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Found 1 Document (0.615 seconds)

BMRB: 19810

2MLA

Solution structure of BmKTX-D19K

Authors

Hong, J., Lin, D., Chen, Z., Wu, Y.

Assembly

BmKTX-D19K

Entity

1. BmKTX-D19K (polymer, Thiol state: all disulfide bound), 37 monomers, 3981.844 Da Detail

VGINVKCKHS GQCLKPCKKA GMRFGKCING KCDCTPK

Formula weight

3981.844 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS7:SG	1:CYS27:SG
2	disulfide	sing	1:CYS13:SG	1:CYS32:SG
3	disulfide	sing	1:CYS17:SG	1:CYS34:SG

Source organism

Scorpiones

Exptl. method

solution NMR

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 96.1 %, Completeness (bb): 93.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	96.1 % (221 of 230)	96.1 % (221 of 230)
Backbone	93.5 % (72 of 77)	93.5 % (72 of 77)
Sidechain	97.4 % (149 of 153)	97.4 % (149 of 153)
Aromatic	85.7 % (6 of 7)	85.7 % (6 of 7)
Methyl	100.0 % (12 of 12)	100.0 % (12 of 12)

1. entity

VGINVKCKHS GQCLKPCKKA GMRFGKCING KCDCTPK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Concentration
1	entity	natural abundance	2 mM
2	D2O	natural abundance	10 %
3	sodium phosphate	natural abundance	25 mM
4	H2O	natural abundance	90 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2MLA, Strand ID: A Detail

Release date

2015-02-22

Citation

Solution structure of BmKTX-D19K
Hong, J., Lin, D., Chen, Z., Wu, Y.
Not known

Related entities 1. BmKTX-D19K, : 1 : 5 : 115 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19810_2mla.nef
Input source #2: Coordindates	2mla.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:7:CYS:SG	A:27:CYS:SG	unknown	unknown	2.025
A:13:CYS:SG	A:32:CYS:SG	unknown	unknown	2.032
A:17:CYS:SG	A:34:CYS:SG	unknown	unknown	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-------
VGINVKCKHSGQCLKPCKKAGMRFGKCINGKCDCTPK
|||||||||||||||||||||||||||||||||||||
VGINVKCKHSGQCLKPCKKAGMRFGKCINGKCDCTPK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	37	0	0	100.0

Content subtype: combined_19810_2mla.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_chem_shift_list_1	Warning	222		100.0 (chain: A, length: 37)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	28 (1)	hbond	51.4 (chain: A, length: 37)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	23 (23)	.	86.5 (chain: A, length: 37)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 222
- Completeness of assignments
  - Entity_assemble_ID: A
- 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)
9	HIS	HD1	8.444
23	ARG	HH21	6.81
23	ARG	HH22	6.81

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	230	219	95.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	73	94.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	146	95.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	12	92.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	7	3	42.9

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: hbond
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 51.4%
- Total number of restraints: 28
- Weight of restraints: 1.0 (28)
- Potential type of restraints: square-well-parabolic (28)
- Range of distance target values: 2.05, 3.05 (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: 37, Sequence coverage: 86.5%
- Total number of restraints: 23
- Total number of restraints per polymer type: 23
- Weight of restraints: 1.0 (23)
- Potential type of restraints: square-well-parabolic (23)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords peptide

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Found 1 Document (0.615 seconds)

BMRB: 19810

Sample

Related entities 1. BmKTX-D19K, : 1 : 5 : 115 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail