BMRBj - BMREntryMaster

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err	Ambig. code
1	1	1	LYS	HA	H	4.17	0.01	1
2	1	1	LYS	HB2	H	1.98	0.01	1
3	1	1	LYS	HB3	H	1.98	0.01	1
4	1	1	LYS	HG2	H	1.55	0.01	1
5	1	1	LYS	HG3	H	1.55	0.01	1
6	1	1	LYS	HD2	H	1.79	0.01	1
7	1	1	LYS	HD3	H	1.79	0.01	1
8	1	1	LYS	HE2	H	3.05	0.01	1
9	1	1	LYS	HE3	H	3.05	0.01	1
10	1	2	THR	H	H	8.57	0.01	1
11	1	2	THR	HA	H	4.56	0.01	1
12	1	2	THR	HB	H	4.34	0.01	1
13	1	2	THR	HG21	H	1.29	0.01	1
14	1	2	THR	HG22	H	1.29	0.01	1
15	1	2	THR	HG23	H	1.29	0.01	1
16	1	3	LYS	H	H	8.47	0.01	1
17	1	3	LYS	HA	H	4.35	0.01	1
18	1	3	LYS	HB2	H	1.92	0.01	2
19	1	3	LYS	HB3	H	1.85	0.01	2
20	1	3	LYS	HG2	H	1.52	0.01	1
21	1	3	LYS	HG3	H	1.52	0.01	1
22	1	3	LYS	HD2	H	1.76	0.01	1
23	1	3	LYS	HD3	H	1.76	0.01	1
24	1	3	LYS	HE2	H	3.04	0.01	1
25	1	3	LYS	HE3	H	3.04	0.01	1
26	1	4	LEU	H	H	7.97	0.01	1
27	1	4	LEU	HA	H	4.45	0.01	1
28	1	4	LEU	HB2	H	1.70	0.01	2
29	1	4	LEU	HB3	H	1.67	0.01	2
30	1	4	LEU	HG	H	1.68	0.01	1
31	1	4	LEU	HD11	H	0.95	0.01	2
32	1	4	LEU	HD12	H	0.95	0.01	2
33	1	4	LEU	HD13	H	0.95	0.01	2
34	1	4	LEU	HD21	H	0.91	0.01	2
35	1	4	LEU	HD22	H	0.91	0.01	2
36	1	4	LEU	HD23	H	0.91	0.01	2
37	1	5	THR	H	H	7.93	0.01	1
38	1	5	THR	HA	H	4.31	0.01	1
39	1	5	THR	HB	H	4.55	0.01	1
40	1	5	THR	HG21	H	1.37	0.01	1
41	1	5	THR	HG22	H	1.37	0.01	1
42	1	5	THR	HG23	H	1.37	0.01	1
43	1	6	GLU	H	H	8.45	0.01	1
44	1	6	GLU	HA	H	4.12	0.01	1
45	1	6	GLU	HB2	H	2.20	0.01	1
46	1	6	GLU	HB3	H	2.20	0.01	1
47	1	6	GLU	HG2	H	2.53	0.01	1
48	1	6	GLU	HG3	H	2.53	0.01	1
49	1	7	GLU	H	H	8.35	0.01	1
50	1	7	GLU	HA	H	4.18	0.01	1
51	1	7	GLU	HB2	H	2.25	0.01	2
52	1	7	GLU	HB3	H	2.13	0.01	2
53	1	7	GLU	HG2	H	2.56	0.01	2
54	1	7	GLU	HG3	H	2.52	0.01	2
55	1	8	GLU	H	H	8.06	0.01	1
56	1	8	GLU	HA	H	4.07	0.01	1
57	1	8	GLU	HB2	H	2.41	0.01	2
58	1	8	GLU	HB3	H	2.12	0.01	2
59	1	8	GLU	HG2	H	2.55	0.01	1
60	1	8	GLU	HG3	H	2.55	0.01	1
61	1	9	LYS	H	H	8.32	0.01	1
62	1	9	LYS	HA	H	3.98	0.01	1
63	1	9	LYS	HB2	H	1.96	0.01	1
64	1	9	LYS	HB3	H	1.96	0.01	1
65	1	9	LYS	HG2	H	1.46	0.01	2
66	1	9	LYS	HG3	H	1.44	0.01	2
67	1	9	LYS	HD2	H	1.72	0.01	1
68	1	9	LYS	HD3	H	1.72	0.01	1
69	1	9	LYS	HE2	H	2.96	0.01	1
70	1	9	LYS	HE3	H	2.96	0.01	1
71	1	10	ASN	H	H	8.25	0.01	1
72	1	10	ASN	HA	H	4.56	0.01	1
73	1	10	ASN	HB2	H	3.01	0.01	2
74	1	10	ASN	HB3	H	2.85	0.01	2
75	1	10	ASN	HD21	H	7.43	0.01	2
76	1	10	ASN	HD22	H	6.77	0.01	2
77	1	11	ARG	H	H	8.15	0.01	1
78	1	11	ARG	HA	H	4.19	0.01	1
79	1	11	ARG	HB2	H	2.07	0.01	2
80	1	11	ARG	HB3	H	2.03	0.01	2
81	1	11	ARG	HG2	H	1.91	0.01	2
82	1	11	ARG	HG3	H	1.73	0.01	2
83	1	11	ARG	HD2	H	3.24	0.01	1
84	1	11	ARG	HD3	H	3.24	0.01	1
85	1	11	ARG	HE	H	7.20	0.01	1
86	1	12	LEU	H	H	8.42	0.01	1
87	1	12	LEU	HA	H	4.21	0.01	1
88	1	12	LEU	HB2	H	1.92	0.01	2
89	1	12	LEU	HB3	H	1.90	0.01	2
90	1	12	LEU	HG	H	1.63	0.01	1
91	1	12	LEU	HD11	H	0.95	0.01	2
92	1	12	LEU	HD12	H	0.95	0.01	2
93	1	12	LEU	HD13	H	0.95	0.01	2
94	1	12	LEU	HD21	H	0.99	0.01	2
95	1	12	LEU	HD22	H	0.99	0.01	2
96	1	12	LEU	HD23	H	0.99	0.01	2
97	1	13	ASN	H	H	8.30	0.01	1
98	1	13	ASN	HA	H	4.50	0.01	1
99	1	13	ASN	HB2	H	3.05	0.01	2
100	1	13	ASN	HB3	H	2.85	0.01	2
101	1	13	ASN	HD21	H	7.67	0.01	2
102	1	13	ASN	HD22	H	6.77	0.01	2
103	1	14	PHE	H	H	8.15	0.01	1
104	1	14	PHE	HA	H	4.34	0.01	1
105	1	14	PHE	HB2	H	3.42	0.01	2
106	1	14	PHE	HB3	H	3.35	0.01	2
107	1	14	PHE	HD1	H	7.26	0.01	3
108	1	14	PHE	HD2	H	7.26	0.01	3
109	1	14	PHE	HE1	H	7.30	0.01	3
110	1	14	PHE	HE2	H	7.30	0.01	3
111	1	15	LEU	H	H	8.50	0.01	1
112	1	15	LEU	HA	H	4.03	0.01	1
113	1	15	LEU	HB2	H	2.01	0.01	2
114	1	15	LEU	HB3	H	1.95	0.01	2
115	1	15	LEU	HG	H	1.66	0.01	1
116	1	15	LEU	HD11	H	0.98	0.01	2
117	1	15	LEU	HD12	H	0.98	0.01	2
118	1	15	LEU	HD13	H	0.98	0.01	2
119	1	15	LEU	HD21	H	0.94	0.01	2
120	1	15	LEU	HD22	H	0.94	0.01	2
121	1	15	LEU	HD23	H	0.94	0.01	2
122	1	16	LYS	H	H	8.51	0.01	1
123	1	16	LYS	HA	H	3.98	0.01	1
124	1	16	LYS	HB2	H	2.06	0.01	2
125	1	16	LYS	HB3	H	1.98	0.01	2
126	1	16	LYS	HG2	H	1.46	0.01	1
127	1	16	LYS	HG3	H	1.46	0.01	1
128	1	16	LYS	HD2	H	1.72	0.01	1
129	1	16	LYS	HD3	H	1.72	0.01	1
130	1	16	LYS	HE2	H	2.98	0.01	1
131	1	16	LYS	HE3	H	2.98	0.01	1
132	1	17	LYS	H	H	7.88	0.01	1
133	1	17	LYS	HA	H	4.11	0.01	1
134	1	17	LYS	HB2	H	2.07	0.01	2
135	1	17	LYS	HB3	H	2.00	0.01	2
136	1	17	LYS	HG2	H	1.48	0.01	1
137	1	17	LYS	HG3	H	1.48	0.01	1
138	1	17	LYS	HD2	H	1.73	0.01	1
139	1	17	LYS	HD3	H	1.73	0.01	1
140	1	17	LYS	HE2	H	3.01	0.01	1
141	1	17	LYS	HE3	H	3.01	0.01	1
142	1	18	ILE	H	H	8.34	0.01	1
143	1	18	ILE	HA	H	3.87	0.01	1
144	1	18	ILE	HB	H	1.83	0.01	1
145	1	18	ILE	HG12	H	1.31	0.01	2
146	1	18	ILE	HG13	H	1.13	0.01	2
147	1	18	ILE	HG21	H	0.82	0.01	1
148	1	18	ILE	HG22	H	0.82	0.01	1
149	1	18	ILE	HG23	H	0.82	0.01	1
150	1	18	ILE	HD11	H	0.71	0.01	1
151	1	18	ILE	HD12	H	0.71	0.01	1
152	1	18	ILE	HD13	H	0.71	0.01	1
153	1	19	SER	H	H	8.21	0.01	1
154	1	19	SER	HA	H	4.28	0.01	1
155	1	19	SER	HB2	H	4.12	0.01	2
156	1	19	SER	HB3	H	4.05	0.01	2
157	1	20	GLN	H	H	7.88	0.01	1
158	1	20	GLN	HA	H	4.21	0.01	1
159	1	20	GLN	HB2	H	2.27	0.01	2
160	1	20	GLN	HB3	H	2.21	0.01	2
161	1	20	GLN	HG2	H	2.63	0.01	2
162	1	20	GLN	HG3	H	2.46	0.01	2
163	1	20	GLN	HE21	H	7.34	0.01	2
164	1	20	GLN	HE22	H	6.67	0.01	2
165	1	21	ARG	H	H	7.86	0.01	1
166	1	21	ARG	HA	H	4.13	0.01	1
167	1	21	ARG	HB2	H	1.93	0.01	1
168	1	21	ARG	HB3	H	1.93	0.01	1
169	1	21	ARG	HG2	H	1.62	0.01	1
170	1	21	ARG	HG3	H	1.62	0.01	1
171	1	21	ARG	HD2	H	3.14	0.01	1
172	1	21	ARG	HD3	H	3.14	0.01	1
173	1	21	ARG	HE	H	7.11	0.01	1
174	1	22	TYR	H	H	8.15	0.01	1
175	1	22	TYR	HA	H	4.45	0.01	1
176	1	22	TYR	HB2	H	3.24	0.01	2
177	1	22	TYR	HB3	H	3.09	0.01	2
178	1	22	TYR	HD1	H	7.15	0.01	3
179	1	22	TYR	HD2	H	7.15	0.01	3
180	1	22	TYR	HE1	H	6.81	0.01	3
181	1	22	TYR	HE2	H	6.81	0.01	3
182	1	23	GLN	H	H	8.13	0.01	1
183	1	23	GLN	HA	H	4.07	0.01	1
184	1	23	GLN	HB2	H	2.21	0.01	2
185	1	23	GLN	HB3	H	2.17	0.01	2
186	1	23	GLN	HG2	H	2.56	0.01	2
187	1	23	GLN	HG3	H	2.41	0.01	2
188	1	23	GLN	HE21	H	7.11	0.01	2
189	1	23	GLN	HE22	H	6.54	0.01	2
190	1	24	LYS	H	H	7.87	0.01	1
191	1	24	LYS	HA	H	4.13	0.01	1
192	1	24	LYS	HB2	H	1.80	0.01	2
193	1	24	LYS	HB3	H	1.75	0.01	2
194	1	24	LYS	HG2	H	1.37	0.01	2
195	1	24	LYS	HG3	H	1.35	0.01	2
196	1	24	LYS	HD2	H	1.63	0.01	1
197	1	24	LYS	HD3	H	1.63	0.01	1
198	1	24	LYS	HE2	H	2.96	0.01	1
199	1	24	LYS	HE3	H	2.96	0.01	1
200	1	25	PHE	H	H	7.77	0.01	1
201	1	25	PHE	HA	H	4.61	0.01	1
202	1	25	PHE	HB2	H	3.23	0.01	2
203	1	25	PHE	HB3	H	3.10	0.01	2
204	1	25	PHE	HD1	H	7.30	0.01	3
205	1	25	PHE	HD2	H	7.30	0.01	3
206	1	25	PHE	HE1	H	7.26	0.01	3
207	1	25	PHE	HE2	H	7.26	0.01	3
208	1	26	ALA	H	H	8.08	0.01	1
209	1	26	ALA	HA	H	4.29	0.01	1
210	1	26	ALA	HB1	H	1.38	0.01	1
211	1	26	ALA	HB2	H	1.38	0.01	1
212	1	26	ALA	HB3	H	1.38	0.01	1
213	1	27	LEU	H	H	7.98	0.01	1
214	1	27	LEU	HA	H	4.44	0.01	1
215	1	27	LEU	HB2	H	1.71	0.01	2
216	1	27	LEU	HB3	H	1.70	0.01	2
217	1	27	LEU	HG	H	1.89	0.01	1
218	1	27	LEU	HD11	H	1.07	0.01	2
219	1	27	LEU	HD12	H	1.07	0.01	2
220	1	27	LEU	HD13	H	1.07	0.01	2
221	1	27	LEU	HD21	H	1.00	0.01	2
222	1	27	LEU	HD22	H	1.00	0.01	2
223	1	27	LEU	HD23	H	1.00	0.01	2
224	1	28	PRO	HA	H	4.29	0.01	1
225	1	28	PRO	HB2	H	2.35	0.01	2
226	1	28	PRO	HB3	H	1.87	0.01	2
227	1	28	PRO	HG2	H	2.21	0.01	2
228	1	28	PRO	HG3	H	1.99	0.01	2
229	1	28	PRO	HD2	H	3.72	0.01	2
230	1	28	PRO	HD3	H	3.63	0.01	2
231	1	29	GLN	H	H	7.52	0.01	1
232	1	29	GLN	HA	H	4.12	0.01	1
233	1	29	GLN	HB2	H	2.20	0.01	1
234	1	29	GLN	HB3	H	2.20	0.01	1
235	1	29	GLN	HG2	H	2.43	0.01	2
236	1	29	GLN	HG3	H	2.40	0.01	2
237	1	29	GLN	HE21	H	7.16	0.01	2
238	1	29	GLN	HE22	H	6.49	0.01	2
239	1	30	TYR	H	H	8.26	0.01	1
240	1	30	TYR	HA	H	4.29	0.01	1
241	1	30	TYR	HB2	H	3.27	0.01	2
242	1	30	TYR	HB3	H	3.21	0.01	2
243	1	30	TYR	HD1	H	7.05	0.01	3
244	1	30	TYR	HD2	H	7.05	0.01	3
245	1	30	TYR	HE1	H	6.77	0.01	3
246	1	30	TYR	HE2	H	6.77	0.01	3
247	1	31	LEU	H	H	8.57	0.01	1
248	1	31	LEU	HA	H	3.96	0.01	1
249	1	31	LEU	HB2	H	1.89	0.01	2
250	1	31	LEU	HB3	H	1.48	0.01	2
251	1	31	LEU	HG	H	1.99	0.01	1
252	1	31	LEU	HD11	H	0.95	0.01	2
253	1	31	LEU	HD12	H	0.95	0.01	2
254	1	31	LEU	HD13	H	0.95	0.01	2
255	1	31	LEU	HD21	H	0.92	0.01	2
256	1	31	LEU	HD22	H	0.92	0.01	2
257	1	31	LEU	HD23	H	0.92	0.01	2
258	1	32	LYS	H	H	7.99	0.01	1
259	1	32	LYS	HA	H	4.04	0.01	1
260	1	32	LYS	HB2	H	1.98	0.01	2
261	1	32	LYS	HB3	H	1.96	0.01	2
262	1	32	LYS	HG2	H	1.47	0.01	1
263	1	32	LYS	HG3	H	1.47	0.01	1
264	1	32	LYS	HD2	H	1.72	0.01	1
265	1	32	LYS	HD3	H	1.72	0.01	1
266	1	32	LYS	HE2	H	2.98	0.01	1
267	1	32	LYS	HE3	H	2.98	0.01	1
268	1	33	THR	H	H	7.76	0.01	1
269	1	33	THR	HA	H	4.13	0.01	1
270	1	33	THR	HB	H	4.41	0.01	1
271	1	33	THR	HG21	H	1.29	0.01	1
272	1	33	THR	HG22	H	1.29	0.01	1
273	1	33	THR	HG23	H	1.29	0.01	1
274	1	34	VAL	H	H	8.13	0.01	1
275	1	34	VAL	HA	H	3.64	0.01	1
276	1	34	VAL	HB	H	2.01	0.01	1
277	1	34	VAL	HG11	H	0.77	0.01	2
278	1	34	VAL	HG12	H	0.77	0.01	2
279	1	34	VAL	HG13	H	0.77	0.01	2
280	1	34	VAL	HG21	H	0.71	0.01	2
281	1	34	VAL	HG22	H	0.71	0.01	2
282	1	34	VAL	HG23	H	0.71	0.01	2
283	1	35	TYR	H	H	8.35	0.01	1
284	1	35	TYR	HA	H	4.30	0.01	1
285	1	35	TYR	HB2	H	3.15	0.01	2
286	1	35	TYR	HB3	H	3.13	0.01	2
287	1	35	TYR	HD1	H	7.12	0.01	3
288	1	35	TYR	HD2	H	7.12	0.01	3
289	1	35	TYR	HE1	H	6.81	0.01	3
290	1	35	TYR	HE2	H	6.81	0.01	3
291	1	36	GLN	H	H	8.09	0.01	1
292	1	36	GLN	HA	H	4.12	0.01	1
293	1	36	GLN	HB2	H	2.21	0.01	2
294	1	36	GLN	HB3	H	2.12	0.01	2
295	1	36	GLN	HG2	H	2.55	0.01	2
296	1	36	GLN	HG3	H	2.39	0.01	2
297	1	36	GLN	HE21	H	7.20	0.01	2
298	1	36	GLN	HE22	H	6.64	0.01	2
299	1	37	HIS	H	H	7.90	0.01	1
300	1	37	HIS	HA	H	4.58	0.01	1
301	1	37	HIS	HB2	H	3.45	0.01	2
302	1	37	HIS	HB3	H	3.22	0.01	2
303	1	37	HIS	HD2	H	7.42	0.01	1
304	1	37	HIS	HE1	H	8.55	0.01	1
305	1	38	GLN	H	H	7.98	0.01	1
306	1	38	GLN	HA	H	4.36	0.01	1
307	1	38	GLN	HB2	H	2.18	0.01	2
308	1	38	GLN	HB3	H	2.07	0.01	2
309	1	38	GLN	HG2	H	2.48	0.01	2
310	1	38	GLN	HG3	H	2.43	0.01	2
311	1	38	GLN	HE21	H	7.22	0.01	2
312	1	38	GLN	HE22	H	6.46	0.01	2
313	1	39	LYS	H	H	7.63	0.01	1
314	1	39	LYS	HA	H	4.31	0.01	1
315	1	39	LYS	HB2	H	1.89	0.01	1
316	1	39	LYS	HB3	H	1.89	0.01	1
317	1	39	LYS	HG2	H	1.40	0.01	1
318	1	39	LYS	HG3	H	1.40	0.01	1
319	1	39	LYS	HD2	H	1.70	0.01	1
320	1	39	LYS	HD3	H	1.70	0.01	1
321	1	39	LYS	HE2	H	3.02	0.01	1
322	1	39	LYS	HE3	H	3.02	0.01	1

