BMRB: 50907

Rules for designing protein fold switches and their implications for the folding code

Authors

He, Y., Chen, Y., Ruan, B., Choi, E.J., Chen, Y., Motabar, D., Solomon, T., Simmerman, R., Kauffman, T., Gallagher, D., Bryan, P.N., Orban, J.

Assembly

A1

Entity

1. A1 (polymer, Thiol state: not present), 56 monomers, 6203.268 Da Detail

NPNLDQKQLA QAKELAIKAL KQYGIGVEKI KLIGNAKTVE AVEKLKQGIL LVYQIE

Formula weight

6203.268 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chemcal Shifts

¹H: 54, ¹³C: 160, ¹⁵N: 54 assignments Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err	Ambig. code
1	1	2	PRO	C	C	176.845	0	1
2	1	2	PRO	CA	C	64.103	0	1
3	1	2	PRO	CB	C	31.994	0	1
4	1	3	ASN	H	H	8.51	0.005	1
5	1	3	ASN	C	C	175.229	0	1
6	1	3	ASN	CA	C	53.695	0.255	1
7	1	3	ASN	CB	C	38.508	0.044	1
8	1	3	ASN	N	N	118.351	0.007	1
9	1	4	LEU	H	H	8.669	0.003	1
10	1	4	LEU	C	C	177.776	0	1
11	1	4	LEU	CA	C	56.372	0.263	1
12	1	4	LEU	CB	C	41.896	0.113	1
13	1	4	LEU	N	N	123.965	0.046	1
14	1	5	ASP	H	H	8.339	0.003	1
15	1	5	ASP	C	C	178.145	0	1
16	1	5	ASP	CA	C	56.01	0.207	1
17	1	5	ASP	CB	C	40.743	0.007	1
18	1	5	ASP	N	N	121.205	0.039	1
19	1	6	GLN	H	H	8.543	0.003	1
20	1	6	GLN	C	C	178.635	0	1
21	1	6	GLN	CA	C	58.415	0.025	1
22	1	6	GLN	CB	C	28.315	0.029	1
23	1	6	GLN	N	N	121.742	0.042	1
24	1	7	LYS	H	H	8.282	0.002	1
25	1	7	LYS	C	C	179.03	0	1
26	1	7	LYS	CA	C	59.389	0.159	1
27	1	7	LYS	CB	C	32.069	0.069	1
28	1	7	LYS	N	N	122.37	0.046	1
29	1	8	GLN	H	H	8.472	0.006	1
30	1	8	GLN	C	C	178.841	0	1
31	1	8	GLN	CA	C	58.939	0.01	1
32	1	8	GLN	CB	C	28.354	0.104	1
33	1	8	GLN	N	N	119.198	0.057	1
34	1	9	LEU	H	H	8.163	0.019	1
35	1	9	LEU	C	C	177.486	0	1
36	1	9	LEU	CA	C	58.7	0.154	1
37	1	9	LEU	CB	C	41.854	0.29	1
38	1	9	LEU	N	N	122.53	0.076	1
39	1	10	ALA	H	H	8.036	0.008	1
40	1	10	ALA	C	C	181.235	0	1
41	1	10	ALA	CA	C	55.418	0.058	1
42	1	10	ALA	CB	C	17.73	0.006	1
43	1	10	ALA	N	N	120.864	0.099	1
44	1	11	GLN	H	H	8.23	0.003	1
45	1	11	GLN	C	C	177.778	0	1
46	1	11	GLN	CA	C	58.804	0.044	1
47	1	11	GLN	CB	C	28.412	0.118	1
48	1	11	GLN	N	N	118.309	0.033	1
49	1	12	ALA	H	H	8.175	0.005	1
50	1	12	ALA	C	C	180.8	0	1
51	1	12	ALA	CA	C	54.993	0.16	1
52	1	12	ALA	CB	C	18.542	0.306	1
53	1	12	ALA	N	N	122.094	0.073	1
54	1	13	LYS	H	H	7.79	0.018	1
55	1	13	LYS	C	C	176.9	0	1
56	1	13	LYS	CA	C	67.73	0	1
57	1	13	LYS	CB	C	31.58	0	1
58	1	13	LYS	N	N	119.3	0.035	1
59	1	14	GLU	H	H	7.84	0.017	1
60	1	14	GLU	C	C	180	0	1
61	1	14	GLU	CA	C	59.37	0.357	1
62	1	14	GLU	CB	C	28.86	0.413	1
63	1	14	GLU	N	N	118.9	0.045	1
64	1	15	LEU	H	H	8.362	0.005	1
65	1	15	LEU	C	C	179.843	0	1
66	1	15	LEU	CA	C	58.15	0.314	1
67	1	15	LEU	CB	C	41.748	0.194	1
68	1	15	LEU	N	N	119.037	0.028	1
69	1	16	ALA	H	H	8.056	0.003	1
70	1	16	ALA	C	C	178.972	0	1
71	1	16	ALA	CA	C	55.465	0.029	1
72	1	16	ALA	CB	C	18.193	0.036	1
73	1	16	ALA	N	N	123.007	0.006	1
74	1	17	ILE	H	H	8.468	0.008	1
75	1	17	ILE	C	C	175.556	0	1
76	1	17	ILE	CA	C	66.21	0.061	1
77	1	17	ILE	CB	C	38.408	0.207	1
78	1	17	ILE	N	N	118.208	0.018	1
79	1	18	LYS	H	H	7.926	0.006	1
80	1	18	LYS	C	C	179.336	0	1
81	1	18	LYS	CA	C	60.109	0.181	1
82	1	18	LYS	CB	C	32.531	0.053	1
83	1	18	LYS	N	N	119.369	0.092	1
84	1	19	ALA	H	H	7.906	0.007	1
85	1	19	ALA	C	C	179.65	0	1
86	1	19	ALA	CA	C	54.836	0.004	1
87	1	19	ALA	CB	C	17.93	0.126	1
88	1	19	ALA	N	N	121.305	0.051	1
89	1	20	LEU	H	H	8.013	0.009	1
90	1	20	LEU	C	C	179.24	0	1
91	1	20	LEU	CA	C	56.612	0.01	1
92	1	20	LEU	CB	C	41.801	0.062	1
93	1	20	LEU	N	N	116.323	0.037	1
94	1	21	LYS	H	H	8.192	0.012	1
95	1	21	LYS	C	C	179.89	0	1
96	1	21	LYS	CA	C	59.909	0.115	1
97	1	21	LYS	CB	C	32.298	0.01	1
98	1	21	LYS	N	N	121.384	0.043	1
99	1	22	GLN	H	H	8.131	0.011	1
100	1	22	GLN	C	C	176.512	0	1
101	1	22	GLN	CA	C	57.893	0.07	1
102	1	22	GLN	CB	C	27.982	0.033	1
103	1	22	GLN	N	N	117.97	0.018	1
104	1	23	TYR	H	H	7.455	0.006	1
105	1	23	TYR	C	C	175.976	0	1
106	1	23	TYR	CA	C	58.386	0.093	1
107	1	23	TYR	CB	C	38.358	0.083	1
108	1	23	TYR	N	N	116.969	0.037	1
109	1	24	GLY	H	H	7.789	0.004	1
110	1	24	GLY	C	C	175.04	0	1
111	1	24	GLY	CA	C	46.913	0.064	1
112	1	24	GLY	N	N	107.807	0.056	1
113	1	25	ILE	H	H	7.522	0.012	1
114	1	25	ILE	C	C	175.895	0	1
115	1	25	ILE	CA	C	61.257	0.054	1
116	1	25	ILE	CB	C	37.276	0.081	1
117	1	25	ILE	N	N	117.67	0.108	1
118	1	26	GLY	H	H	8.462	0.004	1
119	1	26	GLY	C	C	175.105	0	1
120	1	26	GLY	CA	C	45.227	0.055	1
121	1	26	GLY	N	N	111.114	0.027	1
122	1	27	VAL	H	H	8.375	0.001	1
123	1	27	VAL	C	C	177.526	0	1
124	1	27	VAL	CA	C	65.78	0.006	1
125	1	27	VAL	CB	C	31.872	0.016	1
126	1	27	VAL	N	N	117.956	0.031	1
127	1	28	GLU	H	H	9.149	0.002	1
128	1	28	GLU	C	C	179.345	0	1
129	1	28	GLU	CA	C	59.493	0.099	1
130	1	28	GLU	CB	C	28.133	0.026	1
131	1	28	GLU	N	N	120.455	0.014	1
132	1	29	LYS	H	H	7.679	0.003	1
133	1	29	LYS	C	C	178.097	0	1
134	1	29	LYS	CA	C	58.011	0.093	1
135	1	29	LYS	CB	C	32.252	0.13	1
