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Found 1 Document (0.672 seconds)

BMRB: 36180

5ZPV

Solution Structure of Thioredoxin-Like Effector Protein (TRX3) from Edwardsiella tarda

Authors

Sayed, A.M., Mok, Y.K.

Assembly

Thioredoxin (H-type,TRX-H)

Entity

1. Thioredoxin (H-type,TRX-H) (polymer, Thiol state: all free), 122 monomers, 13675.15 Da Detail

MHHHHHHSSG LVPRGSQAAS VEPYSDAAFT QAQASGAPVL VDVYADWCPV CKRQERELTP LFAQPAQRDL RVFKVNFDTQ KAALQQFRVS QQSTLILYRN GQEVRRSIGE TSPSALSDFL TR

Formula weight

13675.15 Da

Source organism

Edwardsiella tarda EIB202

Exptl. method

solution NMR

Refine. method

Data set

assigned_chemical_shifts

Chemcal Shifts

¹H: 347, ¹³C: 188, ¹⁵N: 95 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val
1	1	17	GLN	HA	H	4.311
2	1	17	GLN	HB2	H	1.759
3	1	17	GLN	HB3	H	1.759
4	1	17	GLN	CA	C	55.730
5	1	17	GLN	CB	C	29.950
6	1	18	ALA	H	H	7.926
7	1	18	ALA	HA	H	4.440
8	1	18	ALA	HB1	H	1.300
9	1	18	ALA	HB2	H	1.300
10	1	18	ALA	HB3	H	1.300
11	1	18	ALA	CA	C	51.600
12	1	18	ALA	CB	C	21.660
13	1	18	ALA	N	N	123.500
14	1	19	ALA	H	H	7.874
15	1	19	ALA	HA	H	4.298
16	1	19	ALA	HB1	H	1.162
17	1	19	ALA	HB2	H	1.162
18	1	19	ALA	HB3	H	1.162
19	1	19	ALA	CA	C	52.940
20	1	19	ALA	CB	C	19.530
21	1	19	ALA	N	N	121.800
22	1	20	SER	H	H	7.846
23	1	20	SER	HA	H	4.384
24	1	20	SER	HB2	H	3.732
25	1	20	SER	HB3	H	3.732
26	1	20	SER	CA	C	57.380
27	1	20	SER	CB	C	64.290
28	1	20	SER	N	N	115.900
29	1	21	VAL	H	H	8.116
30	1	21	VAL	HA	H	4.315
31	1	21	VAL	HB	H	1.780
32	1	21	VAL	CA	C	61.600
33	1	21	VAL	CB	C	33.330
34	1	21	VAL	N	N	125.200
35	1	22	GLU	H	H	8.471
36	1	22	GLU	HA	H	4.356
37	1	22	GLU	CA	C	53.230
38	1	22	GLU	N	N	126.800
39	1	24	TYR	H	H	8.909
40	1	24	TYR	HA	H	3.935
41	1	24	TYR	CA	C	56.130
42	1	24	TYR	CB	C	40.060
43	1	24	TYR	N	N	122.500
44	1	25	SER	HA	H	4.036
45	1	25	SER	HB2	H	3.867
46	1	25	SER	HB3	H	3.867
47	1	25	SER	CA	C	57.400
48	1	25	SER	CB	C	65.750
49	1	25	SER	N	N	118.500
50	1	26	ASP	H	H	8.711
51	1	26	ASP	HA	H	4.249
52	1	26	ASP	HB2	H	2.578
53	1	26	ASP	HB3	H	2.578
54	1	26	ASP	CA	C	56.440
55	1	26	ASP	CB	C	40.890
56	1	26	ASP	N	N	123.000
57	1	27	ALA	H	H	8.725
58	1	27	ALA	HA	H	3.981
59	1	27	ALA	HB1	H	1.329
60	1	27	ALA	HB2	H	1.329
61	1	27	ALA	HB3	H	1.329
62	1	27	ALA	CA	C	55.380
63	1	27	ALA	CB	C	18.390
64	1	27	ALA	N	N	121.300
65	1	28	ALA	H	H	7.164
66	1	28	ALA	HA	H	4.109
67	1	28	ALA	CA	C	54.740
68	1	28	ALA	CB	C	19.820
69	1	28	ALA	N	N	119.200
70	1	30	THR	H	H	8.319
71	1	30	THR	HA	H	4.122
72	1	30	THR	HB	H	3.503
73	1	30	THR	CA	C	66.840
74	1	30	THR	CB	C	68.500
75	1	30	THR	N	N	114.936
76	1	31	GLN	H	H	7.553
77	1	31	GLN	HA	H	3.975
78	1	31	GLN	HB2	H	2.057
79	1	31	GLN	HB3	H	2.057
80	1	31	GLN	CA	C	59.020
81	1	31	GLN	CB	C	28.460
82	1	31	GLN	N	N	121.025
83	1	32	ALA	H	H	8.103
84	1	32	ALA	HA	H	3.953
85	1	32	ALA	HB1	H	1.541
86	1	32	ALA	HB2	H	1.541
87	1	32	ALA	HB3	H	1.541
88	1	32	ALA	CA	C	55.280
89	1	32	ALA	CB	C	19.160
90	1	32	ALA	N	N	122.700
91	1	33	GLN	H	H	8.350
92	1	33	GLN	HA	H	4.093
93	1	33	GLN	HB2	H	1.226
94	1	33	GLN	HB3	H	1.226
95	1	33	GLN	CA	C	58.440
96	1	33	GLN	CB	C	29.550
97	1	33	GLN	N	N	118.100
98	1	34	ALA	H	H	7.515
99	1	34	ALA	HA	H	4.157
100	1	34	ALA	HB1	H	1.397
101	1	34	ALA	HB2	H	1.397
102	1	34	ALA	HB3	H	1.397
103	1	34	ALA	CA	C	53.520
104	1	34	ALA	CB	C	18.610
105	1	34	ALA	N	N	120.200
106	1	35	SER	H	H	7.569
107	1	35	SER	HA	H	4.283
108	1	35	SER	HB2	H	4.059
109	1	35	SER	HB3	H	4.059
110	1	35	SER	CA	C	60.180
111	1	35	SER	CB	C	64.820
112	1	35	SER	N	N	112.500
113	1	36	GLY	H	H	7.793
114	1	36	GLY	HA2	H	3.672
115	1	36	GLY	HA3	H	3.672
116	1	36	GLY	CA	C	45.890
117	1	36	GLY	N	N	111.416
118	1	37	ALA	H	H	7.545
119	1	37	ALA	HA	H	4.487
120	1	37	ALA	CA	C	50.860
121	1	37	ALA	CB	C	18.410
122	1	37	ALA	N	N	125.160
123	1	39	VAL	H	H	8.667
124	1	39	VAL	HA	H	5.195
125	1	39	VAL	HB	H	1.922
126	1	39	VAL	CA	C	60.130
127	1	39	VAL	CB	C	36.990
128	1	39	VAL	N	N	122.300
129	1	40	LEU	H	H	9.296
130	1	40	LEU	HA	H	5.714
131	1	40	LEU	HB2	H	2.002
132	1	40	LEU	HB3	H	2.002
133	1	40	LEU	CA	C	52.430
134	1	40	LEU	CB	C	46.490
135	1	40	LEU	N	N	127.930
136	1	41	VAL	H	H	9.829
137	1	41	VAL	HA	H	4.628
138	1	41	VAL	HB	H	1.828
139	1	41	VAL	CA	C	62.250
140	1	41	VAL	CB	C	33.210
141	1	41	VAL	N	N	128.200
142	1	42	ASP	H	H	8.815
143	1	42	ASP	HA	H	5.143
144	1	42	ASP	HB2	H	2.106
145	1	42	ASP	HB3	H	2.106
146	1	42	ASP	CA	C	50.840
147	1	42	ASP	CB	C	40.090
148	1	42	ASP	N	N	126.200
149	1	43	VAL	H	H	8.927
150	1	43	VAL	HA	H	4.875
151	1	43	VAL	HB	H	2.260
152	1	43	VAL	CA	C	61.970
153	1	43	VAL	CB	C	30.920
154	1	43	VAL	N	N	128.853
155	1	44	TYR	H	H	9.039
156	1	44	TYR	HA	H	5.394
157	1	44	TYR	HB2	H	2.617
158	1	44	TYR	HB3	H	2.617
159	1	44	TYR	CA	C	55.530
160	1	44	TYR	CB	C	43.590
161	1	44	TYR	N	N	129.100
162	1	45	ALA	H	H	7.077
163	1	45	ALA	HA	H	4.412
164	1	45	ALA	CA	C	50.360
165	1	45	ALA	CB	C	21.900
166	1	45	ALA	N	N	121.800
167	1	46	ASP	H	H	9.346
168	1	46	ASP	HA	H	4.386
169	1	46	ASP	CA	C	57.140
170	1	46	ASP	CB	C	41.550
171	1	46	ASP	N	N	122.900
172	1	48	CYS	H	H	6.474
173	1	48	CYS	HA	H	4.324
174	1	48	CYS	CA	C	57.070
175	1	48	CYS	CB	C	30.480
176	1	48	CYS	N	N	126.845
177	1	50	VAL	H	H	9.229
178	1	50	VAL	HA	H	3.545
179	1	50	VAL	HB	H	2.167
180	1	50	VAL	CA	C	66.910
181	1	50	VAL	CB	C	32.070
182	1	50	VAL	N	N	127.700
183	1	51	CYS	H	H	9.245
184	1	51	CYS	HA	H	4.196
185	1	51	CYS	HB2	H	2.906
186	1	51	CYS	HB3	H	2.906
187	1	51	CYS	CA	C	63.080
188	1	51	CYS	CB	C	28.390
189	1	51	CYS	N	N	125.500
190	1	52	LYS	H	H	8.025
191	1	52	LYS	HA	H	3.993
192	1	52	LYS	HB2	H	1.686
193	1	52	LYS	HB3	H	1.686
194	1	52	LYS	CA	C	59.590
195	1	52	LYS	CB	C	32.070
196	1	52	LYS	N	N	120.400
197	1	53	ARG	H	H	7.432
198	1	53	ARG	HA	H	4.017
199	1	53	ARG	HB2	H	2.001
200	1	53	ARG	HB3	H	2.001
201	1	53	ARG	CA	C	59.070
202	1	53	ARG	CB	C	29.840
203	1	53	ARG	N	N	120.600
204	1	54	GLN	H	H	8.670
205	1	54	GLN	HA	H	3.521
206	1	54	GLN	HB2	H	1.629
207	1	54	GLN	HB3	H	1.629
208	1	54	GLN	CA	C	60.400
209	1	54	GLN	CB	C	29.040
210	1	54	GLN	N	N	118.223
211	1	55	GLU	H	H	8.267
212	1	55	GLU	HA	H	3.770
213	1	55	GLU	HB2	H	2.013
214	1	55	GLU	HB3	H	2.013
215	1	55	GLU	CA	C	59.870
216	1	55	GLU	CB	C	29.560
217	1	55	GLU	N	N	118.600
218	1	56	ARG	H	H	7.338
219	1	56	ARG	HA	H	3.989
220	1	56	ARG	HB2	H	1.740
221	1	56	ARG	HB3	H	1.740
222	1	56	ARG	CA	C	58.930
223	1	56	ARG	CB	C	30.360
224	1	56	ARG	N	N	118.360
225	1	57	GLU	H	H	7.588
226	1	57	GLU	HA	H	4.552
227	1	57	GLU	HB2	H	1.485
228	1	57	GLU	HB3	H	1.485
229	1	57	GLU	CA	C	56.100
230	1	57	GLU	CB	C	30.150
231	1	57	GLU	N	N	114.941
232	1	58	LEU	H	H	8.713
233	1	58	LEU	HA	H	3.589
234	1	58	LEU	HB2	H	1.474
235	1	58	LEU	HB3	H	1.474
236	1	58	LEU	CA	C	56.780
237	1	58	LEU	CB	C	41.790
238	1	58	LEU	N	N	118.379
239	1	59	THR	H	H	7.315
240	1	59	THR	HA	H	4.274
241	1	59	THR	CA	C	67.820
242	1	59	THR	CB	C	70.180
243	1	59	THR	N	N	112.785
244	1	61	LEU	H	H	6.614
245	1	61	LEU	HA	H	3.988
246	1	61	LEU	HB2	H	1.810
247	1	61	LEU	HB3	H	1.810
248	1	61	LEU	CA	C	57.630
249	1	61	LEU	CB	C	40.900
250	1	61	LEU	N	N	117.800
251	1	62	PHE	H	H	8.101
252	1	62	PHE	HA	H	4.407
253	1	62	PHE	HB2	H	3.340
254	1	62	PHE	HB3	H	3.340
255	1	62	PHE	CA	C	55.710
256	1	62	PHE	CB	C	37.150
257	1	62	PHE	N	N	117.870
258	1	63	ALA	H	H	7.130
259	1	63	ALA	HA	H	4.462
260	1	63	ALA	HB1	H	1.476
261	1	63	ALA	HB2	H	1.476
262	1	63	ALA	HB3	H	1.476
263	1	63	ALA	CA	C	51.980
264	1	63	ALA	CB	C	19.450
265	1	63	ALA	N	N	118.365
266	1	64	GLN	H	H	7.315
267	1	64	GLN	HA	H	4.553
268	1	64	GLN	CA	C	54.260
269	1	64	GLN	CB	C	27.950
270	1	64	GLN	N	N	119.123
271	1	66	ALA	H	H	8.288
272	1	66	ALA	HA	H	4.119
273	1	66	ALA	HB1	H	1.398
274	1	66	ALA	HB2	H	1.398
275	1	66	ALA	HB3	H	1.398
276	1	66	ALA	CA	C	54.610
277	1	66	ALA	CB	C	18.690
278	1	66	ALA	N	N	118.264
279	1	67	GLN	H	H	7.821
280	1	67	GLN	HA	H	4.604
281	1	67	GLN	HB2	H	2.212
282	1	67	GLN	HB3	H	2.212
283	1	67	GLN	CA	C	55.340
284	1	67	GLN	CB	C	29.880
285	1	67	GLN	N	N	114.883
286	1	68	ARG	H	H	7.296
287	1	68	ARG	HA	H	3.805
288	1	68	ARG	HB2	H	1.721
289	1	68	ARG	HB3	H	1.721
290	1	68	ARG	CA	C	59.250
291	1	68	ARG	CB	C	30.040
292	1	68	ARG	N	N	117.885
293	1	69	ASP	H	H	8.134
294	1	69	ASP	HA	H	4.611
295	1	69	ASP	HB2	H	2.564
296	1	69	ASP	HB3	H	2.564
297	1	69	ASP	CA	C	53.970
298	1	69	ASP	CB	C	41.120
299	1	69	ASP	N	N	115.809
300	1	70	LEU	H	H	7.400
301	1	70	LEU	HA	H	4.140
302	1	70	LEU	HB2	H	1.416
303	1	70	LEU	HB3	H	1.416
304	1	70	LEU	CA	C	56.010
305	1	70	LEU	CB	C	43.090
306	1	70	LEU	N	N	121.872
307	1	71	ARG	H	H	8.333
308	1	71	ARG	HA	H	4.529
309	1	71	ARG	HB2	H	1.576
310	1	71	ARG	HB3	H	1.576
311	1	71	ARG	CA	C	53.100
312	1	71	ARG	CB	C	29.800
313	1	71	ARG	N	N	127.280
314	1	72	VAL	H	H	8.350
315	1	72	VAL	HA	H	4.904
316	1	72	VAL	HB	H	1.940
317	1	72	VAL	CA	C	60.640
318	1	72	VAL	CB	C	32.690
319	1	72	VAL	N	N	123.196
320	1	73	PHE	H	H	9.316
321	1	73	PHE	HA	H	5.628
322	1	73	PHE	HB2	H	2.895
323	1	73	PHE	HB3	H	2.895
324	1	73	PHE	CA	C	56.180
325	1	73	PHE	CB	C	43.290
326	1	73	PHE	N	N	124.331
327	1	74	LYS	H	H	8.868
328	1	74	LYS	HA	H	5.183
329	1	74	LYS	HB2	H	1.335
330	1	74	LYS	HB3	H	1.335
331	1	74	LYS	CA	C	55.090
332	1	74	LYS	CB	C	32.330
333	1	74	LYS	N	N	122.728
334	1	75	VAL	H	H	9.384
335	1	75	VAL	HA	H	4.522
336	1	75	VAL	HB	H	1.815
337	1	75	VAL	CA	C	60.240
338	1	75	VAL	CB	C	33.890
339	1	75	VAL	N	N	129.229
340	1	76	ASN	H	H	9.335
341	1	76	ASN	HA	H	3.855
342	1	76	ASN	HB2	H	2.613
343	1	76	ASN	HB3	H	2.613
344	1	76	ASN	CA	C	53.390
345	1	76	ASN	CB	C	38.580
346	1	76	ASN	N	N	127.442
347	1	77	PHE	H	H	9.109
348	1	77	PHE	HA	H	3.741
349	1	77	PHE	HB2	H	2.511
350	1	77	PHE	HB3	H	2.511
351	1	77	PHE	CA	C	60.700
352	1	77	PHE	CB	C	42.030
353	1	77	PHE	N	N	127.000
354	1	78	ASP	H	H	8.117
355	1	78	ASP	HA	H	4.442
356	1	78	ASP	HB2	H	2.703
357	1	78	ASP	HB3	H	2.703
358	1	78	ASP	CA	C	56.750
359	1	78	ASP	CB	C	42.200
360	1	78	ASP	N	N	112.000
361	1	79	THR	H	H	7.241
362	1	79	THR	HA	H	4.580
363	1	79	THR	HB	H	4.386
364	1	79	THR	CA	C	62.050
365	1	79	THR	CB	C	69.420
366	1	79	THR	N	N	105.976
367	1	81	LYS	H	H	7.520
368	1	81	LYS	HA	H	3.682
369	1	81	LYS	HB2	H	1.690
370	1	81	LYS	HB3	H	1.690
371	1	81	LYS	CA	C	58.220
372	1	81	LYS	CB	C	31.680
373	1	81	LYS	N	N	116.454
374	1	82	ALA	H	H	8.616
375	1	82	ALA	HA	H	4.106
376	1	82	ALA	HB1	H	1.393
377	1	82	ALA	HB2	H	1.393
378	1	82	ALA	HB3	H	1.393
379	1	82	ALA	CA	C	55.170
380	1	82	ALA	CB	C	17.780
381	1	82	ALA	N	N	122.152
382	1	83	ALA	H	H	7.500
383	1	83	ALA	HA	H	3.897
384	1	83	ALA	HB1	H	1.039
385	1	83	ALA	HB2	H	1.039
386	1	83	ALA	HB3	H	1.039
387	1	83	ALA	CA	C	54.260
388	1	83	ALA	CB	C	18.300
389	1	83	ALA	N	N	121.109
390	1	84	LEU	H	H	7.394
391	1	84	LEU	HA	H	3.813
392	1	84	LEU	HB2	H	1.880
393	1	84	LEU	HB3	H	1.880
394	1	84	LEU	CA	C	58.150
395	1	84	LEU	CB	C	39.820
396	1	84	LEU	N	N	114.052
397	1	85	GLN	H	H	7.329
398	1	85	GLN	HA	H	4.086
399	1	85	GLN	HB2	H	2.112
400	1	85	GLN	HB3	H	2.112
401	1	85	GLN	CA	C	58.760
402	1	85	GLN	CB	C	28.360
403	1	85	GLN	N	N	116.666
404	1	86	GLN	H	H	7.654
405	1	86	GLN	HA	H	3.872
406	1	86	GLN	HB2	H	1.555
407	1	86	GLN	HB3	H	1.555
408	1	86	GLN	CA	C	58.450
409	1	86	GLN	CB	C	28.230
410	1	86	GLN	N	N	119.849
411	1	87	PHE	H	H	7.571
412	1	87	PHE	HA	H	4.544
413	1	87	PHE	HB2	H	2.368
414	1	87	PHE	HB3	H	2.368
415	1	87	PHE	CA	C	58.680
416	1	87	PHE	CB	C	39.980
417	1	87	PHE	N	N	114.725
418	1	88	ARG	H	H	7.844
419	1	88	ARG	HA	H	3.914
420	1	88	ARG	HB2	H	1.864
421	1	88	ARG	HB3	H	1.864
422	1	88	ARG	CA	C	57.100
423	1	88	ARG	CB	C	26.860
424	1	88	ARG	N	N	118.800
425	1	89	VAL	H	H	8.046
426	1	89	VAL	HA	H	4.261
427	1	89	VAL	HB	H	1.856
428	1	89	VAL	CA	C	61.680
429	1	89	VAL	CB	C	34.660
430	1	89	VAL	N	N	118.500
431	1	90	SER	H	H	8.387
432	1	90	SER	HA	H	4.753
433	1	90	SER	HB2	H	3.809
434	1	90	SER	HB3	H	3.809
435	1	90	SER	CA	C	57.890
436	1	90	SER	CB	C	64.990
437	1	90	SER	N	N	118.600
438	1	91	GLN	H	H	7.598
439	1	91	GLN	HA	H	4.336
440	1	91	GLN	HB2	H	1.739
441	1	91	GLN	HB3	H	1.739
442	1	91	GLN	CA	C	55.840
443	1	91	GLN	CB	C	33.310
444	1	91	GLN	N	N	119.800
445	1	92	GLN	H	H	8.276
446	1	92	GLN	HA	H	3.830
447	1	92	GLN	CA	C	55.210
448	1	92	GLN	CB	C	25.110
449	1	92	GLN	N	N	125.400
450	1	93	SER	H	H	9.139
451	1	93	SER	HA	H	4.540
452	1	93	SER	HB2	H	3.632
453	1	93	SER	HB3	H	3.632
454	1	93	SER	CA	C	60.900
455	1	93	SER	CB	C	64.000
456	1	93	SER	N	N	119.900
457	1	94	THR	H	H	7.022
458	1	94	THR	HA	H	4.958
459	1	94	THR	HB	H	3.823
460	1	94	THR	CA	C	63.450
461	1	94	THR	CB	C	69.720
462	1	94	THR	N	N	119.000
463	1	95	LEU	H	H	8.979
464	1	95	LEU	HA	H	5.457
465	1	95	LEU	HB2	H	1.309
466	1	95	LEU	HB3	H	1.309
467	1	95	LEU	CA	C	52.490
468	1	95	LEU	CB	C	45.030
469	1	95	LEU	N	N	126.700
470	1	96	ILE	H	H	9.151
471	1	96	ILE	HA	H	4.650
472	1	96	ILE	HB	H	1.627
473	1	96	ILE	CA	C	61.410
474	1	96	ILE	CB	C	41.970
475	1	96	ILE	N	N	120.682
476	1	97	LEU	H	H	8.875
477	1	97	LEU	HA	H	5.424
478	1	97	LEU	HB2	H	1.459
479	1	97	LEU	HB3	H	1.459
480	1	97	LEU	CA	C	53.740
481	1	97	LEU	CB	C	46.110
482	1	97	LEU	N	N	128.848
483	1	98	TYR	H	H	10.113
484	1	98	TYR	HA	H	5.245
485	1	98	TYR	HB2	H	2.695
486	1	98	TYR	HB3	H	2.695
487	1	98	TYR	CA	C	56.840
488	1	98	TYR	CB	C	42.310
489	1	98	TYR	N	N	127.176
490	1	99	ARG	H	H	8.560
491	1	99	ARG	HA	H	4.580
492	1	99	ARG	HB2	H	1.691
493	1	99	ARG	HB3	H	1.691
494	1	99	ARG	CA	C	56.420
495	1	99	ARG	CB	C	34.640
496	1	99	ARG	N	N	116.400
497	1	100	ASN	H	H	9.327
498	1	100	ASN	HA	H	4.419
499	1	100	ASN	HB2	H	2.711
500	1	100	ASN	HB3	H	2.711
501	1	100	ASN	CA	C	54.690
502	1	100	ASN	CB	C	37.930
503	1	100	ASN	N	N	122.726
504	1	101	GLY	H	H	9.332
505	1	101	GLY	HA2	H	3.618
506	1	101	GLY	HA3	H	3.618
507	1	101	GLY	CA	C	45.640
508	1	101	GLY	N	N	104.391
509	1	102	GLN	H	H	7.911
510	1	102	GLN	HA	H	4.834
511	1	102	GLN	HB2	H	1.941
512	1	102	GLN	HB3	H	1.941
513	1	102	GLN	CA	C	53.870
514	1	102	GLN	CB	C	32.320
515	1	102	GLN	N	N	118.625
516	1	103	GLU	H	H	9.020
517	1	103	GLU	HA	H	3.533
518	1	103	GLU	HB2	H	1.662
519	1	103	GLU	HB3	H	1.662
520	1	103	GLU	CA	C	57.830
521	1	103	GLU	CB	C	29.310
522	1	103	GLU	N	N	125.500
523	1	104	VAL	H	H	9.686
524	1	104	VAL	HA	H	4.069
525	1	104	VAL	HB	H	1.700
526	1	104	VAL	CA	C	63.340
527	1	104	VAL	CB	C	34.170
528	1	104	VAL	N	N	128.200
529	1	105	ARG	H	H	7.394
530	1	105	ARG	HA	H	4.820
531	1	105	ARG	HB2	H	1.634
532	1	105	ARG	HB3	H	1.634
533	1	105	ARG	CA	C	55.300
534	1	105	ARG	CB	C	32.180
535	1	105	ARG	N	N	113.004
536	1	106	ARG	H	H	8.607
537	1	106	ARG	HB2	H	1.629
538	1	106	ARG	HB3	H	1.629
539	1	106	ARG	CA	C	54.700
540	1	106	ARG	CB	C	35.850
541	1	106	ARG	N	N	115.695
542	1	107	SER	H	H	9.136
543	1	107	SER	HA	H	4.696
544	1	107	SER	HB2	H	3.120
545	1	107	SER	HB3	H	3.120
546	1	107	SER	CA	C	56.620
547	1	107	SER	CB	C	65.730
548	1	107	SER	N	N	116.328
549	1	108	ILE	H	H	8.734
550	1	108	ILE	HA	H	4.389
551	1	108	ILE	HB	H	1.530
552	1	108	ILE	CA	C	61.600
553	1	108	ILE	CB	C	40.940
554	1	108	ILE	N	N	125.145
555	1	109	GLY	H	H	7.917
556	1	109	GLY	HA2	H	3.770
557	1	109	GLY	HA3	H	3.770
558	1	109	GLY	CA	C	46.450
559	1	109	GLY	N	N	114.663
560	1	110	GLU	H	H	8.703
561	1	110	GLU	HA	H	4.033
562	1	110	GLU	CA	C	57.040
563	1	110	GLU	CB	C	30.750
564	1	110	GLU	N	N	121.816
565	1	112	SER	H	H	8.942
566	1	112	SER	HA	H	4.802
567	1	112	SER	CA	C	55.390
568	1	112	SER	CB	C	62.890
569	1	112	SER	N	N	120.700
570	1	114	SER	H	H	7.834
571	1	114	SER	HA	H	4.156
572	1	114	SER	HB2	H	3.808
573	1	114	SER	HB3	H	3.808
574	1	114	SER	CA	C	60.790
575	1	114	SER	CB	C	61.940
576	1	114	SER	N	N	113.046
577	1	115	ALA	H	H	7.274
578	1	115	ALA	HA	H	4.212
579	1	115	ALA	HB1	H	1.397
580	1	115	ALA	HB2	H	1.397
581	1	115	ALA	HB3	H	1.397
582	1	115	ALA	CA	C	54.700
583	1	115	ALA	CB	C	19.210
584	1	115	ALA	N	N	125.687
585	1	116	LEU	H	H	8.527
586	1	116	LEU	HA	H	3.906
587	1	116	LEU	HB2	H	1.663
588	1	116	LEU	HB3	H	1.663
589	1	116	LEU	CA	C	57.820
590	1	116	LEU	CB	C	41.840
591	1	116	LEU	N	N	120.213
592	1	117	SER	H	H	7.858
593	1	117	SER	HA	H	4.009
594	1	117	SER	HB2	H	3.931
595	1	117	SER	HB3	H	3.931
596	1	117	SER	CA	C	61.810
597	1	117	SER	CB	C	62.520
598	1	117	SER	N	N	112.200
599	1	118	ASP	H	H	8.046
600	1	118	ASP	HA	H	4.242
601	1	118	ASP	HB2	H	2.572
602	1	118	ASP	HB3	H	2.572
603	1	118	ASP	CA	C	57.670
604	1	118	ASP	CB	C	40.970
605	1	118	ASP	N	N	121.683
606	1	119	PHE	H	H	8.231
607	1	119	PHE	HA	H	3.981
608	1	119	PHE	HB2	H	3.300
609	1	119	PHE	HB3	H	3.300
610	1	119	PHE	CA	C	61.380
611	1	119	PHE	CB	C	39.250
612	1	119	PHE	N	N	120.060
613	1	120	LEU	H	H	7.511
614	1	120	LEU	HA	H	4.120
615	1	120	LEU	HB2	H	1.871
616	1	120	LEU	HB3	H	1.871
617	1	120	LEU	CA	C	56.380
618	1	120	LEU	CB	C	43.570
619	1	120	LEU	N	N	113.658
620	1	121	THR	H	H	7.782
621	1	121	THR	HA	H	4.310
622	1	121	THR	HB	H	4.149
623	1	121	THR	CA	C	63.520
624	1	121	THR	CB	C	71.110
625	1	121	THR	N	N	108.066
626	1	122	ARG	H	H	7.975
627	1	122	ARG	HA	H	3.990
628	1	122	ARG	CA	C	58.990
629	1	122	ARG	CB	C	30.280
630	1	122	ARG	N	N	128.464

