BMRB Entry 25872

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25872
MolProbity Validation Chart

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Title:
TrkA transmembrane domain NMR structure in DPC micelles
Deposition date:
2015-10-29
Original release date:
2016-11-03
Authors:
Nadezhdin, Kirill; Goncharuk, Sergey; Arseniev, Alexander
Citation:

Citation: Nadezhdin, Kirill; Goncharuk, Sergey; Arseniev, Alexander; Vilar, Marcial. "TrkA transmembrane domain NMR structure in DPC micelles"  .

Assembly members:

Assembly members:
entity, polymer, 39 residues, 4214.127 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: pGEMEX-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKKDETPFGVSVAVGLAVFA CLFLSTLLLVLNKAGRRNK

Data sets:
Data typeCount
13C chemical shifts154
15N chemical shifts37
1H chemical shifts277

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 39 residues - 4214.127 Da.

1   METLYSLYSASPGLUTHRPROPHEGLYVAL
2   SERVALALAVALGLYLEUALAVALPHEALA
3   CYSLEUPHELEUSERTHRLEULEULEUVAL
4   LEUASNLYSALAGLYARGARGASNLYS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; entity 1 mM; DPC, [U-100% 2H], 40 mM; potassium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - visualization

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks