.1	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52V/F70A	L51V/F69A	Beta/Beta	23.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.48	-1.55	-5.08	3.96	18.73	N/A	N/A	N/A	N/A	N/A	-6.32	2.82	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52A/F70L	L51A/F69L	Beta/Beta	23.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	2.52	-1.51	-5.07	3.97	18.8	N/A	N/A	N/A	N/A	N/A	-5.95	2.8	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52A/F70A	L51A/F69A	Beta/Beta	23.8/16.2	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	1.84	-2.19	-3.65	5.39	13.6	N/A	N/A	N/A	N/A	N/A	-7.04	2.6	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52A/V58A	L51A/V57A	Beta/Coil	23.8/40.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.13	-0.9	-5.34	3.7	20.99	N/A	N/A	N/A	N/A	N/A	-6.99	2.97	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
CI2	Hordeum vulgare	83.0	P01053	1coa	I	Alpha Beta	PF00280	1coaI00 (3.30.10.10)	N/A	L52V/V58A	L51V/V57A	Beta/Coil	23.8/40.8	25.0	6.25	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	3.82	-0.21	-6.44	2.6	25.42	N/A	N/A	N/A	N/A	N/A	-6.02	3.05	N/A	N/A	N/A	N/A	N/A	Itzhaki LS, Otzen DE, Fersht AR	The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.	1995.0	7490748	2	N/A	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	WT	WT	N/A	N/A	25.0	7.5	HEPES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.3	N/A	-1.72	N/A	19.87	N/A	N/A	N/A	N/A	N/A	-7.03	1.38	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	WT	WT	N/A	N/A	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.76	N/A	0.2	N/A	-7.12	1.38	N/A	N/A	N/A	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77971	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	Y229L	Y3L	Beta	5.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.68	-1.08	1.93	1.73	-8.23	1.38	N/A	N/A	0.38	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77972	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	I232A	I6A	Beta	37.9	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.38	-1.38	2.41	2.21	-7.85	1.38	N/A	N/A	0.38	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77973	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	L233A	L7A	Beta	4.3	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.74	-1.02	2.37	2.17	-8.62	1.59	N/A	N/A	0.32	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77974	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T237A	T11A	Coil	90.8	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.74	-0.02	1.22	1.02	-6.26	2.18	N/A	N/A	0.02	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77975	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	E241A	E15A	Beta	60.8	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.91	0.15	1.17	0.97	-6.55	1.92	N/A	N/A	-0.19	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77976	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T242A	T16A	Beta	33.8	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.76	0.0	0.85	0.65	-6.98	1.51	N/A	N/A	0.0	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77977	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T244A	T18A	Beta	26.8	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	5.12	0.36	1.35	1.15	-7.22	1.63	N/A	N/A	-0.45	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77978	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	A246G	A20G	Coil	13.2	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.66	-0.1	4.22	4.02	-6.84	2.01	N/A	N/A	0.02	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77979	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	D248A	D22A	Coil	42.9	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.08	-0.68	2.54	2.34	-6.74	2.05	N/A	N/A	0.23	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77980	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T251A	T25A	Helix	30.3	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.45	-0.31	-0.49	-0.69	-6.74	1.55	N/A	N/A	-0.81	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77981	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	A252G	A26G	Helix	0.9	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.17	-1.59	3.72	3.52	-10.3	1.34	N/A	N/A	0.31	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77982	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	K254G	K28G	Helix	59.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	5.42	0.66	0.94	0.74	-7.22	1.88	N/A	N/A	N/A	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77983	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	V255A	V29A	Helix	50.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.45	-0.31	1.1	0.9	-6.69	1.84	N/A	N/A	0.26	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77984	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	F256L	F30L	Helix	2.5	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.64	-0.12	2.53	2.33	-6.74	1.8	N/A	N/A	0.05	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77985	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	K257G	K31G	Helix	41.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.95	-0.81	2.87	2.67	-6.98	1.55	N/A	N/A	0.23	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77986	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	Q258G	Q32G	Helix	66.7	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.81	-0.95	0.98	0.78	-6.69	1.59	N/A	N/A	0.55	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77987	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	Y259A	Y33A	Helix	34.7	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.44	-0.32	1.46	1.26	-6.21	2.26	N/A	N/A	0.2	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77988	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	A260G	A34G	Helix	1.9	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.87	-0.89	3.59	3.39	-7.46	1.76	N/A	N/A	0.21	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77989	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	N261G	N35G	Helix	77.1	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.96	-0.8	3.71	3.51	-7.41	1.67	N/A	N/A	0.19	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77990	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	N263A	N37A	Coil	54.1	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.98	0.22	0.12	-0.08	-6.98	1.55	N/A	N/A	N/A	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77991	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	V265A	V39A	Coil	7.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.27	-0.49	2.67	2.47	-7.03	1.42	N/A	N/A	0.16	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77992	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	G267A	G41A	Coil	22.6	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.84	0.08	5.17	4.97	-8.23	1.84	N/A	N/A	-0.02	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77993	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	Y271L	Y45L	Beta	36.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.01	-1.75	4.21	4.01	-7.89	2.22	N/A	N/A	0.3	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77994	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	D272A	D46A	Beta	49.7	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.89	-2.87	0.32	0.12	-6.88	1.46	N/A	N/A	0.96	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77995	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	D273A	D47A	Coil	55.8	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	5.32	0.56	-0.08	-0.28	-6.26	1.26	N/A	N/A	0.67	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77996	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T275A	T49A	Coil	58.5	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.72	-1.04	0.41	0.21	-7.32	1.59	N/A	N/A	0.84	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77997	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T277A	T51A	Beta	15.5	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.33	-1.43	1.99	1.79	-7.99	1.55	N/A	N/A	0.44	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77998	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	F278L	F52L	Beta	2.5	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.61	-1.15	5.16	4.96	1.73	-9.67	N/A	N/A	0.19	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/77999	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	T279A	T53A	Beta	23.2	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.88	-0.88	2.38	2.18	-8.18	2.01	N/A	N/A	0.27	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/78000	2000.0	10932252	2	yes	2023-06-04 01:00:00
Protein G	Streptococcus sp. GX7805	56.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	V280A	V54A	Beta	0.0	22.0	6.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.97	-0.79	4.46	4.26	-7.94	2.8	N/A	N/A	0.16	N/A	N/A	McCallister, E.L., Alm, E., Baker, D.	Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669–673. https://doi.org/10.1038/78001	2000.0	10932252	2	yes	2023-06-04 01:00:00
C-terminal β-hairpin of protein GB	Streptococcus sp. group G	16.0	P06654	1pgb	A	Alpha Beta	PF01378	1pgbA00 (3.10.20.10)	N/A	N/A	WT	N/A	N/A	21.0	7.0	KPi	0.02	N/A	N/A	N/A	T-jump	thermal denaturation	12.02	N/A	12.02	N/A	0.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Muñoz V, Thompson PA, Hofrichter J, Eaton WA	Folding dynamics and mechanism of beta-hairpin formation. Nature. 1997  390(6656):196-9. https://doi.org/10.1038/36626	1997.0	9367160	Yes	N/A	2023-06-09 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.8	N/A	-0.42	N/A	17.89	N/A	N/A	N/A	N/A	N/A	-3.12	1.12	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	WT	WT	N/A	N/A	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.63	N/A	-0.73	N/A	18.41	N/A	N/A	N/A	N/A	N/A	-2.93	1.21	N/A	N/A	N/A	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2158	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	V27A	V12A	Beta	6.3	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.89	-0.74	1.49	2.22	10.88	N/A	N/A	N/A	N/A	N/A	-3.64	0.92	N/A	N/A	0.25	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2159	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	E29A	E14A	Beta	23.2	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.46	-0.17	-0.29	0.44	16.74	N/A	N/A	N/A	N/A	N/A	-2.89	1.26	N/A	N/A	0.0	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2160	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	I30V	I15V	Beta	2.4	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.78	-0.85	-0.87	-0.14	16.32	N/A	N/A	N/A	N/A	N/A	-2.8	1.26	N/A	N/A	1.0	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2161	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	E35G	E20G	Helix	72.2	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.19	-0.44	0.36	1.09	14.23	N/A	N/A	N/A	N/A	N/A	-2.85	1.3	N/A	N/A	0.22	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2162	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	I38V	I23V	Helix	11.2	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.0	-0.63	-1.3	-0.57	17.99	N/A	N/A	N/A	N/A	N/A	-2.8	1.38	N/A	N/A	9.3	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2163	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	L41V	L26V	Helix	6.7	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.43	-1.2	0.25	0.98	12.97	N/A	N/A	N/A	N/A	N/A	-3.18	1.34	N/A	N/A	0.55	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2164	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	A46G	A31G	Helix	57.5	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.87	0.24	0.21	0.94	16.32	N/A	N/A	N/A	N/A	N/A	-3.01	1.21	N/A	N/A	0.0	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2165	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	D53A	D38A	Coil	55.8	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.61	-0.02	-0.76	-0.03	18.41	N/A	N/A	N/A	N/A	N/A	-2.76	1.17	N/A	N/A	N/A	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2166	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	F54L	F39L	Beta	21.3	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.25	-0.38	2.4	3.13	9.62	N/A	N/A	N/A	N/A	N/A	-2.59	1.09	N/A	N/A	0.11	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2167	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	A65G	A50G	Beta	0.0	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.32	-0.31	1.82	2.55	11.3	N/A	N/A	N/A	N/A	N/A	-3.22	1.0	N/A	N/A	0.11	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2168	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	H66A	H51A	Beta	16.3	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.41	-0.22	0.0	0.73	15.06	N/A	N/A	N/A	N/A	N/A	-3.05	1.34	N/A	N/A	0.17	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2169	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	V67A	V52A	Beta	2.8	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.6	-1.03	0.02	0.75	13.81	N/A	N/A	N/A	N/A	N/A	-2.97	1.21	N/A	N/A	0.59	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2170	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	N73A	N58A	Helix	15.9	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.28	-0.35	-0.41	0.32	16.74	N/A	N/A	N/A	N/A	N/A	-2.89	1.26	N/A	N/A	0.52	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2171	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	Q75G	Q60G	Helix	66.2	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.63	0.0	-0.18	0.55	16.74	N/A	N/A	N/A	N/A	N/A	-3.1	1.3	N/A	N/A	0.48	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2172	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	V79G	V64G	Helix	67.6	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.64	0.01	-0.02	0.71	16.32	N/A	N/A	N/A	N/A	N/A	-3.05	1.26	N/A	N/A	0.43	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2173	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	F80A	F65A	Helix	23.9	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.26	-1.37	0.49	1.22	11.72	N/A	N/A	N/A	N/A	N/A	-3.51	1.3	N/A	N/A	0.53	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2174	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	I86V	I71V	Coil	11.8	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.1	-0.53	1.29	2.02	12.13	N/A	N/A	N/A	N/A	N/A	-3.56	1.17	N/A	N/A	0.21	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2175	1998.0	9799641	2	yes	2023-06-04 01:00:00
ADAh2	Homo sapiens	81.0	P48052	1o6x	A	Alpha Beta	PF02244	1o6xA00 (3.30.70.340)	3.4.17.15	I90A	I75A	Beta	43.2	25.0	7.0	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.8	-0.83	1.52	2.25	10.46	N/A	N/A	N/A	N/A	N/A	-3.01	1.05	N/A	N/A	0.27	N/A	N/A	Villegas, V., Martínez, J.C., Avilés, F.X., Serrano, L.	Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027–1036. https://doi.org/10.1006/jmbi.1998.2176	1998.0	9799641	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	WT	WT	N/A	N/A	25.0	7.0	Tris	0.05	N/A	N/A	N/A	stopped-flow	urea	7.33	N/A	-1.87	N/A	22.79	N/A	N/A	N/A	N/A	N/A	-4.53	0.26	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	WT	WT	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.09	N/A	-4.42	N/A	27.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L3A	L3A	Coil	61.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.75	-0.34	-4.02	0.4	25.0	-2.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	I7V	I7V	Coil	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.62	-0.47	-1.9	2.52	20.0	-7.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	A13G	A13G	Helix	50.9	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.7	-1.39	-4.42	0.0	23.8	-3.3	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.98	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	F15A	F15A	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	1.86	-5.23	-0.82	3.6	6.3	-20.8	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.57	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L16A	L16A	Helix	23.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.35	-1.74	-3.08	1.34	19.8	-7.3	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.52	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L18A	L18A	Helix	11.6	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	4.44	-2.65	-0.87	3.55	12.7	-14.4	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.4	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V19A	V19A	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.08	-2.01	-0.69	3.73	13.6	-13.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.32	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T21A	T21A	Helix	33.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.65	0.56	-3.73	0.69	26.78	-0.32	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T21G	T21G	Helix	33.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.17	-0.92	-2.32	2.1	19.99	-7.11	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T21S	T21S	Helix	33.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.17	0.08	-3.17	1.25	24.3	-2.8	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	I22V	I22V	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.89	-1.2	-1.83	2.59	18.2	-8.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.31	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	A25G	A25G	Coil	67.9	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.38	0.29	-4.42	0.0	27.8	0.7	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T27S	T27S	Coil	18.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.91	-0.18	-3.1	1.32	23.6	-3.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.12	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L33A	L33A	Helix	9.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.89	-1.2	-1.35	3.07	17.0	-10.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.27	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V34A	V34A	Helix	49.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.55	0.46	-4.89	-0.47	29.2	2.1	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V34G	V34G	Helix	49.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.62	-0.47	-4.51	-0.09	26.19	-0.91	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L36A	L36A	Helix	21.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.99	-1.1	-1.31	3.11	17.2	-9.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.25	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V37A	V37A	Helix	1.4	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.62	-0.47	-1.97	2.45	20.2	-6.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T38A	T38A	Helix	52.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.82	0.73	-3.77	0.65	27.29	0.19	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T38G	T38G	Helix	52.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.8	-0.29	-4.14	0.28	25.74	-1.36	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	F40L	F40L	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.0	-0.09	1.95	6.37	11.9	-15.2	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.01	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	T44S	T44S	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.62	-0.47	-5.65	-1.23	28.8	1.7	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	L52A	L52A	Helix	12.2	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.91	-0.18	1.9	6.32	11.8	-15.3	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.03	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	I53V	I53V	Helix	8.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.91	-0.18	-1.97	2.45	20.9	-6.2	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.07	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	I67V	I67V	Helix	2.4	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.11	-0.98	-3.22	1.2	21.9	-5.2	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.41	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V68A	V68A	Helix	1.4	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.02	-1.07	-1.31	3.11	17.2	-9.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.23	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	N69A	N69A	Helix	50.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	7.31	0.22	-4.42	0.0	27.62	0.52	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	N69G	N69G	Helix	50.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.06	-1.03	-4.07	0.35	23.86	-3.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	V71A	V71A	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	5.14	-1.95	-1.31	3.11	15.2	-11.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.36	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	A76G	A76G	Helix	80.2	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.21	-0.88	-3.08	1.34	21.9	-5.2	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.37	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	A77G	A77G	Helix	74.5	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	6.21	-0.88	-3.32	1.1	22.4	-4.7	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.37	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
Im9*	Escherichia coli	86.0	P13479	1imq	A	Mainly Alpha	PF01320	1imqA00 (1.10.1200.20)	N/A	F83A	F83A	Coil	12.2	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	2 mM DTT, 1 mM EDTA	stopped-flow	urea	4.25	-2.84	1.65	6.07	6.1	-21.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.31	N/A	N/A	Friel, C.T., Capaldi, A.P., Radford, S.E.	Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293–305. https://doi.org/10.1016/s0022-2836(02)01249-4	2003.0	12547210	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.36	N/A	-2.77	N/A	27.58	N/A	N/A	N/A	N/A	N/A	-3.39	1.03	N/A	N/A	N/A	N/A	N/A	Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vallée-Bélisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.	Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602–616. https://doi.org/10.1110/ps.041205428	2005.0	15689503	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.72	N/A	-3.0	N/A	26.56	N/A	N/A	N/A	N/A	N/A	-3.02	1.02	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.079	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	N56M	N56M	Coil	43.3	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	9.3	1.58	-1.97	1.03	27.9	1.34	N/A	N/A	N/A	N/A	-3.47	0.94	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.080	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	I58A	I58A	Beta	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	4.72	-3.0	-0.31	2.69	12.47	-14.09	N/A	N/A	N/A	N/A	-2.87	0.94	N/A	N/A	0.6	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.081	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	I58L	I58L	Beta	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.17	-0.55	-2.53	0.47	24.02	-2.54	N/A	N/A	N/A	N/A	-3.07	1.07	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.082	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	I58F	I58F	Beta	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.67	-0.05	-0.87	2.13	21.16	-5.4	N/A	N/A	N/A	N/A	-3.47	0.87	N/A	N/A	0.03	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.083	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	R59A	R59A	Beta	34.3	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.69	0.97	-2.41	0.59	27.5	0.94	N/A	N/A	N/A	N/A	-3.05	0.97	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.084	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V60A	V60A	Beta	1.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	4.96	-2.76	-2.04	0.96	17.33	-9.23	N/A	N/A	N/A	N/A	-3.2	0.92	N/A	N/A	0.63	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.085	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L62A	L62A	Coil	1.8	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.32	-2.4	1.3	4.3	9.96	-16.6	N/A	N/A	N/A	N/A	-3.2	0.67	N/A	N/A	0.39	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.086	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	P63A	P63A	Coil	33.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.34	-1.38	0.54	3.54	14.37	-12.19	N/A	N/A	N/A	N/A	-2.82	0.72	N/A	N/A	0.5	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.087	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	N64A	N64A	Coil	59.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.56	-2.16	-3.22	-0.22	21.75	-4.81	N/A	N/A	N/A	N/A	-3.0	1.09	N/A	N/A	1.3	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.088	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	Q66A	Q66A	Coil	32.3	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.38	-0.34	-2.81	0.19	25.25	-1.31	N/A	N/A	N/A	N/A	-3.22	0.99	N/A	N/A	0.35	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.089	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	T68A	T68A	Coil	31.7	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.26	0.54	-3.0	0.0	27.88	1.32	N/A	N/A	N/A	N/A	-3.15	1.16	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.090	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V69A	V69A	Beta	59.9	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.52	-1.2	-2.41	0.59	22.12	-4.44	N/A	N/A	N/A	N/A	-3.05	1.02	N/A	N/A	0.72	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.091	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V70A	V70A	Beta	13.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.28	-2.44	-2.53	0.47	19.35	-7.21	N/A	N/A	N/A	N/A	-3.2	0.89	N/A	N/A	0.9	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.092	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V72A	V72A	Coil	2.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.52	-1.2	-2.81	0.19	23.12	-3.44	N/A	N/A	N/A	N/A	-3.3	0.99	N/A	N/A	1.01	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.093	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V72I	V72I	Coil	2.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.82	1.1	-0.58	2.42	23.3	-3.26	N/A	N/A	N/A	N/A	-3.74	0.87	N/A	N/A	-0.84	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.094	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	M76A	M76A	Coil	23.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.97	-0.75	-2.21	0.79	22.73	-3.83	N/A	N/A	N/A	N/A	-3.22	1.04	N/A	N/A	0.25	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.095	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	S77A	S77A	Coil	23.8	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.99	-1.73	-2.3	0.7	20.56	-6.0	N/A	N/A	N/A	N/A	-3.02	1.02	N/A	N/A	0.72	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.096	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	S77T	S77T	Coil	23.8	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.85	0.13	-4.61	-1.61	30.85	4.29	N/A	N/A	N/A	N/A	-2.97	1.29	N/A	N/A	0.09	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.097	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L78A	L78A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.99	-1.73	1.8	4.8	10.38	-16.18	N/A	N/A	N/A	N/A	-3.12	0.97	N/A	N/A	0.29	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.098	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	D80A	D80A	Helix	54.0	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.81	-0.91	-3.22	-0.22	24.85	-1.71	N/A	N/A	N/A	N/A	-2.92	1.07	N/A	N/A	0.56	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.099	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C81A	C81A	Helix	2.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.81	0.09	-3.22	-0.22	27.33	0.77	N/A	N/A	N/A	N/A	-2.9	1.04	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.100	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C81I	C81I	Helix	2.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	10.12	2.4	-0.78	2.22	27.0	0.44	N/A	N/A	N/A	N/A	-3.77	0.94	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.101	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L82A	L82A	Helix	3.7	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.12	-1.6	-0.16	2.84	15.56	-11.0	N/A	N/A	N/A	N/A	-4.61	1.14	N/A	N/A	0.39	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.102	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	A85G	A85G	Helix	4.7	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.27	-1.45	-1.31	1.69	18.79	-7.77	N/A	N/A	N/A	N/A	-3.67	0.92	N/A	N/A	0.56	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.103	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L86A	L86A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.53	-2.19	1.02	4.02	11.17	-15.39	N/A	N/A	N/A	N/A	-3.17	0.67	N/A	N/A	0.44	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.104	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	R89L	R89L	Helix	33.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	10.33	2.61	-3.22	-0.22	33.57	7.01	N/A	N/A	N/A	N/A	-3.12	1.14	N/A	N/A	1.2	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.105	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L91A	L91A	Coil	39.6	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.49	-0.23	-0.73	2.27	20.38	-6.18	N/A	N/A	N/A	N/A	-3.72	0.94	N/A	N/A	0.1	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.106	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	P93A	P93A	Coil	2.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.22	0.5	-2.3	0.7	26.06	-0.5	N/A	N/A	N/A	N/A	-3.32	0.92	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.107	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C95A	C95A	Coil	51.9	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.05	-0.67	-3.0	0.0	24.88	-1.68	N/A	N/A	N/A	N/A	-2.75	1.07	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.108	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C96A	C96A	Beta	14.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.15	0.43	-0.11	2.89	20.44	-6.12	N/A	N/A	N/A	N/A	-3.22	0.89	N/A	N/A	-0.1	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.109	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C96L	C96L	Beta	14.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.36	-0.36	-3.22	-0.22	26.22	-0.34	N/A	N/A	N/A	N/A	-2.73	1.21	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.110	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	C96M	C96M	Beta	14.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.9	0.18	-3.51	-0.51	28.26	1.7	N/A	N/A	N/A	N/A	-3.1	1.16	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.111	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	A97G	A97G	Beta	0.9	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.05	-0.67	-1.56	1.44	21.33	-5.23	N/A	N/A	N/A	N/A	-2.9	0.92	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.112	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V98A	V98A	Beta	2.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.73	-1.99	-1.24	1.76	17.26	-9.3	N/A	N/A	N/A	N/A	-2.28	0.92	N/A	N/A	0.48	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.113	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	R100A	R100A	Beta	10.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.5	-0.22	-1.61	1.39	22.57	-3.99	N/A	N/A	N/A	N/A	-2.95	0.97	N/A	N/A	0.21	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.114	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	E104A	E104A	Coil	61.3	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.08	0.36	-2.53	0.47	26.28	-0.28	N/A	N/A	N/A	N/A	-3.2	0.92	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.115	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	K109A	K109A	Coil	22.0	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	8.01	0.29	-1.66	1.34	23.97	-2.59	N/A	N/A	N/A	N/A	-3.25	0.84	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.116	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L112A	L112A	Coil	15.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.07	-1.65	1.01	4.01	12.54	-14.02	N/A	N/A	N/A	N/A	-2.48	0.89	N/A	N/A	0.41	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.117	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	D117A	D117A	Coil	55.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.38	-0.34	-2.3	0.7	23.98	-2.58	N/A	N/A	N/A	N/A	-3.12	1.02	N/A	N/A	0.2	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.118	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	A118G	A118G	Helix	1.9	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.51	-1.21	-0.73	2.27	17.94	-8.62	N/A	N/A	N/A	N/A	-2.6	1.14	N/A	N/A	0.39	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.119	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	A118L	A118L	Helix	1.9	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.28	-0.44	1.17	4.17	15.14	-11.42	N/A	N/A	N/A	N/A	-2.85	0.77	N/A	N/A	0.11	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.120	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L121A	L121A	Coil	9.1	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.73	-0.99	0.67	3.67	14.99	-11.57	N/A	N/A	N/A	N/A	-2.82	0.99	N/A	N/A	0.26	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.121	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	E124A	E124A	Coil	22.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.55	-0.17	-2.66	0.34	25.31	-1.25	N/A	N/A	N/A	N/A	-3.0	0.99	N/A	N/A	N/A	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.122	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	E125A	E125A	Beta	24.7	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.91	-0.81	-2.81	0.19	24.09	-2.47	N/A	N/A	N/A	N/A	-3.0	1.07	N/A	N/A	0.86	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.123	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	L126A	L126A	Beta	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.34	-2.38	0.83	3.83	11.16	-15.4	N/A	N/A	N/A	N/A	-3.32	0.79	N/A	N/A	0.45	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.124	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	V128A	V128A	Beta	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.5	-2.22	1.16	4.16	10.74	-15.82	N/A	N/A	N/A	N/A	-3.0	0.82	N/A	N/A	0.42	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.125	2007.0	17137592	2	yes	2023-06-04 01:00:00
raf RBD	Homo sapiens	79.0	P04049	1rfa	A	Alpha Beta	PF02196	1rfaA00 (3.10.20.90)	2.7.11.1	D129A	D129A	Beta	20.2	25.0	7.0	Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.43	-0.29	-2.41	0.59	24.37	-2.19	N/A	N/A	N/A	N/A	-3.1	1.14	N/A	N/A	0.38	N/A	N/A	Campbell-Valois, F.-X., Michnick, S.W.	The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559–1577. https://doi.org/10.1016/j.jmb.2006.10.126	2007.0	17137592	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	E12A	E12A	Beta	53.1	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.83	-0.12	-2.86	0.38	23.6	-1.21	N/A	N/A	N/A	N/A	-4.82	2.51	N/A	N/A	0.24	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4236	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	V15A	V15A	Beta	11.3	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	7.06	0.11	0.81	4.05	15.23	-9.58	N/A	N/A	N/A	N/A	-5.07	2.24	N/A	N/A	-0.03	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4237	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	I17A	I17A	Helix	1.2	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	7.03	0.08	-1.08	2.16	19.75	-5.06	N/A	N/A	N/A	N/A	-4.56	2.83	N/A	N/A	-0.04	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4238	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	S18A	S18A	Helix	60.0	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.95	0.0	-3.02	0.22	24.27	-0.54	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-0.02	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4239	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	V23A	V23A	Beta	0.0	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.45	-0.5	-3.35	-0.11	23.85	-0.96	N/A	N/A	N/A	N/A	-4.6	2.66	N/A	N/A	1.27	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4241	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	R25A	R25A	Beta	47.6	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.53	-0.42	-3.02	0.22	23.22	-1.59	N/A	N/A	N/A	N/A	-4.46	2.53	N/A	N/A	0.65	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4242	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	G27A	G27A	Coil	77.4	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.45	-1.5	-3.44	-0.2	21.63	-3.18	N/A	N/A	N/A	N/A	-4.68	2.75	N/A	N/A	1.15	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4243	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	I30A	I30A	Beta	0.0	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	4.91	-2.04	-0.62	2.62	13.43	-11.38	N/A	N/A	N/A	N/A	-6.38	2.7	N/A	N/A	0.44	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4244	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	S31A	S31A	Beta	12.3	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.82	-0.13	-4.61	-1.37	27.82	2.68	N/A	N/A	N/A	N/A	-3.95	2.85	N/A	N/A	-0.1	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4245	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	F32A	F32A	Beta	0.5	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.25	-1.7	-0.97	2.27	15.15	-9.67	N/A	N/A	N/A	N/A	-5.55	2.63	N/A	N/A	0.43	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4246	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	D35A	D35A	Beta	27.0	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.67	-0.28	-2.59	0.65	22.55	-2.26	N/A	N/A	N/A	N/A	-4.17	2.53	N/A	N/A	0.3	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4247	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	G37A	G37A	Coil	27.4	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.71	-0.24	-2.53	0.71	22.51	-2.34	N/A	N/A	N/A	N/A	-4.29	2.41	N/A	N/A	0.25	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4248	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	T41A	T41A	Beta	48.6	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.63	-0.32	-2.12	1.12	21.3	-3.51	N/A	N/A	N/A	N/A	-4.26	2.46	N/A	N/A	0.22	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4249	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	R43A	R43A	Beta	61.7	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.75	-0.2	-2.48	0.76	22.47	-2.34	N/A	N/A	N/A	N/A	-4.34	2.48	N/A	N/A	0.21	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4250	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	A45G	A45G	Beta	32.1	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.66	-1.29	-2.35	0.89	19.5	-5.31	N/A	N/A	N/A	N/A	-4.21	2.66	N/A	N/A	0.59	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4251	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	V46A	V46A	Beta	9.9	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.7	-0.25	-0.7	2.54	17.99	-6.82	N/A	N/A	N/A	N/A	-5.65	2.78	N/A	N/A	0.09	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4252	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	S47A	S47A	Beta	41.5	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.9	-0.05	-3.61	-0.37	25.61	0.75	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-0.17	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4253	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	A51G	A51G	Coil	10.4	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.16	-0.79	-0.43	2.81	16.02	-8.79	N/A	N/A	N/A	N/A	-5.19	2.46	N/A	N/A	0.22	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4254	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	L55A	L55A	Helix	0.0	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	5.52	-1.43	2.07	5.31	8.41	-16.4	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.21	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4255	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	L56A	L56A	Helix	20.1	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.27	-0.68	-1.43	1.81	18.74	-6.07	N/A	N/A	N/A	N/A	-4.92	2.68	N/A	N/A	0.27	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4256	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	Q57G	Q57G	Helix	47.5	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.55	-0.4	-2.9	0.34	23.01	-1.8	N/A	N/A	N/A	N/A	-4.36	2.66	N/A	N/A	0.54	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4257	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	L59A	L59A	Helix	6.1	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.27	-0.68	-2.78	0.46	22.01	-2.8	N/A	N/A	N/A	N/A	-4.36	2.68	N/A	N/A	0.6	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4258	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	WT(Y34W)	WT(Y34W)	N/A	N/A	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.95	N/A	-3.24	N/A	24.81	N/A	N/A	N/A	N/A	N/A	-4.24	2.51	N/A	N/A	N/A	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4234	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	V4A	V4A	Beta	1.4	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.92	-0.03	0.37	3.61	15.9	-8.87	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.01	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4234	2000.0	11124040	2	yes	2023-06-04 01:00:00
Sso7d (Y34W)	Saccharolobus solfataricus	64.0	P39476	1bnz	A	Mainly Beta	PF02294	1bnzA00 (2.40.50.40)	N/A	K7A	K7A	Beta	67.3	20.0	6.1	MES	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	6.98	0.03	-2.75	0.49	23.68	-1.13	N/A	N/A	N/A	N/A	-4.14	2.48	N/A	N/A	-0.06	Y34W	Y34W	Guerois, R., Serrano, L.	The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967–982. https://doi.org/10.1006/jmbi.2000.4235	2000.0	11124040	2	yes	2023-06-04 01:00:00
CspB Bs	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	WT	WT	N/A	N/A	25.0	7.0	N/A	N/A	N/A	N/A	N/A	stopped-flow	GuHCl	6.32	N/A	2.3	N/A	11.13	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Perl, D., Welker, C., Schindler, T., Schröder, K., Marahiel, M.A., Jaenicke, R., Schmid, F.X.	Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol. 5, 229–235. https://doi.org/10.1038/nsb0398-229	1998.0	9501917	N/A	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	WT(E3L)	WT(E3L)	N/A	N/A	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.99	N/A	0.47	N/A	15.6	N/A	N/A	N/A	N/A	N/A	-2.3	0.32	5.97	N/A	N/A	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.011	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	L2A	L2A	Beta	37.2	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.87	-0.12	0.57	0.1	15.1	N/A	N/A	N/A	N/A	N/A	-2.3	0.32	5.76	N/A	-0.4	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.012	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	L3E	L3E	N/A	N/A	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.17	-0.82	1.52	1.05	11.1	N/A	N/A	N/A	N/A	N/A	-2.38	0.32	4.12	N/A	0.44	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.013	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	K5A	K5A	Beta	49.3	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.1	-1.89	1.02	0.55	9.8	N/A	N/A	N/A	N/A	N/A	-2.81	0.32	3.12	N/A	0.78	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.014	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	V6T	V6T	Beta	1.4	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	4.39	-2.6	0.67	0.2	8.9	N/A	N/A	N/A	N/A	N/A	-3.22	0.34	2.51	N/A	0.96	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.015	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	K7A	K7A	Beta	36.6	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.27	-1.72	0.67	0.2	11	N/A	N/A	N/A	N/A	N/A	-2.59	0.32	3.78	N/A	0.89	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.016	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	N10A	N10A	Beta	36.9	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.56	-1.43	0.82	0.35	11.3	N/A	N/A	N/A	N/A	N/A	-2.76	0.26	3.76	N/A	0.79	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.017	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	E12A	E12A	Coil	100.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	7.11	0.12	0.54	0.07	15.8	N/A	N/A	N/A	N/A	N/A	-2.51	0.32	5.57	N/A	-1.5	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.018	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	K13A	K13A	Coil	69.8	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	7.34	0.35	0.28	-0.19	16.9	N/A	N/A	N/A	N/A	N/A	-2.5	0.33	5.98	N/A	-0.62	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.019	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	F15A	F15A	Beta	27.4	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.3	-1.69	1.95	1.48	8	N/A	N/A	N/A	N/A	N/A	-2.32	0.37	2.99	N/A	0.53	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.020	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	F17A	F17A	Beta	29.4	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.82	-0.17	2.35	1.88	10.7	N/A	N/A	N/A	N/A	N/A	-2.3	0.39	3.98	N/A	0.08	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.021	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	I18V	I18V	Beta	0.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.61	-0.38	3.45	2.98	7.6	N/A	N/A	N/A	N/A	N/A	-2.44	0.29	2.78	N/A	0.11	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.022	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	E19A	E19A	Beta	49.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	7.08	0.09	0.41	-0.06	16	N/A	N/A	N/A	N/A	N/A	-2.47	0.3	5.77	N/A	-0.5	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.023	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	D25A	D25A	Coil	39.9	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.5	-0.49	1.03	0.56	13.1	N/A	N/A	N/A	N/A	N/A	-2.36	0.44	4.69	N/A	-0.48	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.024	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	V26T	V26T	Beta	6.3	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.18	-1.81	1.16	0.69	9.6	N/A	N/A	N/A	N/A	N/A	-2.54	0.36	3.32	N/A	0.72	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.025	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	A32G	A32G	Helix	11.3	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.8	-0.19	1.65	1.18	12.3	N/A	N/A	N/A	N/A	N/A	-2.25	0.32	4.79	N/A	0.15	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.026	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	I33A	I33A	Beta	3.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.94	-0.05	4.41	3.94	6.1	N/A	N/A	N/A	N/A	N/A	-2.3	0.19	2.44	N/A	0.01	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.027	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	L41A	L41A	Coil	4.3	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.55	-1.44	3.11	2.64	5.9	N/A	N/A	N/A	N/A	N/A	-2.56	0.32	2.03	N/A	0.36	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.028	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	Q45A	Q45A	Coil	18.7	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.76	-0.23	1.17	0.7	13.4	N/A	N/A	N/A	N/A	N/A	-2.37	0.38	4.88	N/A	-0.27	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.029	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	F49A	F49A	Beta	0.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	5.22	-1.77	4.94	4.47	0.7	N/A	N/A	N/A	N/A	N/A	-1.67	0.05	0.39	N/A	N/A	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.030	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	F49L	F49L	Beta	0.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.81	-0.18	1.49	1.02	12.7	N/A	N/A	N/A	N/A	N/A	-2.3	0.44	4.46	N/A	0.14	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.031	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	I51A	I51A	Beta	29.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.55	-0.44	3.49	3.02	7.3	N/A	N/A	N/A	N/A	N/A	-2.3	0.34	2.79	N/A	0.13	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.032	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	A60G	A60G	Beta	1.9	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.46	-0.53	3.91	3.44	6.1	N/A	N/A	N/A	N/A	N/A	-2.3	0.17	2.48	N/A	0.14	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.033	2004.0	15147842	2	yes	2023-06-04 01:00:00
CspB Bs (E3L)	Bacillus subtilis	67.0	P32081	1csp	A	Mainly Beta	PF00313	1cspA00 (2.40.50.140)	N/A	V63A	V63A	Beta	0.0	15.0	7.0	Sodium Cacodylate	0.1	N/A	N/A	N/A	stopped-flow	urea	6.25	-0.74	5.06	4.59	2.9	N/A	N/A	N/A	N/A	N/A	-1.3	0.18	1.94	N/A	N/A	E3L	E3L	Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.	The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555–569. https://doi.org/10.1016/j.jmb.2004.04.034	2004.0	15147842	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	WT	WT	N/A	N/A	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.52	N/A	-6.44	N/A	34.5	N/A	N/A	N/A	N/A	N/A	-5.38	3.63	N/A	N/A	N/A	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20340	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	F6A	F5A	Helix	0.5	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.88	0.36	0.01	6.45	20.5	-14.1	N/A	N/A	N/A	N/A	-6.53	1.66	N/A	N/A	-0.06	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20340	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	A10G	A9G	Helix	0.0	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.81	0.29	-2.29	4.15	25.6	-8.89	N/A	N/A	N/A	N/A	-5.68	2.48	N/A	N/A	-0.08	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20341	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	V13A	V12A	Helix	1.4	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.85	-0.67	-6.25	0.19	32.6	-1.99	N/A	N/A	N/A	N/A	-5.43	3.66	N/A	N/A	0.78	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20342	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L16A	L15A	Coil	16.5	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.81	-0.71	-3.12	3.32	25.3	-9.29	N/A	N/A	N/A	N/A	-5.77	3.23	N/A	N/A	0.17	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20343	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L25A	L25A	Helix	31.7	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.94	0.42	-3.88	2.56	29.6	-4.92	N/A	N/A	N/A	N/A	-5.43	3.08	N/A	N/A	-0.2	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20344	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L26A	L27A	Helix	4.9	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.32	-2.2	-5.24	1.2	26.7	-7.82	N/A	N/A	N/A	N/A	-6.43	3.31	N/A	N/A	0.65	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20345	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	Y29A	Y28A	Helix	29.3	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	9.42	0.9	-0.08	6.36	21.9	-12.6	N/A	N/A	N/A	N/A	-5.86	1.87	N/A	N/A	-0.16	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20346	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L31A	L30A	Helix	15.2	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.21	-0.31	-0.51	5.93	20.1	-14.4	N/A	N/A	N/A	N/A	-6.31	2.45	N/A	N/A	0.05	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20347	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	Y32A	Y31A	Helix	13.1	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.66	-0.86	-1.49	4.95	21.1	-13.4	N/A	N/A	N/A	N/A	-5.58	2.59	N/A	N/A	0.15	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20348	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	A35G	A34G	Helix	2.8	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.75	-0.77	-1.62	4.82	21.6	-12.9	N/A	N/A	N/A	N/A	-6.27	2.45	N/A	N/A	0.14	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20349	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	K55A	K54A	Helix	22.0	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.65	0.13	-5.42	1.02	32.5	-2.04	N/A	N/A	N/A	N/A	-5.19	3.4	N/A	N/A	-0.15	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20350	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	A58G	A57G	Helix	31.1	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.55	0.03	-2.39	4.05	25.3	-9.28	N/A	N/A	N/A	N/A	-5.17	3.28	N/A	N/A	-0.01	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20351	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L62A	L61A	Coil	18.9	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	8.7	0.18	-2.12	4.32	25.0	-9.54	N/A	N/A	N/A	N/A	-5.31	2.77	N/A	N/A	-0.04	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20352	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	A70G	A69G	Helix	0.0	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.88	-1.64	-2.26	4.18	21.1	-13.4	N/A	N/A	N/A	N/A	-6.06	2.89	N/A	N/A	0.28	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20353	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	Y74A	Y73A	Helix	0.0	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.12	-2.4	0.13	6.57	13.8	-20.7	N/A	N/A	N/A	N/A	-6.42	2.39	N/A	N/A	0.27	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20354	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	I75A	I74A	Helix	36.7	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	9.07	0.55	-1.25	5.19	23.8	-10.7	N/A	N/A	N/A	N/A	-6.2	2.21	N/A	N/A	-0.12	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20355	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	V78A	V77A	Helix	0.0	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.64	-0.88	-6.92	-0.48	33.6	-0.91	N/A	N/A	N/A	N/A	-5.69	3.69	N/A	N/A	2.24	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20356	2005.0	15690348	2	yes	2023-06-04 01:00:00
yACBP	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)	79.0	P31787	1st7	A	Mainly Alpha	PF00887	1st7A00 (1.20.80.10)	N/A	L81A	L80A	Helix	4.3	5.0	5.3	Na-acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	4.61	-3.91	-5.09	1.35	22.4	-12.1	N/A	N/A	N/A	N/A	-6.23	3.84	N/A	N/A	0.74	N/A	N/A	Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.	Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80–90. https://doi.org/10.1002/prot.20357	2005.0	15690348	2	yes	2023-06-04 01:00:00
Cold shock-like protein	Thermotoga maritima	66.0	O54310	1g6p	A	Mainly Beta	PF00313	1g6pA00 (2.40.50.140)	N/A	N/A	WT	N/A	N/A	25.0	7.0	Na cacodylate-HCI	0.1	N/A	N/A	N/A	stopped-flow	GdmCl	6.34	N/A	-4.02	N/A	25.6	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Perl D, Welker C, Schindler T, Schröder K, Marahiel MA, Jaenicke R, Schmid FX	Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229	1998.0	9501917	Yes	N/A	2023-06-09 01:00:00
