BMRBj - BMREntryMaster

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err
1	1	1	PRO	HA	H	4.414	0.002
2	1	1	PRO	HB2	H	2.474	0.001
3	1	1	PRO	HB3	H	2.010	0.000
4	1	1	PRO	HG2	H	2.099	0.001
5	1	1	PRO	HG3	H	2.058	0.001
6	1	1	PRO	HD2	H	3.423	0.005
7	1	1	PRO	HD3	H	3.390	0.001
8	1	1	PRO	CA	C	65.535	0.000
9	1	1	PRO	CB	C	35.551	0.000
10	1	2	MET	H	H	8.807	0.004
11	1	2	MET	HA	H	4.451	0.001
12	1	2	MET	HB2	H	2.067	0.011
13	1	2	MET	HB3	H	2.048	0.022
14	1	2	MET	HG2	H	2.583	0.002
15	1	2	MET	HE1	H	2.073	0.003
16	1	2	MET	HE2	H	2.073	0.003
17	1	2	MET	HE3	H	2.073	0.003
18	1	2	MET	CA	C	59.857	0.000
19	1	2	MET	CB	C	29.661	0.032
20	1	2	MET	CG	C	35.179	0.000
21	1	2	MET	CE	C	19.900	0.000
22	1	2	MET	N	N	121.101	0.000
23	1	3	LYS	H	H	8.451	0.001
24	1	3	LYS	HA	H	4.153	0.002
25	1	3	LYS	HB2	H	1.762	0.007
26	1	3	LYS	HB3	H	1.827	0.009
27	1	3	LYS	HG2	H	1.478	0.001
28	1	3	LYS	HG3	H	1.387	0.002
29	1	3	LYS	HD2	H	1.679	0.001
30	1	3	LYS	HD3	H	1.694	0.001
31	1	3	LYS	HE2	H	2.961	0.001
32	1	3	LYS	HE3	H	2.944	0.001
33	1	3	LYS	CA	C	61.352	0.000
34	1	3	LYS	CB	C	35.838	0.006
35	1	3	LYS	CG	C	28.284	0.008
36	1	3	LYS	CD	C	30.405	0.022
37	1	3	LYS	CE	C	45.297	0.002
38	1	3	LYS	N	N	121.558	0.000
39	1	4	LEU	H	H	7.782	0.002
40	1	4	LEU	HA	H	4.228	0.002
41	1	4	LEU	HB2	H	1.629	0.001
42	1	4	LEU	HB3	H	1.621	0.001
43	1	4	LEU	HG	H	1.577	0.002
44	1	4	LEU	HD11	H	0.909	0.002
45	1	4	LEU	HD12	H	0.909	0.002
46	1	4	LEU	HD13	H	0.909	0.002
47	1	4	LEU	HD21	H	0.862	0.002
48	1	4	LEU	HD22	H	0.862	0.002
49	1	4	LEU	HD23	H	0.862	0.002
50	1	4	LEU	CA	C	59.620	0.000
51	1	4	LEU	CB	C	45.573	0.008
52	1	4	LEU	CG	C	26.964	0.000
53	1	4	LEU	CD1	C	27.179	0.000
54	1	4	LEU	CD2	C	26.237	0.000
55	1	4	LEU	N	N	120.307	0.000
56	1	5	LEU	H	H	7.661	0.003
57	1	5	LEU	HA	H	4.158	0.004
58	1	5	LEU	HB2	H	1.706	0.002
59	1	5	LEU	HB3	H	1.695	0.000
60	1	5	LEU	HG	H	1.604	0.001
61	1	5	LEU	HD11	H	0.909	0.015
62	1	5	LEU	HD12	H	0.909	0.015
63	1	5	LEU	HD13	H	0.909	0.015
64	1	5	LEU	HD21	H	0.845	0.000
65	1	5	LEU	HD22	H	0.845	0.000
66	1	5	LEU	HD23	H	0.845	0.000
67	1	5	LEU	CA	C	60.119	0.000
68	1	5	LEU	CB	C	45.227	0.000
69	1	5	LEU	CG	C	26.676	0.000
70	1	5	LEU	CD1	C	27.397	0.000
71	1	5	LEU	CD2	C	26.519	0.000
72	1	5	LEU	N	N	119.672	0.000
73	1	6	LYS	H	H	7.917	0.001
74	1	6	LYS	HA	H	4.122	0.000
75	1	6	LYS	HB2	H	1.866	0.002
76	1	6	LYS	HB3	H	1.810	0.000
77	1	6	LYS	HG2	H	1.499	0.000
78	1	6	LYS	HG3	H	1.419	0.000
79	1	6	LYS	HD2	H	1.673	0.001
80	1	6	LYS	HD3	H	1.685	0.000
81	1	6	LYS	HE2	H	2.946	0.000
82	1	6	LYS	HE3	H	2.959	0.000
83	1	6	LYS	CA	C	61.245	0.000
84	1	6	LYS	CB	C	36.240	0.005
85	1	6	LYS	CG	C	28.492	0.005
