BMRBj - BMREntryMaster

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err	Ambig. code
1	1	1	THR	HA	H	4.14	0.01	1
2	1	1	THR	HB	H	4.57	0.01	1
3	1	1	THR	HG21	H	1.46	0.01	1
4	1	1	THR	HG22	H	1.46	0.01	1
5	1	1	THR	HG23	H	1.46	0.01	1
6	1	2	LYS	H	H	8.94	0.01	1
7	1	2	LYS	HA	H	4.30	0.01	1
8	1	2	LYS	HB2	H	1.93	0.01	2
9	1	2	LYS	HB3	H	1.89	0.01	2
10	1	2	LYS	HG2	H	1.56	0.01	2
11	1	2	LYS	HG3	H	1.53	0.01	2
12	1	2	LYS	HD2	H	1.76	0.01	1
13	1	2	LYS	HD3	H	1.76	0.01	1
14	1	2	LYS	HE2	H	3.04	0.01	1
15	1	2	LYS	HE3	H	3.04	0.01	1
16	1	3	LEU	H	H	7.87	0.01	1
17	1	3	LEU	HA	H	4.40	0.01	1
18	1	3	LEU	HB2	H	1.70	0.01	2
19	1	3	LEU	HB3	H	1.67	0.01	2
20	1	3	LEU	HD11	H	0.99	0.01	2
21	1	3	LEU	HD12	H	0.99	0.01	2
22	1	3	LEU	HD13	H	0.99	0.01	2
23	1	3	LEU	HD21	H	0.94	0.01	2
24	1	3	LEU	HD22	H	0.94	0.01	2
25	1	3	LEU	HD23	H	0.94	0.01	2
26	1	4	THR	H	H	7.76	0.01	1
27	1	4	THR	HA	H	4.24	0.01	1
28	1	4	THR	HB	H	4.49	0.01	1
29	1	4	THR	HG21	H	1.34	0.01	1
30	1	4	THR	HG22	H	1.34	0.01	1
31	1	4	THR	HG23	H	1.34	0.01	1
32	1	5	GLU	H	H	8.28	0.01	1
33	1	5	GLU	HA	H	4.13	0.01	1
34	1	5	GLU	HB2	H	2.23	0.01	1
35	1	5	GLU	HB3	H	2.23	0.01	1
36	1	5	GLU	HG2	H	2.56	0.01	1
37	1	5	GLU	HG3	H	2.56	0.01	1
38	1	6	GLU	H	H	8.32	0.01	1
39	1	6	GLU	HA	H	4.18	0.01	1
40	1	6	GLU	HB2	H	2.31	0.01	2
41	1	6	GLU	HB3	H	2.19	0.01	2
42	1	6	GLU	HG2	H	2.61	0.01	2
43	1	6	GLU	HG3	H	2.55	0.01	2
44	1	7	GLU	H	H	8.22	0.01	1
45	1	7	GLU	HA	H	4.10	0.01	1
46	1	7	GLU	HB2	H	2.49	0.01	2
47	1	7	GLU	HB3	H	2.36	0.01	2
48	1	7	GLU	HG2	H	2.62	0.01	1
49	1	7	GLU	HG3	H	2.62	0.01	1
50	1	8	LYS	H	H	8.35	0.01	1
51	1	8	LYS	HA	H	4.00	0.01	1
52	1	8	LYS	HB2	H	1.99	0.01	1
53	1	8	LYS	HB3	H	1.99	0.01	1
54	1	8	LYS	HG2	H	1.46	0.01	2
55	1	8	LYS	HG3	H	1.48	0.01	2
56	1	8	LYS	HD2	H	1.75	0.01	1
57	1	8	LYS	HD3	H	1.75	0.01	1
58	1	8	LYS	HE2	H	2.99	0.01	1
59	1	8	LYS	HE3	H	2.99	0.01	1
60	1	9	ASN	H	H	8.23	0.01	1
61	1	9	ASN	HA	H	4.57	0.01	1
62	1	9	ASN	HB2	H	3.02	0.01	2
63	1	9	ASN	HB3	H	2.88	0.01	2
64	1	9	ASN	HD21	H	7.43	0.01	2
65	1	9	ASN	HD22	H	6.74	0.01	2
66	1	10	ARG	H	H	8.18	0.01	1
67	1	10	ARG	HA	H	4.21	0.01	1
68	1	10	ARG	HB2	H	2.09	0.01	2
69	1	10	ARG	HB3	H	2.07	0.01	2
70	1	10	ARG	HG2	H	1.92	0.01	2
71	1	10	ARG	HG3	H	1.74	0.01	2
72	1	10	ARG	HD2	H	3.27	0.01	1
73	1	10	ARG	HD3	H	3.27	0.01	1
74	1	10	ARG	HE	H	7.15	0.01	1
75	1	11	LEU	H	H	8.43	0.01	1
76	1	11	LEU	HA	H	4.22	0.01	1
77	1	11	LEU	HB2	H	1.95	0.01	2
78	1	11	LEU	HB3	H	1.93	0.01	2
79	1	11	LEU	HG	H	1.66	0.01	1
80	1	11	LEU	HD11	H	1.00	0.01	2
81	1	11	LEU	HD12	H	1.00	0.01	2
82	1	11	LEU	HD13	H	1.00	0.01	2
83	1	11	LEU	HD21	H	0.93	0.01	2
84	1	11	LEU	HD22	H	0.93	0.01	2
85	1	11	LEU	HD23	H	0.93	0.01	2
86	1	12	ASN	H	H	8.31	0.01	1
87	1	12	ASN	HA	H	4.52	0.01	1
