BMRB Entry 16794

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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/BMR16794
MolProbity Validation Chart

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Title:
NMR Solution Structure of Q7A1E8 protein from Staphylococcus aureus: Northeast Structural Genomics Consortium target: ZR215
Deposition date:
2010-03-28
Original release date:
2012-08-03
Authors:
Swapna, G.V.T.; Montelione, Alexander; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano
Citation:

Citation: Swapna, G.V.T.; Montelione, Alexander; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano. "NMR solution structure of Q7A1E8 protein from Staphylococcus aureus, Northeast Structural Genomics Consortium target: ZR215"  .

Assembly members:

Assembly members:
ZR215, polymer, 80 residues, 9438.43 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ZR215: MAGDPMTFYNFIMGFQNDNT PFGILAEHVSEDKAFPRLEE RHQVIRAYVMSNYTDHQLIE TTNRAISLYMANLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts255
15N chemical shifts79
1H chemical shifts506

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ZR2151

Entities:

Entity 1, ZR215 80 residues - 9438.43 Da.

Residues 1-5 represent the N-terminal tag and 73-80 represent the C-terminal hexa-His tag

1   METALAGLYASPPROMETTHRPHETYRASN
2   PHEILEMETGLYPHEGLNASNASPASNTHR
3   PROPHEGLYILELEUALAGLUHISVALSER
4   GLUASPLYSALAPHEPROARGLEUGLUGLU
5   ARGHISGLNVALILEARGALATYRVALMET
6   SERASNTYRTHRASPHISGLNLEUILEGLU
7   THRTHRASNARGALAILESERLEUTYRMET
8   ALAASNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: ZR215, [U-100% 13C; U-100% 15N], 0.71 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v2.3, Goddard - data analysis, peak picking

VNMRJ v2.1B, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis, geometry optimization, structure solution

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

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

AVS, Moseley and Montelione - chemical shift validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constriants

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

SWS Q7A1E8-STAAW

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