BMRBj - BMREntryMaster

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BMRB: 52018

8FWJ

Backbone 1H, 13C, and 15N chemical shift assignments of the ground state and the fold-switched state of KaiB-RS

Authors

Wayment-Steele, H., Ojoawo, A.M., Otten, R., Apitz, J., Pitsawong, W., Ovchinnikov, S., Colwell, L.

Assembly

KaiB-RS

Entity

1. KaiB-RS (polymer, Thiol state: all free), 90 monomers, 10174.88 × 2 Da Detail

MGRRLVLYVA GQTPKSLAAI SNLRRICEEN LPGQYEVEVI DLKQNPRLAK EHSIVAIPTL VRELPVPIRK IIGDLSDKEQ VLVNLKMDME

Total weight

20349.76 Da

Max. entity weight

10174.88 Da

Source organism

Cereibacter sphaeroides

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chemical Shifts 1

¹H: 83, ¹³C: 170, ¹⁵N: 83 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val
1	1	1	MET	H	H	8.444
2	1	1	MET	CA	C	54.93
3	1	1	MET	CB	C	33.18
4	1	1	MET	N	N	118.8
5	1	2	GLY	H	H	8.22
6	1	2	GLY	CA	C	45.22
7	1	2	GLY	N	N	109.3
8	1	3	ARG	H	H	7.886
9	1	3	ARG	CA	C	55.69
10	1	3	ARG	CB	C	32.15
11	1	3	ARG	N	N	120.4
12	1	4	ARG	H	H	8.726
13	1	4	ARG	CA	C	56.1
14	1	4	ARG	CB	C	31.83
15	1	4	ARG	N	N	124.3
16	1	5	LEU	H	H	8.854
17	1	5	LEU	CA	C	53.95
18	1	5	LEU	CB	C	43.94
19	1	5	LEU	N	N	127.6
20	1	6	VAL	H	H	9.019
21	1	6	VAL	CA	C	61.21
22	1	6	VAL	CB	C	32.67
23	1	6	VAL	N	N	125
24	1	7	LEU	H	H	8.95
25	1	7	LEU	CA	C	54.37
26	1	7	LEU	CB	C	42.98
27	1	7	LEU	N	N	126.8
28	1	8	TYR	H	H	8.324
29	1	8	TYR	CA	C	56.71
30	1	8	TYR	CB	C	38.2
31	1	8	TYR	N	N	121.6
32	1	9	VAL	H	H	9.033
33	1	9	VAL	CA	C	58.01
34	1	9	VAL	CB	C	34.9
35	1	9	VAL	N	N	117
36	1	10	ALA	H	H	9.177
37	1	10	ALA	CA	C	51
38	1	10	ALA	CB	C	19.2
39	1	10	ALA	N	N	125.8
40	1	11	GLY	H	H	7.993
41	1	11	GLY	CA	C	44.8
42	1	11	GLY	N	N	108.9
43	1	12	GLN	H	H	8.05
44	1	12	GLN	CA	C	55.39
45	1	12	GLN	CB	C	31.92
46	1	12	GLN	N	N	114.1
47	1	13	THR	H	H	9.079
48	1	13	THR	CA	C	58.53
49	1	13	THR	CB	C	69.88
50	1	13	THR	N	N	115.2
51	1	14	PRO	CA	C	66.24
52	1	15	LYS	H	H	8.058
53	1	15	LYS	CA	C	59.15
54	1	15	LYS	CB	C	32.57
55	1	15	LYS	N	N	115.2
56	1	16	SER	H	H	8.834
57	1	16	SER	CA	C	62.38
58	1	16	SER	N	N	121.8
59	1	17	LEU	H	H	8.597
60	1	17	LEU	CA	C	58.14
61	1	17	LEU	CB	C	41.73
62	1	17	LEU	N	N	125.4