88	1	12	ASN	HB2	H	3.05	0.01	2
89	1	12	ASN	HB3	H	2.87	0.01	2
90	1	12	ASN	HD21	H	7.67	0.01	2
91	1	12	ASN	HD22	H	6.77	0.01	2
92	1	13	PHE	H	H	8.15	0.01	1
93	1	13	PHE	HA	H	4.34	0.01	1
94	1	13	PHE	HB2	H	3.42	0.01	2
95	1	13	PHE	HB3	H	3.35	0.01	2
96	1	13	PHE	HD1	H	7.26	0.01	3
97	1	13	PHE	HD2	H	7.26	0.01	3
98	1	13	PHE	HE1	H	7.31	0.01	3
99	1	13	PHE	HE2	H	7.31	0.01	3
100	1	13	PHE	HZ	H	7.28	0.01	1
101	1	14	LEU	H	H	8.51	0.01	1
102	1	14	LEU	HA	H	4.03	0.01	1
103	1	14	LEU	HB2	H	2.03	0.01	2
104	1	14	LEU	HB3	H	1.98	0.01	2
105	1	14	LEU	HG	H	1.66	0.01	1
106	1	14	LEU	HD11	H	1.00	0.01	2
107	1	14	LEU	HD12	H	1.00	0.01	2
108	1	14	LEU	HD13	H	1.00	0.01	2
109	1	14	LEU	HD21	H	0.95	0.01	2
110	1	14	LEU	HD22	H	0.95	0.01	2
111	1	14	LEU	HD23	H	0.95	0.01	2
112	1	15	LYS	H	H	8.51	0.01	1
113	1	15	LYS	HA	H	3.97	0.01	1
114	1	15	LYS	HB2	H	2.07	0.01	2
115	1	15	LYS	HB3	H	2.00	0.01	2
116	1	15	LYS	HG2	H	1.48	0.01	1
117	1	15	LYS	HG3	H	1.48	0.01	1
118	1	15	LYS	HD2	H	1.72	0.01	1
119	1	15	LYS	HD3	H	1.72	0.01	1
120	1	15	LYS	HE2	H	3.00	0.01	1
121	1	15	LYS	HE3	H	3.00	0.01	1
122	1	16	LYS	H	H	7.87	0.01	1
123	1	16	LYS	HA	H	4.18	0.01	1
124	1	16	LYS	HB2	H	2.05	0.01	2
125	1	16	LYS	HB3	H	1.94	0.01	2
126	1	16	LYS	HG2	H	1.48	0.01	1
127	1	16	LYS	HG3	H	1.48	0.01	1
128	1	16	LYS	HD2	H	1.69	0.01	1
129	1	16	LYS	HD3	H	1.69	0.01	1
130	1	16	LYS	HE2	H	3.01	0.01	1
131	1	16	LYS	HE3	H	3.01	0.01	1
132	1	17	ILE	H	H	8.31	0.01	1
133	1	17	ILE	HA	H	3.90	0.01	1
134	1	17	ILE	HB	H	1.85	0.01	1
135	1	17	ILE	HG12	H	1.31	0.01	2
136	1	17	ILE	HG13	H	1.14	0.01	2
137	1	17	ILE	HG21	H	0.80	0.01	1
138	1	17	ILE	HG22	H	0.80	0.01	1
139	1	17	ILE	HG23	H	0.80	0.01	1
140	1	17	ILE	HD11	H	0.72	0.01	1
141	1	17	ILE	HD12	H	0.72	0.01	1
142	1	17	ILE	HD13	H	0.72	0.01	1
143	1	18	SER	H	H	8.16	0.01	1
144	1	18	SER	HA	H	4.29	0.01	1
145	1	18	SER	HB2	H	4.10	0.01	2
146	1	18	SER	HB3	H	4.03	0.01	2
147	1	19	GLN	H	H	7.79	0.01	1
148	1	19	GLN	HA	H	4.21	0.01	1
149	1	19	GLN	HB2	H	2.24	0.01	2
150	1	19	GLN	HB3	H	2.19	0.01	2
151	1	19	GLN	HG2	H	2.63	0.01	2
152	1	19	GLN	HG3	H	2.46	0.01	2
153	1	19	GLN	HE21	H	7.36	0.01	2
154	1	19	GLN	HE22	H	6.66	0.01	2
155	1	20	ARG	H	H	7.81	0.01	1
156	1	20	ARG	HA	H	4.16	0.01	1
157	1	20	ARG	HB2	H	1.86	0.01	1
158	1	20	ARG	HB3	H	1.86	0.01	1
159	1	20	ARG	HG2	H	1.53	0.01	1
160	1	20	ARG	HG3	H	1.53	0.01	1
161	1	20	ARG	HD2	H	3.12	0.01	1
162	1	20	ARG	HD3	H	3.12	0.01	1
163	1	20	ARG	HE	H	7.08	0.01	1
164	1	21	TYR	H	H	7.97	0.01	1
165	1	21	TYR	HA	H	4.52	0.01	1
166	1	21	TYR	HB2	H	3.23	0.01	2
167	1	21	TYR	HB3	H	3.02	0.01	2
168	1	21	TYR	HD1	H	7.17	0.01	3
169	1	21	TYR	HD2	H	7.17	0.01	3
170	1	21	TYR	HE1	H	6.81	0.01	3
171	1	21	TYR	HE2	H	6.81	0.01	3
172	1	22	GLN	H	H	7.97	0.01	1
173	1	22	GLN	HA	H	4.18	0.01	1
174	1	22	GLN	HB2	H	2.15	0.01	1
175	1	22	GLN	HB3	H	2.15	0.01	1
176	1	22	GLN	HG2	H	2.47	0.01	2
177	1	22	GLN	HG3	H	2.41	0.01	2
178	1	22	GLN	HE21	H	7.23	0.01	2
179	1	22	GLN	HE22	H	6.57	0.01	2
180	1	23	LYS	H	H	7.88	0.01	1
181	1	23	LYS	HA	H	4.19	0.01	1
182	1	23	LYS	HB2	H	1.75	0.01	2
183	1	23	LYS	HB3	H	1.69	0.01	2
184	1	23	LYS	HG2	H	1.36	0.01	2
185	1	23	LYS	HG3	H	1.31	0.01	2
186	1	23	LYS	HD2	H	1.65	0.01	1
187	1	23	LYS	HD3	H	1.65	0.01	1
188	1	23	LYS	HE2	H	2.97	0.01	1
189	1	23	LYS	HE3	H	2.97	0.01	1
190	1	24	PHE	H	H	7.77	0.01	1
191	1	24	PHE	HA	H	4.61	0.01	1
192	1	24	PHE	HB2	H	3.23	0.01	2
193	1	24	PHE	HB3	H	3.06	0.01	2
194	1	24	PHE	HD1	H	7.29	0.01	3
195	1	24	PHE	HD2	H	7.29	0.01	3
196	1	24	PHE	HE1	H	7.32	0.01	3
197	1	24	PHE	HE2	H	7.32	0.01	3
198	1	25	ALA	H	H	7.85	0.01	1
199	1	25	ALA	HA	H	4.36	0.01	1
200	1	25	ALA	HB1	H	1.36	0.01	1
201	1	25	ALA	HB2	H	1.36	0.01	1
202	1	25	ALA	HB3	H	1.36	0.01	1
203	1	26	LEU	H	H	7.59	0.01	1
204	1	26	LEU	HA	H	4.57	0.01	1
205	1	26	LEU	HB2	H	1.67	0.01	2
206	1	26	LEU	HB3	H	1.64	0.01	2
207	1	26	LEU	HG	H	1.74	0.01	1
208	1	26	LEU	HD11	H	1.01	0.01	2
209	1	26	LEU	HD12	H	1.01	0.01	2
210	1	26	LEU	HD13	H	1.01	0.01	2
211	1	26	LEU	HD21	H	0.97	0.01	2
212	1	26	LEU	HD22	H	0.97	0.01	2
213	1	26	LEU	HD23	H	0.97	0.01	2
214	1	27	PRO	HA	H	4.33	0.01	1
215	1	27	PRO	HB2	H	2.27	0.01	2
216	1	27	PRO	HB3	H	1.76	0.01	2
217	1	27	PRO	HG2	H	2.05	0.01	1
218	1	27	PRO	HG3	H	2.05	0.01	1
219	1	27	PRO	HD2	H	3.80	0.01	2
220	1	27	PRO	HD3	H	3.61	0.01	2
221	1	28	GLN	H	H	8.21	0.01	1
222	1	28	GLN	HA	H	4.14	0.01	1
223	1	28	GLN	HB2	H	2.02	0.01	1
224	1	28	GLN	HB3	H	2.02	0.01	1
225	1	28	GLN	HG2	H	2.27	0.01	1
226	1	28	GLN	HG3	H	2.27	0.01	1
227	1	28	GLN	HE21	H	7.27	0.01	2
228	1	28	GLN	HE22	H	6.48	0.01	2
229	1	29	TYR	H	H	7.66	0.01	1
230	1	29	TYR	HA	H	4.58	0.01	1
231	1	29	TYR	HB2	H	3.16	0.01	2
232	1	29	TYR	HB3	H	3.06	0.01	2
233	1	29	TYR	HD1	H	7.14	0.01	3
234	1	29	TYR	HD2	H	7.14	0.01	3
235	1	29	TYR	HE1	H	6.84	0.01	3
236	1	29	TYR	HE2	H	6.84	0.01	3
237	1	30	LEU	H	H	7.62	0.01	1
238	1	30	LEU	HA	H	4.39	0.01	1
239	1	30	LEU	HB2	H	1.67	0.01	2
240	1	30	LEU	HB3	H	1.65	0.01	2
241	1	30	LEU	HG	H	1.63	0.01	1
242	1	30	LEU	HD11	H	0.93	0.01	2
243	1	30	LEU	HD12	H	0.93	0.01	2
244	1	30	LEU	HD13	H	0.93	0.01	2
245	1	30	LEU	HD21	H	0.96	0.01	2
246	1	30	LEU	HD22	H	0.96	0.01	2
247	1	30	LEU	HD23	H	0.96	0.01	2
248	1	31	LYS	H	H	7.67	0.01	1
249	1	31	LYS	HA	H	4.37	0.01	1
250	1	31	LYS	HB2	H	1.97	0.01	2
251	1	31	LYS	HB3	H	1.84	0.01	2
252	1	31	LYS	HG2	H	1.48	0.01	1
253	1	31	LYS	HG3	H	1.48	0.01	1
254	1	31	LYS	HE2	H	2.97	0.01	1
255	1	31	LYS	HE3	H	2.97	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 : 2 : 2 : 6 entities Detail