B-domain of staphylococcal proteinA	Staphylococcus aureus	58.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	N/A	WT	N/A	N/A	37.0	5.0	Na Acetate	0.02	N/A	N/A	N/A	N/A	GdmCl	11.7	N/A	4.22	N/A	19.28	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Myers JK, Oas TG	Preorganized secondary structure as an important determinant of fast protein folding. Nat Struct Biol. 2001 8(6):552-8	2001.0	11373626	Yes	N/A	2023-06-09 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	WT(N239H/Q243W)	WT(N29H/Q33W)	N/A	N/A	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.77	N/A	2.13	N/A	16.44	-4.06	N/A	N/A	N/A	N/A	-4.18	1.88	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	N222A	N12A	Helix	47.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.08	0.31	2.18	0.05	17.11	-3.39	N/A	N/A	N/A	N/A	-4.52	1.76	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	N222G	N12G	Helix	47.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.55	-0.22	3.19	1.06	13.26	-7.24	N/A	N/A	N/A	N/A	-4.14	1.76	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.044	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	E226A	E16A	Helix	67.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.76	-0.01	1.95	-0.18	16.86	-3.64	N/A	N/A	N/A	N/A	-3.97	2.13	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.045	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	E226G	E16G	Helix	67.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.25	-0.52	3.82	1.69	11.0	-9.5	N/A	N/A	N/A	N/A	-4.44	1.59	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.046	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	I227V	I17V	Helix	0.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.55	-0.22	4.41	2.28	10.25	-10.25	N/A	N/A	N/A	N/A	-4.77	1.51	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.047	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L228G	L18G	Coil	26.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	7.62	-1.15	3.08	0.95	11.25	-9.25	N/A	N/A	N/A	N/A	-4.73	2.01	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.048	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L230A	L18A	Coil	26.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.88	0.11	6.53	4.4	5.82	-14.68	N/A	N/A	N/A	N/A	-4.77	1.97	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.049	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	R238A	R28A	Helix	10.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.38	-0.39	3.58	1.45	11.88	-8.62	N/A	N/A	N/A	N/A	-3.97	1.76	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.050	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	R238G	R28G	Helix	10.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	7.14	-1.63	5.25	3.12	4.69	-15.81	N/A	N/A	N/A	N/A	-4.64	1.55	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.051	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	I242V	I32V	Helix	0.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.02	-0.75	3.07	0.94	12.26	-8.24	N/A	N/A	N/A	N/A	-4.48	1.76	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.052	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S244A	S34A	Helix	30.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.79	1.02	2.24	0.11	18.7	-1.8	N/A	N/A	N/A	N/A	-4.9	1.55	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.053	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S244G	S34G	Helix	30.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.91	0.14	2.84	0.71	15.06	-5.44	N/A	N/A	N/A	N/A	-5.02	1.88	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.054	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L245A	L35A	Helix	9.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.43	-0.34	4.3	2.17	10.25	-10.25	N/A	N/A	N/A	N/A	-4.69	2.13	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.055	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S250G	S40G	Coil	57.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.82	0.05	2.47	0.34	15.73	-4.77	N/A	N/A	N/A	N/A	-4.31	2.22	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.056	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S252A	S42A	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.42	0.65	1.0	-1.13	20.84	0.34	N/A	N/A	N/A	N/A	-4.02	2.43	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.057	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S252G	S42G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.06	0.29	3.58	1.45	13.56	-6.94	N/A	N/A	N/A	N/A	-4.52	2.01	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.058	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L255A	L45A	Helix	11.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.33	-0.44	5.22	3.09	7.7	-12.8	N/A	N/A	N/A	N/A	-5.44	1.63	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.059	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	K261A	K51A	Helix	80.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.41	0.64	2.53	0.4	17.07	-3.43	N/A	N/A	N/A	N/A	-4.85	1.51	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.060	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	K261G	K51G	Helix	80.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.8	0.03	4.05	1.92	11.8	-8.7	N/A	N/A	N/A	N/A	-4.69	1.38	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.061	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (N31H/Q35W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L262A	L52A	Helix	31.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.79	0.02	4.43	2.3	10.79	-9.71	N/A	N/A	N/A	N/A	-4.56	1.67	N/A	N/A	N/A	N239H/Q243W	N29H/Q33W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.062	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	WT(E258W)	WT(E48W)	N/A	N/A	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.29	N/A	3.44	N/A	19.46	-1.04	N/A	N/A	N/A	N/A	-4.69	1.72	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	N222A	N12A	Helix	47.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.96	-0.33	2.48	-0.96	21.0	0.5	N/A	N/A	N/A	N/A	-4.18	2.18	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	N222G	N12G	Helix	47.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.8	-0.49	3.98	0.54	16.9	-3.6	N/A	N/A	N/A	N/A	-4.35	1.88	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.044	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	E226A	E16A	Helix	67.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.41	0.12	3.62	0.18	19.33	-1.17	N/A	N/A	N/A	N/A	-4.52	1.67	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.045	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	E226G	E16G	Helix	67.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.52	-0.77	4.59	1.15	14.73	-5.77	N/A	N/A	N/A	N/A	-4.44	1.84	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.046	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	I227V	I17V	Helix	0.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.56	-0.73	4.92	1.48	13.97	-6.53	N/A	N/A	N/A	N/A	-4.52	1.97	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.047	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L228G	L18G	Coil	26.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.97	-1.32	4.37	0.93	13.85	-6.65	N/A	N/A	N/A	N/A	-5.19	1.8	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.048	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L230A	L20A	Coil	11.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.62	-0.67	7.29	3.85	8.24	-12.26	N/A	N/A	N/A	N/A	-4.1	2.22	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.049	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	R238A	R28A	Helix	10.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.53	-0.76	5.11	1.67	13.43	-7.07	N/A	N/A	N/A	N/A	-4.52	1.21	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.050	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	R238G	R28G	Helix	10.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.91	-2.38	6.28	2.84	6.53	-13.97	N/A	N/A	N/A	N/A	-5.65	1.21	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.051	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	I242V	I32V	Helix	0.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.44	-0.85	3.65	0.21	16.86	-3.64	N/A	N/A	N/A	N/A	-4.31	2.22	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.052	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S244A	S34A	Helix	30.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.48	0.19	2.4	-1.04	22.51	2.01	N/A	N/A	N/A	N/A	-4.18	1.92	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.053	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S244G	S34G	Helix	30.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.41	-0.88	3.52	0.08	17.07	-3.43	N/A	N/A	N/A	N/A	-4.44	1.84	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.054	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L245A	L35A	Helix	9.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.95	-1.34	5.64	2.2	10.71	-9.79	N/A	N/A	N/A	N/A	-5.31	1.84	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.055	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S250G	S40G	Coil	57.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.12	-0.17	4.49	1.05	16.4	-4.1	N/A	N/A	N/A	N/A	-4.77	1.38	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.056	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S252A	S42A	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	12.1	0.81	3.32	-0.12	21.76	1.26	N/A	N/A	N/A	N/A	-4.73	1.55	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.057	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	S252G	S42G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.06	-0.23	4.66	1.22	15.86	-4.64	N/A	N/A	N/A	N/A	-4.56	1.88	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.058	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L255A	L45A	Helix	11.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.42	-0.87	5.73	2.29	11.63	-8.87	N/A	N/A	N/A	N/A	-5.19	1.51	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.059	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	K261A	K51A	Helix	80.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.64	0.35	3.16	-0.28	21.0	0.5	N/A	N/A	N/A	N/A	-4.69	1.67	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.060	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	K261G	K51G	Helix	80.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.91	-0.38	5.14	1.7	14.31	-6.19	N/A	N/A	N/A	N/A	-4.35	1.59	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.061	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (E50W)	Staphylococcus aureus	60.0	P38507	1bdc	A	Mainly Alpha	PF02216	1bdcA00 (1.20.5.420)	N/A	L262A	L52A	Helix	31.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.83	-0.46	5.73	2.29	12.64	-7.86	N/A	N/A	N/A	N/A	-4.85	1.51	N/A	N/A	N/A	E258W	E48W	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.062	2007.0	17628591	2	yes	2023-06-04 01:00:00
Cold shock protein CspA	Escherichia coli (strain K12)	69.0	P0A9X9	1mjc	A	Mainly Beta	PF00313	1mjcA00 (2.40.50.140)	N/A	N/A	WT	N/A	N/A	25.0	7.0	KPi	0.05	N/A	N/A	N/A	stopped-flow	urea	5.29	N/A	1.44	N/A	9.54	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM	Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7(2):470-9	1998.0	9521124	Yes	N/A	2023-06-09 01:00:00
Phosphocarrier protein HPr	Escherichia coli (strain K12)	85.0	P0AA04	1opd	A	Alpha Beta	PF00381	1opdA00 (3.30.1340.10)	N/A	N/A	WT	N/A	N/A	20.0	7.0	Phosphate	0.1	N/A	N/A	N/A	stopped-flow	GdnHCl	2.7	N/A	-6.17	N/A	21.61	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM	Slow cooperative folding of a small globular protein HPr. Biochemistry. 37(2):622-37	1998.0	9425085	Yes	N/A	2023-06-09 01:00:00
TRF1 Myb domain (Telomeric repeat-binding factor 1)	Homo sapiens	53.0	P54274	1ba5	A	Mainly Alpha	PF00249	1ba5A00 (1.10.10.60)	N/A	N/A	WT	N/A	N/A	25.0	5.7	Na Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.91	N/A	1.16	N/A	11.8	N/A	N/A	N/A	N/A	N/A	-3.6	0.38	N/A	0.9	N/A	N/A	N/A	Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR	Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100	2003.0	14595026	Yes	N/A	2023-06-09 01:00:00
RAP1 Myb domain (Telomeric repeat-binding factor 2-interacting protein 1)	Homo sapiens	59.0	Q9NYB0	1fex	A	Mainly Alpha	PF08914	1fexA00 (1.10.10.60)	N/A	N/A	WT	N/A	N/A	25.0	5.7	Na Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.73	N/A	2.89	N/A	13.05	N/A	N/A	N/A	N/A	N/A	-2.85	0.63	N/A	0.82	N/A	N/A	N/A	Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR	Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100	2003.0	14595026	Yes	N/A	2023-06-09 01:00:00
c-Myb-transforming protein (Transcriptional activator Myb)	Mus musculus	53.0	P06876	1idy	A	Mainly Alpha	PF00249	1idyA00 (1.10.10.60)	N/A	N/A	WT(I155L)	N/A	N/A	25.0	5.7	Na Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.19	N/A	1.67	N/A	17.45	N/A	N/A	N/A	N/A	N/A	-2.72	0.71	N/A	0.79	N/A	N/A	I155L	Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR	Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100	2003.0	14595026	Yes	N/A	2023-06-09 01:00:00
Yes kinase-associated protein (Transcriptional coactivator YAP1)	Homo sapiens	45.0	P46937	1jmq	A	Mainly Beta	PF00397	1jmqA00 (2.20.70.10)	N/A	N/A	WT	N/A	N/A	25.0	7.0	NaPi	0.02	N/A	N/A	N/A	continuous-flow	urea	8.4	N/A	6.7	N/A	4.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proc. Natl. Acad. Sci. U.S.A. 98, 13002–13007. https://doi.org/10.1073/pnas.221467198	2001.0	11687613	Yes	N/A	2023-06-09 01:00:00
SH3 domain of the phosphatidylinositol 3-kinase regulatory subunit alpha	Bos taurus	84.0	P23727	1pnj	A	Mainly Beta	N/A	1pnjA00 (2.30.30.40)	N/A	N/A	WT	N/A	N/A	20.0	7.2	NaPi	0.02	N/A	N/A	N/A	manual mixing	GdmCl	-1.04	N/A	-7.31	N/A	15.27	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM	Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J Mol Biol. 276(3):657-67. https://doi.org/10.1006/jmbi.1997.1553	1998.0	9551103	Yes	N/A	2023-06-09 01:00:00
18th module of muscle protein twitchin	Caenorhabditis elegans	93.0	Q23551	1wit	A	Mainly Beta	PF07679	1witA00 (2.60.40.10)	2.7.11.1	N/A	WT	N/A	N/A	20.0	5.0	Na Acetate	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	0.41	N/A	-8.18	N/A	20.93	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.7	N/A	N/A	N/A	Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J   Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39	Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39. https://doi.org/10.1006/jmbi.1996.0665	1996.0	8969309	Yes	N/A	2023-06-09 01:00:00
Acylphosphatase-1	Homo sapiens	99.0	P07311	2vh7	A	Alpha Beta	PF00708	2vh7A00 (3.30.70.100)	3.6.1.7	N/A	WT	N/A	N/A	28.0	5.5	Na Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	0.84	N/A	-6.5	N/A	18.37	N/A	N/A	N/A	N/A	N/A	-5.1	2.0	2.6	N/A	N/A	N/A	N/A	Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G	Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38(7):2135-42. https://doi.org/10.1021/bi9822630	1999.0	10026297	Yes	N/A	2023-06-09 01:00:00
apocytochrome b5	Bos taurus	93.0	P00171	1cyo	A	Alpha Beta	PF00173	1cyoA00 (3.10.120.10)	N/A	N/A	WT	N/A	N/A	10.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	2.97	N/A	-1.43	N/A	10.35	N/A	N/A	N/A	N/A	N/A	-5.59	2.4	1.58	N/A	N/A	N/A	N/A	Manyusa S, Whitford D	Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 38(29):9533-40. https://doi.org/10.1021/bi990550d	1999.0	10413531	Yes	N/A	2023-06-09 01:00:00
hbLBD (Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial)	Homo sapiens	84.0	P11182	1k8m	A	Mainly Beta	PF00364	1k8mA00 (2.40.50.100)	2.3.1.168	N/A	WT	N/A	N/A	22.0	7.5	KPi	0.05	N/A	N/A	N/A	manual mixing	urea	-0.94	N/A	-8.05	N/A	17.45	N/A	N/A	N/A	N/A	N/A	-1.2	0.98	4.8	N/A	N/A	N/A	N/A	Naik MT, Chang YC, Huang TH	Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex. FEBS Lett. 530(1-3):133-8. https://doi.org/10.1016/s0014-5793(02)03444-0	2002.0	12387880	Yes	N/A	2023-06-09 01:00:00
Protein p13 MTCP-1	Homo sapiens	117.0	P56278	1qtu	A	Mainly Beta	PF01840	1qtuA00 (2.40.15.10)	N/A	N/A	WT	N/A	N/A	21.0	7.0	Tris	0.05	N/A	N/A	N/A	manual mixing	GdmCl	-0.36	N/A	-11.11	N/A	26.28	N/A	N/A	N/A	N/A	N/A	-9.76	3.0	2.2	N/A	N/A	N/A	N/A	Roumestand C, Boyer M, Guignard L, Barthe P, Royer CA	Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13. J Mol Biol. 312(1):247-59. https://doi.org/10.1006/jmbi.2001.4928	2001.0	11545600	Yes	N/A	2023-06-09 01:00:00
Trp-cage protein	N/A	20.0	N/A	1l2y	A	N/A	N/A	N/A	N/A	N/A	WT	N/A	N/A	23.0	7.0	Phosphate	0.1	N/A	N/A	N/A	T-jump	thermal denaturation	12.39	N/A	11.32	N/A	2.62	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Qiu L, Pabit SA, Roitberg AE, Hagen SJ	Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J Am Chem Soc. 124(44):12952-3. https://doi.org/10.1021/ja0279141	2002.0	12405814	Yes	N/A	2023-06-09 01:00:00
α3D	N/A	73.0	N/A	2a3d	A	N/A	N/A	N/A	N/A	N/A	WT	N/A	N/A	25.0	2.2	Phosphate	0.05	N/A	N/A	N/A	T-jump	thermal denaturation or urea	12.24	N/A	7.83	N/A	10.93	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F	Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A. 100(26):15486-91. https://doi.org/10.1073/pnas.2136623100	2003.0	14671331	Yes	N/A	2023-06-09 01:00:00
Villin-1	Gallus gallus	126.0	P02640	2vik	A	Alpha Beta	PF00626	2vikA00 (3.40.20.10)	N/A	N/A	WT	N/A	N/A	37.0	4.1	Acetate	0.05	N/A	N/A	1 mM beta-ME	stopped-flow	urea	6.8	N/A	-2.8	N/A	24.74	N/A	N/A	N/A	N/A	N/A	-4.64	1.72	N/A	N/A	N/A	N/A	N/A	Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI	Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry. 37(41):14508-18. https://doi.org/10.1021/bi980889k	1998.0	9772179	Yes	N/A	2023-06-09 01:00:00
C-domain of development-specific protein S	Myxococcus xanthus	90.0	P02966	1prs	A	Mainly Beta	PF00030	1prsA01 (2.60.20.10)/1prsA02 (2.60.20.10)	N/A	N/A	WT	N/A	N/A	20.0	7.0	MOPS	0.025	N/A	N/A	N/A	manual mixing	urea	-2.04	N/A	-9.25	N/A	17.56	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Wenk M, Jaenicke R, Mayr EM	Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30.https://doi.org/10.1016/s0014-5793(98)01287-3	1998.0	9821973	Yes	N/A	2023-06-09 01:00:00
N-domain of development-specific protein S	Myxococcus xanthus	82.0	P02966	1prs	A	Mainly Beta	PF00030	1prsA01 (2.60.20.10)/1prsA02 (2.60.20.10)	N/A	N/A	WT	N/A	N/A	20.0	7.0	MOPS	0.025	N/A	N/A	N/A	manual mixing	urea	3.04	N/A	-9.37	N/A	30.23	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Wenk M, Jaenicke R, Mayr EM	Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30. https://doi.org/10.1016/s0014-5793(98)01287-3	1998.0	9821973	Yes	N/A	2023-06-09 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	L145A	L125A	Beta	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.78	-1.06	-15.19	1.77	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.36	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	I27A	I7A	Beta	1.2	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.39	-0.45	-11.75	5.21	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.08	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	I40A	I20A	Beta	4.1	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.23	-0.61	-13.53	3.43	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	V42A	V22A	Coil	2.8	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.43	-0.41	-14.54	2.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.14	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	V51A	V31A	Beta	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.74	-1.1	-15.23	1.73	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.39	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	L53A	L33A	Beta	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.01	-0.83	-14.96	2.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.29	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	W68A	W48A	Coil	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.09	-1.75	-13.05	3.91	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.3	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	L70A	L50A	Beta	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.47	-1.37	-15.3	1.66	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.44	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	V80G	V60G	Helix	19.7	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.91	-0.93	-12.64	4.32	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.18	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	I101A	I81A	Coil	26.6	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.01	-0.83	-15.37	1.59	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.33	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	A102G	A82G	Beta	7.5	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.81	-1.03	-15.16	1.8	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.36	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	V115A	V95A	Beta	11.3	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.2	-0.64	-15.98	0.98	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.38	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	F117A	F97A	Beta	5.6	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	3.89	-0.95	-13.46	3.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.21	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	Y128A	Y108A	Beta	4.1	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	2.77	-2.07	-12.97	3.99	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.33	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	F130A	F110A	Beta	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.42	-0.42	-8.9	8.06	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.05	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	M141A	M121A	Coil	0.0	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.56	-0.28	-12.39	4.57	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.06	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	WT	WT	N/A	N/A	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.84	N/A	-16.96	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	N/A	2023-06-04 01:00:00
Azurin	Pseudomonas aeruginosa	128.0	P00282	1azu	A	Mainly Beta	PF00127	1azuA00 (2.60.40.420)	N/A	V25A	V5A	Beta	17.6	25.0	7.0	TRIS	0.1	N/A	N/A	N/A	stopped-flow	GuHCl	4.6	-0.24	-15.59	1.37	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	N/A	Wilson, C.J., Wittung-Stafshede, P.	Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054–10062. https://doi.org/10.1021/bi050342n	2005.0	16042382	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	K130G	K164G	Helix	61.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	10.69	-1.56	7.75	1.4	7.29	-7.35	N/A	N/A	N/A	N/A	-3.05	0.63	N/A	N/A	0.57	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.111	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	R131G	R165G	Helix	56.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	10.69	-1.56	7.26	0.91	8.51	-6.13	N/A	N/A	N/A	N/A	-2.72	0.71	N/A	N/A	0.76	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.113	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A133G	A167G	Helix	19.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.03	-1.22	7.54	1.19	8.66	-5.98	N/A	N/A	N/A	N/A	-2.64	0.71	N/A	N/A	0.64	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.114	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A97G	A131G	Coil	24.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.98	-0.27	8.19	1.84	9.4	-5.24	N/A	N/A	N/A	N/A	-2.64	0.63	N/A	N/A	0.2	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.082	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	M98A	M132A	Coil	28.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.78	-0.47	7.38	1.03	10.9	-3.74	N/A	N/A	N/A	N/A	-2.72	0.67	N/A	N/A	0.4	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.083	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A100G	A134G	Helix	44.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.85	-0.4	7.18	0.83	11.57	-3.07	N/A	N/A	N/A	N/A	-2.85	0.67	N/A	N/A	0.4	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.084	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A101G	A135G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.61	-0.64	9.21	2.86	5.94	-8.7	N/A	N/A	N/A	N/A	-2.55	0.59	N/A	N/A	0.18	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.085	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	L104A	L138A	Helix	17.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.29	-0.96	8.85	2.5	6.04	-8.6	N/A	N/A	N/A	N/A	-2.97	0.33	N/A	N/A	0.33	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.086	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A105G	A139G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.07	-1.18	9.1	2.75	4.86	-9.78	N/A	N/A	N/A	N/A	-2.55	0.59	N/A	N/A	0.3	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.087	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	L108A	L142A	Helix	58.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.1	-1.15	9.31	2.96	4.44	-10.2	N/A	N/A	N/A	N/A	-2.93	0.59	N/A	N/A	0.28	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.088	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	I110A	I144A	Coil	11.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.08	-1.17	8.96	2.61	5.25	-9.39	N/A	N/A	N/A	N/A	-2.38	0.59	N/A	N/A	0.31	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.089	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	A112G	A146G	Coil	8.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.47	-0.78	8.72	2.37	6.83	-7.81	N/A	N/A	N/A	N/A	-2.8	0.46	N/A	N/A	0.3	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.091	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	V115A	V149A	Coil	2.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.29	-0.96	8.1	1.75	7.9	-6.74	N/A	N/A	N/A	N/A	-3.18	0.59	N/A	N/A	0.38	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.094	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	T118S	T152S	Coil	73.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.78	-0.47	7.39	1.04	10.86	-3.78	N/A	N/A	N/A	N/A	-2.89	0.59	N/A	N/A	0.4	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.096	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	P120A	P154A	Coil	90.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.16	-1.09	7.01	0.66	10.27	-4.37	N/A	N/A	N/A	N/A	-2.76	0.63	N/A	N/A	0.8	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.097	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	P120G	P154G	Coil	90.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	10.55	-1.7	7.86	1.51	6.65	-7.99	N/A	N/A	N/A	N/A	-2.93	0.75	N/A	N/A	0.58	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.098	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	V123A	V157A	Beta	15.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.85	-0.4	7.74	1.39	10.18	-4.46	N/A	N/A	N/A	N/A	-2.76	0.54	N/A	N/A	0.3	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.099	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	I124A	I158A	Coil	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	10.82	-1.43	8.07	1.72	6.81	-7.83	N/A	N/A	N/A	N/A	-2.93	0.59	N/A	N/A	0.45	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.100	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	T125A	T159A	Coil	21.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	10.93	-1.32	7.94	1.59	7.42	-7.22	N/A	N/A	N/A	N/A	-3.05	0.71	N/A	N/A	0.48	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.102	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	V126A	V160A	Helix	31.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.92	-0.33	8.39	2.04	8.74	-5.9	N/A	N/A	N/A	N/A	-2.72	0.42	N/A	N/A	0.21	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.104	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	E127G	E161G	Helix	58.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	11.14	-1.11	6.86	0.51	10.62	-4.02	N/A	N/A	N/A	N/A	-2.89	0.5	N/A	N/A	0.9	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.106	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	D128N	D162N	Helix	16.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	9.64	-2.61	7.74	1.39	4.69	-9.95	N/A	N/A	N/A	N/A	-2.64	0.67	N/A	N/A	0.65	L112A/Y132W	N/A	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.108	2008.0	18625240	2	yes	2023-06-04 01:00:00
