BMRBj - BMREntryMaster

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err
1	1	1	PRO	HA	H	4.382	0.002
2	1	1	PRO	HB2	H	2.459	0.005
3	1	1	PRO	HB3	H	1.980	0.000
4	1	1	PRO	HG2	H	2.052	0.000
5	1	1	PRO	HG3	H	2.011	0.001
6	1	1	PRO	HD2	H	3.398	0.001
7	1	1	PRO	HD3	H	3.381	0.001
8	1	1	PRO	CA	C	62.293	0.000
9	1	1	PRO	CB	C	32.463	0.000
10	1	2	MET	H	H	8.645	0.002
11	1	2	MET	HA	H	4.454	0.002
12	1	2	MET	HB2	H	2.079	0.000
13	1	2	MET	HB3	H	2.015	0.002
14	1	2	MET	HG2	H	2.595	0.001
15	1	2	MET	HG3	H	2.555	0.002
16	1	2	MET	HE1	H	2.050	0.004
17	1	2	MET	HE2	H	2.050	0.004
18	1	2	MET	HE3	H	2.050	0.004
19	1	2	MET	CA	C	56.224	0.000
20	1	2	MET	CB	C	32.640	0.054
21	1	2	MET	CG	C	31.922	0.005
22	1	2	MET	CE	C	16.487	0.000
23	1	2	MET	N	N	120.280	0.000
24	1	3	ALA	H	H	8.253	0.003
25	1	3	ALA	HA	H	4.162	0.002
26	1	3	ALA	HB1	H	1.390	0.002
27	1	3	ALA	HB2	H	1.390	0.002
28	1	3	ALA	HB3	H	1.390	0.002
29	1	3	ALA	CA	C	53.859	0.000
30	1	3	ALA	CB	C	18.628	0.000
31	1	3	ALA	N	N	124.396	0.000
32	1	4	LYS	H	H	7.907	0.001
33	1	4	LYS	HA	H	4.195	0.002
34	1	4	LYS	HB2	H	1.838	0.010
35	1	4	LYS	HB3	H	1.750	0.005
36	1	4	LYS	HG2	H	1.435	0.001
37	1	4	LYS	HG3	H	1.397	0.001
38	1	4	LYS	HD2	H	1.695	0.001
39	1	4	LYS	HD3	H	1.665	0.000
40	1	4	LYS	HE2	H	2.968	0.001
41	1	4	LYS	HE3	H	2.944	0.001
42	1	4	LYS	CA	C	57.153	0.000
43	1	4	LYS	CB	C	32.679	0.024
44	1	4	LYS	CG	C	25.205	0.008
45	1	4	LYS	CD	C	29.080	0.000
46	1	4	LYS	CE	C	42.170	0.000
47	1	4	LYS	N	N	116.497	0.000
48	1	5	LEU	H	H	7.705	0.001
49	1	5	LEU	HA	H	4.343	0.004
50	1	5	LEU	HB2	H	1.646	0.000
51	1	5	LEU	HB3	H	1.635	0.001
52	1	5	LEU	HG	H	1.617	0.000
53	1	5	LEU	HD11	H	0.904	0.001
54	1	5	LEU	HD12	H	0.904	0.001
55	1	5	LEU	HD13	H	0.904	0.001
56	1	5	LEU	HD21	H	0.841	0.000
57	1	5	LEU	HD22	H	0.841	0.000
58	1	5	LEU	HD23	H	0.841	0.000
59	1	5	LEU	CA	C	55.493	0.000
60	1	5	LEU	CB	C	42.954	0.001
61	1	5	LEU	CG	C	27.212	0.000
62	1	5	LEU	CD1	C	24.120	0.000
63	1	5	LEU	CD2	C	23.174	0.000
64	1	5	LEU	N	N	122.029	0.000
65	1	6	LEU	H	H	7.675	0.002
66	1	6	LEU	HA	H	4.291	0.002
67	1	6	LEU	HB2	H	1.769	0.001
68	1	6	LEU	HB3	H	1.734	0.003
69	1	6	LEU	HG	H	1.625	0.000
70	1	6	LEU	HD11	H	0.939	0.003
71	1	6	LEU	HD12	H	0.939	0.003
72	1	6	LEU	HD13	H	0.939	0.003
73	1	6	LEU	HD21	H	0.879	0.001
74	1	6	LEU	HD22	H	0.879	0.001
75	1	6	LEU	HD23	H	0.879	0.001
76	1	6	LEU	CA	C	55.809	0.000
77	1	6	LEU	CB	C	40.220	0.004
78	1	6	LEU	CG	C	27.251	0.000
79	1	6	LEU	CD1	C	24.112	0.000
80	1	6	LEU	CD2	C	23.086	0.000
81	1	6	LEU	N	N	120.409	0.000
82	1	7	PRO	HA	H	4.217	0.004
83	1	7	PRO	HB2	H	2.329	0.004
84	1	7	PRO	HB3	H	1.822	0.002
85	1	7	PRO	HG2	H	2.083	0.006
86	1	7	PRO	HG3	H	1.963	0.006
87	1	7	PRO	HD2	H	3.714	0.001
88	1	7	PRO	HD3	H	3.621	0.002
89	1	7	PRO	CA	C	65.880	0.000
90	1	7	PRO	CB	C	31.319	0.000
91	1	8	ARG	H	H	7.457	0.001
92	1	8	ARG	HA	H	4.068	0.004
93	1	8	ARG	HB2	H	1.975	0.001
94	1	8	ARG	HB3	H	1.915	0.000
95	1	8	ARG	HG2	H	1.751	0.001
96	1	8	ARG	HG3	H	1.656	0.003
97	1	8	ARG	HD2	H	3.180	0.001
98	1	8	ARG	HD3	H	3.152	0.002
99	1	8	ARG	HE	H	7.199	0.001
100	1	8	ARG	CA	C	58.583	0.000
101	1	8	ARG	CB	C	30.033	0.000
102	1	8	ARG	CG	C	27.600	0.000
103	1	8	ARG	CD	C	43.391	0.034
104	1	8	ARG	N	N	115.174	0.000
105	1	9	ILE	H	H	7.793	0.002
106	1	9	ILE	HA	H	3.792	0.003
107	1	9	ILE	HB	H	1.953	0.001
108	1	9	ILE	HG12	H	1.129	0.002
109	1	9	ILE	HG13	H	1.589	0.001
110	1	9	ILE	HG21	H	0.889	0.001
111	1	9	ILE	HG22	H	0.889	0.001
112	1	9	ILE	HG23	H	0.889	0.001
113	1	9	ILE	HD11	H	0.812	0.013
114	1	9	ILE	HD12	H	0.812	0.013
115	1	9	ILE	HD13	H	0.812	0.013
116	1	9	ILE	CA	C	64.095	0.000
117	1	9	ILE	CB	C	38.244	0.000
118	1	9	ILE	CG1	C	28.303	0.006
119	1	9	ILE	CG2	C	16.695	0.000
120	1	9	ILE	CD1	C	12.353	0.000
121	1	9	ILE	N	N	119.933	0.000
122	1	10	LYS	H	H	8.200	0.001
123	1	10	LYS	HA	H	3.890	0.002
124	1	10	LYS	HB2	H	1.784	0.001
125	1	10	LYS	HB3	H	1.843	0.002
126	1	10	LYS	HG2	H	1.335	0.004
127	1	10	LYS	HG3	H	1.475	0.001
128	1	10	LYS	HD2	H	1.645	0.000
129	1	10	LYS	HD3	H	1.625	0.001
130	1	10	LYS	CA	C	59.868	0.000
131	1	10	LYS	CB	C	32.805	0.000
132	1	10	LYS	CG	C	25.345	0.000
133	1	10	LYS	CD	C	29.329	0.004
134	1	10	LYS	N	N	119.698	0.000
135	1	11	LYS	H	H	7.691	0.001
136	1	11	LYS	HA	H	3.947	0.003
137	1	11	LYS	HB2	H	1.796	0.000
138	1	11	LYS	HB3	H	1.880	0.001
139	1	11	LYS	HG2	H	1.438	0.000
140	1	11	LYS	HG3	H	1.382	0.006
141	1	11	LYS	HD2	H	1.656	0.000
142	1	11	LYS	HD3	H	1.679	0.000
143	1	11	LYS	HE2	H	2.966	0.001
144	1	11	LYS	HE3	H	2.997	0.000
145	1	11	LYS	CA	C	59.498	0.000
146	1	11	LYS	CB	C	32.647	0.013
147	1	11	LYS	CG	C	24.531	0.010
148	1	11	LYS	CD	C	29.432	0.006
149	1	11	LYS	CE	C	42.345	0.000
150	1	11	LYS	N	N	116.350	0.000
151	1	12	LYS	H	H	7.634	0.001
152	1	12	LYS	HA	H	4.048	0.004
153	1	12	LYS	HB2	H	1.954	0.002
154	1	12	LYS	HB3	H	1.988	0.003
155	1	12	LYS	HG2	H	1.537	0.001
156	1	12	LYS	HG3	H	1.407	0.001
157	1	12	LYS	HD2	H	1.663	0.001
158	1	12	LYS	HD3	H	1.605	0.004
159	1	12	LYS	HE2	H	2.970	0.000
160	1	12	LYS	HE3	H	2.986	0.000
161	1	12	LYS	CA	C	59.047	0.000
162	1	12	LYS	CB	C	32.331	0.000
163	1	12	LYS	CG	C	25.254	0.006
164	1	12	LYS	CD	C	29.642	0.005
165	1	12	LYS	CE	C	41.974	0.003
166	1	12	LYS	N	N	119.147	0.000
167	1	13	ILE	H	H	8.079	0.002
168	1	13	ILE	HA	H	3.729	0.003
169	1	13	ILE	HB	H	1.906	0.001
170	1	13	ILE	HG12	H	1.087	0.001
171	1	13	ILE	HG21	H	0.852	0.004
172	1	13	ILE	HG22	H	0.852	0.004
173	1	13	ILE	HG23	H	0.852	0.004
174	1	13	ILE	HD11	H	0.775	0.001
175	1	13	ILE	HD12	H	0.775	0.001
176	1	13	ILE	HD13	H	0.775	0.001
177	1	13	ILE	CA	C	64.725	0.000
178	1	13	ILE	CB	C	38.194	0.000
179	1	13	ILE	CG1	C	28.351	0.000
180	1	13	ILE	CG2	C	16.536	0.000
181	1	13	ILE	CD1	C	12.697	0.000
182	1	13	ILE	N	N	120.178	0.000
183	1	14	LEU	H	H	8.170	0.002
184	1	14	LEU	HA	H	4.084	0.002
185	1	14	LEU	HB2	H	1.816	0.001
186	1	14	LEU	HB3	H	1.779	0.003
187	1	14	LEU	HG	H	1.521	0.001
188	1	14	LEU	HD11	H	0.852	0.002
189	1	14	LEU	HD12	H	0.852	0.002
190	1	14	LEU	HD13	H	0.852	0.002
191	1	14	LEU	HD21	H	0.828	0.001
192	1	14	LEU	HD22	H	0.828	0.001
193	1	14	LEU	HD23	H	0.828	0.001
194	1	14	LEU	CA	C	57.553	0.000
195	1	14	LEU	CB	C	41.764	0.014
196	1	14	LEU	CG	C	27.958	0.000
197	1	14	LEU	CD1	C	24.845	0.000
198	1	14	LEU	CD2	C	22.592	0.000
199	1	14	LEU	N	N	119.887	0.000
200	1	15	ALA	H	H	7.889	0.001
201	1	15	ALA	HA	H	4.139	0.009
202	1	15	ALA	HB1	H	1.470	0.002
203	1	15	ALA	HB2	H	1.470	0.002
204	1	15	ALA	HB3	H	1.470	0.002
205	1	15	ALA	CA	C	54.259	0.000
206	1	15	ALA	CB	C	18.169	0.000
207	1	15	ALA	N	N	120.106	0.000
208	1	16	ALA	H	H	7.667	0.001
209	1	16	ALA	HA	H	4.187	0.002
210	1	16	ALA	HB1	H	1.451	0.004
211	1	16	ALA	HB2	H	1.451	0.004
212	1	16	ALA	HB3	H	1.451	0.004
213	1	16	ALA	CA	C	53.594	0.000
214	1	16	ALA	CB	C	18.531	0.000
215	1	16	ALA	N	N	119.488	0.000
216	1	17	ALA	H	H	7.889	0.001
217	1	17	ALA	HA	H	4.128	0.002
218	1	17	ALA	HB1	H	1.235	0.003
219	1	17	ALA	HB2	H	1.235	0.003
220	1	17	ALA	HB3	H	1.235	0.003
221	1	17	ALA	CA	C	53.347	0.000
222	1	17	ALA	CB	C	18.643	0.000
223	1	17	ALA	N	N	119.825	0.000
224	1	18	PHE	H	H	7.767	0.001
225	1	18	PHE	HA	H	4.564	0.004
226	1	18	PHE	HB2	H	3.217	0.002
227	1	18	PHE	HB3	H	2.999	0.005
228	1	18	PHE	CA	C	57.831	0.000
229	1	18	PHE	CB	C	39.199	0.024
230	1	18	PHE	N	N	116.592	0.000
231	1	19	LYS	H	H	7.707	0.001
232	1	19	LYS	HA	H	4.289	0.006
233	1	19	LYS	HB2	H	1.801	0.001
234	1	19	LYS	HB3	H	1.880	0.004
235	1	19	LYS	HG2	H	1.391	0.000
236	1	19	LYS	HG3	H	1.435	0.001
237	1	19	LYS	HD2	H	1.658	0.001
238	1	19	LYS	HD3	H	1.668	0.000
239	1	19	LYS	HE2	H	2.947	0.001
240	1	19	LYS	HE3	H	2.994	0.000
241	1	19	LYS	CA	C	58.048	0.000
242	1	19	LYS	CB	C	32.494	0.002
243	1	19	LYS	CG	C	24.706	0.005
244	1	19	LYS	CD	C	29.201	0.002
245	1	19	LYS	CE	C	42.161	0.000
246	1	19	LYS	N	N	119.027	0.000

Protein Blocks Logo

Calculated from 10 models in PDB: 6CSZ, 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	PaDBS1R3	natural abundance	1 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	PaDBS1R3	natural abundance	1 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	PaDBS1R3	natural abundance	1 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	PaDBS1R3	natural abundance	1 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	bmr30440_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	OK

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr30440_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	246		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: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 19, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 158
  - ¹³C chemical shifts: 71
  - ¹⁵N chemical shifts: 17
- 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	136	128	94.1
¹³C chemical shifts	100	71	71.0
¹⁵N chemical shifts	18	17	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	36	100.0
¹³C chemical shifts	38	19	50.0
¹⁵N chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	100	92	92.0
¹³C chemical shifts	62	52	83.9
¹⁵N chemical shifts	1	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	15	100.0
¹³C chemical shifts	15	15	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: 30440

Experiments performed 4 experiments Detail

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Chemical shift validation 3 contents Detail