63	1	18	ALA	H	H	7.631
64	1	18	ALA	CA	C	54.85
65	1	18	ALA	CB	C	18.01
66	1	18	ALA	N	N	122
67	1	19	ALA	H	H	7.964
68	1	19	ALA	CA	C	55.05
69	1	19	ALA	CB	C	18.46
70	1	19	ALA	N	N	122.2
71	1	20	ILE	H	H	8.46
72	1	20	ILE	CA	C	65.5
73	1	20	ILE	CB	C	37.73
74	1	20	ILE	N	N	119
75	1	21	SER	H	H	8.084
76	1	21	SER	CA	C	62.22
77	1	21	SER	N	N	116
78	1	22	ASN	H	H	8.208
79	1	22	ASN	CA	C	56.11
80	1	22	ASN	CB	C	38.17
81	1	22	ASN	N	N	121
82	1	23	LEU	H	H	8.659
83	1	23	LEU	CA	C	58.44
84	1	23	LEU	CB	C	41.63
85	1	23	LEU	N	N	121.8
86	1	24	ARG	H	H	8.429
87	1	24	ARG	CA	C	60.84
88	1	24	ARG	CB	C	29.98
89	1	24	ARG	N	N	117.9
90	1	25	ARG	H	H	7.846
91	1	25	ARG	CA	C	59.66
92	1	25	ARG	CB	C	29.75
93	1	25	ARG	N	N	120
94	1	26	ILE	H	H	8.556
95	1	26	ILE	CA	C	64.85
96	1	26	ILE	CB	C	38.25
97	1	26	ILE	N	N	120
98	1	27	CYS	H	H	8.174
99	1	27	CYS	CA	C	65.26
100	1	27	CYS	CB	C	26.45
101	1	27	CYS	N	N	118.1
102	1	28	GLU	H	H	7.912
103	1	28	GLU	CA	C	58.78
104	1	28	GLU	CB	C	30.28
105	1	28	GLU	N	N	117.2
106	1	29	GLU	H	H	8.545
107	1	29	GLU	CA	C	58.18
108	1	29	GLU	CB	C	30.77
109	1	29	GLU	N	N	115
110	1	30	ASN	H	H	8.265
111	1	30	ASN	CA	C	54.74
112	1	30	ASN	CB	C	40.41
113	1	30	ASN	N	N	114.9
114	1	31	LEU	H	H	7.712
115	1	31	LEU	CA	C	52.51
116	1	31	LEU	CB	C	42.93
117	1	31	LEU	N	N	121.2
118	1	32	PRO	CA	C	64.46
119	1	32	PRO	CB	C	31.14
120	1	33	GLY	H	H	8.979
121	1	33	GLY	CA	C	45.67
122	1	33	GLY	N	N	111.3
123	1	34	GLN	H	H	8.068
124	1	34	GLN	CA	C	58.36
125	1	34	GLN	CB	C	30.53
126	1	34	GLN	N	N	119.2
127	1	35	TYR	H	H	9.096
128	1	35	TYR	CA	C	57.45
129	1	35	TYR	CB	C	42.66
130	1	35	TYR	N	N	118
131	1	36	GLU	H	H	8.478
132	1	36	GLU	CA	C	54.83
133	1	36	GLU	CB	C	32
134	1	36	GLU	N	N	122.6
135	1	37	VAL	H	H	8.876
136	1	37	VAL	CA	C	61.96
137	1	37	VAL	CB	C	33.4
138	1	37	VAL	N	N	124.8
139	1	38	GLU	H	H	9.148
140	1	38	GLU	CA	C	54.61
141	1	38	GLU	CB	C	33.44
142	1	38	GLU	N	N	131.1
143	1	39	VAL	H	H	8.557
144	1	39	VAL	CA	C	61.12
145	1	39	VAL	CB	C	33.57
146	1	39	VAL	N	N	124.4
147	1	40	ILE	H	H	9.146
148	1	40	ILE	CA	C	60.08
149	1	40	ILE	CB	C	38.96
150	1	40	ILE	N	N	130.9
151	1	41	ASP	H	H	8.669
152	1	41	ASP	CA	C	52.41
153	1	41	ASP	CB	C	41.24
154	1	41	ASP	N	N	126.9
155	1	42	LEU	H	H	9.524
156	1	42	LEU	CA	C	56.29
157	1	42	LEU	CB	C	42.5
158	1	42	LEU	N	N	127.7
159	1	43	LYS	H	H	8.821
160	1	43	LYS	CA	C	58.31
161	1	43	LYS	CB	C	31.65
162	1	43	LYS	N	N	118.9
163	1	44	GLN	H	H	7.571
164	1	44	GLN	CA	C	55.73
165	1	44	GLN	CB	C	29.76
166	1	44	GLN	N	N	116.2
167	1	45	ASN	H	H	7.824
168	1	45	ASN	CA	C	51.22
169	1	45	ASN	CB	C	39.81
170	1	45	ASN	N	N	116.9
171	1	46	PRO	CA	C	64.49
172	1	46	PRO	CB	C	32.03
173	1	47	ARG	H	H	8.32
174	1	47	ARG	CA	C	57.54
175	1	47	ARG	CB	C	29.78
176	1	47	ARG	N	N	118.3
177	1	48	LEU	H	H	7.696
178	1	48	LEU	CA	C	55.3
179	1	48	LEU	CB	C	42.02
180	1	48	LEU	N	N	119.6
181	1	49	ALA	H	H	7.851
182	1	49	ALA	CA	C	53.42
183	1	49	ALA	CB	C	19.04
184	1	49	ALA	N	N	122.3
185	1	50	LYS	H	H	7.919
186	1	50	LYS	CA	C	56.58
187	1	50	LYS	CB	C	32.76
188	1	50	LYS	N	N	118.4
189	1	51	GLU	H	H	8.009
190	1	51	GLU	CA	C	56.75
191	1	51	GLU	CB	C	29.95
192	1	51	GLU	N	N	120.1
193	1	52	HIS	H	H	8.1
194	1	52	HIS	CA	C	55.79
195	1	52	HIS	CB	C	30.54
196	1	52	HIS	N	N	119.4
197	1	53	SER	H	H	8.166
198	1	53	SER	CA	C	58.32
199	1	53	SER	CB	C	63.76
200	1	53	SER	N	N	116.7
201	1	54	ILE	H	H	8.246
202	1	54	ILE	CA	C	61.65
203	1	54	ILE	CB	C	38.57
204	1	54	ILE	N	N	122.5
205	1	55	VAL	H	H	8.03
206	1	55	VAL	CA	C	61.87
207	1	55	VAL	CB	C	33.1
208	1	55	VAL	N	N	123.1
209	1	56	ALA	H	H	8.422
210	1	56	ALA	CA	C	52.17
211	1	56	ALA	CB	C	19.38
212	1	56	ALA	N	N	128
213	1	57	ILE	H	H	8.479
214	1	57	ILE	CA	C	63.31
215	1	57	ILE	CB	C	36.35
216	1	57	ILE	N	N	122.5
217	1	58	PRO	CB	C	31.44
218	1	59	THR	H	H	7.659
219	1	59	THR	CA	C	64.98
220	1	59	THR	CB	C	68.78
221	1	59	THR	N	N	112.4
222	1	60	LEU	H	H	7.878
223	1	60	LEU	CA	C	57.13
224	1	60	LEU	CB	C	42.38
225	1	60	LEU	N	N	122.1
226	1	61	VAL	H	H	7.773
227	1	61	VAL	CA	C	63.97
228	1	61	VAL	CB	C	31.7
229	1	61	VAL	N	N	113.3
230	1	62	ARG	H	H	7.299
231	1	62	ARG	CA	C	58.41
232	1	62	ARG	CB	C	30.09
233	1	62	ARG	N	N	117.5
234	1	63	GLU	H	H	7.84
235	1	63	GLU	CA	C	55.9
236	1	63	GLU	CB	C	29.98
237	1	63	GLU	N	N	115.2
238	1	64	LEU	H	H	7.622
239	1	64	LEU	CA	C	52.97
240	1	64	LEU	CB	C	40.97
241	1	64	LEU	N	N	120.6
242	1	65	PRO	CA	C	62.95
243	1	65	PRO	CB	C	33.14
244	1	66	VAL	H	H	8.95
245	1	66	VAL	CA	C	68.71