POB (L146A/Y166W)	Pyrobaculum aerophilum	51.0	Q8ZUR6	1w4j	A	Few Secondary Structures	PF02817	1w4jA00 (4.10.320.10)	2.3.1.12	WT(L112A/Y132W)	WT(L22A/Y42W)	N/A	N/A	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump or continuous-flow	thermal or GuHCl	12.25	N/A	6.35	N/A	14.64	N/A	N/A	N/A	N/A	N/A	-2.93	0.71	N/A	N/A	N/A	L112A/Y132W	WT	Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.	Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224–237. https://doi.org/10.1016/j.jmb.2008.06.081	2008.0	18625240	2	yes	2023-06-04 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	WT	WT	N/A	N/A	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.78	N/A	2.65	N/A	12.5	N/A	N/A	N/A	N/A	N/A	-3.18	0.84	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	2	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	T596S	T11S	Coil	51.4	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.65	-0.13	3.04	0.39	11.23	-1.27	N/A	N/A	N/A	N/A	-3.18	0.84	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L599A	L14A	Helix	35.4	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.44	-0.34	2.4	-0.25	12.28	-0.22	N/A	N/A	N/A	N/A	-3.05	0.96	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603A	L18A	Helix	14.6	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.44	-0.34	1.1	-1.55	15.44	2.94	N/A	N/A	N/A	N/A	-3.6	0.84	N/A	N/A	-0.26	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	V608A	V23A	Helix	2.8	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.58	-1.2	3.56	0.91	7.36	-5.14	N/A	N/A	N/A	N/A	-2.13	0.71	N/A	N/A	0.57	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	A610G	A25G	Helix	23.6	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.61	-1.17	4.43	1.78	5.31	-7.19	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	0.39	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I611V	I26V	Helix	1.8	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.78	0.0	3.14	0.49	11.3	-1.2	N/A	N/A	N/A	N/A	-3.89	0.75	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	T614S	T29S	Coil	17.6	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.24	-0.54	2.4	-0.25	11.79	-0.71	N/A	N/A	N/A	N/A	-2.72	0.84	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	A618G	A33G	Helix	48.1	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.04	0.26	3.04	0.39	12.18	-0.32	N/A	N/A	N/A	N/A	-3.51	0.63	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	A619G	A34G	Helix	37.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.01	0.23	3.22	0.57	11.67	-0.83	N/A	N/A	N/A	N/A	-3.43	0.84	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L620A	L35A	Helix	29.3	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.86	0.08	3.22	0.57	11.3	-1.2	N/A	N/A	N/A	N/A	-3.43	0.84	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L628A	L43A	Helix	17.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.65	-0.13	0.26	-2.39	18.0	5.5	N/A	N/A	N/A	N/A	-3.77	1.09	N/A	N/A	-0.05	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	V629A	V44A	Helix	14.1	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.45	-1.33	4.25	1.6	5.36	-7.14	N/A	N/A	N/A	N/A	-2.59	0.59	N/A	N/A	0.45	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	A630G	A45G	Helix	50.0	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.17	-0.61	3.3	0.65	9.43	-3.07	N/A	N/A	N/A	N/A	-3.43	0.71	N/A	N/A	0.47	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	Y631A	Y46A	Helix	39.6	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.5	-0.28	4.14	1.49	8.18	-4.32	N/A	N/A	N/A	N/A	-3.18	0.84	N/A	N/A	0.15	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	V635A	V50A	Helix	12.0	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.55	-0.23	3.56	0.91	9.72	-2.78	N/A	N/A	N/A	N/A	-2.59	0.75	N/A	N/A	0.2	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	Y650A	Y65A	Helix	41.0	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.5	-0.28	3.26	0.61	10.33	-2.17	N/A	N/A	N/A	N/A	-4.18	0.84	N/A	N/A	0.43	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L652A	L67A	Helix	23.2	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.38	-0.4	3.4	0.75	9.7	-2.8	N/A	N/A	N/A	N/A	-3.77	0.84	N/A	N/A	-0.03	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L653A	L68A	Helix	5.5	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.56	-2.22	1.95	-0.7	8.79	-3.71	N/A	N/A	N/A	N/A	-2.51	1.09	N/A	N/A	1.43	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	A654G	A69G	Helix	54.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.09	-0.69	2.56	-0.09	11.04	-1.46	N/A	N/A	N/A	N/A	-3.31	0.92	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I657V	I72V	Helix	22.5	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.78	0.0	3.18	0.53	11.21	-1.29	N/A	N/A	N/A	N/A	-3.56	0.75	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	Y658A	Y73A	Helix	57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.7	0.92	2.71	0.06	14.59	2.09	N/A	N/A	N/A	N/A	-3.72	0.92	N/A	N/A	1.0	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I660V	I75V	Helix	11.2	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.74	-0.04	3.18	0.53	11.11	-1.39	N/A	N/A	N/A	N/A	-3.1	0.63	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L664A	L79A	Helix	61.6	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.65	-0.13	2.08	-0.57	13.57	1.07	N/A	N/A	N/A	N/A	-3.39	0.88	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603/I611V	L18A/I26V	Helix/Helix	14.6/1.8	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.51	-1.27	1.28	-1.37	12.74	0.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603/L628A	L18A/L43A	Helix/Helix	14.6/17.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.94	-1.84	-1.35	-4.0	17.76	5.26	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603/Y650A	L18A/Y65A	Helix/Helix	14.6/41.0	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.72	-1.06	1.55	-1.1	12.59	0.09	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603/L652A	L18A/L67A	Helix/Helix	14.6/23.2	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.84	-0.94	2.12	-0.53	11.5	-1.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L603/Y658A	L18A/Y73A	Helix/Helix	14.6/57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.74	-0.04	0.53	-2.12	17.56	5.06	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I611/L611A	I26V/L43A	Helix/Helix	1.8/17.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.48	-1.3	0.83	-1.82	13.76	1.26	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I611/L652A	I26V/L67A	Helix/Helix	1.8/23.2	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.17	-0.61	3.64	0.99	8.6	-3.9	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	I611/Y658A	I26V/Y73A	Helix/Helix	1.8/57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.37	0.59	2.94	0.29	13.23	0.73	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L628/L652A	L43A/L67A	Helix/Helix	17.7/23.2	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.49	-1.29	0.34	-2.31	14.98	2.48	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L628/Y658A	L43A/Y73A	Helix/Helix	17.7/57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.89	-0.89	0.1	-2.55	16.54	4.04	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	Y650/Y658A	Y65A/Y73A	Helix/Helix	41.0/57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.55	-0.23	3.43	0.78	10.04	-2.46	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
CBP, KIX domain	Mus musculus	86.0	P45481	1sb0	A	Mainly Alpha	PF02172	1sb0A00 (1.10.246.20)	2.3.1.48	L652/Y658A	L67A/Y73A	Helix/Helix	23.2/57.7	20.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.44	-0.34	3.26	0.61	10.18	-2.32	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S	The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289	2017.0	28459531	Yes	yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I860A	I860A	Beta	1.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.37	-2.06	-8.2	1.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.6	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L863A	L863A	Coil	7.3	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.65	-2.34	-4.84	4.78	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.33	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3529	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	P865A	P865A	Coil	44.9	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.95	-0.74	-8.79	0.83	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.47	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	T867S	T867S	Coil	12.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.46	-1.23	-8.8	0.82	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.6	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3530	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	T867A	T867A	Coil	12.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.88	-0.81	-7.12	2.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.25	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	Y869F	Y869F	Beta	4.1	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.53	-2.22	-6.56	3.06	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.42	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3531	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	V871A	V871A	Beta	0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.87	-2.56	-7.44	2.18	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.54	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L873A	L873A	Beta	0.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.22	-1.47	-5.93	3.69	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.29	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3532	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	S875A	S875A	Beta	0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.47	-0.22	-9.91	-0.29	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	G878A	G878A	Coil	42.9	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.33	-0.36	-8.28	1.34	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.21	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3533	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	S882A	S882A	Coil	6.2	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.55	-0.14	-5.0	4.62	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.03	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	P884A	P884A	Coil	51.5	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.6	-0.09	-9.53	0.09	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3534	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	A885G	A885G	Beta	26.4	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.3	-0.39	-8.17	1.45	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.21	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	E887A	E887A	Beta	36.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.9	0.21	-12.13	-2.51	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.08	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3535	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	E887G	E887G	Beta	36.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.64	-0.05	-9.1	0.52	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.09	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	F889A	F889A	Beta	8.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.7	-0.99	-1.44	8.18	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.11	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3536	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	T891S	T891S	Coil	17.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.16	-0.53	-6.91	2.71	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.16	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	T891A	T891A	Coil	17.6	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.09	-0.6	-4.43	5.19	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.11	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3537	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L893A	L893A	N/A	N/A	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.7	0.01	-9.53	0.09	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I860A/V871A	I860A/V871A	Beta/Beta	1.8/0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-2.3	-3.99	-5.74	3.88	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.51	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3538	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	WT	WT	N/A	N/A	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.69	N/A	-9.62	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517	2000.0	10704314	Yes	yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L803A	L803A	Coil	37.2	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.55	-0.14	-6.2	3.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.04	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	P806A	P806A	Coil	5.1	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.53	-0.16	-5.16	4.46	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.04	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I809V	I809V	Beta	7.7	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.46	-0.23	-9.55	0.07	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3518	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I809A	I809A	Beta	7.7	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.2	-0.49	-5.28	4.34	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.1	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	V811A	V811A	Beta	21.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.17	-0.52	-7.85	1.77	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.23	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3519	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	A819G	A819G	Beta	2.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.02	-0.67	-5.56	4.06	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.14	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I821V	I821V	Beta	0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.07	-0.62	-9.86	-0.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3520	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I821A	I821A	Beta	0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.71	-2.4	-5.82	3.8	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.39	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	P826A	P826A	Coil	2.9	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	2.13	0.44	-6.26	3.36	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-0.1	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3521	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I830V	I830V	Coil	2.4	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.54	-0.15	-9.23	0.39	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I830A	I830A	Coil	2.4	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.39	-0.3	-7.59	2.03	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.13	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3522	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I833V	I833V	Beta	1.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.31	-0.38	-9.16	0.46	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I833A	I833A	Beta	1.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.66	-1.03	-5.12	4.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.19	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3523	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L835A	L835A	Beta	0.0	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.82	-2.51	-4.89	4.73	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.35	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	Y837F	Y837F	Beta	17.1	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.74	0.05	-8.83	0.79	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3524	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	Y837A	Y837A	Beta	17.1	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-2.04	-3.73	-6.23	3.39	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.53	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	P843A	P843A	Coil	82.4	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.81	-0.88	-9.73	-0.11	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3525	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	G844A	G844A	Coil	90.5	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	1.6	-0.09	-9.12	0.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I849A	I849A	Beta	21.9	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.76	-2.45	-8.38	1.24	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.67	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3526	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	L851A	L851A	Beta	4.9	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.43	-2.12	-6.69	2.93	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.42	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	Y858A	Y858A	Beta	30.2	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.82	-0.87	-8.16	1.46	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.38	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3527	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	Y858G	Y858G	Beta	30.2	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	-0.03	-1.72	-4.35	5.27	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.25	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Tenascin, TNfn3 domain	Homo sapiens	92.0	P24821	1ten	A	Mainly Beta	PF00041	1tenA00 (2.60.40.10)	N/A	I860V	I860V	Beta	1.8	25.0	5.0	Sodium Acetate	0.05	N/A	N/A	N/A	stopped-flow	alkaline unfolding (pH 12.4)	0.8	-0.89	-9.11	0.51	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.64	N/A	N/A	Hamill SJ, Steward A, Clarke J	The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3528	2000.0	10704314	Yes	Yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	WT	WT	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.0	N/A	1.06	N/A	13.97	N/A	N/A	N/A	N/A	N/A	-3.14	1.13	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	V244A	V4A	Helix	28.2	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.8	-0.2	2.56	1.5	9.97	-4.1	N/A	N/A	N/A	N/A	-3.1	1.21	N/A	N/A	0.16	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	E245A	E5A	Helix	78.4	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.91	-0.09	0.99	-0.07	13.92	-0.13	N/A	N/A	N/A	N/A	-2.76	1.05	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A245G	A5G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.62	-0.38	1.69	0.63	11.61	-2.34	N/A	N/A	N/A	N/A	-2.76	1.09	N/A	N/A	0.31	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	D246A	D6A	Helix	49.7	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.86	-0.14	1.22	0.16	13.25	-0.79	N/A	N/A	N/A	N/A	-2.85	1.09	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A246G	A6G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.55	-0.45	1.5	0.44	11.87	-1.3	N/A	N/A	N/A	N/A	-2.8	1.26	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	I247V	I7V	Helix	8.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.91	-0.09	1.84	0.78	11.92	-2.09	N/A	N/A	N/A	N/A	-3.14	1.05	N/A	N/A	0.14	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A249G	A9G	Helix	55.7	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.31	-0.69	2.89	1.83	8.05	-5.94	N/A	N/A	N/A	N/A	-2.89	0.79	N/A	N/A	0.29	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	K250A	K10A	Helix	67.3	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.44	0.44	0.41	-0.65	16.55	2.51	N/A	N/A	N/A	N/A	-2.68	0.88	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A250G	A10G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.55	-0.45	1.48	0.42	11.93	-4.64	N/A	N/A	N/A	N/A	-1.51	0.92	N/A	N/A	0.45	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A253G	A13G	Helix	49.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.4	-0.6	2.77	1.71	8.53	-5.44	N/A	N/A	N/A	N/A	-3.1	1.05	N/A	N/A	0.26	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	I255V	I15V	Helix	24.9	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.55	-0.45	1.92	0.86	10.9	-3.22	N/A	N/A	N/A	N/A	-2.55	0.84	N/A	N/A	0.38	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	L261A	L21A	Coil	11.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.17	0.17	4.7	3.64	5.81	-8.16	N/A	N/A	N/A	N/A	-2.89	1.09	N/A	N/A	-0.04	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A266G	A26G	Helix	65.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.55	-0.45	1.44	0.38	12.04	-2.05	N/A	N/A	N/A	N/A	-3.22	1.0	N/A	N/A	0.58	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	I269V	I29V	Helix	20.7	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.55	-0.45	1.03	-0.03	12.99	-0.96	N/A	N/A	N/A	N/A	-3.1	1.09	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	N270A	N30A	Helix	61.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.5	0.5	0.79	-0.27	15.78	1.8	N/A	N/A	N/A	N/A	-2.59	0.92	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A270G	A30G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.99	-1.01	1.06	0.0	11.59	-4.48	N/A	N/A	N/A	N/A	-2.93	0.96	N/A	N/A	0.84	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	V272A	V32A	Helix	2.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.21	-0.79	2.4	1.34	8.98	-5.15	N/A	N/A	N/A	N/A	-3.89	1.21	N/A	N/A	0.4	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	K273A	K33A	Helix	42.9	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.68	-0.32	2.07	1.01	10.86	-3.26	N/A	N/A	N/A	N/A	-3.05	0.79	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A273G	A33G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.3	-1.7	2.17	1.11	7.35	-3.1	N/A	N/A	N/A	N/A	-3.14	0.79	N/A	N/A	0.92	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A283G	A43G	Helix	15.1	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.21	-0.79	1.74	0.68	10.53	-3.51	N/A	N/A	N/A	N/A	-2.85	0.84	N/A	N/A	0.56	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	I284V	I44V	Helix	11.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.8	-0.2	2.59	1.53	9.92	-4.1	N/A	N/A	N/A	N/A	-3.93	0.75	N/A	N/A	0.13	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	L287A	L47A	Helix	0.0	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.8	-0.2	4.94	3.88	4.38	-9.67	N/A	N/A	N/A	N/A	-5.23	1.38	N/A	N/A	0.06	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	W288F	W48F	Helix	10.6	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.4	-0.6	4.38	3.32	4.74	-9.2	N/A	N/A	N/A	N/A	-4.18	0.59	N/A	N/A	0.15	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	W290F	W50F	Helix	24.2	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.89	-1.11	3.91	2.85	4.64	-9.37	N/A	N/A	N/A	N/A	-3.14	0.67	N/A	N/A	0.28	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	K292A	K52A	Helix	58.5	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	7.09	0.09	2.3	1.24	11.26	-2.8	N/A	N/A	N/A	N/A	-2.97	0.96	N/A	N/A	N/A	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	A292G	A52G	N/A	N/A	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	6.48	-0.52	3.47	2.41	7.09	-4.06	N/A	N/A	N/A	N/A	-3.18	0.75	N/A	N/A	0.36	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
Nucleophosmin, Cter-NPM1 domain	Homo sapiens	52.0	P06748	2vxd	A	Mainly Alpha	PF16276	2vxdA00 (1.10.10.2100)	N/A	L294A	L54A	Coil	59.8	10.0	7.0	Sodium Phosphate	0.05	N/A	N/A	1 mM DTT	stopped-flow	urea	5.99	-1.01	3.91	2.85	4.89	-9.0	N/A	N/A	N/A	N/A	-2.09	0.71	N/A	N/A	0.26	N/A	N/A	Scaloni F, Federici L, Brunori M, Gianni S	Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107	2010.0	20212148	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	WT	WT	N/A	N/A	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.7	N/A	1.3	N/A	15.23	N/A	N/A	N/A	N/A	N/A	-4.23	-0.64	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	W390F	W11F	Coil	18.9	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.61	-0.09	2.58	1.28	11.72	-3.51	N/A	N/A	N/A	N/A	-4.27	-0.59	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	T392A	T13A	Coil	56.3	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.9	0.2	3.3	2.0	10.88	-4.35	N/A	N/A	N/A	N/A	-4.64	-0.5	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	E394A	E15A	Helix	75.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.46	-0.24	1.19	-0.11	14.64	-0.59	N/A	N/A	N/A	N/A	-4.52	-0.82	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	E394G	E15G	Helix	75.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.19	-0.51	2.03	0.73	12.13	-3.1	N/A	N/A	N/A	N/A	-4.9	-0.8	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A396G	A17G	Helix	7.5	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.93	-0.77	2.39	1.09	10.88	-4.35	N/A	N/A	N/A	N/A	-4.18	-0.69	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q398A	Q19A	Helix	51.5	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.64	-0.06	1.06	-0.24	15.48	0.25	N/A	N/A	N/A	N/A	-4.13	-0.68	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q398G	Q19G	Helix	51.5	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.45	-1.25	1.92	0.62	10.46	-4.77	N/A	N/A	N/A	N/A	-4.16	-0.81	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A399G	A20G	Helix	3.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.11	-0.59	3.37	2.07	8.79	-6.44	N/A	N/A	N/A	N/A	-5.1	-0.88	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	L403A	L24A	Helix	0.0	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.74	-1.96	0.88	-0.42	11.3	-3.93	N/A	N/A	N/A	N/A	-4.81	-0.51	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	K405A	K26A	Helix	51.7	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.59	-0.11	1.12	-0.18	15.06	-0.17	N/A	N/A	N/A	N/A	-4.01	-0.69	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	K405G	K26G	Helix	51.7	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.51	-1.19	1.01	-0.29	12.97	-2.26	N/A	N/A	N/A	N/A	-4.52	-0.74	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	E406A	E27A	Helix	61.9	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.25	-0.45	2.31	1.01	11.72	-3.51	N/A	N/A	N/A	N/A	-4.18	-0.61	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	E406G	E27G	Helix	61.9	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.86	-1.84	2.38	1.08	7.95	-7.28	N/A	N/A	N/A	N/A	-4.27	-0.65	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	V409A	V30A	Coil	1.4	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.32	-3.38	3.22	1.92	2.51	-12.72	N/A	N/A	N/A	N/A	-4.39	-1.13	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	P410G	P31G	Coil	41.2	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.99	-1.71	1.63	0.33	10.04	-5.19	N/A	N/A	N/A	N/A	-4.18	-0.75	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	N412G	N33G	Coil	84.1	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.31	-0.39	1.63	0.33	13.39	-1.84	N/A	N/A	N/A	N/A	-4.23	-0.67	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	S414A	S35A	Coil	32.3	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.7	-2.0	1.28	-0.02	10.46	-4.77	N/A	N/A	N/A	N/A	-4.16	-0.74	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	W415F	W36F	Helix	16.3	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.63	-0.07	1.22	-0.08	15.06	-0.17	N/A	N/A	N/A	N/A	-4.31	-0.64	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q417A	Q38A	Helix	59.1	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.89	-0.81	1.36	0.06	12.97	-2.26	N/A	N/A	N/A	N/A	-4.23	-0.7	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q417G	Q38G	Helix	59.1	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.6	-2.1	1.48	0.18	9.62	-5.61	N/A	N/A	N/A	N/A	-4.69	-0.74	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A418G	A39G	Helix	0.0	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.91	-2.79	1.63	0.33	7.53	-7.7	N/A	N/A	N/A	N/A	-4.69	-0.84	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	M421A	M42A	Helix	47.3	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.46	-1.24	1.96	0.66	10.46	-4.77	N/A	N/A	N/A	N/A	-3.98	-0.72	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	I422V	I43V	Helix	0.0	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.86	-0.84	2.36	1.06	10.46	-4.77	N/A	N/A	N/A	N/A	-4.31	-0.76	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	I423A	I44A	Helix	40.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.54	0.84	2.16	0.86	15.06	-0.17	N/A	N/A	N/A	N/A	-4.39	-0.64	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	I423G	I44G	Helix	40.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.73	1.03	3.3	2.0	12.97	-2.26	N/A	N/A	N/A	N/A	-4.39	-0.77	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	D425N	D46N	Coil	17.8	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.01	-2.69	3.61	2.31	3.35	-11.88	N/A	N/A	N/A	N/A	-4.18	-0.67	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	P426G	P47G	Helix	29.4	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.54	-1.16	1.97	0.67	10.88	-4.35	N/A	N/A	N/A	N/A	-4.73	-0.65	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Y428F	Y49F	Helix	8.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.59	0.89	2.56	1.26	14.23	-1.0	N/A	N/A	N/A	N/A	-4.39	-0.63	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Y428A	Y49A	Helix	8.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.0	-0.7	5.01	3.71	3.77	-11.46	N/A	N/A	N/A	N/A	-4.18	-0.63	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	S429A	S50A	Helix	59.2	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.49	-0.21	1.31	0.01	14.64	-0.59	N/A	N/A	N/A	N/A	-3.87	-0.67	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	S429G	S50G	Helix	59.2	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.93	0.23	1.06	-0.24	16.32	1.09	N/A	N/A	N/A	N/A	-4.44	-0.72	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A430G	A51G	Helix	5.7	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.2	-0.5	3.26	1.96	9.2	-6.03	N/A	N/A	N/A	N/A	-3.9	-0.79	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	L431A	L52A	Coil	0.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	T-jump	heat	6.02	-1.68	5.94	4.64	3.14	-12.09	N/A	N/A	N/A	N/A	-4.52	-0.63	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A432G	A53G	Coil	94.3	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.32	0.62	2.7	1.4	13.39	-1.84	N/A	N/A	N/A	N/A	-4.02	-0.8	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	S435A	S56A	Helix	43.1	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.24	-0.46	1.87	0.57	12.55	-2.68	N/A	N/A	N/A	N/A	-3.92	-0.54	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	S435G	S56G	Helix	43.1	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.52	0.82	3.09	1.79	12.97	-2.26	N/A	N/A	N/A	N/A	-4.85	-0.37	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q439A	Q60A	Helix	63.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.41	0.71	1.03	-0.27	17.15	1.92	N/A	N/A	N/A	N/A	-4.27	-0.65	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Q439G	Q60G	Helix	63.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.99	-0.71	1.95	0.65	11.72	-3.51	N/A	N/A	N/A	N/A	-4.11	-0.74	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A440G	A61G	Helix	0.0	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.67	-2.03	3.26	1.96	5.86	-9.37	N/A	N/A	N/A	N/A	-3.73	-0.79	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	A443G	A64G	Helix	30.2	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	6.36	-1.34	2.41	1.11	9.2	-6.03	N/A	N/A	N/A	N/A	-3.65	-0.79	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	Y444F	Y65F	Helix	3.6	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.07	-0.63	2.21	0.91	11.3	-3.93	N/A	N/A	N/A	N/A	-3.76	-0.73	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	V446A	V67A	Helix	70.4	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	8.34	0.64	1.06	-0.24	17.15	1.92	N/A	N/A	N/A	N/A	-4.18	-0.62	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
FF domain from HYPA/FBP11	Homo sapiens	70.0	O75400	1uzc	A	Mainly Alpha	PF01846	1uzcA00 (1.10.10.440)	N/A	V446G	V67G	Helix	70.4	10.0	5.7	Na-Acetate	0.05	N/A	N/A	N/A	stopped-flow	urea	7.77	0.07	1.46	0.16	15.06	-0.17	N/A	N/A	N/A	N/A	-4.09	-0.57	N/A	N/A	N/A	N/A	N/A	Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR	The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067	2005.0	15935381	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	WT	WT	N/A	N/A	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.77	N/A	-1.97	N/A	11.74	N/A	N/A	N/A	N/A	N/A	-2.47	0.59	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	T159S	T1S	Coil	82.4	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.56	-0.21	-1.56	0.41	10.21	-1.53	N/A	N/A	N/A	N/A	-2.47	0.5	N/A	N/A	0.28	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	Y160A	Y2A	Beta	51.8	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.15	-0.62	-0.37	1.6	6.24	-5.5	N/A	N/A	N/A	N/A	-2.47	0.29	N/A	N/A	0.26	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	V161A	V3A	Beta	0.7	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	1.53	-1.24	-1.11	0.86	6.54	-5.2	N/A	N/A	N/A	N/A	-3.14	0.33	N/A	N/A	0.58	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	A163G	A5G	Beta	4.7	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	0.53	-2.24	-1.02	0.95	3.84	-7.9	N/A	N/A	N/A	N/A	-2.64	0.5	N/A	N/A	0.7	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	L164A	L6A	Coil	47.0	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.08	-0.69	-0.4	1.57	6.14	-5.6	N/A	N/A	N/A	N/A	-2.85	0.54	N/A	N/A	0.3	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	F165A	F7A	Coil	58.4	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	1.86	-0.91	-1.56	0.41	8.47	-3.27	N/A	N/A	N/A	N/A	-2.76	0.46	N/A	N/A	0.68	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	F177A	F19A	Beta	6.1	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	0.96	-1.81	0.21	2.18	1.86	-9.88	N/A	N/A	N/A	N/A	-2.38	0.29	N/A	N/A	0.45	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	F182A	F24A	Beta	54.8	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	1.31	-1.46	-0.36	1.61	4.14	-7.6	N/A	N/A	N/A	N/A	-2.93	0.5	N/A	N/A	0.47	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	I183V	I25V	Beta	0.0	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	1.81	-0.96	-0.45	1.52	5.6	-6.14	N/A	N/A	N/A	N/A	-2.93	0.33	N/A	N/A	0.38	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	H184A	H26A	Beta	41.8	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	3.5	0.73	-1.47	0.5	12.31	0.57	N/A	N/A	N/A	N/A	-2.59	0.63	N/A	N/A	N/A	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	S189A	S31A	Coil	76.9	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.4	-0.37	-0.87	1.1	8.1	-3.64	N/A	N/A	N/A	N/A	-2.8	0.33	N/A	N/A	0.24	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	A197G	A39G	Beta	25.5	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.77	0.0	-0.08	1.89	7.06	-4.68	N/A	N/A	N/A	N/A	-2.97	0.25	N/A	N/A	-0.03	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	H199A	H41A	Coil	66.3	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.56	-0.21	-0.58	1.39	7.78	-3.96	N/A	N/A	N/A	N/A	-2.72	0.29	N/A	N/A	0.11	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	T202S	T44S	Beta	68.3	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.64	-0.13	-0.63	1.34	8.1	-3.64	N/A	N/A	N/A	N/A	-2.89	0.21	N/A	N/A	0.07	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	Y209A	Y51A	Helix	36.0	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.4	-0.37	-0.84	1.13	8.03	-3.71	N/A	N/A	N/A	N/A	-2.38	0.59	N/A	N/A	0.23	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	T211S	T53S	Beta	42.3	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.4	-0.37	-1.47	0.5	9.59	-2.15	N/A	N/A	N/A	N/A	-2.22	0.5	N/A	N/A	0.41	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	A212G	A54G	Beta	59.4	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.79	0.02	-0.48	1.49	8.1	-3.64	N/A	N/A	N/A	N/A	-2.3	0.5	N/A	N/A	-0.05	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
Grb2-SH3	Homo sapiens	56.0	P62993	2vwf	A	Mainly Beta	PF00018	2vwfA00 (2.30.30.40)	N/A	V213A	V55A	Coil	35.2	22.0	7.2	NaPi	0.05	N/A	N/A	N/A	stopped-flow	urea	2.72	-0.05	-0.8	1.17	8.72	-3.02	N/A	N/A	N/A	N/A	-1.97	0.96	N/A	N/A	-0.01	N/A	N/A	Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S	Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320	2018.0	30091591	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	WT(H125W)	WT(H142W)	N/A	N/A	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	11.17	N/A	6.65	N/A	10.67	N/A	N/A	N/A	N/A	N/A	-2.34	0.54	N/A	N/A	N/A	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L114A	L131A	Coil	6.7	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.34	-0.83	7.32	0.67	7.11	-3.56	N/A	N/A	N/A	N/A	-2.09	0.75	N/A	N/A	0.52	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	S115G	S132G	Coil	34.6	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.61	-0.56	6.49	-0.16	9.67	-1.0	N/A	N/A	N/A	N/A	-2.09	0.88	N/A	N/A	0.55	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	I118A	I135A	Helix	4.7	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.47	-0.7	8.37	1.72	4.94	-5.73	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	0.32	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L121A	L138A	Helix	25.6	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.18	-0.99	8.58	1.93	3.77	-6.9	N/A	N/A	N/A	N/A	-1.92	0.67	N/A	N/A	0.35	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	A123G	A140G	Helix	52.8	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.36	-0.81	7.14	0.49	7.57	-3.1	N/A	N/A	N/A	N/A	-1.76	0.96	N/A	N/A	0.49	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L127A	L144A	Coil	24.4	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.41	-0.76	8.29	1.64	5.02	-5.65	N/A	N/A	N/A	N/A	-1.72	0.75	N/A	N/A	0.31	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	A129G	A146G	Helix	18.9	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.75	-0.42	6.81	0.16	9.29	-1.38	N/A	N/A	N/A	N/A	-2.09	0.84	N/A	N/A	0.42	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	A131G	A148G	Helix	61.3	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.69	-0.48	6.36	-0.29	10.21	-0.46	N/A	N/A	N/A	N/A	-1.8	1.17	N/A	N/A	0.52	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	I132V	I149V	Coil	8.3	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.44	-0.73	6.48	-0.17	9.37	-1.3	N/A	N/A	N/A	N/A	-1.97	0.92	N/A	N/A	0.59	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	T135S	T152S	Coil	73.9	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.02	-1.15	8.63	1.98	3.26	-7.41	N/A	N/A	N/A	N/A	-2.01	0.63	N/A	N/A	0.39	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	V137G	V154G	Coil	80.3	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.24	-0.93	6.63	-0.02	8.49	-2.18	N/A	N/A	N/A	N/A	-1.97	1.0	N/A	N/A	0.54	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L141A	L158A	Coil	3.0	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	9.54	-1.63	8.73	2.08	1.92	-8.75	N/A	N/A	N/A	N/A	-2.01	0.96	N/A	N/A	0.4	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	T142S	T159S	Coil	23.2	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.25	-0.92	7.68	1.03	6.07	-4.6	N/A	N/A	N/A	N/A	-2.22	0.84	N/A	N/A	0.39	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	D145N	D162N	Helix	18.4	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	9.48	-1.69	8.09	1.44	3.26	-7.41	N/A	N/A	N/A	N/A	-2.01	0.71	N/A	N/A	0.48	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	V146A	V163A	Helix	2.1	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	9.9	-1.27	9.06	2.41	1.97	-8.7	N/A	N/A	N/A	N/A	-2.01	0.67	N/A	N/A	0.31	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	H149G	H166G	Helix	24.5	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.35	-0.82	8.71	2.06	3.89	-6.78	N/A	N/A	N/A	N/A	-1.88	0.88	N/A	N/A	0.25	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (H142W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L150A	L167A	Helix	28.7	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.42	-0.75	6.65	0.0	8.91	-1.76	N/A	N/A	N/A	N/A	-2.26	0.67	N/A	N/A	0.71	H125W	H142W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (L131W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	WT(L114W)	WT(L131W)	N/A	N/A	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	10.4	N/A	6.46	N/A	9.29	N/A	N/A	N/A	N/A	N/A	-2.18	0.71	N/A	N/A	N/A	L114W	L131W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
BBL domain (L131W)	Escherichia coli	45.0	P0AFG6	2wxc	A	Few Secondary Structures	PF02817	2wxcA00 (4.10.320.10)	2.3.1.61	L150A	L167A	Helix	28.7	10.0	7.0	KPi	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	9.6	-0.8	7.0	0.54	6.11	-3.18	N/A	N/A	N/A	N/A	-2.3	0.59	N/A	N/A	0.61	L114W	L131W	Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR	The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011	2009.0	19445954	Yes	yes	2023-06-11 01:00:00
RIBOSOMAL PROTEIN S6	Thermus thermophylus	101.0	P23370	1ris	A	Alpha Beta	PF01250	1risA00 (3.30.70.60)	N/A	WT	WT	N/A	N/A	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.83	N/A	-8.59	N/A	35.56	N/A	N/A	N/A	N/A	N/A	-5.06	2.47	3.47	N/A	N/A	N/A	N/A	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	WT(W95F)	WT(W95F)	N/A	N/A	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	7.32	N/A	-10.92	N/A	45.1	N/A	N/A	N/A	N/A	N/A	-6.32	2.26	3.86	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	Y10A	Y10A	Beta	9.9	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.38	-0.94	-5.55	5.37	29.5	-15.6	N/A	N/A	N/A	N/A	-7.2	1.97	2.36	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	T12A	T12A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	8.27	0.95	-8.68	2.24	41.88	-3.22	N/A	N/A	N/A	N/A	-6.28	2.05	3.71	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	F14A	F14A	Beta	0.5	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	4.58	-2.74	-7.97	2.95	31.0	-14.1	N/A	N/A	N/A	N/A	-6.99	2.09	2.51	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	V16A	V16A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.36	-0.96	-6.59	4.33	31.97	-13.13	N/A	N/A	N/A	N/A	-6.78	1.97	2.69	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	M25A	M25A	Helix	2.7	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.7	-0.62	-10.87	0.05	43.39	-1.71	N/A	N/A	N/A	N/A	-6.19	2.38	3.72	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	F29A	F29A	Helix	2.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.34	-1.98	-9.79	1.13	37.36	-7.74	N/A	N/A	N/A	N/A	-6.07	2.26	3.3	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	V32A	V32A	Helix	6.3	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.92	-1.4	-7.48	3.44	33.1	-12.0	N/A	N/A	N/A	N/A	-6.36	2.01	2.9	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	F35A	F35A	Helix	9.6	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.13	-1.19	-7.48	3.44	33.64	-11.46	N/A	N/A	N/A	N/A	-6.07	1.97	3.09	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	I36A	I36A	Helix	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.39	-1.93	-6.86	4.06	30.29	-14.81	N/A	N/A	N/A	N/A	-8.58	2.18	2.07	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	I43A	I43A	Beta	23.1	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.79	-0.53	-6.79	4.13	33.56	-11.54	N/A	N/A	N/A	N/A	-7.57	2.13	2.54	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	E46A	E46A	Beta	42.8	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.79	-0.53	-10.71	0.21	43.22	-1.88	N/A	N/A	N/A	N/A	-5.65	2.09	4.11	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	D48A	D48A	Beta	38.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	7.25	-0.07	-7.6	3.32	36.69	-8.41	N/A	N/A	N/A	N/A	-6.15	2.18	3.26	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	R65A	R65A	Beta	3.6	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	7.02	-0.3	-8.38	2.54	38.03	-7.07	N/A	N/A	N/A	N/A	-6.4	2.18	3.27	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	F67A	F67A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.07	-2.25	-7.83	3.09	31.84	-13.26	N/A	N/A	N/A	N/A	-6.99	2.43	2.49	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	V69A	V69A	Beta	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	5.07	-2.25	-9.47	1.45	35.86	-9.24	N/A	N/A	N/A	N/A	-6.99	2.09	2.91	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	F71A	F71A	Beta	0.5	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	4.74	-2.58	-7.69	3.23	30.71	-14.39	N/A	N/A	N/A	N/A	-7.74	2.05	2.3	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	L78A	L78A	Helix	0.0	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.86	-0.46	-7.12	3.8	34.56	N/A	N/A	N/A	N/A	N/A	-6.49	1.88	3.04	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	L82A	L82A	Helix	0.6	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	6.75	-0.57	-3.8	7.12	26.11	N/A	N/A	N/A	N/A	N/A	-6.53	1.84	2.3	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
30S ribosomal protein S6	Aquifex aeolicus	110.0	O66474	2j5a	A	Alpha Beta	PF01250	2j5aA00 (3.30.70.60)	N/A	L86A	L86A	Helix	1.2	25.0	6.3	MES	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	7.21	-0.11	-6.68	4.24	34.31	N/A	N/A	N/A	N/A	N/A	-6.53	2.05	2.94	N/A	N/A	W95F	W95F	Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M	Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016	2007.0	17056063	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	WT	WT	N/A	N/A	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.52	N/A	-2.73	N/A	16.99	N/A	N/A	N/A	N/A	N/A	-1.44	3.22	N/A	N/A	N/A	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	I6V	I6V	Coil	26.0	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.17	-0.35	-1.31	1.42	12.84	-4.15	N/A	N/A	N/A	N/A	-1.34	2.85	N/A	N/A	0.49	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	Y8A	Y8A	Beta	34.7	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.22	-0.3	-2.17	0.56	14.98	-2.01	N/A	N/A	N/A	N/A	-1.06	3.13	N/A	N/A	0.3	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	S9A	S9A	Coil	23.8	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.25	-0.27	-2.62	0.11	16.11	-0.88	N/A	N/A	N/A	N/A	-1.11	3.22	N/A	N/A	0.45	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	K11A	K11A	Coil	48.8	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.31	-0.21	-3.24	-0.51	17.7	0.71	N/A	N/A	N/A	N/A	-1.11	3.29	N/A	N/A	-0.23	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	F17L	F17L	Beta	26.4	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	2.13	-2.39	1.24	3.97	2.09	-14.9	N/A	N/A	N/A	N/A	N/A	2.28	N/A	N/A	0.48	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	E18A	E18A	Beta	14.4	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	2.07	-2.45	-2.53	0.2	10.75	-6.24	N/A	N/A	N/A	N/A	-1.65	3.11	N/A	N/A	1.1	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	V22A	V22A	Beta	0.0	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	3.66	-0.86	-0.48	2.25	9.71	-7.28	N/A	N/A	N/A	N/A	-1.62	2.64	N/A	N/A	0.32	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	L24A	L24A	Coil	0.6	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	3.59	-0.93	2.2	4.93	3.26	-13.73	N/A	N/A	N/A	N/A	N/A	2.16	N/A	N/A	N/A	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	V32A	V32A	Coil	2.8	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.21	-0.31	-0.53	2.2	11.09	-5.9	N/A	N/A	N/A	N/A	-1.15	2.75	N/A	N/A	0.15	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	S39A	S39A	Coil	45.4	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.12	-0.4	-0.54	2.19	10.92	-6.07	N/A	N/A	N/A	N/A	-1.29	2.71	N/A	N/A	0.27	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	L46A	L46A	Helix	22.0	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.09	-0.43	0.63	3.36	8.12	-8.87	N/A	N/A	N/A	N/A	-0.99	2.56	N/A	N/A	0.12	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	V55A	V55A	Beta	59.2	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.28	-0.24	-0.05	2.68	10.13	-6.86	N/A	N/A	N/A	N/A	-1.53	2.64	N/A	N/A	0.13	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	V55G	V55G	Beta	59.2	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.18	-0.34	1.52	4.25	6.23	-10.76	N/A	N/A	N/A	N/A	-1.46	2.21	N/A	N/A	0.09	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	M58L	M58L	Beta	53.7	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.15	-0.37	-1.24	1.49	12.64	-4.35	N/A	N/A	N/A	N/A	-1.2	2.85	N/A	N/A	0.41	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	P62A	P62A	Coil	75.0	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	5.4	0.88	-3.96	-1.23	21.92	4.93	N/A	N/A	N/A	N/A	-1.39	3.27	N/A	N/A	0.35	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	P64A	P64A	Coil	32.4	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.34	-0.18	-1.14	1.59	12.84	-4.15	N/A	N/A	N/A	N/A	-0.52	2.85	N/A	N/A	0.25	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	H65A	H65A	Coil	10.3	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	3.98	-0.54	-2.85	-0.12	15.98	-1.01	N/A	N/A	N/A	N/A	-1.39	3.29	N/A	N/A	0.51	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	L67A	L67A	Beta	2.4	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	3.81	-0.71	0.84	3.57	6.95	-10.04	N/A	N/A	N/A	N/A	-1.2	2.49	N/A	N/A	0.2	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	F69L	F69L	Beta	0.5	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.2	-0.32	1.41	4.14	6.57	-10.42	N/A	N/A	N/A	N/A	-1.88	2.38	N/A	N/A	N/A	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	R70A	R70A	Beta	29.8	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	2.91	-1.61	1.6	4.33	3.1	-13.89	N/A	N/A	N/A	N/A	-2.05	2.09	N/A	N/A	0.32	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
CKS1	Homo sapiens	79.0	P61024	1dkt	A	Alpha Beta	PF01111	1dktA00 (3.30.170.10)	N/A	R71A	R71A	Beta	22.6	10.0	7.5	Tris-HCl	0.05	N/A	N/A	1 mM EDTA	stopped-flow	urea	4.49	-0.03	-0.42	2.31	11.51	-5.48	N/A	N/A	N/A	N/A	-1.15	2.75	N/A	N/A	0.03	N/A	N/A	Seeliger MA, Breward SE, Itzhaki LS	Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0	2003.0	12473461	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	WT(L30W)	WT(L31W)	N/A	N/A	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.06	N/A	2.08	N/A	14.07	N/A	N/A	N/A	N/A	N/A	-1.76	0.88	-2.64	N/A	N/A	N/A	N/A	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	Y4A	Y5A	Coil	8.1	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	Y4F	Y5F	Coil	8.1	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.82	-0.24	5.35	3.27	5.81	-8.26	N/A	N/A	N/A	N/A	-1.67	0.92	-2.59	N/A	0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	S5A	S6A	Coil	61.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	S5G	S6G	Coil	61.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	L7A	L8A	Coil	37.2	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	6.21	-1.85	4.25	2.17	4.61	-9.46	N/A	N/A	N/A	N/A	-2.18	0.67	-2.85	N/A	0.5	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	T8S	T9S	Coil	27.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	T8A	T9A	Coil	27.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	6.4	-1.66	3.0	0.92	8.0	-6.07	N/A	N/A	N/A	N/A	-1.84	1.17	-3.01	N/A	0.6	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V9A	V10A	Helix	45.8	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V9G	V10G	Helix	45.8	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.58	-0.48	2.08	0.0	12.94	-1.13	N/A	N/A	N/A	N/A	-1.76	1.13	-2.89	N/A	0.3	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V9A	V10A/V11A	Helix/Helix	45.8/61.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V10A	V11A	Helix	61.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V10G	V11G	Helix	61.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	Q11A	Q12A	Helix	55.1	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.04	-0.02	4.61	2.53	8.07	-6.0	N/A	N/A	N/A	N/A	-2.97	0.08	-3.05	N/A	0.0	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	Q11G	Q12G	Helix	55.1	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	6.94	-1.12	4.25	2.17	6.33	-7.74	N/A	N/A	N/A	N/A	-2.13	0.75	-2.89	N/A	0.3	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	L12A	L13A	Helix	0.0	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.1	0.04	3.0	0.92	12.0	-2.07	N/A	N/A	N/A	N/A	-1.8	0.92	-2.76	N/A	0.0	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	K13A	K14A	Helix	44.9	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.18	0.12	3.69	1.61	10.56	-3.51	N/A	N/A	N/A	N/A	-1.8	0.92	-2.72	N/A	-0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	K13G	K14G	Helix	44.9	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.35	-0.71	5.14	3.06	5.2	-8.87	N/A	N/A	N/A	N/A	-2.26	0.5	-2.76	N/A	0.2	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	D14A	D15A	Helix	60.7	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	L15A	L16A	Helix	17.7	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	6.95	-1.11	4.38	2.3	6.05	-8.02	N/A	N/A	N/A	N/A	-2.72	0.33	-3.01	N/A	0.5	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	L16A	L17A	Helix	0.0	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.4	-0.66	8.01	5.93	-1.44	-15.51	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	-0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	K18A	K19A	Helix	76.1	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	R19A	R20A	Helix	33.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.22	-0.84	7.38	5.3	-0.38	-14.45	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	S22A	S23A	Coil	48.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.26	0.2	4.38	2.3	9.13	-4.94	N/A	N/A	N/A	N/A	-2.05	0.63	-2.68	N/A	-0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	V23A	V24A	Coil	26.8	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.01	-0.05	3.69	1.61	10.16	-3.91	N/A	N/A	N/A	N/A	-1.8	0.63	-2.43	N/A	0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	K27A	K28A	Helix	31.2	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	Q32A	Q33A	Helix	62.6	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	R33A	R34A	Helix	23.4	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	8.73	0.67	6.51	4.43	5.22	-8.85	N/A	N/A	N/A	N/A	-2.47	0.01	-2.47	N/A	-0.5	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	L34A	L35A	Helix	0.0	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	5.94	-2.12	7.26	5.18	-3.11	-17.18	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	I35A	I36A	Helix	24.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.67	-0.39	3.0	0.92	10.99	-3.08	N/A	N/A	N/A	N/A	-1.51	1.21	-2.72	N/A	0.2	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	I35V	I36V	Helix	24.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.78	-0.28	3.69	1.61	9.62	-4.45	N/A	N/A	N/A	N/A	-1.97	0.42	-2.38	N/A	0.3	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	D37A	D38A	Helix	12.9	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	D38A	D39A	Helix	39.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.82	-0.24	6.06	3.98	4.14	-9.93	N/A	N/A	N/A	N/A	-1.42	0.5	-1.97	N/A	0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	D38N	D39N	Helix	39.3	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	7.86	-0.2	6.49	4.41	3.22	-10.85	N/A	N/A	N/A	N/A	-1.84	0.46	-2.3	N/A	0.1	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	E39Q	E40Q	Helix	65.5	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
SAP (L31W) domain of THO1	Saccharomyces cerevisiae	49.0	P40040	2wqg	A	Mainly Alpha	PF02037	2wqgA00 (1.10.720.30)	N/A	E40G	E41G	Coil	54.6	10.0	6.0	MES	0.05	N/A	N/A	N/A	T-jump	thermal denaturation	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	L30W	L31W	Dodson CA, Arbely E	Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002	2015.0	26073259	Yes	yes	2023-06-11 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I98K/N102I/G106L	I98K/N102I/G106L	Helix/Helix/Coil	37.3/59.2/100.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.56	N/A	-0.25	N/A	11.92	-10.2	N/A	N/A	N/A	N/A	-3.51	3.64	N/A	N/A	0.11	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	V69G	V69G	Helix	11.3	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.48	-1.54	0.74	4.65	6.78	-15.34	N/A	N/A	N/A	N/A	-3.05	3.18	N/A	N/A	0.25	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I72A	I72A	Helix	2.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.12	-1.9	2.37	6.28	1.86	-20.25	N/A	N/A	N/A	N/A	-4.27	2.97	N/A	N/A	0.23	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	D73A	D73A	Helix	38.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.15	0.13	-1.11	2.8	15.51	-6.61	N/A	N/A	N/A	N/A	-3.47	2.8	N/A	N/A	-0.05	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L76A	L76A	Helix	25.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.07	-2.95	-0.89	3.02	7.33	-14.79	N/A	N/A	N/A	N/A	-4.1	3.01	N/A	N/A	0.5	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	V84A	V84A	Helix	14.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.43	-0.59	-0.92	2.99	13.24	-8.88	N/A	N/A	N/A	N/A	-3.43	2.89	N/A	N/A	0.11	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A87G	A87G	Helix	2.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.99	-1.03	0.53	4.44	8.58	-13.54	N/A	N/A	N/A	N/A	-5.06	2.26	N/A	N/A	0.19	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A90G	A90G	Helix	21.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.09	-0.93	-0.87	3.04	12.28	-9.84	N/A	N/A	N/A	N/A	-3.43	2.72	N/A	N/A	0.23	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A91G	A91G	Helix	0.9	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.46	-0.56	-1.66	2.25	15.17	-6.94	N/A	N/A	N/A	N/A	-4.14	3.05	N/A	N/A	0.2	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L94A	L94A	Helix	3.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.63	-0.39	-1.66	2.25	15.6	-6.52	N/A	N/A	N/A	N/A	-3.64	3.01	N/A	N/A	0.15	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I98A	I98A	Helix	37.3	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.36	-0.66	1.33	5.24	7.52	-14.6	N/A	N/A	N/A	N/A	-3.43	3.01	N/A	N/A	0.11	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	Y101A	Y101A	Helix	16.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.73	-0.29	-4.61	-0.7	23.12	1.0	N/A	N/A	N/A	N/A	-2.72	4.98	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	Y105A	Y105A	Coil	28.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.54	-0.48	-0.4	3.51	12.24	-9.88	N/A	N/A	N/A	N/A	-2.26	2.68	N/A	N/A	0.12	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I98V/N102A	I98V/N102A	Helix/Helix	37.3/59.2	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.87	N/A	-3.91	N/A	21.77	-0.35	N/A	N/A	N/A	N/A	-3.14	4.02	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I98L/N102D/G106R	I98L/N102D/G106R	Helix/Helix/Coil	37.3/59.2/100.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.79	N/A	-3.51	N/A	20.56	-1.56	N/A	N/A	N/A	N/A	-3.31	4.06	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I98V/N102G	I98V/N102G	Helix/Helix	37.3/59.2	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.54	N/A	-1.43	N/A	14.79	-7.33	N/A	N/A	N/A	N/A	-3.26	3.43	N/A	N/A	0.16	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	R34A	R34A	Helix	29.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.53	-0.49	-0.58	3.33	12.66	-9.45	N/A	N/A	N/A	N/A	-3.14	2.68	N/A	N/A	0.13	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	R34G	R34G	Helix	29.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.01	-1.01	0.61	4.52	8.43	-13.69	N/A	N/A	N/A	N/A	-4.18	2.68	N/A	N/A	0.18	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A36G	A36G	Helix	16.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.27	-0.75	-0.24	3.67	11.16	-10.96	N/A	N/A	N/A	N/A	-3.35	3.51	N/A	N/A	0.17	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A37G	A37G	Helix	2.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	2.98	-2.04	1.13	5.04	4.58	-17.54	N/A	N/A	N/A	N/A	-3.85	2.97	N/A	N/A	0.29	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L38G	L38G	Helix	59.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.42	-0.6	-2.04	1.87	16.0	-6.12	N/A	N/A	N/A	N/A	-2.68	2.55	N/A	N/A	0.24	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A40G	A40G	Helix	3.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.82	-0.2	-1.71	2.2	16.19	-5.93	N/A	N/A	N/A	N/A	-3.43	3.35	N/A	N/A	0.08	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L48A	L48A	Coil	28.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.6	-0.42	-0.92	2.99	13.66	-8.46	N/A	N/A	N/A	N/A	-3.47	2.72	N/A	N/A	0.07	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	K51G	K51G	Coil	47.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.08	0.06	-1.61	2.3	16.58	-5.54	N/A	N/A	N/A	N/A	-3.01	3.05	N/A	N/A	-0.03	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	M58A	M58A	Coil	58.5	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.32	-0.7	-0.97	2.94	13.09	-9.03	N/A	N/A	N/A	N/A	-2.85	3.01	N/A	N/A	0.14	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	F61A	F61A	Helix	7.1	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.72	-0.3	1.24	5.15	8.63	-13.49	N/A	N/A	N/A	N/A	-3.31	2.18	N/A	N/A	0.15	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	F65A	F65A	Helix	5.1	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.82	-1.2	0.59	4.5	8.01	-14.1	N/A	N/A	N/A	N/A	-3.26	2.8	N/A	N/A	0.37	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L68A	L68A	Helix	17.1	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	3.66	-1.36	-0.92	2.99	11.33	-10.78	N/A	N/A	N/A	N/A	-3.35	3.43	N/A	N/A	0.21	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	WT(M7W/R98I/N99R/H102N/R106G)	WT	N/A	N/A	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.02	N/A	-3.91	N/A	22.12	N/A	N/A	N/A	N/A	N/A	-3.35	3.68	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L3A	L3A	Helix	42.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.86	-0.16	-1.27	2.64	15.19	-6.92	N/A	N/A	N/A	N/A	-3.18	3.18	N/A	N/A	0.06	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	W7M	W7M	Helix	50.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.71	-0.31	-2.66	1.25	18.26	-3.85	N/A	N/A	N/A	N/A	-3.14	3.6	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L10A	L10A	Helix	24.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.81	-0.21	-0.87	3.04	14.07	-8.05	N/A	N/A	N/A	N/A	-2.72	3.6	N/A	N/A	0.06	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L14A	L14A	Helix	2.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.79	-0.23	-0.82	3.09	13.9	-8.22	N/A	N/A	N/A	N/A	-3.05	2.85	N/A	N/A	0.07	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	K15A	K15A	Helix	50.7	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.16	0.14	-3.51	0.4	21.46	-0.66	N/A	N/A	N/A	N/A	-3.43	3.6	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	I17A	I17A	Helix	1.2	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.01	-0.01	-1.66	2.25	16.52	-5.6	N/A	N/A	N/A	N/A	-3.47	2.34	N/A	N/A	0.01	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	E18A	E18A	Helix	36.6	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.14	0.12	-5.81	-1.9	27.12	5.0	N/A	N/A	N/A	N/A	-2.85	5.23	N/A	N/A	0.05	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A20G	A20G	Coil	0.0	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.75	-0.27	-0.84	3.07	13.86	-8.26	N/A	N/A	N/A	N/A	-2.8	3.18	N/A	N/A	0.08	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	A23G	A23G	Helix	26.4	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.99	-0.03	-2.12	1.79	17.62	-4.5	N/A	N/A	N/A	N/A	-3.68	3.43	N/A	N/A	0.01	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	K27A	K27A	Helix	48.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	5.2	0.18	-3.51	0.4	21.56	-0.55	N/A	N/A	N/A	N/A	-3.14	3.14	N/A	N/A	N/A	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	K27G	K27G	Helix	48.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.45	-0.57	-2.81	1.1	18.01	-4.11	N/A	N/A	N/A	N/A	-3.14	3.51	N/A	N/A	0.33	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	L30A	L30A	Helix	1.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.22	-0.8	0.18	4.09	10.0	-12.12	N/A	N/A	N/A	N/A	-5.1	2.22	N/A	N/A	0.17	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
Rd-apocyt b562 (de novo)	Escherichia coli	106.0	P0ABE7	1yyj	A	N/A	N/A	N/A	N/A	M33A	M33A	Helix	4.8	25.0	5.0	NaAcetate	0.05	N/A	N/A	N/A	stopped-flow	urea	4.2	-0.82	0.29	4.2	9.68	-12.43	N/A	N/A	N/A	N/A	-2.97	3.18	N/A	N/A	0.16	M7W/R98I/N99R/H102N/R106G	N/A	Chu R, Pei W, Takei J, Bai Y.	Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n	2002.0	12069590	2	N/A	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E258G	E48G	Helix	45.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.97	-0.51	5.54	2.32	13.47	-7.03	N/A	N/A	N/A	N/A	-5.61	0.5	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.099	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	A259G	A49G	Helix	0.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.39	-1.09	6.08	2.86	10.71	-9.79	N/A	N/A	N/A	N/A	-6.28	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.100	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	K261A	K51A	Helix	62.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.07	-0.41	2.21	-1.01	21.97	1.47	N/A	N/A	N/A	N/A	-4.23	1.34	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.101	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	K261G	K51G	Helix	62.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.77	-0.71	3.93	0.71	16.95	-3.55	N/A	N/A	N/A	N/A	-4.27	1.38	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.102	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L262A	L52A	Helix	34.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.84	-0.64	5.02	1.8	14.43	-6.07	N/A	N/A	N/A	N/A	-4.52	1.05	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.103	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L262G	L52G	Helix	34.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.74	-0.74	8.12	4.9	6.49	-14.01	N/A	N/A	N/A	N/A	-5.19	1.51	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.104	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	D264A	D54A	Helix	63.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.41	-0.07	2.67	-0.55	21.67	1.17	N/A	N/A	N/A	N/A	-4.6	1.26	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.105	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	D264G	D54G	Helix	63.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.37	-0.11	5.28	2.06	15.1	-5.4	N/A	N/A	N/A	N/A	-4.9	0.59	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.106	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	A265G	A55G	Helix	84.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.45	-0.03	5.09	1.87	15.77	-4.73	N/A	N/A	N/A	N/A	-5.02	0.88	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.107	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	WT(Y225W)	WT	N/A	N/A	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.48	N/A	3.22	N/A	20.5	N/A	N/A	N/A	N/A	N/A	-4.81	1.0	N/A	N/A	N/A	Y225W	WT	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q221A	Q11A	Helix	58.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.2	-0.28	2.59	-0.63	21.34	0.84	N/A	N/A	N/A	N/A	-4.52	1.46	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.043	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q221G	Q11G	Helix	58.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.77	-0.71	3.11	-0.11	19.0	-1.5	N/A	N/A	N/A	N/A	-4.35	1.67	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.044	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N222A	N12A	Helix	58.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.52	0.04	2.53	-0.69	22.3	1.8	N/A	N/A	N/A	N/A	-4.77	1.46	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.045	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N222G	N12G	Helix	58.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.05	-0.43	3.47	0.25	18.79	-1.71	N/A	N/A	N/A	N/A	-4.6	1.46	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.046	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	A223G	A13G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.74	-0.74	5.1	1.88	13.97	-6.53	N/A	N/A	N/A	N/A	-4.98	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.047	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	F224A	F14A	Helix	37.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.57	-0.91	3.29	0.07	18.03	-2.47	N/A	N/A	N/A	N/A	-4.98	0.84	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.048	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	F224G	F14G	Helix	37.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.2	-1.28	5.41	2.19	11.88	-8.62	N/A	N/A	N/A	N/A	-5.65	0.46	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.049	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E226A	E16A	Helix	39.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.66	-0.82	3.03	-0.19	18.91	-1.59	N/A	N/A	N/A	N/A	-3.97	1.13	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.050	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E226G	E16G	Helix	39.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.59	-0.89	4.16	0.94	15.94	-4.56	N/A	N/A	N/A	N/A	-4.9	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.051	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	I227V	I17V	Helix	0.6	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.13	-1.35	3.13	-0.09	13.18	-7.32	N/A	N/A	N/A	N/A	-4.6	1.13	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.052	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L228A	L18A	Helix	33.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.04	-1.44	2.46	-0.76	18.79	-1.71	N/A	N/A	N/A	N/A	-4.39	1.59	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.054	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L228G	L18G	Helix	33.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.78	-1.7	3.26	0.04	16.15	-4.35	N/A	N/A	N/A	N/A	-5.23	1.63	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.055	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L230A	L20A	Coil	4.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.18	-0.3	7.17	3.95	9.92	-10.58	N/A	N/A	N/A	N/A	-5.61	1.09	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.056	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L230G	L20G	Coil	4.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.04	-1.44	9.68	6.46	0.88	-19.62	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.057	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	P231G	P21G	Coil	58.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.98	-0.5	4.26	1.04	16.65	-3.85	N/A	N/A	N/A	N/A	-4.44	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.058	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N232G	N22G	Coil	32.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.7	0.22	6.28	3.06	13.43	-7.07	N/A	N/A	N/A	N/A	-4.81	1.34	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.059	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L233A	L23A	Coil	4.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.17	-2.31	9.17	5.95	0.0	-20.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.060	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E236A	E26A	Helix	78.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.51	0.03	3.15	-0.07	20.71	0.21	N/A	N/A	N/A	N/A	-4.9	1.05	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.062	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E236G	E26G	Helix	78.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.72	-1.76	2.19	-1.03	18.66	-1.84	N/A	N/A	N/A	N/A	-4.23	1.59	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.063	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q237A	Q27A	Helix	39.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.78	-0.7	5.47	2.25	13.18	-7.32	N/A	N/A	N/A	N/A	-4.69	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.064	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q237G	Q27G	Helix	39.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.48	-2.0	6.92	3.7	6.36	-14.14	N/A	N/A	N/A	N/A	-6.19	0.92	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.065	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	R238A	R28A	Helix	18.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.33	-1.15	4.25	1.03	15.06	-5.44	N/A	N/A	N/A	N/A	-4.31	0.79	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.066	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	R238G	R28G	Helix	18.5	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.77	-2.71	5.41	2.19	8.33	-12.17	N/A	N/A	N/A	N/A	-5.77	0.5	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.067	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N239A	N29A	Helix	52.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.57	0.09	2.56	-0.66	22.34	1.84	N/A	N/A	N/A	N/A	-4.56	1.38	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.068	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N239G	N29G	Helix	52.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.09	-1.39	2.39	-0.83	19.08	-1.42	N/A	N/A	N/A	N/A	-4.85	1.59	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.069	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	G240A	G30A	Helix	39.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	12.53	1.05	3.45	0.23	23.14	2.64	N/A	N/A	N/A	N/A	-4.39	1.13	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.070	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	G240S	G30S	Helix	39.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.9	0.42	3.27	0.05	22.18	1.68	N/A	N/A	N/A	N/A	-4.35	1.09	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.071	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	G240T	G30T	Helix	39.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.5	0.02	3.08	-0.14	21.25	0.75	N/A	N/A	N/A	N/A	-4.31	1.34	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.072	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	G240I	G30I	Helix	39.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	12.1	0.62	4.23	1.01	20.75	0.25	N/A	N/A	N/A	N/A	-4.56	0.92	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.073	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	G240V	G30V	Helix	39.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.69	0.21	3.19	-0.03	20.88	0.38	N/A	N/A	N/A	N/A	-4.48	1.46	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.074	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	F241A	F31A	Helix	7.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.12	-1.36	6.35	3.13	9.37	-11.13	N/A	N/A	N/A	N/A	-7.2	1.17	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.075	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	F241G	F31G	Helix	7.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	7.33	-4.15	6.89	3.67	1.09	-19.41	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.076	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	I242V	I32V	Helix	8.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.21	-1.27	3.91	0.69	15.61	-4.89	N/A	N/A	N/A	N/A	-4.56	1.34	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.077	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	I242A	I32A	Helix	8.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.1	-1.38	4.76	1.54	13.22	-7.28	N/A	N/A	N/A	N/A	-5.4	0.67	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.078	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	I242G	I32G	Helix	8.3	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	8.83	-2.65	4.89	1.67	9.75	-10.75	N/A	N/A	N/A	N/A	-6.57	1.0	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.079	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q243A	Q33A	Helix	59.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.95	-0.53	2.17	-1.05	21.76	1.26	N/A	N/A	N/A	N/A	-4.48	1.8	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.080	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	Q243G	Q33G	Helix	59.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.6	-1.88	2.04	-1.18	18.74	-1.76	N/A	N/A	N/A	N/A	-4.64	2.13	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.081	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	S244A	S34A	Helix	36.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.81	0.33	3.18	-0.04	21.42	0.92	N/A	N/A	N/A	N/A	-4.56	0.79	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.082	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	S244G	S34G	Helix	36.2	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.61	-0.87	3.68	0.46	17.15	-3.35	N/A	N/A	N/A	N/A	-4.94	0.79	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.083	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L245A	L35A	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.83	-1.65	5.29	2.07	11.25	-9.25	N/A	N/A	N/A	N/A	-5.31	0.79	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.084	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L245G	L35G	Helix	0.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.36	-2.12	5.75	2.53	8.95	-11.55	N/A	N/A	N/A	N/A	-7.49	1.21	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.085	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	P249G	P39G	Helix	25.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.41	-1.07	4.87	1.65	13.72	-6.78	N/A	N/A	N/A	N/A	-4.94	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.086	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	S250G	S40G	Helix	83.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.88	-0.6	4.01	0.79	17.03	-3.47	N/A	N/A	N/A	N/A	-4.81	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.087	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	S252A	S42A	Helix	10.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.84	0.36	3.11	-0.11	21.63	1.13	N/A	N/A	N/A	N/A	-4.56	0.92	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.088	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	S252G	S42G	Helix	10.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.95	-0.53	4.21	0.99	16.69	-3.81	N/A	N/A	N/A	N/A	-4.52	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.089	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	A253G	A43G	Helix	65.1	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.9	-0.58	4.08	0.86	16.95	-3.55	N/A	N/A	N/A	N/A	-4.85	0.75	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.090	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N254A	N44A	Helix	65.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.43	-1.05	1.35	-1.87	22.51	2.01	N/A	N/A	N/A	N/A	-3.72	1.72	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.091	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	N254G	N44G	Helix	65.0	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.65	-0.83	3.67	0.45	17.28	-3.22	N/A	N/A	N/A	N/A	-4.56	0.92	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.092	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L255A	L45A	Helix	7.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.07	-1.41	4.19	0.97	14.56	-5.94	N/A	N/A	N/A	N/A	-4.56	1.42	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.093	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L255G	L45G	Helix	7.9	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.71	-1.77	7.03	3.81	6.65	-13.85	N/A	N/A	N/A	N/A	-7.45	0.54	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.094	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L256A	L46A	Helix	26.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.75	-0.73	4.47	1.25	15.56	-4.94	N/A	N/A	N/A	N/A	-5.56	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.095	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	L256G	L46G	Helix	26.8	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	9.94	-1.54	6.41	3.19	8.74	-11.76	N/A	N/A	N/A	N/A	-7.45	0.71	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.096	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	A257G	A47G	Helix	38.7	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	10.24	-1.24	3.95	0.73	15.61	-4.89	N/A	N/A	N/A	N/A	-4.48	N/A	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.097	2007.0	17628591	2	yes	2023-06-04 01:00:00
BdpA (Y17W)	Staphylococcus aureus	62.0	P38507	1ss1	A	Mainly Alpha	PF02216	1ss1A00 (1.20.5.420)	N/A	E258A	E48A	Helix	45.4	25.0	5.5	Sodium Acetate	0.05	N/A	N/A	N/A	T-jump	thermal	11.08	-0.4	3.0	-0.22	20.0	-0.5	N/A	N/A	N/A	N/A	-4.44	1.17	N/A	N/A	N/A	Y225W	N/A	Sato, S., Fersht, A.R.	Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254–267. https://doi.org/10.1016/j.jmb.2007.06.098	2007.0	17628591	2	yes	2023-06-04 01:00:00
Cold shock protein CspB	Bacillus caldolyticus	66.0	P41016	1c9o	A	Mainly Beta	PF00313	1c9oA00 (2.40.50.140)	N/A	N/A	WT	N/A	N/A	25.0	7.0	Na cacodylate-HCI	0.1	N/A	N/A	N/A	stopped-flow	GdmCl	7.22	N/A	-0.45	N/A	19.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Perl D, Welker C, Schindler T, Schröder K, Marahiel MA, Jaenicke R, Schmid FX	Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229	1998.0	9501917	Yes	N/A	2023-06-09 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	WT	WT	N/A	N/A	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	12.13	N/A	4.28	N/A	3.26	N/A	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	I400A	I3A	Coil	28.4	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.99	3.99	6.02	6.02	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	I400V	I3V	Coil	28.4	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.32	4.32	4.04	4.04	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	T401A	T4A	Beta	57.0	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.32	4.32	4.52	4.52	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	T401S	T4S	Beta	57.0	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.38	4.38	4.01	4.01	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	Y402F	Y5F	Beta	8.6	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.56	4.56	6.36	6.36	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	R403A	R6A	Beta	58.9	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.09	4.09	4.06	4.06	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	V404A	V7A	Beta	4.9	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.64	3.64	5.86	5.86	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	R405A	R8A	Coil	63.7	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.83	3.83	3.89	3.89	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	S409A	S12A	Coil	50.8	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.13	2.13	4.61	4.61	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	L410A	L13A	Helix	26.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.04	3.04	5.6	5.6	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	S411A	S14A	Helix	63.8	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	5.01	5.01	3.18	3.18	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	S411G	S14G	Helix	63.8	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.76	3.76	3.04	3.04	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	S412A	S15A	Helix	49.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.34	4.34	4.57	4.57	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	S412G	S15G	Helix	49.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.09	3.09	3.22	3.22	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	I413V	I16V	Helix	3.6	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.33	3.33	4.47	4.47	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	A414G	A17G	Helix	3.8	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.03	2.03	5.01	5.01	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	K415A	K18A	Helix	84.9	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.47	4.47	3.26	3.26	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	K415G	K18G	Helix	84.9	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.94	2.94	3.69	3.69	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	R416A	R19A	Helix	87.5	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.32	4.32	2.4	2.4	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	H417A	H20A	Helix	30.4	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.32	4.32	5.35	5.35	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	G418A	G21A	Coil	70.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.56	2.56	3.53	3.53	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	V419A	V22A	Coil	10.6	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.94	2.94	4.79	4.79	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	I421A	I24A	Helix	10.1	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	2.89	2.89	3.58	3.58	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	I421V	I24V	Helix	10.1	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.14	4.14	2.77	2.77	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	K422A	K25A	Helix	70.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.79	4.79	2.94	2.94	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	K422G	K25G	Helix	70.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.08	4.08	3.22	3.22	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	D423A	D26A	Helix	22.7	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.56	3.56	3.93	3.93	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	V424A	V27A	Helix	0.7	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.14	3.14	6.25	6.25	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	M425A	M28A	Helix	58.5	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.5	3.5	4.06	4.06	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	R426A	R29A	Helix	76.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.22	4.22	3.53	3.53	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	R426G	R29G	Helix	76.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.04	4.04	4.51	4.51	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	T431S	T34S	Helix	29.6	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.5	4.5	4.36	4.36	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	L434A	L37A	Coil	23.8	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.53	3.53	5.48	5.48	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	D438A	D41A	Beta	30.7	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.53	4.53	5.08	5.08	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	L440M	L43M	Beta	4.3	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.87	3.87	4.94	4.94	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	T441A	T44A	Beta	28.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.53	3.53	4.44	4.44	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	T441S	T44S	Beta	28.2	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.66	3.66	4.43	4.43	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	L442M	L45M	Coil	0.0	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	3.85	3.85	4.14	4.14	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
LysM domain of Membrane-bound lytic murein transglycosylase D	Escherichia coli	48.0	P0AEZ7	1e0g	A	Alpha Beta	PF01476	1e0gA00 (3.10.350.10)	4.2.2.n1	F443L	F46L	Coil	47.7	11.0	7.0	MOPS	0.05	N/A	N/A	N/A	stopped-flow	GdmCl	N/A	N/A	N/A	N/A	N/A	N/A	4.01	4.01	3.97	3.97	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Nickson AA, Stoll KE, Clarke J	Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020	2008.0	18538343	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D127G	D127G	Helix	62.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.81	0.12	-1.8	1.09	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	S128A	S128A	Helix	32.3	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.61	-0.08	-3.55	-0.66	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	S128G	S128G	Helix	32.3	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.85	0.16	-2.54	0.35	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	I129A	I129A	Helix	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.76	0.07	1.46	4.35	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D131A	D131A	Helix	78.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.78	0.09	-4.36	-1.47	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D131G	D131G	Helix	78.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.83	0.14	-2.36	0.53	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R132A	R132A	Helix	65.7	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.69	0.0	-2.7	0.19	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R132G	R132G	Helix	65.7	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.76	0.07	-0.49	2.4	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	Y133A	Y133A	Coil	31.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.66	-0.03	1.36	4.25	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	T138A	T138A	Helix	44.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.22	0.53	-3.14	-0.25	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	T138G	T138G	Helix	44.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.56	-0.13	-2.44	0.45	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D139A	D139A	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.37	-0.32	-2.63	0.26	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D139G	D139G	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.77	-0.92	-1.87	1.02	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R140A	R140A	Helix	5.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.28	0.59	-3.47	-0.58	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V141A	V141A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.64	-1.05	-1.61	1.28	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R142A	R142A	Helix	72.6	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.47	-0.22	-1.56	1.33	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R142G	R142G	Helix	72.6	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.48	-1.21	-0.41	2.48	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D143A	D143A	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.53	-0.16	-2.86	0.03	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D143G	D143G	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.3	-1.39	0.58	3.47	N/A	7.11	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	S144A	S144A	Helix	2.3	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.74	1.05	-3.2	-0.31	N/A	8.79	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L145M	L145M	Helix	12.8	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.14	-0.55	0.84	3.73	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R146A	R146A	Helix	60.9	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.4	-0.29	-2.4	0.49	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R146G	R146G	Helix	60.9	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.0	-0.69	-0.47	2.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	W148F	W148F	Helix	4.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.01	0.32	3.45	6.34	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	N150A	N150A	Helix	66.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.83	0.14	-2.95	-0.06	N/A	8.37	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	N150G	N150G	Helix	66.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.47	-0.22	-2.14	0.75	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	H160A	H160A	Helix	8.7	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.38	0.69	-4.14	-1.25	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L161A	L161A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	1.39	-2.3	2.19	5.08	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V162A	V162A	Helix	3.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.77	-0.92	-0.31	2.58	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L165A	L165A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	1.95	-1.74	2.95	5.84	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R166A	R166A	Helix	48.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.09	-0.6	0.59	3.48	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R166G	R166G	Helix	48.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.56	-1.13	1.81	4.7	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	S167A	S167A	Helix	59.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.23	0.54	-4.1	-1.21	N/A	7.11	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	S167G	S167G	Helix	59.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.33	-0.36	-2.67	0.22	N/A	7.11	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	C168A	C168A	Coil	3.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.74	0.05	-2.26	0.63	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V173A	V173A	Helix	7.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.37	-0.32	-0.29	2.6	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D175A	D175A	Helix	46.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.64	-0.05	-2.36	0.53	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D175G	D175G	Helix	46.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.14	-0.55	-0.92	1.97	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L176A	L176A	Helix	40.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.22	-0.47	-2.0	0.89	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V177A	V177A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.18	-0.51	1.84	4.73	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	Q178A	Q178A	Helix	21.7	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.89	0.2	-2.5	0.39	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	Q178G	Q178G	Helix	21.7	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.3	-0.39	-1.14	1.75	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V180A	V180A	Helix	0.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.85	0.16	-2.93	-0.04	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	WT	WT	N/A	N/A	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.69	N/A	-2.89	N/A	N/A	5.86	N/A	0.76	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	C98A	C98A	Helix	45.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.87	0.18	-3.68	-0.79	N/A	7.53	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	C98G	C98G	Helix	45.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.26	-0.43	-2.35	0.54	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	F101A	F101A	Helix	26.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.3	-1.39	0.58	3.47	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	N102A	N102A	Helix	53.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	4.06	0.37	-2.91	-0.02	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	N102G	N102G	Helix	53.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.5	-0.19	-2.3	0.59	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	V103A	V103A	Helix	1.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.58	-0.11	-0.28	2.61	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	I104A	I104A	Helix	3.6	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.48	-1.21	0.56	3.45	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	W112A	W112A	Helix	0.9	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	2.3	-1.39	3.3	6.19	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R113A	R113A	Helix	21.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.95	0.26	-2.24	0.65	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R113G	R113G	Helix	21.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.64	-0.05	-0.42	2.47	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R114A	R114A	Helix	32.3	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.83	0.14	-2.17	0.72	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R114G	R114G	Helix	32.3	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.33	-0.36	0.05	2.94	N/A	6.69	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L115M	L115M	Helix	1.2	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.09	-0.6	-0.38	2.51	N/A	5.86	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R117A	R117A	Helix	64.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.85	0.16	-1.95	0.94	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	R117G	R117G	Helix	64.5	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.43	-0.26	-0.23	2.66	N/A	4.6	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	L119M	L119M	Helix	2.4	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.33	-0.36	1.41	4.3	N/A	5.44	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	I126A	I126A	Helix	3.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.58	-0.11	-0.86	2.03	N/A	5.02	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
FADD-DD Fas-associated death domain protein	Homo sapiens	100.0	Q13158	1e41	A	Mainly Alpha	PF00531	1e41A00 (1.10.533.10)	N/A	D127A	D127A	Helix	62.0	25.0	7.0	Phosphate	0.05	N/A	N/A	5 mM DTT	stopped-flow	Urea	N/A	N/A	N/A	N/A	N/A	N/A	3.89	0.2	-3.66	-0.77	N/A	6.28	N/A	N/A	N/A	N/A	N/A	Steward A, McDowell GS ,Clarke J	Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425–437. https://doi.org/10.1016/j.jmb.2009.04.004	2009.0	19362094	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	WT	WT	N/A	N/A	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.76	N/A	-0.11	N/A	17.02	N/A	N/A	N/A	N/A	N/A	-1.88	0.84	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	F5L	F5L	Beta	1.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.65	-0.11	1.32	1.43	13.21	-3.81	N/A	N/A	N/A	N/A	-2.05	0.92	N/A	N/A	0.06	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K7M	K7M	Coil	58.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.03	0.27	-0.12	-0.01	17.71	0.69	N/A	N/A	N/A	N/A	-1.8	0.96	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	D8N	D8N	Coil	69.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.44	-0.32	0.29	0.4	15.24	-1.78	N/A	N/A	N/A	N/A	-1.88	0.96	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	D8A	D8A	Coil	69.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.44	-0.32	1.38	1.49	12.54	-4.48	N/A	N/A	N/A	N/A	-1.92	1.05	N/A	N/A	0.18	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	V9A	V9A	Beta	9.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.34	-0.42	2.22	2.33	10.21	-6.81	N/A	N/A	N/A	N/A	-1.92	1.13	N/A	N/A	0.14	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K10M	K10M	Coil	100.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.72	-0.04	-0.4	-0.29	17.64	0.62	N/A	N/A	N/A	N/A	-1.8	0.92	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K10E	K10E	Coil	100.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.97	0.21	0.07	0.18	17.1	0.08	N/A	N/A	N/A	N/A	-1.92	0.75	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K12G	K12G	Coil	45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.06	0.3	0.02	0.13	17.44	0.42	N/A	N/A	N/A	N/A	-1.8	0.71	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K14M	K14M	Coil	64.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.82	0.06	0.12	0.23	16.6	-0.42	N/A	N/A	N/A	N/A	-1.8	0.96	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K14A	K14A	Coil	64.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.61	-0.15	0.76	0.87	14.49	-2.53	N/A	N/A	N/A	N/A	-1.84	0.92	N/A	N/A	0.12	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K14G	K14G	Coil	64.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.62	-0.14	1.6	1.71	12.44	-4.58	N/A	N/A	N/A	N/A	-1.88	1.05	N/A	N/A	0.07	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K15M	K15M	Coil	73.7	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.02	0.26	0.79	0.9	15.44	-1.58	N/A	N/A	N/A	N/A	-1.84	0.88	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	K15G	K15G	Coil	73.7	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.58	-0.18	2.42	2.53	10.31	-6.71	N/A	N/A	N/A	N/A	-2.01	0.92	N/A	N/A	0.06	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	E17Q	E17Q	Coil	40.2	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.34	-0.42	-0.2	-0.09	16.2	-0.82	N/A	N/A	N/A	N/A	-1.97	0.92	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	E17A	E17A	Coil	40.2	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.27	-0.49	1.85	1.96	10.95	-6.07	N/A	N/A	N/A	N/A	-2.13	N/A	N/A	N/A	0.2	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I18V	I18V	Beta	49.7	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.77	0.01	-0.11	0.0	17.05	0.03	N/A	N/A	N/A	N/A	-1.88	0.88	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I18A	I18A	Beta	49.7	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.25	-0.51	2.55	2.66	9.17	-7.85	N/A	N/A	N/A	N/A	-2.18	0.79	N/A	N/A	0.15	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A22G	A22G	Coil	58.5	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.62	-0.14	0.29	0.4	15.68	-1.34	N/A	N/A	N/A	N/A	-1.97	0.92	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	D23A	D23A	Helix	55.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.19	-0.57	-1.02	-0.91	17.86	0.84	N/A	N/A	N/A	N/A	-1.72	1.26	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	G24A	G24A	Helix	47.6	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.76	0.0	-0.6	-0.49	18.23	1.21	N/A	N/A	N/A	N/A	-3.64	2.38	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A26G	A26G	Helix	0.0	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.7	-0.06	2.55	2.66	10.28	-6.74	N/A	N/A	N/A	N/A	-2.26	0.96	N/A	N/A	0.02	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	F31A	F31A	Coil	29.4	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.0	-0.76	2.89	3.0	7.71	-9.31	N/A	N/A	N/A	N/A	-1.84	0.96	N/A	N/A	0.16	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	G34A	G34A	Coil	45.2	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.19	-0.57	0.66	0.77	13.7	-3.32	N/A	N/A	N/A	N/A	-3.97	2.13	N/A	N/A	0.4	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	L35A	L35A	Coil	16.5	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.34	-0.42	1.4	1.51	12.24	-4.78	N/A	N/A	N/A	N/A	-2.22	0.92	N/A	N/A	0.21	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A36G	A36G	Beta	1.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.33	-0.43	1.9	2.01	10.98	-6.04	N/A	N/A	N/A	N/A	-2.51	0.84	N/A	N/A	0.16	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I37V	I37V	Beta	28.4	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.78	0.02	-0.15	-0.04	17.17	0.15	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I37A	I37A	Beta	28.4	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.4	-0.36	1.24	1.35	12.78	-4.24	N/A	N/A	N/A	N/A	-2.13	0.71	N/A	N/A	0.17	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	E38A	E38A	Beta	51.5	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.62	-0.14	0.05	0.16	16.28	-0.74	N/A	N/A	N/A	N/A	-1.8	0.88	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A39G	A39G	Coil	14.2	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.38	-0.38	1.81	1.92	11.32	-5.7	N/A	N/A	N/A	N/A	-2.3	0.92	N/A	N/A	0.14	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	T40S	T40S	Coil	26.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.52	-0.24	0.62	0.73	14.62	-2.4	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	0.25	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A42G	A42G	Helix	62.3	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.59	-0.17	0.36	0.47	15.44	-1.58	N/A	N/A	N/A	N/A	-1.92	0.79	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	L44A	L44A	Helix	27.4	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.43	-0.33	2.18	2.29	10.53	-6.49	N/A	N/A	N/A	N/A	-2.13	0.54	N/A	N/A	0.11	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A46G	A46G	Helix	35.8	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.62	-0.14	0.97	1.08	14.0	-3.02	N/A	N/A	N/A	N/A	-1.97	0.79	N/A	N/A	0.15	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	L47A	L47A	Helix	17.7	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.48	-0.28	0.7	0.81	14.32	-2.7	N/A	N/A	N/A	N/A	-1.88	0.84	N/A	N/A	0.2	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A49G	A49G	Helix	77.4	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.71	-0.05	0.18	0.29	16.18	-0.84	N/A	N/A	N/A	N/A	-1.92	0.84	N/A	N/A	N/A	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	M1A/K12M	M1A/K12M	Coil/Coil	26.1/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.72	-0.04	0.72	0.83	14.87	-2.15	N/A	N/A	N/A	N/A	-1.92	0.54	N/A	N/A	0.21	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	V3A/K12M	V3A/K12M	Beta/Coil	0.0/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	5.56	-1.2	1.74	1.85	9.46	-7.56	N/A	N/A	N/A	N/A	-2.34	0.75	N/A	N/A	0.31	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I4A/K12M	I4A/K12M	Beta/Coil	3.0/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.51	-0.25	1.54	1.65	12.31	-4.71	N/A	N/A	N/A	N/A	-2.22	0.5	N/A	N/A	0.19	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	L6A/K12M	L6A/K12M	Coil/Coil	31.1/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.79	0.03	2.53	2.64	10.55	-6.47	N/A	N/A	N/A	N/A	-1.88	0.63	N/A	N/A	0.12	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	I18A/K12M	I18A/K12M	Beta/Coil	49.7/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.02	0.26	2.35	2.46	11.57	-5.45	N/A	N/A	N/A	N/A	-2.01	0.29	N/A	N/A	0.1	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	V21A/K12M	V21A/K12M	Coil/Coil	9.2/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	6.33	-0.43	1.67	1.78	11.55	-5.47	N/A	N/A	N/A	N/A	-2.3	0.71	N/A	N/A	0.25	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	L35A/K12M	L35A/K12M	Coil/Coil	16.5/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.14	0.38	0.73	0.84	15.88	-1.14	N/A	N/A	N/A	N/A	-2.01	0.63	N/A	N/A	0.11	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A36G/K12M	A36G/K12M	Beta/Coil	1.9/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.14	0.38	1.42	1.53	14.17	-2.85	N/A	N/A	N/A	N/A	-2.09	N/A	N/A	N/A	0.1	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
NTL9	Geobacillus stearothermophilus	56.0	P02417	2hbb	A	Alpha Beta	PF01281	2hbbA00 (3.40.5.10)	N/A	A39G/K12M	A39G/K12M	Coil/Coil	14.2/45.9	25.0	5.45	Sodium Acetate	0.02	N/A	N/A	N/A	stopped-flow	GuHCl	7.21	0.45	1.42	1.53	14.35	-2.67	N/A	N/A	N/A	N/A	-1.97	0.63	N/A	N/A	0.08	N/A	N/A	Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP	The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034	2017.0	28494951	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	N/A	WT(D17E/Y28K/E43W)	N/A	N/A	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow or T-Jump Fluorescence Sectroscopy	GndHCl	8.96	N/A	0.88	N/A	20.02	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	I803V	I17V	Helix	19.5	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.39	-0.57	1.63	0.75	16.75	-3.27	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.43	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	L806A	L20A	Helix	0.6	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.68	-0.28	4.58	3.7	10.16	-9.86	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.07	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	A809G	A23G	N/A	N/A	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	9.05	0.09	1.31	0.43	19.18	-0.84	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	I811V	I25V	Coil	10.1	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.68	-0.28	0.88	0.0	19.33	-0.69	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	Y815A	Y29A	Helix	41.0	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.41	-0.55	1.22	0.34	17.81	-2.21	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.61	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	I816V	I30V	Helix	10.7	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.24	-0.72	1.44	0.56	16.85	-3.17	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.56	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	L818A	L32A	Helix	34.1	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.58	-0.38	1.55	0.67	17.42	-2.6	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.37	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	A822G	A36G	Coil	30.2	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.1	-0.86	2.77	1.89	13.21	-6.81	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.31	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	T824S	T38S	Coil	64.1	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	9.01	0.05	1.34	0.46	19.0	-1.02	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	V825A	V39A	Coil	26.8	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.95	-0.01	3.81	2.93	12.73	-7.29	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.0	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	V828A	V42A	Helix	0.0	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.19	-0.77	5.35	4.47	7.04	-12.98	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.15	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	L831A	L45A	Helix	32.3	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.14	-0.82	2.03	1.15	15.14	-4.88	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.42	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	I835A	I49A	Helix	20.7	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.81	-0.15	1.95	1.07	17.0	-3.02	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.12	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(D27E/Y28K/E43W)	Finegoldia magna	50.0	Q51918	2fs1	A	Mainly Alpha	PF17573	2fs1A00 (1.10.8.40)	N/A	L836A	L50A	Helix	21.3	25.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	GndHCl	8.54	-0.42	3.04	2.16	13.63	-6.39	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.16	N/A	D17E/Y28K/E43W	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	N/A	WT(T51K/F52A)	N/A	N/A	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.81	N/A	1.34	N/A	16.03	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I803V	I17V	Helix	23.7	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.9	-0.91	0.88	-0.46	14.91	-1.12	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L806A	L20A	Helix	1.8	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.34	-0.47	4.91	3.57	6.02	-10.01	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.12	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A809G	A23G	Helix	26.4	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.0	-0.81	2.64	1.3	10.8	-5.23	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.37	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I811V	I25V	Coil	28.4	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.96	0.15	1.16	-0.18	16.85	0.82	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A812G	A26G	Coil	42.5	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.19	-0.62	1.39	0.05	14.37	-1.66	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.91	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	Y815A	Y29A	Helix	36.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.17	-1.64	2.48	1.14	9.14	-6.89	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.59	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I816V	I30V	Helix	11.8	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.02	-0.79	1.34	0.0	14.07	-1.96	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.98	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L818A	L32A	Helix	29.3	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.09	-0.72	2.4	1.06	11.62	-4.41	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.41	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A820G	A34G	Helix	37.7	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.9	-0.91	1.06	-0.28	14.47	-1.56	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.4	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A822G	A36G	Coil	6.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.0	-0.81	3.04	1.7	9.81	-6.22	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.32	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	T824S	T38S	Coil	58.5	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.74	-0.07	2.3	0.96	13.48	-2.55	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.07	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	V825A	V39A	Helix	17.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.94	0.13	3.3	1.96	11.5	-4.53	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.07	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	V828A	V42A	Helix	0.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.38	-0.43	4.78	3.44	6.44	-9.59	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.11	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	T830S	T44S	Helix	50.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	8.01	0.2	1.13	-0.21	17.05	1.02	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga77 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L831A	L45A	Helix	25.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.22	-0.59	2.71	1.37	11.17	-4.86	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.3	N/A	T51K/F52A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	WT	WT	N/A	N/A	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.31	N/A	1.86	N/A	13.5	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A798G	A12G	Helix	0.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	8.52	1.21	6.91	5.05	3.99	-9.51	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.32	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I803V	I17V	Helix	23.7	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.55	-0.76	2.04	0.18	11.17	-2.33	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.81	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L806A	L20A	Helix	1.8	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.51	-0.8	5.63	3.77	2.18	-11.32	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.18	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A809G	A23G	Helix	26.4	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.65	-0.66	3.61	1.75	7.53	-5.97	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.27	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I811V	I25V	Coil	28.4	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.31	0.0	2.03	0.17	13.08	-0.42	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A812G	A26G	Coil	42.5	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.63	-0.68	2.3	0.44	10.73	-2.77	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.61	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	Y815A	Y29A	Helix	36.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	5.35	-1.96	3.47	1.61	4.66	-8.84	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.55	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I816V	I30V	Helix	11.8	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.21	-1.1	2.24	0.38	9.84	-3.66	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.74	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A820G	A34G	Helix	37.7	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.02	-1.29	1.81	-0.05	10.43	-3.07	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	1.04	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	A822G	A36G	Coil	6.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	5.3	-2.01	3.74	1.88	3.87	-9.63	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.52	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	T824S	T38S	Coil	58.5	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.09	-0.22	2.77	0.91	10.7	-2.8	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.2	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	V825A	V39A	Helix	17.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.86	-0.45	3.66	1.8	7.93	-5.57	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.2	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	V828A	V42A	Helix	0.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	6.41	-0.9	5.56	3.7	2.11	-11.39	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.2	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	T830S	T44S	Helix	50.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.48	0.17	1.96	0.1	13.68	0.18	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L831A	L45A	Helix	25.6	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.57	0.26	4.14	2.28	8.5	-5.0	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.07	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	I835A	I49A	Helix	1.2	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.1	-0.21	3.93	2.07	7.85	-5.65	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.09	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	L836A	L50A	Helix	28.0	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	7.59	0.28	4.49	2.63	7.68	-5.82	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.12	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
PSD1(Ga88 mutant)	Finegoldia magna	50.0	N/A	2jws	A	N/A	N/A	N/A	N/A	T837S	T51S	Helix	73.9	10.0	7.2	Sodium Phosphate	0.05	N/A	N/A	N/A	stopped-flow, or T-Jump Fluorescence Sectroscopy	urea	8.02	0.71	1.46	-0.4	16.25	2.75	N/A	N/A	N/A	N/A	N/A	N/A	N/A	N/A	0.64	N/A	N/A	Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.	Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109	2012.0	22652570	2	yes	2023-06-11 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y449F	Y20F	Beta	10.4	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.99	-0.06	6.98	1.15	7.03	-2.85	N/A	N/A	N/A	N/A	-2.89	1.47	N/A	N/A	0.05	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.076	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y450A	Y21A	Beta	26.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.2	-0.85	8.01	2.18	2.8	-7.11	N/A	N/A	N/A	N/A	-4.6	2.13	N/A	N/A	0.28	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.077	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	N452A	N23A	Coil	27.4	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.26	0.21	6.13	0.3	9.67	-0.29	N/A	N/A	N/A	N/A	-2.72	1.72	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.079	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	R453A	R24A	Coil	73.8	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.64	-0.41	6.82	0.99	6.61	-3.26	N/A	N/A	N/A	N/A	-2.47	1.23	N/A	N/A	0.29	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.080	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T454A	T25A	Coil	54.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	8.32	-1.73	8.59	2.76	N/A	-10.5	N/A	N/A	N/A	N/A	-5.56	2.05	N/A	N/A	0.39	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.081	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T454S	T25S	Coil	54.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.54	-0.51	7.24	1.41	5.4	-4.52	N/A	N/A	N/A	N/A	-3.05	2.05	N/A	N/A	0.27	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.082	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	W459A	W30A	Coil	64.8	25.0	7.0	N/A	N/A	N/A	N/A	N/A	continuous-flow	urea	10.62	N/A	8.56	N/A	5.05	N/A	N/A	N/A	N/A	N/A	-0.8	0.28	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proc. Natl. Acad. Sci. U.S.A. 98, 13002–13007. https://doi.org/10.1073/pnas.221467198	2001.0	11687613	N/A	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	WT	WT	N/A	N/A	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.05	N/A	5.83	N/A	9.92	N/A	N/A	N/A	N/A	N/A	-2.43	1.96	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.050	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T432A	T3A	Coil	62.7	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.95	-0.1	5.89	0.06	9.54	-0.38	N/A	N/A	N/A	N/A	-2.51	1.96	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.051	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	A433G	A4G	Coil	63.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.38	0.33	6.45	0.62	9.2	-0.67	N/A	N/A	N/A	N/A	-3.05	1.47	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.052	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	V434A	V5A	Coil	61.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.36	0.31	6.15	0.32	9.83	-0.04	N/A	N/A	N/A	N/A	-2.89	1.64	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.053	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	V434G	V5G	Coil	61.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.28	0.23	6.48	0.65	8.91	-1.0	N/A	N/A	N/A	N/A	-2.8	1.39	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.054	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	S435A	S6A	Coil	59.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.68	-0.37	5.86	0.03	8.95	-0.92	N/A	N/A	N/A	N/A	-2.3	2.37	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.055	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	E436A	E7A	Coil	48.5	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.43	-0.62	6.13	0.3	7.74	-2.18	N/A	N/A	N/A	N/A	-2.34	1.64	N/A	N/A	0.67	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.056	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	W437F	W8F	Coil	15.9	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.35	-0.7	8.08	2.25	2.97	-6.9	N/A	N/A	N/A	N/A	-3.05	3.19	N/A	N/A	0.24	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.057	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T438A	T9A	Beta	33.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.2	0.15	7.65	1.82	5.98	-3.89	N/A	N/A	N/A	N/A	-3.18	1.23	N/A	N/A	-0.09	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.058	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T438G	T9G	Beta	33.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.22	-0.83	5.89	0.06	7.82	-2.09	N/A	N/A	N/A	N/A	-3.35	1.88	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.059	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T438S	T9S	Beta	33.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.59	-0.46	5.44	-0.39	9.71	-0.17	N/A	N/A	N/A	N/A	-2.3	2.37	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.060	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	E439A	E10A	Beta	55.7	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.76	0.71	6.48	0.65	10.04	0.63	N/A	N/A	N/A	N/A	-2.93	1.64	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.061	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y440A	Y11A	Beta	53.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.44	-0.61	6.35	0.52	7.28	-2.64	N/A	N/A	N/A	N/A	-2.22	2.21	N/A	N/A	0.55	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.062	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y440F	Y11F	Beta	53.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.76	-0.29	6.15	0.32	8.45	-1.42	N/A	N/A	N/A	N/A	-2.55	1.8	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.063	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T442A	T13A	Coil	26.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.1	0.05	7.32	1.49	6.53	-3.39	N/A	N/A	N/A	N/A	-2.97	1.47	N/A	N/A	-0.03	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.064	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T442G	T13G	Coil	26.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.39	0.34	7.21	1.38	7.45	-2.43	N/A	N/A	N/A	N/A	-2.51	1.8	N/A	N/A	-0.32	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.065	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T442S	T13S	Coil	26.1	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.01	-0.04	6.19	0.36	8.95	-0.96	N/A	N/A	N/A	N/A	-2.59	2.21	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.066	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	A443G	A14G	Coil	100.0	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.44	-0.61	6.11	0.28	7.78	-2.09	N/A	N/A	N/A	N/A	-3.43	1.64	N/A	N/A	0.69	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.067	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	D444A	D15A	Coil	95.7	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.44	-0.61	5.97	0.14	8.12	-1.76	N/A	N/A	N/A	N/A	-3.01	1.8	N/A	N/A	0.82	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.068	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	D444G	D15G	Coil	95.7	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.52	-0.53	5.99	0.16	8.24	-1.63	N/A	N/A	N/A	N/A	-2.59	2.05	N/A	N/A	0.77	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.069	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	L465V	L36V	Coil	14.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.17	0.12	6.91	1.08	7.66	-2.22	N/A	N/A	N/A	N/A	-2.97	1.31	N/A	N/A	-0.13	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.098	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	L455A	L26A	Coil	73.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.98	-0.07	6.75	0.92	7.53	-2.34	N/A	N/A	N/A	N/A	-2.55	0.9	N/A	N/A	0.08	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.083	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	L455G	L26G	Coil	73.2	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	11.09	1.04	4.55	-1.28	15.31	5.4	N/A	N/A	N/A	N/A	-1.8	1.96	N/A	N/A	0.45	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.084	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	E456A	E27A	Beta	61.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.83	-0.22	7.43	1.6	5.65	-4.27	N/A	N/A	N/A	N/A	-2.38	1.88	N/A	N/A	0.12	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.085	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	S457A	S28A	Beta	50.8	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.53	0.48	6.29	0.46	9.92	0.04	N/A	N/A	N/A	N/A	-2.89	2.05	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.086	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	S457G	S28G	Beta	50.8	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.15	0.1	6.25	0.42	9.12	-0.79	N/A	N/A	N/A	N/A	-2.76	2.54	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.087	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T458A	T29A	Beta	30.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.57	-0.48	5.94	0.11	8.54	-1.38	N/A	N/A	N/A	N/A	-2.89	1.8	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.088	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T458G	T29G	Beta	30.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.75	-0.3	8.9	3.07	1.97	-7.91	N/A	N/A	N/A	N/A	-3.64	1.96	N/A	N/A	0.09	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.089	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T458S	T29S	Beta	30.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.16	0.11	6.68	0.85	8.12	-1.76	N/A	N/A	N/A	N/A	-2.68	1.64	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.090	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	W459A	W30A	Coil	64.8	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.8	-0.25	6.94	1.11	6.69	-3.18	N/A	N/A	N/A	N/A	-2.43	1.88	N/A	N/A	0.19	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.091	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	E460T	E31T	Coil	77.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.21	0.16	6.13	0.3	9.54	-0.33	N/A	N/A	N/A	N/A	-2.72	1.72	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.093	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	K461R	K32R	Coil	28.3	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.35	0.3	6.31	0.48	9.5	-0.42	N/A	N/A	N/A	N/A	-3.01	1.88	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.094	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	E464A	E35A	Coil	21.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.07	0.02	6.35	0.52	8.79	-1.13	N/A	N/A	N/A	N/A	-2.76	1.31	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.096	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	L465A	L36A	Coil	14.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.54	0.49	7.93	2.1	6.11	-3.81	N/A	N/A	N/A	N/A	-3.51	1.15	N/A	N/A	-0.3	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.097	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	G445A	G16A	Coil	66.7	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	7.28	-2.77	5.44	-0.39	5.31	-5.56	N/A	N/A	N/A	N/A	-4.81	2.37	N/A	N/A	1.17	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.070	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	K446A	K17A	Coil	56.6	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.62	-0.43	6.02	0.19	8.45	-1.46	N/A	N/A	N/A	N/A	-2.55	1.96	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.071	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T447A	T18A	Beta	28.9	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	9.15	-0.9	5.91	0.08	7.61	-2.26	N/A	N/A	N/A	N/A	-3.26	2.13	N/A	N/A	0.93	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.072	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	T447G	T18G	Beta	28.9	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	8.29	-1.76	6.46	0.63	4.31	-4.77	N/A	N/A	N/A	N/A	-4.6	3.11	N/A	N/A	0.73	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.073	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y448A	Y19A	Beta	23.4	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.28	0.23	7.42	1.59	7.11	-2.8	N/A	N/A	N/A	N/A	-3.26	2.13	N/A	N/A	0.11	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.074	2006.0	16784750	2	yes	2023-06-04 01:00:00
FBP28	Mus musculus	37.0	Q8CGF7	1e0l	A	N/A	PF00397	N/A	N/A	Y448F	Y19F	Beta	23.4	10.0	6.5	MOPS	0.02	N/A	N/A	N/A	T-jump	GuHCl	10.12	0.07	5.77	-0.06	10.21	0.29	N/A	N/A	N/A	N/A	-2.76	2.62	N/A	N/A	N/A	N/A	N/A	Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.	Petrovich, M., Jonsson, A.L., Ferguson, N., Daggett, V., Fersht, A.R., 2006. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. J. Mol. Biol. 360, 865–881. https://doi.org/10.1016/j.jmb.2006.05.075	2006.0	16784750	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	I113V	I110V	Beta	0.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.09	-0.46	0.75	-0.32	-4.85	2.09	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14929	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	V114A	V111A	Coil	66.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.6	-0.95	1.33	0.26	-5.31	2.47	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14930	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	N115A	N112A	Coil	83.4	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.64	0.09	1.5	0.43	-4.69	1.97	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14931	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	N116A	N113A	Coil	45.9	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.91	0.36	1.3	0.23	-3.93	2.47	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14932	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	G119A	G116A	Coil	41.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.99	-0.56	1.02	-0.05	-3.85	2.3	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14933	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	W121A	W118A	Beta	10.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.03	-0.52	2.83	1.76	-6.78	1.88	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14934	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	W122A	W119A	Beta	13.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.24	-0.31	2.97	1.9	-4.85	1.46	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14935	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	W122I	W119I	Beta	13.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.45	0.9	3.3	2.23	-4.6	2.59	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14936	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L123A	L120A	Beta	65.9	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.1	-1.45	2.52	1.45	-7.87	1.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14937	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	A124G	A121G	Beta	3.8	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.71	-1.84	0.86	-0.21	-7.11	1.63	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14938	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	H125A	H122A	Beta	42.4	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.47	-0.08	2.0	0.93	-4.14	2.43	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14939	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S126A	S123A	Beta	0.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.23	-2.32	1.29	0.22	-6.28	1.84	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14940	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L127A	L124A	Coil	67.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.82	-0.73	1.38	0.31	-5.02	2.13	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14941	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S128A	S125A	Coil	58.5	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.98	-0.57	0.07	-1.0	-5.02	2.55	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14942	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	T129A	T126A	Coil	52.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	0.99	-2.56	1.59	0.52	-7.7	1.97	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14943	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	G130A	G127A	Coil	48.8	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.39	-2.16	1.02	-0.05	-6.32	1.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14944	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Q131A	Q128A	Coil	63.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.29	-0.26	1.41	0.34	-4.31	2.05	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14945	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	T132A	T129A	Beta	68.3	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.33	-1.22	1.65	0.58	-5.77	2.34	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14946	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	G133A	G130A	Beta	7.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.79	0.24	4.59	3.52	-6.69	1.51	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14947	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Y134A	Y131A	Beta	29.3	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.1	-1.45	2.34	1.27	-6.86	1.63	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14948	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	I135A	I132A	Beta	0.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.34	-2.21	2.02	0.95	-6.86	1.92	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14949	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	P136A	P133A	Beta	0.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.98	-0.57	2.89	1.82	-5.69	1.88	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14950	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S137A	S134A	Helix	16.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	4.06	0.51	1.14	0.07	-4.14	2.43	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14951	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	N138A	N135A	Helix	38.9	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.55	0.0	1.28	0.21	-3.64	2.43	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14952	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Y139A	Y136A	Helix	3.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.48	-0.07	0.65	-0.42	-4.44	1.97	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14953	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	V140A	V137A	Beta	8.5	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.67	0.12	3.29	2.22	-4.81	1.84	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14954	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	A141G	A138G	Beta	2.8	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.59	0.04	1.97	0.9	-4.69	2.3	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14955	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	P142A	P139A	Beta	38.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.64	0.09	1.44	0.37	-4.35	2.01	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14956	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S143A	S140A	Coil	23.8	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.66	0.11	0.4	-0.67	-3.97	2.47	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14957	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	D144A	D141A	Coil	92.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.69	0.14	0.98	-0.09	-3.85	2.38	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14958	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Alpha Beta/Mainly Alpha/Mainly Beta	PF00018/PF07714/PF00017	1fmkA04 (1.10.510.10)/1fmkA01 (2.30.30.40)/1fmkA03 (3.30.200.20)/1fmkA02 (3.30.505.10)	2.7.10.2	WT	WT	N/A	N/A	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.55	N/A	1.07	N/A	-4.27	2.26	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14901	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	T88A	T85A	Beta	25.4	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.67	0.12	2.35	1.28	-4.23	1.92	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14902	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	F89A	F86A	Beta	2.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.41	-0.14	2.39	1.32	-4.44	2.13	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14903	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	F89I	F86I	Beta	2.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.67	0.12	4.06	2.99	-4.52	1.84	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14904	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	V90A	V87A	Beta	19.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.45	-0.1	3.79	2.72	-3.56	2.3	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14905	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	A91G	A88G	Beta	1.9	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.46	-0.09	2.73	1.66	-4.52	1.97	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14906	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L92A	L89A	Coil	20.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.62	0.07	3.87	2.8	-5.02	1.51	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14907	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Y93A	Y90A	Coil	26.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.59	0.04	1.68	0.61	-4.02	2.09	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14908	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	D94A	D91A	Coil	51.5	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.7	0.15	2.02	0.95	-4.1	1.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14909	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Y95A	Y92A	Beta	3.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.4	-0.15	4.94	3.87	N/A	1.63	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14910	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Y95F	Y92F	Beta	3.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.54	-0.01	1.37	0.3	-4.06	2.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14911	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S97A	S94A	Coil	35.4	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.8	0.25	0.47	-0.6	-4.02	2.3	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14912	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	R98A	R95A	Coil	12.9	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.64	0.09	1.22	0.15	-4.52	2.55	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14913	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	T99A	T96A	Coil	23.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.69	0.14	1.1	0.03	-4.23	2.18	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14914	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	T101A	T98A	Coil	61.3	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.6	0.05	1.14	0.07	-4.18	2.18	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14915	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	D102A	D99A	Beta	7.4	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.43	-0.12	1.91	0.84	-4.44	2.13	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14916	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L103A	L100A	Coil	3.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.76	-0.79	3.44	2.37	-6.07	1.88	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14917	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	S104A	S101A	Coil	47.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.49	-0.06	2.4	1.33	-3.97	2.43	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14918	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	F105A	F102A	Beta	5.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.17	-1.38	3.21	2.14	N/A	1.67	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14919	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	K106A	K103A	Coil	57.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.6	0.05	1.79	0.72	-4.23	2.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14920	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	K107A	K104A	Coil	51.2	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.73	0.18	1.45	0.38	-3.68	2.05	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14921	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	G108A	G105A	Coil	54.8	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	2.3	-1.25	2.74	1.67	-6.44	1.8	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14922	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	E109A	E106A	Coil	4.1	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.5	-2.05	2.34	1.27	-4.56	2.72	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14923	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	R110A	R107A	Beta	62.5	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.43	-0.12	1.45	0.38	-4.18	2.38	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14924	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L111A	L108A	Beta	0.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.4	-2.15	2.61	1.54	N/A	N/A	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14925	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	L111V	L108V	Beta	0.0	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.1	-0.45	2.68	1.61	-4.31	2.34	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14926	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	Q112A	Q109A	Beta	19.7	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	3.17	-0.38	1.0	-0.07	-4.64	2.3	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14927	1999.0	10542092	2	yes	2023-06-04 01:00:00
src SHR	Homo sapiens	64.0	P12931	1fmk	A	Mainly Beta	PF00018/PF07714/PF00017	1fmkA01 (2.30.30.40)	2.7.10.2	I113A	I110A	Beta	0.6	22.0	6.0	Phosphate	0.05	N/A	N/A	N/A	stopped-flow	GuHCl	N/A	N/A	N/A	N/A	N/A	N/A	1.4	-2.15	-0.63	-1.7	-5.82	2.13	N/A	N/A	N/A	N/A	N/A	Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.	Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016–1024. https://doi.org/10.1038/14928	1999.0	10542092	2	yes	2023-06-04 01:00:00