Release date

2018-02-20

Citation

The antimicrobial peptides casocidins I and II: Solution structural studies in water and different membrane-mimetic environments
Mercurio, F.A., Scaloni, A., Caira, S., Leone, M.
Peptides (2018), 114, 50-58, PubMed 30243923 , DOI 10.1016/j.peptides.2018.09.004 , Abstract

Related entities 1. Alpha-S2-casein, : 1 : 1 : 2 : 15 entities Detail

Experiments performed 3 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	Casocidin-I	natural abundance		950 uM

#	Name	Isotope labeling	Type	Concentration
1	Casocidin-I	natural abundance		950 uM

#	Name	Isotope labeling	Type	Concentration
1	Casocidin-I	natural abundance		950 uM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34238_6fs5.nef
Input source #2: Coordindates	6fs5.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---------
KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK
|||||||||||||||||||||||||||||||||||||||
KTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	39	0	0	100.0

Content subtype: combined_34238_6fs5.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	nef_chemical_shift_list_assigned_chemical_shifts_1	OK	253		100.0 (chain: A, length: 39)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	780 (1)	noe	97.4 (chain: A, length: 39)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	Warning	206 (197)	.	100.0 (chain: A, length: 39)

Assigned chemical shifts

Saveframe: nef_chemical_shift_list_assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 39, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 253
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	289	286	99.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	76	98.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	212	210	99.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	22	91.7

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 39, Sequence coverage: 97.4%
- Total number of restraints: 780
- Weight of restraints: 1.0 (780)
- Potential type of restraints: upper-bound-parabolic (780)
- Range of distance target values: 3.01, 8.65 (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_3
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 39, Sequence coverage: 100.0%
- Total number of restraints: 197
- Total number of restraints per polymer type: 197
- Weight of restraints: 1.0 (197)
- Potential type of restraints: square-well-parabolic (197)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords ANTIMICROBIAL PROTEIN, Antimicrobial peptide, TFE

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Found 1 Document (0.99 seconds)

BMRB: 34238

Related entities 1. Alpha-S2-casein, : 1 : 1 : 2 : 15 entities Detail

Experiments performed 3 experiments Detail

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NMR combined restraints 4 contents Detail