136	1	29	LYS	N	N	118.086	0.053	1
137	1	30	ILE	H	H	7.589	0.004	1
138	1	30	ILE	C	C	179.159	0	1
139	1	30	ILE	CA	C	65.716	0.018	1
140	1	30	ILE	CB	C	37.63	0.108	1
141	1	30	ILE	N	N	119.845	0.095	1
142	1	31	LYS	H	H	8.168	0.004	1
143	1	31	LYS	C	C	178.589	0	1
144	1	31	LYS	CA	C	59.079	0.225	1
145	1	31	LYS	CB	C	32.155	0.038	1
146	1	31	LYS	N	N	120.071	0.028	1
147	1	32	LEU	H	H	7.421	0.007	1
148	1	32	LEU	C	C	180.184	0	1
149	1	32	LEU	CA	C	58.181	0.017	1
150	1	32	LEU	CB	C	41.819	0.138	1
151	1	32	LEU	N	N	118.404	0.023	1
152	1	33	ILE	H	H	7.574	0.004	1
153	1	33	ILE	C	C	177.924	0	1
154	1	33	ILE	CA	C	64.204	0.08	1
155	1	33	ILE	CB	C	36.574	0.034	1
156	1	33	ILE	N	N	118.327	0.031	1
157	1	34	GLY	H	H	7.931	0.004	1
158	1	34	GLY	C	C	175.382	0	1
159	1	34	GLY	CA	C	47.166	0	1
160	1	34	GLY	N	N	104.028	0.027	1
161	1	35	ASN	H	H	7.55	0.006	1
162	1	35	ASN	C	C	175.486	0	1
163	1	35	ASN	CA	C	52.767	0.019	1
164	1	35	ASN	CB	C	39.319	0.029	1
165	1	35	ASN	N	N	116.759	0.086	1
166	1	36	ALA	H	H	7.41	0.002	1
167	1	36	ALA	C	C	178.717	0	1
168	1	36	ALA	CA	C	53.13	0.026	1
169	1	36	ALA	CB	C	19.651	0	1
170	1	36	ALA	N	N	124.852	0.02	1
171	1	37	LYS	H	H	8.919	0.003	1
172	1	37	LYS	C	C	176.772	0	1
173	1	37	LYS	CA	C	57.032	0.025	1
174	1	37	LYS	CB	C	34.469	0.051	1
175	1	37	LYS	N	N	116.324	0.056	1
176	1	38	THR	H	H	7.13	0.001	1
177	1	38	THR	C	C	174.654	0	1
178	1	38	THR	CA	C	58.594	0.145	1
179	1	38	THR	CB	C	73.236	0.043	1
180	1	38	THR	N	N	105.112	0.013	1
181	1	39	VAL	H	H	9.196	0.005	1
182	1	39	VAL	C	C	178.361	0	1
183	1	39	VAL	CA	C	67.055	0.032	1
184	1	39	VAL	CB	C	31.354	0.006	1
185	1	39	VAL	N	N	121.702	0.039	1
186	1	40	GLU	H	H	9.008	0.006	1
187	1	40	GLU	C	C	175.903	0	1
188	1	40	GLU	CA	C	60.334	0.04	1
189	1	40	GLU	CB	C	28.445	0.007	1
190	1	40	GLU	N	N	121.224	0.062	1
191	1	41	ALA	H	H	8.156	0.012	1
192	1	41	ALA	C	C	181.606	0	1
193	1	41	ALA	CA	C	55.227	0.127	1
194	1	41	ALA	CB	C	18.107	0.192	1
195	1	41	ALA	N	N	122.4	0.087	1
196	1	42	VAL	H	H	8.288	0.003	1
197	1	42	VAL	C	C	177.323	0	1
198	1	42	VAL	CA	C	60.68	0.04	1
199	1	42	VAL	CB	C	33.222	0.094	1
200	1	42	VAL	N	N	118.52	0.044	1
201	1	43	GLU	H	H	7.891	0.004	1
202	1	43	GLU	C	C	178.755	0	1
203	1	43	GLU	CA	C	59.392	0.355	1
204	1	43	GLU	CB	C	28.936	0.461	1
205	1	43	GLU	N	N	118.324	0.042	1
206	1	44	LYS	H	H	8.133	0.002	1
207	1	44	LYS	C	C	180.618	0	1
208	1	44	LYS	CA	C	59.45	0.152	1
209	1	44	LYS	CB	C	32.447	0.061	1