Experiments performed 3 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	Casocidin II	natural abundance		1.2 mM

#	Name	Isotope labeling	Type	Concentration
1	Casocidin II	natural abundance		1.2 mM

#	Name	Isotope labeling	Type	Concentration
1	Casocidin II	natural abundance		1.2 mM

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34237_6fs4.nef
Input source #2: Coordindates	6fs4.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--
TKLTEEEKNRLNFLKKISQRYQKFALPQYLK
|||||||||||||||||||||||||||||||
TKLTEEEKNRLNFLKKISQRYQKFALPQYLK
--------10--------20--------30-

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	31	0	0	100.0

Content subtype: combined_34237_6fs4.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	225		100.0 (chain: A, length: 31)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	661 (1)	noe	100.0 (chain: A, length: 31)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	Warning	183 (171)	.	100.0 (chain: A, length: 31)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 31, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 225
- 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	230	225	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	61	60	98.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	169	165	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	15	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	17	94.4

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 31, Sequence coverage: 100.0%
- Total number of restraints: 660
- Weight of restraints: 1.0 (660)
- Potential type of restraints: upper-bound-parabolic (660)
- Range of distance target values: 3.02, 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: 31, Sequence coverage: 100.0%
- Total number of restraints: 171
- Total number of restraints per polymer type: 171
- Weight of restraints: 1.0 (171)
- Potential type of restraints: square-well-parabolic (171)
- 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 (0.506 seconds)

BMRB: 34237

Related entities 1. Alpha-S2-casein, : 1 : 2 : 2 : 6 entities Detail

Experiments performed 3 experiments Detail

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Sample

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NMR combined restraints 4 contents Detail