BMRB Entry 25270

Title:
SpoVM P9A mutant structure
Deposition date:
2014-10-07
Original release date:
2015-03-30
Authors:
Tian, Fang; Gill, Richard
Citation:

Citation: Tian, Fang; Gill, Richard; Castaining, Jean-Philippe; Hsin, Jen; Tan, Irene; Wang, Xingshen; Huang, Kerwyn-Casey; Ramamurthi, Kumaran. "Structural and mechanistic basis for the geometric-driven subcellular localization of a small protein"  Nat. Struct. Biol. ., .-..

Assembly members:

Assembly members:
Molecule_1, polymer, 26 residues, 2996.7227 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pKR209

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_1: MKFYTIKLAKFLGGIVRAML GSFRKD

Data sets:
Data typeCount
1H chemical shifts176
13C chemical shifts97
15N chemical shifts24

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 26 residues - 2996.7227 Da.

1   METLYSPHETYRTHRILELYSLEUALALYS
2   PHELEUGLYGLYILEVALARGALAMETLEU
3   GLYSERPHEARGLYSASP

Samples:

sample_1: Molecule_1, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 16 mM; sodium chloride 80 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 310 K; pH: 6; pressure: 1 atm; ionic strength: 80 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

Related Database Links:

PDB

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