BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	82.8 % (341 of 412)	94.0 % (205 of 218)	64.2 % (102 of 159)	97.1 % (34 of 35)
Backbone	84.0 % (168 of 200)	98.5 % (66 of 67)	70.3 % (71 of 101)	96.9 % (31 of 32)
Sidechain	84.1 % (206 of 245)	92.1 % (139 of 151)	70.3 % (64 of 91)	100.0 % (3 of 3)
Aromatic	43.2 % (19 of 44)	81.8 % (18 of 22)	0.0 % (0 of 21)	100.0 % (1 of 1)
Methyl	96.2 % (25 of 26)	100.0 % (13 of 13)	92.3 % (12 of 13)

1. entity 1

DCLGAFRKCI PDNDKCCRPN LVCSRLHRWC KYVF

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 Pa, Temperature 298 K, pH 3.5 (±0.5), Details 2 mg/mL [AFLR]GpTx-1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	[AFLR]GpTx-1	natural abundance		2 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 Pa, Temperature 298 K, pH 3.5 (±0.5), Details 2 mg/mL [AFLR]GpTx-1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	[AFLR]GpTx-1	natural abundance		2 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 6MK5, Strand ID: A Detail

Release date

2018-09-25

Citation

Peptide-membrane interactions affect the inhibitory potency and selectivity of spider toxins ProTx-II and GpTx-1
Lawrence, N., Wu, B., Ligutti, J., Cheneval, O., Agwa, A.J., Benfield, A.H., Biswas, K., Craik, D.J., Miranda, L.P., Henriques, S.T., Schroeder, C.I.
ACS Chem. Biol. (2018), 14, 118-130, PubMed 30507158 , DOI 10.1021/acschembio.8b00989 , Abstract

Related entities 1. Toxin GTx1-15, : 1 : 106 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30522_6mk5.nef
Input source #2: Coordindates	6mk5.cif
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)
A:2:CYS:SG	A:17:CYS:SG	oxidized, CA 54.631, CB 44.07 ppm	oxidized, CA 56.085, CB 41.794 ppm	2.044
A:9:CYS:SG	A:23:CYS:SG	oxidized, CA 53.491, CB 46.344 ppm	oxidized, CA 56.021, CB 37.735 ppm	2.016
A:16:CYS:SG	A:30:CYS:SG	oxidized, CA 56.409, CB 38.483 ppm	oxidized, CA 54.697, CB 39.085 ppm	2.031

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----
DCLGAFRKCIPDNDKCCRPNLVCSRLHRWCKYVF
||||||||||||||||||||||||||||||||||
DCLGAFRKCIPDNDKCCRPNLVCSRLHRWCKYVF

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	34	0	0	100.0

Content subtype: combined_30522_6mk5.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	341		100.0 (chain: A, length: 34)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	506 (1)	noe	100.0 (chain: A, length: 34)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	6 (1)	hbond	17.6 (chain: A, length: 34)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	39 (39)	.	79.4 (chain: A, length: 34)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 34, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 209
  - ¹³C chemical shifts: 96
  - ¹⁵N chemical shifts: 36
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
8	LYS	HZ1	7.652
8	LYS	HZ2	7.652
8	LYS	HZ3	7.652
8	LYS	NZ	124.166
15	LYS	HZ1	7.481
15	LYS	HZ2	7.481
15	LYS	HZ3	7.481
15	LYS	NZ	108.545

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	218	203	93.1
¹³C chemical shifts	159	96	60.4
¹⁵N chemical shifts	39	34	87.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	67	66	98.5
¹³C chemical shifts	68	34	50.0
¹⁵N chemical shifts	32	31	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	151	137	90.7
¹³C chemical shifts	91	62	68.1
¹⁵N chemical shifts	7	3	42.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	11	84.6
¹³C chemical shifts	13	10	76.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	18	81.8
¹³C chemical shifts	21	0	0.0
¹⁵N chemical shifts	1	1	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 34, Sequence coverage: 100.0%
- Total number of restraints: 506
- Weight of restraints: 1.0 (506)
- Potential type of restraints: square-well-parabolic (506)
- Range of distance target values: 1.42, 2.75 (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
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 34, Sequence coverage: 17.6%
  - Total number of restraints: 6
  - Weight of restraints: 1.0 (6)
  - Potential type of restraints: square-well-parabolic (6)
  - Range of distance target values: 1.15, 1.65 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 34, Sequence coverage: 79.4%
- Total number of restraints: 39
- Total number of restraints per polymer type: 39
- Weight of restraints: 1.0 (39)
- Potential type of restraints: square-well-parabolic (39)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords GpTx-1 analogue, TOXIN, peptide-membrane interactions, spider toxin, voltage-sensitive sodium channels

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BMRB: 30522

Sample #1

Sample #2

Related entities 1. Toxin GTx1-15, : 1 : 106 entities Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail