BMRB Entry 15608

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15608
MolProbity Validation Chart

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Title:
NMR STRUCTURE OF PROTEIN VPA0419 FROM VIBRIO PARAHAEMOLYTICUS: NORTHEAST STRUCTURAL GENOMICS TARGET VPR68.
Deposition date:
2007-12-28
Original release date:
2008-02-13
Authors:
SINGARAPU, KIRAN KUMAR; SUKUMARAN, DINESH; ELETSKI, ALEX; PARISH, DAVID; Zhao, Li; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS
Citation:

Citation: SINGARAPU, KIRAN KUMAR; SUKUMARAN, DINESH; Xiao, Rong; Acton, THOMAS; Montelione, Gaetano; SZYPERSKI, THOMAS. "NMR STRUCTURE OF PROTEIN VPA0419 FROM VIBRIO PARAHAEMOLYTICUS: NORTHEAST STRUCTURAL GENOMICS TARGET VPR68."  .

Assembly members:

Assembly members:
VPA0419, polymer, 91 residues, 10301.690 Da.

Natural source:

Natural source:   Common Name: Vibrio parahaemolyticus   Taxonomy ID: 670   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio parahaemolyticus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VPA0419: AGEIGFIIKEGDEVADVTIF AETKDALESELAKYIELAKS VCAGVEYNVSELTEESKELT ARFKFEVSAEKLIFELKTRS LARLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts86
1H chemical shifts623

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1VPA04191

Entities:

Entity 1, VPA0419 91 residues - 10301.690 Da.

1   ALAGLYGLUILEGLYPHEILEILELYSGLU
2   GLYASPGLUVALALAASPVALTHRILEPHE
3   ALAGLUTHRLYSASPALALEUGLUSERGLU
4   LEUALALYSTYRILEGLULEUALALYSSER
5   VALCYSALAGLYVALGLUTYRASNVALSER
6   GLULEUTHRGLUGLUSERLYSGLULEUTHR
7   ALAARGPHELYSPHEGLUVALSERALAGLU
8   LYSLEUILEPHEGLULEULYSTHRARGSER
9   LEUALAARGLEUGLUHISHISHISHISHIS
10   HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.07 mM; NaCl 100 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4,3 D GFT HNNACBCAsample_1isotropicsample_conditions_1
4,3 D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D HABCABCONHNsample_1isotropicsample_conditions_1
4,3D GFT HCCH COSYsample_1isotropicsample_conditions_1
3D HCCH COSYsample_1isotropicsample_conditions_1
3D SimNOESYsample_1isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

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

PSVS, Bhattacharya and Montelione - validation

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAC61762
GB AGB11762 AGQ94127 AGQ97242 AHJ02336 AKU56863
REF NP_799929 WP_005480806 WP_005488152 WP_024701459 WP_025565380

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