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.24 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.03 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 5ZPV, Strand ID: A Detail

Release date

2018-05-26

Citation

Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-κB
Sayed, A., Chakraborty, S., Leung, K.Y., Sugii, S., Mok, Y.K.
Int. J. Biol. Macromol. (2020), 148, 89-101, PubMed 31945434 , DOI 10.1016/j.ijbiomac.2020.01.114 , Abstract

Related entities 1. Thioredoxin (H-type,TRX-H), : 1 : 1 : 81 entities Detail

Experiments performed 5 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	TRX3	[U-13C; U-15N]	protein	0.5 mM
2	phosphate	natural abundance	buffer	20 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

#	Name	Isotope labeling	Type	Concentration
1	TRX3	[U-13C; U-15N]	protein	0.5 mM
2	phosphate	natural abundance	buffer	20 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

#	Name	Isotope labeling	Type	Concentration
1	TRX3	[U-13C; U-15N]	protein	0.5 mM
2	phosphate	natural abundance	buffer	20 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

#	Name	Isotope labeling	Type	Concentration
1	TRX3	[U-13C; U-15N]	protein	0.5 mM
2	phosphate	natural abundance	buffer	20 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

#	Name	Isotope labeling	Type	Concentration
1	TRX3	[U-13C; U-15N]	protein	0.5 mM
2	phosphate	natural abundance	buffer	20 mM
3	H2O	natural abundance	solvent	90 %
4	D2O	[U-2H]	solvent	10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36180_5zpv.nef
Input source #2: Coordindates	5zpv.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

------------------------10--------20--------30--------40--------50--------60--------70--------80----
MHHHHHHSSGLVPRGSQAASVEPYSDAAFTQAQASGAPVLVDVYADWCPVCKRQERELTPLFAQPAQRDLRVFKVNFDTQKAALQQFRVSQQSTLILYRN
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MHHHHHHSSGLVPRGSQAASVEPYSDAAFTQAQASGAPVLVDVYADWCPVCKRQERELTPLFAQPAQRDLRVFKVNFDTQKAALQQFRVSQQSTLILYRN
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

----90-------100------
GQEVRRSIGETSPSALSDFLTR
||||||||||||||||||||||
GQEVRRSIGETSPSALSDFLTR
-------110-------120--

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	122	0	0	100.0

Content subtype: combined_36180_5zpv.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	610		78.7 (chain: A, length: 122)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	919 (1)	noe	83.6 (chain: A, length: 122)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	168 (168)	.	82.8 (chain: A, length: 122)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 122, Sequence coverage: 78.7%
- Total number of assignments
  - ¹H chemical shifts: 327
  - ¹³C chemical shifts: 188
  - ¹⁵N chemical shifts: 95
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	730	327	44.8
¹³C chemical shifts	544	188	34.6
¹⁵N chemical shifts	140	95	67.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	242	192	79.3
¹³C chemical shifts	244	96	39.3
¹⁵N chemical shifts	115	95	82.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	488	135	27.7
¹³C chemical shifts	300	92	30.7
¹⁵N chemical shifts	25	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	64	10	15.6
¹³C chemical shifts	64	13	20.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	0	0.0
¹³C chemical shifts	59	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 122, Sequence coverage: 83.6%
- Total number of restraints: 919
- Weight of restraints: 1.0 (919)
- Potential type of restraints: upper-bound-parabolic (919)
- Range of distance target values: 2.9, 7.4 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 122, Sequence coverage: 82.8%
- Total number of restraints: 168
- Total number of restraints per polymer type: 168
- Weight of restraints: 1.0 (168)
- Potential type of restraints: square-well-parabolic (168)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Inhibitor, OXIDOREDUCTASE, Redox activity, active site, reactivity, thiol-disulfide oxidoreductase

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BMRB: 36180

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Thioredoxin (H-type,TRX-H), : 1 : 1 : 81 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 4 contents Detail