BMRB Entry 15833

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15833
MolProbity Validation Chart

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Title:
NMR CHEMICAL SHIFT ASSIGNMENTS OF PUTATIVE UNCHARACTERIZED PROTEIN. FROM METHANOCALDOCOCCUS JANNASCHII, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET GsR195
Deposition date:
2008-06-27
Original release date:
2008-08-22
Authors:
LIU, GAOHUA; ZHAO, LI; CICCOSANTI, COLLEEN; JIANG, MEI; XIAO, RONG; SWAPNA, G.V.T; NAIR, RAJESH; EVERETT, JOHN; ACTON, THOMAS; ROST, BURKHARD; Montelione, GAETANO
Citation:

Citation: LIU, GAOHUA; XIAO, RONG; Montelione, GAETANO. "N.A."  .

Assembly members:

Assembly members:
GsR195, polymer, 146 residues, 16006.114 Da.

Natural source:

Natural source:   Common Name: Methanococcus jannaschii   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus jannaschii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GsR195: MTQKFTKDMTFAQALQTHPG VAGVLRSYNLGCIGCMGAQN ESLEQGANAHGLNVEDILRD LNALALEHHHHHHMTQKFTK DMTFAQALQTHPGVAGVLRS YNLGCIGCMGAQNESLEQGA NAHGLNVEDILRDLNALALE HHHHHH

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts77
1H chemical shifts459

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GsR1951

Entities:

Entity 1, GsR195 146 residues - 16006.114 Da.

1   METTHRGLNLYSPHETHRLYSASPMETTHR
2   PHEALAGLNALALEUGLNTHRHISPROGLY
3   VALALAGLYVALLEUARGSERTYRASNLEU
4   GLYCYSILEGLYCYSMETGLYALAGLNASN
5   GLUSERLEUGLUGLNGLYALAASNALAHIS
6   GLYLEUASNVALGLUASPILELEUARGASP
7   LEUASNALALEUALALEUGLUHISHISHIS
8   HISHISHISMETTHRGLNLYSPHETHRLYS
9   ASPMETTHRPHEALAGLNALALEUGLNTHR
10   HISPROGLYVALALAGLYVALLEUARGSER
11   TYRASNLEUGLYCYSILEGLYCYSMETGLY
12   ALAGLNASNGLUSERLEUGLUGLNGLYALA
13   ASNALAHISGLYLEUASNVALGLUASPILE
14   LEUARGASPLEUASNALALEUALALEUGLU
15   HISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.11 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: entity, [U-10% 13C; U-100% 15N], 1.48 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D SIMULTANEOUS CN-NOESYsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONHNsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis, peak picking

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY v1.3.1, Bartels et al. - data analysis

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 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