246	1	66	VAL	CB	C	30.11
247	1	66	VAL	N	N	124.3
248	1	67	PRO	CA	C	65.83
249	1	67	PRO	CB	C	31.79
250	1	68	ILE	H	H	6.95
251	1	68	ILE	CA	C	63.45
252	1	68	ILE	CB	C	37.93
253	1	68	ILE	N	N	111.4
254	1	69	ARG	H	H	7.997
255	1	69	ARG	CA	C	60.48
256	1	69	ARG	CB	C	30.64
257	1	69	ARG	N	N	120.5
258	1	70	LYS	H	H	8.263
259	1	70	LYS	CA	C	59.36
260	1	70	LYS	CB	C	32.3
261	1	70	LYS	N	N	119
262	1	71	ILE	H	H	7.042
263	1	71	ILE	CA	C	64.63
264	1	71	ILE	CB	C	38.42
265	1	71	ILE	N	N	119
266	1	72	ILE	H	H	7.924
267	1	72	ILE	CA	C	64.34
268	1	72	ILE	CB	C	36.2
269	1	72	ILE	N	N	118.7
270	1	73	GLY	H	H	8.264
271	1	73	GLY	CA	C	47.36
272	1	73	GLY	N	N	107.6
273	1	74	ASP	H	H	8.219
274	1	74	ASP	CA	C	57.48
275	1	74	ASP	CB	C	39.97
276	1	74	ASP	N	N	123
277	1	75	LEU	H	H	8.333
278	1	75	LEU	CA	C	57.62
279	1	75	LEU	CB	C	43.39
280	1	75	LEU	N	N	119.9
281	1	76	SER	H	H	8.167
282	1	76	SER	CA	C	59.91
283	1	76	SER	CB	C	63.89
284	1	76	SER	N	N	113.4
285	1	77	ASP	H	H	8.698
286	1	77	ASP	CA	C	56.5
287	1	77	ASP	CB	C	41.87
288	1	77	ASP	N	N	119.3
289	1	78	LYS	H	H	7.894
290	1	78	LYS	CA	C	57.86
291	1	78	LYS	CB	C	32.74
292	1	78	LYS	N	N	117.6
293	1	79	GLU	H	H	8.315
294	1	79	GLU	CA	C	56.25
295	1	79	GLU	CB	C	29.89
296	1	79	GLU	N	N	115
297	1	80	GLN	H	H	6.959
298	1	80	GLN	CA	C	56.94
299	1	80	GLN	CB	C	26.35
300	1	80	GLN	N	N	110.3
301	1	81	VAL	H	H	7.613
302	1	81	VAL	CA	C	61.52
303	1	81	VAL	CB	C	33.64
304	1	81	VAL	N	N	108.6
305	1	82	LEU	H	H	7.339
306	1	82	LEU	CA	C	55.1
307	1	82	LEU	CB	C	43.69
308	1	82	LEU	N	N	122
309	1	84	ASN	H	H	8.002
310	1	84	ASN	CA	C	52.09
311	1	84	ASN	CB	C	40.96
312	1	84	ASN	N	N	114.1
313	1	85	LEU	H	H	8.437
314	1	85	LEU	CA	C	54.53
315	1	85	LEU	CB	C	46.57
316	1	85	LEU	N	N	122.9
317	1	86	LYS	H	H	9.212
318	1	86	LYS	CA	C	55.1
319	1	86	LYS	CB	C	36.63
320	1	86	LYS	N	N	123.4
321	1	87	MET	H	H	8.723
322	1	87	MET	CA	C	54.3
323	1	87	MET	CB	C	35.83
324	1	87	MET	N	N	122.5
325	1	88	ASP	H	H	8.685
326	1	88	ASP	CA	C	54.49
327	1	88	ASP	CB	C	42.1
328	1	88	ASP	N	N	123.9
329	1	89	MET	H	H	8.603
330	1	89	MET	CA	C	55.26
331	1	89	MET	CB	C	33.3
332	1	89	MET	N	N	120.6
333	1	90	GLU	H	H	8.067
334	1	90	GLU	CA	C	58.14
335	1	90	GLU	CB	C	31.08
336	1	90	GLU	N	N	126.1

Chemical Shifts 2

¹H: 72, ¹³C: 181, ¹⁵N: 72 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val
337	1	1	MET	H	H	8.444
338	1	1	MET	CA	C	54.93
339	1	1	MET	CB	C	33.18
340	1	1	MET	N	N	118.8
341	1	2	GLY	H	H	8.22
342	1	2	GLY	CA	C	45.22
343	1	2	GLY	N	N	109.3
344	1	3	ARG	H	H	7.886
345	1	3	ARG	CA	C	55.69
346	1	3	ARG	CB	C	32.15
347	1	3	ARG	N	N	120.4
348	1	4	ARG	H	H	8.726
349	1	4	ARG	CA	C	56.1
350	1	4	ARG	CB	C	31.83
351	1	4	ARG	N	N	124.3
352	1	5	LEU	H	H	8.854
353	1	5	LEU	CA	C	53.95
354	1	5	LEU	CB	C	43.94
355	1	5	LEU	N	N	127.6
356	1	6	VAL	H	H	9.019
357	1	6	VAL	CA	C	61.21
358	1	6	VAL	CB	C	32.67
359	1	6	VAL	N	N	125
360	1	7	LEU	H	H	8.95
361	1	7	LEU	CA	C	54.37
362	1	7	LEU	CB	C	42.98
363	1	7	LEU	N	N	126.8
364	1	8	TYR	H	H	8.324
365	1	8	TYR	CA	C	56.71
366	1	8	TYR	CB	C	38.2
367	1	8	TYR	N	N	121.6
368	1	9	VAL	H	H	9.033
369	1	9	VAL	CA	C	58.01
370	1	9	VAL	CB	C	34.9
371	1	9	VAL	N	N	117
372	1	10	ALA	H	H	9.177
373	1	10	ALA	CA	C	51
374	1	10	ALA	CB	C	19.2
375	1	10	ALA	N	N	125.8
376	1	11	GLY	H	H	7.993
377	1	11	GLY	CA	C	44.8
378	1	11	GLY	N	N	108.9
379	1	12	GLN	H	H	8.05
380	1	12	GLN	CA	C	55.39
381	1	12	GLN	CB	C	31.92
382	1	12	GLN	N	N	114.1
383	1	13	THR	H	H	9.079
384	1	13	THR	CA	C	58.53
385	1	13	THR	CB	C	69.88
386	1	13	THR	N	N	115.2
387	1	14	PRO	CA	C	66.24
388	1	15	LYS	H	H	8.058
389	1	15	LYS	CA	C	59.15
390	1	15	LYS	CB	C	32.57
391	1	15	LYS	N	N	115.2
392	1	16	SER	H	H	8.834
393	1	16	SER	CA	C	62.38
394	1	16	SER	N	N	121.8
395	1	17	LEU	H	H	8.597
396	1	17	LEU	CA	C	58.14
397	1	17	LEU	CB	C	41.73
398	1	17	LEU	N	N	125.4
399	1	18	ALA	H	H	7.631
400	1	18	ALA	CA	C	54.85
401	1	18	ALA	CB	C	18.01
402	1	18	ALA	N	N	122
403	1	19	ALA	H	H	7.964
404	1	19	ALA	CA	C	55.05
405	1	19	ALA	CB	C	18.46
406	1	19	ALA	N	N	122.2
407	1	20	ILE	H	H	8.46
408	1	20	ILE	CA	C	65.5
409	1	20	ILE	CB	C	37.73
410	1	20	ILE	N	N	119
411	1	21	SER	H	H	8.084
412	1	21	SER	CA	C	62.22
413	1	21	SER	N	N	116
414	1	22	ASN	H	H	8.208
415	1	22	ASN	CA	C	56.11
416	1	22	ASN	CB	C	38.17
417	1	22	ASN	N	N	121
418	1	23	LEU	H	H	8.659
419	1	23	LEU	CA	C	58.44
420	1	23	LEU	CB	C	41.63
421	1	23	LEU	N	N	121.8
422	1	24	ARG	H	H	8.429
423	1	24	ARG	CA	C	60.84
424	1	24	ARG	CB	C	29.98
425	1	24	ARG	N	N	117.9
426	1	25	ARG	H	H	7.846
427	1	25	ARG	CA	C	59.66
428	1	25	ARG	CB	C	29.75
429	1	25	ARG	N	N	120
430	1	26	ILE	H	H	8.556
431	1	26	ILE	CA	C	64.85
432	1	26	ILE	CB	C	38.25
433	1	26	ILE	N	N	120
434	1	27	CYS	H	H	8.174
435	1	27	CYS	CA	C	65.26
436	1	27	CYS	CB	C	26.45
437	1	27	CYS	N	N	118.1
438	1	28	GLU	H	H	7.912
439	1	28	GLU	CA	C	58.78
440	1	28	GLU	CB	C	30.28
441	1	28	GLU	N	N	117.2
442	1	29	GLU	H	H	8.545
443	1	29	GLU	CA	C	58.18
444	1	29	GLU	CB	C	30.77
445	1	29	GLU	N	N	115
446	1	30	ASN	H	H	8.265
