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Found 1 Document (0.506 seconds)

BMRB: 34453

6THI

Solution structure of MeuNaTxalpha-1 toxin from Mesobuthus Eupeus

Authors

Mineev, K.S., Kuzmenkov, A.I., Khusainov, G.A., Arseniev, A.S., Vassilevski, A.A.

Assembly

Sodium channel neurotoxin MeuNaTxalpha-1

Entity

1. Sodium channel neurotoxin MeuNaTxalpha-1 (polymer, Thiol state: all disulfide bound), 64 monomers, 7186.065 Da Detail

VRDGYIADDK NCAYFCGRNA YCDEECKKKG AESGYCQWAG QYGNACWCYK LPDKVPIKVS GKCN

Formula weight

7186.065 Da

Entity Connection

disulfide 5 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS12:SG	1:CYS63:SG
2	disulfide	sing	1:CYS16:SG	1:CYS22:SG
3	disulfide	sing	1:CYS16:SG	1:CYS36:SG
4	disulfide	sing	1:CYS22:SG	1:CYS46:SG
5	disulfide	sing	1:CYS26:SG	1:CYS48:SG

Source organism

Mesobuthus eupeus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.4 %, Completeness: 83.0 %, Completeness (bb): 73.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	83.0 % (606 of 730)	97.9 % (374 of 382)	60.5 % (167 of 276)	90.3 % (65 of 72)
Backbone	73.2 % (278 of 380)	97.0 % (129 of 133)	50.3 % (93 of 185)	90.3 % (56 of 62)
Sidechain	94.3 % (384 of 407)	98.4 % (245 of 249)	87.8 % (130 of 148)	90.0 % (9 of 10)
Aromatic	82.9 % (68 of 82)	100.0 % (41 of 41)	64.1 % (25 of 39)	100.0 % (2 of 2)
Methyl	100.0 % (36 of 36)	100.0 % (18 of 18)	100.0 % (18 of 18)

1. entity 1

VRDGYIADDK NCAYFCGRNA YCDEECKKKG AESGYCQWAG QYGNACWCYK LPDKVPIKVS GKCN

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 7 (±0.1), Details 2 mM MeuNaTx1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	MeuNaTx1	natural abundance		2 (±0.2) mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6THI, Strand ID: A Detail

Release date

2020-07-12

Citation

Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels
Mineev, K.S., Kuzmenkov, A.I., Khusainov, G.A., Arseniev, A.S., Vassilevski, A.A.
Mol. Cell. Proteomics. (2012), 11, M111.012054-M111.012054, PubMed 21969612 , DOI 10.1074/mcp.M111.012054 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 17988 released on 2011-11-16
Title Evolutionary diversification of Mesobuthus {alpha}-scorpion toxins affecting sodium channels.

Related entities 1. Sodium channel neurotoxin MeuNaTxalpha-1, : 1 : 1 : 1 : 165 entities Detail

Experiments performed 5 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34453_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)
1:12:CYS:SG	1:63:CYS:SG	oxidized, CB 43.821 ppm	oxidized, CB 41.542 ppm	n/a
1:16:CYS:SG	1:22:CYS:SG	oxidized, CB 47.904 ppm	oxidized, CA 58.667, CB 33.226 ppm	n/a
1:16:CYS:SG	1:36:CYS:SG	oxidized, CB 47.904 ppm	oxidized, CA 54.55, CB 37.241 ppm	n/a
1:22:CYS:SG	1:46:CYS:SG	oxidized 37.5%, reduced 62.5%, CA 58.667, CB 33.226 ppm	oxidized 95.6%, reduced 4.4%, CA 53.12, CB 34.1 ppm	n/a
1:26:CYS:SG	1:48:CYS:SG	oxidized, CA 57.763, CB 35.62 ppm	oxidized, CA 50.413, CB 38.183 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr34453_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	631		98.4 (chain: 1, length: 64)
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: 64, Sequence coverage: 98.4%
- Total number of assignments
  - ¹H chemical shifts: 410
  - ¹³C chemical shifts: 156
  - ¹⁵N chemical shifts: 65
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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	382	374	97.9
¹³C chemical shifts	276	156	56.5
¹⁵N chemical shifts	72	65	90.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	129	97.0
¹³C chemical shifts	128	26	20.3
¹⁵N chemical shifts	62	56	90.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	249	245	98.4
¹³C chemical shifts	148	130	87.8
¹⁵N chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	18	100.0
¹³C chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	41	41	100.0
¹³C chemical shifts	39	25	64.1
¹⁵N chemical shifts	2	2	100.0

Keywords Sodium channel blocker, Toxin, alpha-toxin

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Found 1 Document (0.506 seconds)

BMRB: 34453

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Sodium channel neurotoxin MeuNaTxalpha-1, : 1 : 1 : 1 : 165 entities Detail

Experiments performed 5 experiments Detail

Instrument

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Chemical shift validation 3 contents Detail