210	1	44	LYS	N	N	119.157	0.074	1
211	1	45	LEU	H	H	8.121	0.006	1
212	1	45	LEU	C	C	179.176	0	1
213	1	45	LEU	CA	C	57.906	0.223	1
214	1	45	LEU	CB	C	43.05	0.039	1
215	1	45	LEU	N	N	121.425	0.073	1
216	1	46	LYS	H	H	8.639	0.002	1
217	1	46	LYS	C	C	177.615	0	1
218	1	46	LYS	CA	C	60.562	0.022	1
219	1	46	LYS	CB	C	32.374	0.026	1
220	1	46	LYS	N	N	120.015	0.082	1
221	1	47	GLN	H	H	8.499	0.018	1
222	1	47	GLN	C	C	179.164	0	1
223	1	47	GLN	CA	C	58.676	0.008	1
224	1	47	GLN	CB	C	27.733	0.14	1
225	1	47	GLN	N	N	115.908	0.042	1
226	1	48	GLY	H	H	8.04	0.005	1
227	1	48	GLY	C	C	176.524	0	1
228	1	48	GLY	CA	C	47.117	0.01	1
229	1	48	GLY	N	N	106.203	0.024	1
230	1	49	ILE	H	H	8.118	0.008	1
231	1	49	ILE	C	C	177.902	0	1
232	1	49	ILE	CA	C	64.635	0.074	1
233	1	49	ILE	CB	C	38.15	0.245	1
234	1	49	ILE	N	N	122.673	0.106	1
235	1	50	LEU	H	H	8.057	0.005	1
236	1	50	LEU	C	C	178.862	0	1
237	1	50	LEU	CA	C	57.54	0.078	1
238	1	50	LEU	CB	C	41.366	0.021	1
239	1	50	LEU	N	N	118.231	0.015	1
240	1	51	LEU	H	H	7.636	0.005	1
241	1	51	LEU	C	C	179.216	0	1
242	1	51	LEU	CA	C	58.016	0.288	1
243	1	51	LEU	CB	C	42.186	0.067	1
244	1	51	LEU	N	N	118.824	0.033	1
245	1	52	VAL	H	H	7.308	0.005	1
246	1	52	VAL	C	C	176.813	0	1
247	1	52	VAL	CA	C	64.153	0.039	1
248	1	52	VAL	CB	C	31.79	0.005	1
249	1	52	VAL	N	N	115.415	0.093	1
250	1	53	TYR	H	H	7.529	0.003	1
251	1	53	TYR	C	C	178.33	0	1
252	1	53	TYR	CA	C	59.053	0.087	1
253	1	53	TYR	CB	C	38.867	0.008	1
254	1	53	TYR	N	N	118.527	0.059	1
255	1	54	GLN	H	H	7.931	0.008	1
256	1	54	GLN	C	C	175.334	0	1
257	1	54	GLN	CA	C	56.148	0.064	1
258	1	54	GLN	CB	C	28.468	0.163	1
259	1	54	GLN	N	N	119.539	0.085	1
260	1	55	ILE	H	H	8.031	0.003	1
261	1	55	ILE	C	C	175.553	0	1
262	1	55	ILE	CA	C	61.227	0.118	1
263	1	55	ILE	CB	C	38.897	0.056	1
264	1	55	ILE	N	N	121.835	0.051	1
265	1	56	GLU	H	H	8.088	0.004	1
266	1	56	GLU	CA	C	58.362	0	1
267	1	56	GLU	CB	C	31.006	0	1
268	1	56	GLU	N	N	130.027	0.031	1

Release date

2021-04-21

Citation

Design and characterization of a protein fold switching network
He, Y., Chen, Y., Ruan, B., Choi, E.J., Chen, Y., Motabar, D., Solomon, T., Simmerman, R., Kauffman, T., Gallagher, D., Bryan, P.N., Orban, J.
Nat. Commun. (2023), 14, 431-431, PubMed 36702827 , DOI 10.1038/s41467-023-36065-3 , Abstract

Entries sharing articles BMRB: 7 entries Detail

Related entities 1. A1, : 1 : 1 : 118 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail