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BMRB: 30847

7LGV

NMR structure of Beta-KTx14.3

Authors

Carranza-Gonzalez, L.E., Titaux-Delgado, G.A., del Rio-Portilla, J.F.

Assembly

Neurotoxin beta-KTx 14.3

Entity

1. Neurotoxin beta-KTx 14.3 (polymer, Thiol state: all disulfide bound), 48 monomers, 5264.020 Da Detail

IAGVADLNNM SQLGCPFIEK WCEDHCESKK QVGKCENFDC SCVKLGGK

Formula weight

5264.02 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS15:SG	1:CYS35:SG
2	disulfide	sing	1:CYS22:SG	1:CYS40:SG
3	disulfide	sing	1:CYS26:SG	1:CYS42:SG

Source organism

Lychas mucronatus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chemcal Shifts

¹H: 257 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val	Val err
1	1	2	ALA	H	H	8.646	0.000
2	1	2	ALA	HA	H	4.387	0.000
3	1	2	ALA	HB1	H	1.403	0.000
4	1	2	ALA	HB2	H	1.403	0.000
5	1	2	ALA	HB3	H	1.403	0.000
6	1	3	GLY	H	H	8.411	0.000
7	1	3	GLY	HA2	H	3.946	0.000
8	1	3	GLY	HA3	H	3.946	0.000
9	1	4	VAL	H	H	7.935	0.000
10	1	4	VAL	HA	H	4.107	0.000
11	1	4	VAL	HB	H	2.036	0.000
12	1	4	VAL	HG11	H	0.903	0.000
13	1	4	VAL	HG12	H	0.903	0.000
14	1	4	VAL	HG13	H	0.903	0.000
15	1	4	VAL	HG21	H	0.903	0.000
16	1	4	VAL	HG22	H	0.903	0.000
17	1	4	VAL	HG23	H	0.903	0.000
18	1	5	ALA	H	H	8.409	0.000
19	1	5	ALA	HA	H	4.283	0.000
20	1	5	ALA	HB1	H	1.344	0.000
21	1	5	ALA	HB2	H	1.344	0.000
22	1	5	ALA	HB3	H	1.344	0.000
23	1	6	ASP	H	H	8.322	0.000
24	1	6	ASP	HA	H	4.672	0.000
25	1	6	ASP	HB2	H	2.805	0.000
26	1	6	ASP	HB3	H	2.925	0.000
27	1	7	LEU	H	H	8.162	0.000
28	1	7	LEU	HA	H	4.252	0.000
29	1	7	LEU	HB2	H	1.585	0.000
30	1	7	LEU	HB3	H	1.585	0.000
31	1	7	LEU	HD11	H	0.823	0.000
32	1	7	LEU	HD12	H	0.823	0.000
33	1	7	LEU	HD13	H	0.823	0.000
34	1	7	LEU	HD21	H	0.901	0.000
35	1	7	LEU	HD22	H	0.901	0.000
36	1	7	LEU	HD23	H	0.901	0.000
37	1	8	ASN	H	H	8.243	0.000
38	1	8	ASN	HA	H	4.618	0.000
39	1	8	ASN	HB2	H	2.731	0.000
40	1	8	ASN	HB3	H	2.809	0.000
41	1	8	ASN	HD21	H	6.871	0.000
42	1	8	ASN	HD22	H	7.568	0.000
43	1	9	ASN	H	H	8.080	0.000
44	1	9	ASN	HA	H	4.562	0.000
45	1	9	ASN	HB2	H	2.665	0.000
46	1	9	ASN	HB3	H	2.711	0.000
47	1	10	MET	H	H	8.190	0.000
48	1	10	MET	HA	H	4.301	0.000
49	1	10	MET	HB2	H	1.811	0.000
50	1	10	MET	HB3	H	2.400	0.000
51	1	10	MET	HG2	H	2.518	0.000
52	1	10	MET	HG3	H	2.518	0.000
53	1	10	MET	HE1	H	1.952	0.000
54	1	10	MET	HE2	H	1.952	0.000
55	1	10	MET	HE3	H	1.952	0.000
56	1	11	SER	H	H	8.607	0.000
57	1	11	SER	HA	H	4.046	0.000
58	1	11	SER	HB2	H	3.881	0.000
59	1	11	SER	HB3	H	3.881	0.000
60	1	15	CYS	H	H	7.983	0.000
61	1	15	CYS	HA	H	4.532	0.000
62	1	15	CYS	HB2	H	2.692	0.000
63	1	15	CYS	HB3	H	3.450	0.000
64	1	17	PHE	H	H	7.230	0.000
65	1	17	PHE	HA	H	4.273	0.000
66	1	17	PHE	HB2	H	3.027	0.000
67	1	17	PHE	HB3	H	3.441	0.000
68	1	17	PHE	HD1	H	7.326	0.000
69	1	17	PHE	HD2	H	7.326	0.000
70	1	17	PHE	HE1	H	7.455	0.000
71	1	17	PHE	HE2	H	7.455	0.000
72	1	17	PHE	HZ	H	7.382	0.000
73	1	18	ILE	H	H	7.896	0.000
74	1	18	ILE	HA	H	4.300	0.000
75	1	18	ILE	HB	H	1.789	0.000
76	1	18	ILE	HG12	H	1.566	0.000
77	1	18	ILE	HG13	H	1.566	0.000
78	1	18	ILE	HG21	H	1.107	0.000
79	1	18	ILE	HG22	H	1.107	0.000
80	1	18	ILE	HG23	H	1.107	0.000
81	1	18	ILE	HD11	H	0.870	0.000
82	1	18	ILE	HD12	H	0.870	0.000
83	1	18	ILE	HD13	H	0.870	0.000
84	1	19	GLU	H	H	8.391	0.000
85	1	19	GLU	HA	H	4.454	0.002
86	1	19	GLU	HB2	H	1.842	0.000
87	1	19	GLU	HB3	H	1.979	0.000
88	1	19	GLU	HG2	H	2.131	0.000
89	1	19	GLU	HG3	H	2.454	0.000
90	1	20	LYS	H	H	7.464	0.000
91	1	20	LYS	HA	H	3.881	0.000
92	1	20	LYS	HB2	H	2.461	0.000
93	1	20	LYS	HB3	H	2.461	0.000
94	1	20	LYS	HG2	H	0.717	0.000
95	1	20	LYS	HG3	H	0.717	0.000
96	1	20	LYS	HD2	H	1.174	0.000
97	1	20	LYS	HD3	H	1.174	0.000
98	1	21	TRP	H	H	7.075	0.000
99	1	21	TRP	HA	H	4.802	0.002
100	1	21	TRP	HB2	H	3.396	0.000
101	1	21	TRP	HB3	H	3.517	0.000
102	1	21	TRP	HD1	H	7.205	0.000
103	1	21	TRP	HE1	H	10.323	0.000
104	1	21	TRP	HE3	H	7.487	0.000
105	1	21	TRP	HZ2	H	7.584	0.000
106	1	21	TRP	HZ3	H	7.092	0.000
107	1	21	TRP	HH2	H	7.209	0.000
108	1	22	CYS	H	H	9.425	0.000
109	1	22	CYS	HA	H	4.636	0.002
110	1	22	CYS	HB2	H	2.739	0.000
111	1	22	CYS	HB3	H	3.281	0.000
112	1	24	ASP	H	H	8.395	0.003
113	1	24	ASP	HA	H	4.677	0.000
114	1	24	ASP	HB2	H	2.814	0.000
115	1	24	ASP	HB3	H	2.914	0.000
116	1	25	HIS	H	H	8.483	0.001
117	1	25	HIS	HA	H	4.467	0.000
118	1	25	HIS	HB2	H	3.341	0.002
119	1	25	HIS	HB3	H	3.562	0.000
120	1	25	HIS	HD2	H	8.730	0.000
121	1	25	HIS	HE1	H	7.014	0.000
122	1	26	CYS	H	H	8.453	0.000
123	1	26	CYS	HA	H	4.153	0.000
124	1	26	CYS	HB2	H	2.406	0.000
125	1	26	CYS	HB3	H	3.338	0.000
126	1	27	GLU	H	H	8.779	0.000
127	1	27	GLU	HA	H	4.439	0.000
128	1	27	GLU	HB2	H	2.256	0.000
129	1	27	GLU	HB3	H	2.256	0.000
130	1	27	GLU	HG2	H	2.403	0.000
131	1	27	GLU	HG3	H	2.686	0.000
132	1	28	SER	H	H	7.781	0.000
133	1	28	SER	HA	H	4.352	0.000
134	1	28	SER	HB2	H	4.031	0.001
135	1	28	SER	HB3	H	4.031	0.001
136	1	29	LYS	H	H	7.347	0.000
137	1	29	LYS	HA	H	4.548	0.000
138	1	29	LYS	HB2	H	1.677	0.001
139	1	29	LYS	HB3	H	1.965	0.000
140	1	29	LYS	HG2	H	1.304	0.000
141	1	29	LYS	HG3	H	1.304	0.000
142	1	29	LYS	HD2	H	1.529	0.000
143	1	29	LYS	HD3	H	1.529	0.000
144	1	29	LYS	HE2	H	2.768	0.000
145	1	29	LYS	HE3	H	2.899	0.000
146	1	30	LYS	H	H	8.051	0.000
147	1	30	LYS	HA	H	3.959	0.000
148	1	30	LYS	HB2	H	2.006	0.000
149	1	30	LYS	HB3	H	2.092	0.000
150	1	30	LYS	HG2	H	1.381	0.001
151	1	30	LYS	HG3	H	1.381	0.001
152	1	30	LYS	HD2	H	1.688	0.000
153	1	30	LYS	HD3	H	1.688	0.000
154	1	31	GLN	H	H	7.665	0.000
155	1	31	GLN	HA	H	4.602	0.000
156	1	31	GLN	HB2	H	1.482	0.000
157	1	31	GLN	HB3	H	2.045	0.000
158	1	31	GLN	HG2	H	2.123	0.000
159	1	31	GLN	HG3	H	2.318	0.000
160	1	31	GLN	HE21	H	6.496	0.000
161	1	31	GLN	HE22	H	6.964	0.000
162	1	32	VAL	H	H	8.564	0.000
163	1	32	VAL	HA	H	4.450	0.000
164	1	32	VAL	HB	H	1.987	0.000
165	1	32	VAL	HG11	H	0.896	0.000
166	1	32	VAL	HG12	H	0.896	0.000
167	1	32	VAL	HG13	H	0.896	0.000
168	1	32	VAL	HG21	H	0.896	0.000
169	1	32	VAL	HG22	H	0.896	0.000
170	1	32	VAL	HG23	H	0.896	0.000
171	1	33	GLY	H	H	8.660	0.000
172	1	33	GLY	HA2	H	3.358	0.000
173	1	33	GLY	HA3	H	5.297	0.000
174	1	34	LYS	H	H	8.793	0.000
175	1	34	LYS	HA	H	4.553	0.000
176	1	34	LYS	HB2	H	1.683	0.000
177	1	34	LYS	HB3	H	1.782	0.000
178	1	34	LYS	HG2	H	1.307	0.000
179	1	34	LYS	HG3	H	1.307	0.000
180	1	34	LYS	HD2	H	1.615	0.000
181	1	34	LYS	HD3	H	1.615	0.000
182	1	34	LYS	HE2	H	2.894	0.000
183	1	34	LYS	HE3	H	2.894	0.000
184	1	35	CYS	H	H	8.803	0.000
185	1	35	CYS	HA	H	5.231	0.000
186	1	35	CYS	HB2	H	2.866	0.000
187	1	35	CYS	HB3	H	3.022	0.000
188	1	36	GLU	H	H	9.206	0.000
189	1	36	GLU	HA	H	4.477	0.000
190	1	36	GLU	HB2	H	1.831	0.000
191	1	36	GLU	HB3	H	1.942	0.000
192	1	36	GLU	HG2	H	2.320	0.000
193	1	36	GLU	HG3	H	2.362	0.000
194	1	37	ASN	H	H	9.011	0.000
195	1	37	ASN	HA	H	3.716	0.000
196	1	37	ASN	HB2	H	2.873	0.000
197	1	37	ASN	HB3	H	2.904	0.000
198	1	37	ASN	HD21	H	6.775	0.000
199	1	37	ASN	HD22	H	7.527	0.000
200	1	38	PHE	H	H	7.586	0.000
201	1	38	PHE	HA	H	4.153	0.000
202	1	38	PHE	HB2	H	2.869	0.000
203	1	38	PHE	HB3	H	3.382	0.000
204	1	38	PHE	HD1	H	6.832	0.000
205	1	38	PHE	HD2	H	6.832	0.000
206	1	38	PHE	HE1	H	7.382	0.000
207	1	38	PHE	HE2	H	7.382	0.000
208	1	38	PHE	HZ	H	7.000	0.000
209	1	39	ASP	H	H	7.761	0.000
210	1	39	ASP	HA	H	4.795	0.000
211	1	39	ASP	HB2	H	2.802	0.000
212	1	39	ASP	HB3	H	2.802	0.000
213	1	40	CYS	H	H	8.482	0.000
214	1	40	CYS	HA	H	5.120	0.000
215	1	40	CYS	HB2	H	2.713	0.000
216	1	40	CYS	HB3	H	2.957	0.000
217	1	41	SER	H	H	8.832	0.000
218	1	41	SER	HA	H	4.764	0.000
219	1	41	SER	HB2	H	3.677	0.000
220	1	41	SER	HB3	H	3.845	0.000
221	1	42	CYS	H	H	8.494	0.000
222	1	42	CYS	HA	H	5.737	0.000
223	1	42	CYS	HB2	H	2.676	0.000
224	1	42	CYS	HB3	H	3.120	0.000
225	1	43	VAL	H	H	9.338	0.000
226	1	43	VAL	HA	H	4.405	0.000
227	1	43	VAL	HB	H	2.042	0.000
228	1	43	VAL	HG11	H	0.783	0.000
229	1	43	VAL	HG12	H	0.783	0.000
230	1	43	VAL	HG13	H	0.783	0.000
231	1	43	VAL	HG21	H	0.862	0.000
232	1	43	VAL	HG22	H	0.862	0.000
233	1	43	VAL	HG23	H	0.862	0.000
234	1	44	LYS	H	H	8.321	0.000
235	1	44	LYS	HA	H	4.356	0.000
236	1	44	LYS	HB2	H	1.818	0.000
237	1	44	LYS	HB3	H	1.818	0.000
238	1	44	LYS	HG2	H	1.425	0.000
239	1	44	LYS	HG3	H	1.425	0.000
240	1	44	LYS	HD2	H	1.700	0.000
241	1	44	LYS	HD3	H	1.700	0.000
242	1	45	LEU	H	H	8.493	0.000
243	1	45	LEU	HA	H	4.305	0.000
244	1	45	LEU	HB2	H	1.606	0.000
245	1	45	LEU	HB3	H	1.606	0.000
246	1	45	LEU	HD11	H	0.856	0.000
247	1	45	LEU	HD12	H	0.856	0.000
248	1	45	LEU	HD13	H	0.856	0.000
249	1	45	LEU	HD21	H	0.888	0.000
250	1	45	LEU	HD22	H	0.888	0.000
251	1	45	LEU	HD23	H	0.888	0.000
252	1	46	GLY	H	H	8.512	0.000
253	1	46	GLY	HA2	H	3.969	0.000
254	1	46	GLY	HA3	H	3.969	0.000
255	1	47	GLY	H	H	8.254	0.000
256	1	47	GLY	HA2	H	3.962	0.000
257	1	47	GLY	HA3	H	3.962	0.000

Release date

2021-03-02

Citation

Beta-KTx14.3, a scorpion toxin, blocks the human potassium channel KCNQ1
Titaux-Delgado, G.A., Lopez-Giraldo, A.E., Carrillo, E., Cofas-Vargas, L.F., Carranza-Gonzalez, L.E., Lopez-Vera, E., Garcia-Hernandez, E., del Rio-Portilla, J.F.
Biochim. Biophys. Acta. Proteins Proteom. (2023), 1871, 140906-140906, PubMed 36918120 , DOI 10.1016/j.bbapap.2023.140906 , Abstract

Related entities 1. Neurotoxin beta-KTx 14.3, : 1 : 2 : 15 entities Detail

Experiments performed 4 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	Beta-KTx14.3	natural abundance		0.8 (±0.02) mg/mL

#	Name	Isotope labeling	Type	Concentration
1	Beta-KTx14.3	natural abundance		0.8 (±0.02) mg/mL

#	Name	Isotope labeling	Type	Concentration
1	Beta-KTx14.3	natural abundance		0.8 (±0.02) mg/mL

#	Name	Isotope labeling	Type	Concentration
1	Beta-KTx14.3	natural abundance		0.8 (±0.02) mg/mL

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30847_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:15:CYS:SG	1:35:CYS:SG	unknown	unknown	n/a
1:22:CYS:SG	1:40:CYS:SG	unknown	unknown	n/a
1:26:CYS:SG	1:42:CYS:SG	unknown	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr30847_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	257		85.4 (chain: 1, length: 48)
1	Chemical shift references	chem_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 48, Sequence coverage: 85.4%
- Total number of assignments
  - ¹H chemical shifts: 257
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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	285	227	79.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	100	86	86.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	185	141	76.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	15	78.9

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

Keywords Beta-KTX, disulfide bond, ion channel, toxin

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Found 1 Document (0.492 seconds)

BMRB: 30847

Related entities 1. Neurotoxin beta-KTx 14.3, : 1 : 2 : 15 entities Detail

Experiments performed 4 experiments Detail

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Chemical shift validation 3 contents Detail