86	1	6	LYS	CD	C	30.126	0.001
87	1	6	LYS	CE	C	45.529	0.003
88	1	6	LYS	N	N	118.783	0.000
89	1	7	ARG	H	H	7.860	0.001
90	1	7	ARG	HA	H	4.206	0.005
91	1	7	ARG	HB2	H	1.887	0.005
92	1	7	ARG	HB3	H	1.706	0.001
93	1	7	ARG	HG2	H	1.616	0.005
94	1	7	ARG	HG3	H	1.636	0.009
95	1	7	ARG	HD2	H	3.166	0.010
96	1	7	ARG	HD3	H	3.142	0.004
97	1	7	ARG	HE	H	7.208	0.001
98	1	7	ARG	CA	C	56.195	0.000
99	1	7	ARG	CB	C	30.559	0.003
100	1	7	ARG	CG	C	30.160	0.003
101	1	7	ARG	CD	C	46.231	0.013
102	1	7	ARG	N	N	118.924	0.000
103	1	8	LEU	H	H	8.063	0.001
104	1	8	LEU	HA	H	4.250	0.005
105	1	8	LEU	HB2	H	1.691	0.003
106	1	8	LEU	HB3	H	1.717	0.000
107	1	8	LEU	HG	H	1.604	0.001
108	1	8	LEU	HD11	H	0.890	0.003
109	1	8	LEU	HD12	H	0.890	0.003
110	1	8	LEU	HD13	H	0.890	0.003
111	1	8	LEU	HD21	H	0.829	0.003
112	1	8	LEU	HD22	H	0.829	0.003
113	1	8	LEU	HD23	H	0.829	0.003
114	1	8	LEU	CA	C	59.624	0.000
115	1	8	LEU	CB	C	45.638	0.006
116	1	8	LEU	CG	C	27.053	0.000
117	1	8	LEU	CD1	C	27.530	0.000
118	1	8	LEU	CD2	C	26.023	0.000
119	1	8	LEU	N	N	120.348	0.000
120	1	9	GLY	H	H	8.137	0.001
121	1	9	GLY	HA2	H	3.889	0.015
122	1	9	GLY	HA3	H	3.820	0.001
123	1	9	GLY	CA	C	49.734	0.037
124	1	9	GLY	N	N	106.621	0.000
125	1	10	LYS	H	H	7.937	0.001
126	1	10	LYS	HA	H	4.138	0.000
127	1	10	LYS	HB2	H	1.893	0.003
128	1	10	LYS	HB3	H	1.831	0.000
129	1	10	LYS	HG2	H	1.419	0.000
130	1	10	LYS	HG3	H	1.500	0.000
131	1	10	LYS	HD2	H	1.695	0.000
132	1	10	LYS	HD3	H	1.705	0.007
133	1	10	LYS	HE2	H	2.948	0.000
134	1	10	LYS	HE3	H	2.959	0.000
135	1	10	LYS	CA	C	61.788	0.000
136	1	10	LYS	CB	C	36.000	0.002
137	1	10	LYS	CG	C	28.372	0.001
138	1	10	LYS	CD	C	30.009	0.002
139	1	10	LYS	CE	C	45.055	0.005
140	1	10	LYS	N	N	120.822	0.000
141	1	11	LYS	H	H	7.930	0.000
142	1	11	LYS	HA	H	4.160	0.000
143	1	11	LYS	HB2	H	1.820	0.001
144	1	11	LYS	HB3	H	1.907	0.000
145	1	11	LYS	HG2	H	1.419	0.000
146	1	11	LYS	HG3	H	1.501	0.000
147	1	11	LYS	HD2	H	1.698	0.006
148	1	11	LYS	HD3	H	1.709	0.000
149	1	11	LYS	HE2	H	2.935	0.000
150	1	11	LYS	HE3	H	2.964	0.000
151	1	11	LYS	CA	C	61.479	0.000
152	1	11	LYS	CB	C	35.888	0.000
153	1	11	LYS	CG	C	28.197	0.002
154	1	11	LYS	CD	C	30.324	0.001
155	1	11	LYS	CE	C	45.421	0.004
156	1	11	LYS	N	N	119.429	0.000
157	1	12	ILE	H	H	7.952	0.001
158	1	12	ILE	HA	H	3.946	0.006
159	1	12	ILE	HB	H	1.845	0.002
160	1	12	ILE	HG12	H	1.149	0.002
161	1	12	ILE	HG13	H	1.543	0.002
162	1	12	ILE	HG21	H	0.888	0.002
163	1	12	ILE	HG22	H	0.888	0.002
164	1	12	ILE	HG23	H	0.888	0.002
165	1	12	ILE	HD11	H	0.826	0.002
166	1	12	ILE	HD12	H	0.826	0.002
167	1	12	ILE	HD13	H	0.826	0.002
168	1	12	ILE	CA	C	65.489	0.000
169	1	12	ILE	CB	C	41.930	0.000
170	1	12	ILE	CG1	C	31.244	0.021
171	1	12	ILE	CG2	C	20.222	0.000
172	1	12	ILE	CD1	C	15.905	0.000
173	1	12	ILE	N	N	119.206	0.000
174	1	13	ARG	H	H	7.885	0.001
175	1	13	ARG	HA	H	4.158	0.003
176	1	13	ARG	HB2	H	1.702	0.001
177	1	13	ARG	HB3	H	1.840	0.003
178	1	13	ARG	HG2	H	1.581	0.002
179	1	13	ARG	HG3	H	1.611	0.006
180	1	13	ARG	HD2	H	3.172	0.005
181	1	13	ARG	HD3	H	3.136	0.003
182	1	13	ARG	HE	H	7.161	0.001
183	1	13	ARG	CA	C	56.945	0.000
184	1	13	ARG	CB	C	30.575	0.000
185	1	13	ARG	CG	C	30.288	0.001
186	1	13	ARG	CD	C	46.544	0.004
187	1	13	ARG	N	N	121.013	0.000
188	1	14	LEU	H	H	7.936	0.001
189	1	14	LEU	HA	H	4.240	0.003
190	1	14	LEU	HB2	H	1.679	0.000
191	1	14	LEU	HB3	H	1.735	0.001
192	1	14	LEU	HG	H	1.596	0.001
193	1	14	LEU	HD11	H	0.900	0.001
194	1	14	LEU	HD12	H	0.900	0.001
195	1	14	LEU	HD13	H	0.900	0.001
196	1	14	LEU	HD21	H	0.850	0.001
197	1	14	LEU	HD22	H	0.850	0.001
198	1	14	LEU	HD23	H	0.850	0.001
199	1	14	LEU	CA	C	59.876	0.000
200	1	14	LEU	CB	C	45.831	0.005
201	1	14	LEU	CG	C	27.167	0.000
202	1	14	LEU	CD1	C	27.808	0.000
203	1	14	LEU	CD2	C	26.882	0.000
204	1	14	LEU	N	N	120.224	0.000
205	1	15	ALA	H	H	7.964	0.001
206	1	15	ALA	HA	H	4.167	0.000
207	1	15	ALA	HB1	H	1.419	0.000
208	1	15	ALA	HB2	H	1.419	0.000
209	1	15	ALA	HB3	H	1.419	0.000
210	1	15	ALA	CA	C	60.145	0.000
211	1	15	ALA	CB	C	21.684	0.000
212	1	15	ALA	N	N	122.069	0.000
213	1	16	ALA	H	H	7.903	0.001
214	1	16	ALA	HA	H	4.176	0.007
215	1	16	ALA	HB1	H	1.381	0.002
216	1	16	ALA	HB2	H	1.381	0.002
217	1	16	ALA	HB3	H	1.381	0.002
218	1	16	ALA	CA	C	60.868	0.000
219	1	16	ALA	CB	C	21.860	0.000
220	1	16	ALA	N	N	119.923	0.000
221	1	17	ALA	H	H	7.705	0.003
222	1	17	ALA	HA	H	4.202	0.002
223	1	17	ALA	HB1	H	1.266	0.003
224	1	17	ALA	HB2	H	1.266	0.003
225	1	17	ALA	HB3	H	1.266	0.003
226	1	17	ALA	CA	C	60.930	0.000
227	1	17	ALA	CB	C	22.084	0.000
228	1	17	ALA	N	N	123.661	0.000
229	1	18	PHE	H	H	7.735	0.001
230	1	18	PHE	HA	H	4.579	0.002
231	1	18	PHE	HB2	H	3.216	0.001
232	1	18	PHE	HB3	H	2.998	0.001
233	1	18	PHE	CA	C	60.934	0.000
234	1	18	PHE	CB	C	42.640	0.000
235	1	18	PHE	N	N	117.370	0.000
236	1	19	LYS	H	H	7.704	0.002
237	1	19	LYS	HA	H	4.247	0.000
238	1	19	LYS	HB2	H	1.757	0.000
239	1	19	LYS	HB3	H	1.849	0.000
240	1	19	LYS	HG2	H	1.371	0.000
241	1	19	LYS	HG3	H	1.426	0.001
242	1	19	LYS	HD2	H	1.656	0.001
243	1	19	LYS	HD3	H	1.681	0.000
244	1	19	LYS	HE2	H	2.935	0.000
245	1	19	LYS	HE3	H	2.956	0.000
246	1	19	LYS	CA	C	59.749	0.000
247	1	19	LYS	CB	C	36.512	0.005
248	1	19	LYS	CG	C	27.722	0.002
249	1	19	LYS	CD	C	30.292	0.002
250	1	19	LYS	CE	C	45.619	0.014
251	1	19	LYS	N	N	120.226	0.000

Protein Blocks Logo

Calculated from 10 models in PDB: 6CSK, Strand ID: A Detail

Release date

2018-03-26

Citation

An N-capping asparagine-lysine-proline (NKP) motif contributes to a hybrid flexible/stable multifunctional peptide scaffold
Cardoso, M.H., Chan, L.Y., Candido, E.S., Buccini, D.F., Rezende, S.B., Torres, M., Oshiro, K., Silva, I.C., Goncalves, S., Lu, T.K., Santos, N.C., de la Fuente-Nunez, C., Craik, D.J., Franco, O.L.
Chem. Sci. (2022), 13, 9410-9424, PubMed 36093022 , DOI 10.1039/d1sc06998e , Abstract

Experiments performed 4 experiments Detail

#	Name	Isotope labeling	Concentration
1	PaDBS1R2	natural abundance	1.0 mM
2	TFE	natural abundance	30 %
3	H2O	natural abundance	60 %
4	D2O	natural abundance	10 %
5	DSS	natural abundance	10 %

#	Name	Isotope labeling	Concentration
1	PaDBS1R2	natural abundance	1.0 mM
2	TFE	natural abundance	30 %
3	H2O	natural abundance	60 %
4	D2O	natural abundance	10 %
5	DSS	natural abundance	10 %

#	Name	Isotope labeling	Concentration
1	PaDBS1R2	natural abundance	1.0 mM
2	TFE	natural abundance	30 %
3	H2O	natural abundance	60 %
4	D2O	natural abundance	10 %
5	DSS	natural abundance	10 %

#	Name	Isotope labeling	Concentration
1	PaDBS1R2	natural abundance	1.0 mM
2	TFE	natural abundance	30 %
3	H2O	natural abundance	60 %
4	D2O	natural abundance	10 %
5	DSS	natural abundance	10 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30439_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: bmr30439_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	251		100.0 (chain: 1, length: 19)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 19, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 160
  - ¹³C chemical shifts: 73
  - ¹⁵N chemical shifts: 18
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- 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	138	132	95.7
¹³C chemical shifts	99	73	73.7
¹⁵N chemical shifts	20	18	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	38	100.0
¹³C chemical shifts	38	19	50.0
¹⁵N chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	100	94	94.0
¹³C chemical shifts	61	54	88.5
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	14	14	100.0

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

Keywords ANTIMICROBIAL PROTEIN, Antibiotics, Antimicrobial Peptide, Bacterial Resistance, Cationic Peptide

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BMRB: 30439

Experiments performed 4 experiments Detail

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Chemical shift validation 3 contents Detail