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Biological Magnetic Resonance Data Bank


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BMRB Entry 16517

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16517
MolProbity Validation Chart

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Title: Solution structure of an arsenate reductase (ArsC) related protein from Brucella melitensis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target BrabA.00007.a.   PubMed: 21904062

Deposition date: 2009-09-23 Original release date: 2009-10-23

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 1129-1136 (2011).

Assembly members:
BR7, polymer, 120 residues, Formula weight is not available

Natural source:   Common Name: Brucella melitensis   Taxonomy ID: 29459   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Brucella melitensis

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

Entity Sequences (FASTA):
BR7: GPGSMSVTIYGIKNCDTMKK ARIWLEDHGIDYTFHDYKKE GLDAETLDRFLKTVPWEQLL NRAGTTFRKLPEDVRSNVDA ASARELMLAQPSMVKRPVLE RDGKLMVGFKPAQYEAYFKL

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts118
1H chemical shifts772

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BR71

Entities:

Entity 1, BR7 120 residues - Formula weight is not available

1   GLYPROGLYSERMETSERVALTHRILETYR
2   GLYILELYSASNCYSASPTHRMETLYSLYS
3   ALAARGILETRPLEUGLUASPHISGLYILE
4   ASPTYRTHRPHEHISASPTYRLYSLYSGLU
5   GLYLEUASPALAGLUTHRLEUASPARGPHE
6   LEULYSTHRVALPROTRPGLUGLNLEULEU
7   ASNARGALAGLYTHRTHRPHEARGLYSLEU
8   PROGLUASPVALARGSERASNVALASPALA
9   ALASERALAARGGLULEUMETLEUALAGLN
10   PROSERMETVALLYSARGPROVALLEUGLU
11   ARGASPGLYLYSLEUMETVALGLYPHELYS
12   PROALAGLNTYRGLUALATYRPHELYSLEU

Samples:

sample_1: BR7 1.5 ± 0.2 mM; sodium chloride 100 ± 3 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; H2O 90%; D2O 10%

sample_2: BR7 1.0 ± 0.2 mM; sodium chloride 100 ± 3 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 7.1; pressure: 1.0 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
deuterium exchangesample_2isotropicsample_conditions_1
3D HBHA_CO_NHsample_1isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
EMBL CAJ10355 CDL75783
GB AAL52738 AAN29316 AAX73792 ABQ60828 ABX61465
REF WP_002963533 WP_004682989 WP_006079395 WP_006173775 WP_008508080

Download simulated HSQC data in one of the following formats:
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