447	1	30	ASN	CA	C	54.74
448	1	30	ASN	CB	C	40.41
449	1	30	ASN	N	N	114.9
450	1	31	LEU	H	H	7.712
451	1	31	LEU	CA	C	52.51
452	1	31	LEU	CB	C	42.93
453	1	31	LEU	N	N	121.2
454	1	32	PRO	CA	C	64.46
455	1	32	PRO	CB	C	31.14
456	1	33	GLY	H	H	8.979
457	1	33	GLY	CA	C	45.67
458	1	33	GLY	N	N	111.3
459	1	34	GLN	H	H	8.068
460	1	34	GLN	CA	C	58.36
461	1	34	GLN	CB	C	30.53
462	1	34	GLN	N	N	119.2
463	1	35	TYR	H	H	9.096
464	1	35	TYR	CA	C	57.45
465	1	35	TYR	CB	C	42.66
466	1	35	TYR	N	N	118
467	1	36	GLU	H	H	8.478
468	1	36	GLU	CA	C	54.83
469	1	36	GLU	CB	C	32
470	1	36	GLU	N	N	122.6
471	1	37	VAL	H	H	8.876
472	1	37	VAL	CA	C	61.96
473	1	37	VAL	CB	C	33.4
474	1	37	VAL	N	N	124.8
475	1	38	GLU	H	H	9.148
476	1	38	GLU	CA	C	54.61
477	1	38	GLU	CB	C	33.44
478	1	38	GLU	N	N	131.1
479	1	39	VAL	H	H	8.557
480	1	39	VAL	CA	C	61.12
481	1	39	VAL	CB	C	33.57
482	1	39	VAL	N	N	124.4
483	1	40	ILE	H	H	9.146
484	1	40	ILE	CA	C	60.08
485	1	40	ILE	CB	C	38.96
486	1	40	ILE	N	N	130.9
487	1	41	ASP	H	H	8.669
488	1	41	ASP	CA	C	52.41
489	1	41	ASP	CB	C	41.24
490	1	41	ASP	N	N	126.9
491	1	42	LEU	H	H	9.524
492	1	42	LEU	CA	C	56.29
493	1	42	LEU	CB	C	42.5
494	1	42	LEU	N	N	127.7
495	1	43	LYS	C	C	178.288
496	1	43	LYS	CA	C	58.538
497	1	43	LYS	CB	C	32.141
498	1	44	GLN	H	H	7.178
499	1	44	GLN	C	C	176.171
500	1	44	GLN	CA	C	56.563
501	1	44	GLN	CB	C	29.631
502	1	44	GLN	N	N	115.819
503	1	45	ASN	H	H	7.568
504	1	45	ASN	CA	C	51.2
505	1	45	ASN	CB	C	39.712
506	1	45	ASN	N	N	113.704
507	1	47	ARG	C	C	178.248
508	1	47	ARG	CA	C	58.357
509	1	47	ARG	CB	C	29.399
510	1	48	LEU	H	H	7.597
511	1	48	LEU	C	C	177.49
512	1	48	LEU	CA	C	56.209
513	1	48	LEU	CB	C	40.831
514	1	48	LEU	N	N	117.646
515	1	49	ALA	H	H	7.452
516	1	49	ALA	C	C	178.129
517	1	49	ALA	CA	C	54.119
518	1	49	ALA	CB	C	19.363
519	1	49	ALA	N	N	120.714
520	1	50	LYS	H	H	7.279
521	1	50	LYS	CA	C	58.841
522	1	50	LYS	CB	C	32.59
523	1	50	LYS	N	N	115.59
524	1	51	GLU	C	C	177.811
525	1	51	GLU	CA	C	59.855
526	1	51	GLU	CB	C	29.348
527	1	52	HIS	H	H	8.244
528	1	52	HIS	C	C	173.699
529	1	52	HIS	CA	C	55.04
530	1	52	HIS	CB	C	30.711
531	1	52	HIS	N	N	114.131
532	1	53	SER	H	H	7.613
533	1	53	SER	CA	C	58.232
534	1	53	SER	CB	C	60.893
535	1	53	SER	N	N	114.435
536	1	55	VAL	C	C	175.42
537	1	55	VAL	CA	C	62.287
538	1	56	ALA	H	H	8.264
539	1	56	ALA	CA	C	52.144
540	1	56	ALA	CB	C	19.397
541	1	56	ALA	N	N	127.194
542	1	58	PRO	C	C	176.446
543	1	58	PRO	CA	C	63.185
544	1	58	PRO	CB	C	34.268
545	1	59	THR	H	H	8.095
546	1	59	THR	C	C	171.389
547	1	59	THR	CA	C	63.968
548	1	59	THR	CB	C	73.609
549	1	59	THR	N	N	114.141
550	1	60	LEU	H	H	9.473
551	1	60	LEU	C	C	173.993
552	1	60	LEU	CA	C	53.287
553	1	60	LEU	CB	C	44.884
554	1	60	LEU	N	N	129.959
555	1	61	VAL	H	H	9.892
556	1	61	VAL	C	C	175.477
557	1	61	VAL	CA	C	60.848
558	1	61	VAL	CB	C	34.682
559	1	61	VAL	N	N	127.13
560	1	62	ARG	H	H	9.151
561	1	62	ARG	CA	C	55.195
562	1	62	ARG	CB	C	30.922
563	1	62	ARG	N	N	128.566
564	1	63	GLU	H	H	8.189
565	1	63	GLU	CA	C	58.45
566	1	63	GLU	CB	C	32.182
567	1	63	GLU	N	N	127.356
568	1	64	LEU	H	H	7.665
569	1	64	LEU	CA	C	52.064
570	1	64	LEU	CB	C	46.346
571	1	64	LEU	N	N	114.713
572	1	70	LYS	CA	C	55.403
573	1	70	LYS	CB	C	34.972
574	1	71	ILE	H	H	9.445
575	1	71	ILE	CA	C	60.882
576	1	71	ILE	CB	C	40.66
577	1	71	ILE	N	N	125.244
578	1	72	ILE	H	H	8.604
579	1	72	ILE	C	C	176.494
580	1	72	ILE	CA	C	60.965
581	1	72	ILE	CB	C	39.696
582	1	72	ILE	N	N	126.759
583	1	73	GLY	H	H	8.071
584	1	73	GLY	C	C	171.847
585	1	73	GLY	CA	C	44.434
586	1	73	GLY	N	N	112.653
587	1	74	ASP	H	H	7.997
588	1	74	ASP	CA	C	53.666
589	1	74	ASP	CB	C	40.66
590	1	74	ASP	N	N	115.426
591	1	75	LEU	H	H	8.546
592	1	75	LEU	C	C	177.672
593	1	75	LEU	CA	C	57.653
594	1	75	LEU	CB	C	43.363
595	1	75	LEU	N	N	122.787
596	1	76	SER	H	H	8.252
597	1	76	SER	CA	C	60.06
598	1	76	SER	CB	C	63.963
599	1	76	SER	N	N	113.492
600	1	77	ASP	C	C	175.545
601	1	77	ASP	CA	C	52.31
602	1	77	ASP	CB	C	39.372
603	1	78	LYS	H	H	8.007
604	1	78	LYS	C	C	177.473
605	1	78	LYS	CA	C	60.226
606	1	78	LYS	CB	C	32.62
607	1	78	LYS	N	N	124.957
608	1	79	GLU	H	H	8.331
609	1	79	GLU	C	C	178.864
610	1	79	GLU	CA	C	59.737
611	1	79	GLU	CB	C	28.896
612	1	79	GLU	N	N	117.113
613	1	80	GLN	H	H	7.541
614	1	80	GLN	CA	C	58.246
615	1	80	GLN	CB	C	28.562
616	1	80	GLN	N	N	118.09
617	1	81	VAL	CA	C	67.213
618	1	81	VAL	CB	C	31.868
619	1	82	LEU	H	H	8.317
620	1	82	LEU	C	C	179.533
621	1	82	LEU	CA	C	58.67
622	1	82	LEU	CB	C	41.432
623	1	82	LEU	N	N	118.21
624	1	83	VAL	H	H	7.973
625	1	83	VAL	C	C	178.301
626	1	83	VAL	CA	C	66.213
627	1	83	VAL	CB	C	31.643
628	1	83	VAL	N	N	117.342
629	1	84	ASN	H	H	7.693
630	1	84	ASN	CA	C	56.329
631	1	84	ASN	CB	C	40.482
632	1	84	ASN	N	N	118.588
633	1	85	LEU	H	H	8.058
634	1	85	LEU	C	C	178.25
635	1	85	LEU	CA	C	56.214
636	1	85	LEU	CB	C	42.23
637	1	85	LEU	N	N	116.928
638	1	86	LYS	H	H	7.711
639	1	86	LYS	C	C	176.744
640	1	86	LYS	CA	C	57.458
641	1	86	LYS	CB	C	32.9
642	1	86	LYS	N	N	118.943
643	1	87	MET	H	H	7.882
644	1	87	MET	C	C	176.206
645	1	87	MET	CA	C	56.371
646	1	87	MET	CB	C	33.14
647	1	87	MET	N	N	121.163
648	1	88	ASP	H	H	8.571
649	1	88	ASP	C	C	175.587
650	1	88	ASP	CA	C	55.138
651	1	88	ASP	CB	C	41.038
652	1	88	ASP	N	N	119.588
653	1	89	MET	H	H	7.986
654	1	89	MET	C	C	175.21
655	1	89	MET	CA	C	55.631
656	1	89	MET	CB	C	33.57
657	1	89	MET	N	N	118.808
658	1	90	GLU	H	H	7.987
659	1	90	GLU	CA	C	58.148
660	1	90	GLU	CB	C	31.148
661	1	90	GLU	N	N	126.472

Release date

2023-07-09

Citation

Predicting multiple conformations via sequence clustering and AlphaFold2
Wayment-Steele, H., Ojoawo, A.M., Otten, R., Apitz, J., Pitsawong, W., Homberger, M., Ovchinnikov, S., Colwell, L., Kern, D.
Nature (2023), 625, 832-839, PubMed 37956700 , DOI 10.1038/s41586-023-06832-9 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 31107 released on 2023-10-08
    Title Solution NMR structure of KaiB variant from Thermosynechococcus elongatus vestitus (KaiBTV-4)
  BMRB: 52017 released on 2023-07-09
    Title KaiBRS-3m

Related entities 1. KaiB-RS, : 1 : 46 entities Detail

Experiments performed 5 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	Wildtype KaiB-RS	[U-99% 13C; U-99% 15N]		1.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Wildtype KaiB-RS	[U-99% 13C; U-99% 15N]		1.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Wildtype KaiB-RS	[U-99% 13C; U-99% 15N]		1.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Wildtype KaiB-RS	[U-99% 13C; U-99% 15N]		1.8 mM

#	Name	Isotope labeling	Type	Concentration
1	Wildtype KaiB-RS	[U-99% 13C; U-99% 15N]		1.8 mM

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr52018_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr52018_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	336	98.9 (chain: 1, length: 90)
2	Assigned chemical shifts	assigned_chemical_shifts_2	OK	325	91.1 (chain: 1, length: 90)
1	Chemical shift references	chem_shift_reference_1	Warning	3	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 90, Sequence coverage: 98.9%
- Total number of assignments
  - ¹H chemical shifts: 83
  - ¹³C chemical shifts: 170
  - ¹⁵N chemical shifts: 83
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: assigned_chemical_shifts_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 90, Sequence coverage: 91.1%
- Total number of assignments
  - ¹H chemical shifts: 72
  - ¹³C chemical shifts: 181
  - ¹⁵N chemical shifts: 72
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	568	83	14.6
¹³C chemical shifts	418	170	40.7
¹⁵N chemical shifts	99	83	83.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	178	83	46.6
¹³C chemical shifts	180	88	48.9
¹⁵N chemical shifts	84	83	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	390	0	0.0
¹³C chemical shifts	238	82	34.5
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	68	0	0.0
¹³C chemical shifts	68	5	7.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	0	0.0
¹³C chemical shifts	10	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	568	72	12.7
¹³C chemical shifts	418	181	43.3
¹⁵N chemical shifts	99	72	72.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	178	72	40.4
¹³C chemical shifts	180	107	59.4
¹⁵N chemical shifts	84	72	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	390	0	0.0
¹³C chemical shifts	238	74	31.1
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	68	0	0.0
¹³C chemical shifts	68	5	7.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	0	0.0
¹³C chemical shifts	10	0	0.0

Keywords Computational biology and bioinformatics, NMR spectroscopy, Protein folding, Protein structure predictions, Structural biology

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BMRB: 52018

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. KaiB-RS, : 1 : 46 entities Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 4 contents Detail