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Biological Magnetic Resonance Data Bank


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BMRB Entry 25195

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25195
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Title: Solution structure of a putative arsenate reductase from Brucella melitensis. Seattle Structural Genomics Center for Infectious Disease target BrabA.00073.a

Deposition date: 2014-09-02 Original release date: 2014-09-15

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephan; Van Voorhis, Wesley; Myler, Peter. "Solution NMR structure of an arsenate reductase from Brucella melitensis."  Not known ., .-..

Assembly members:
entity, polymer, 136 residues, 15166.851 Da.

Natural source:   Common Name: a-proteobacteria   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):
entity: MAHHHHHHMGTLEAQTQGPG SMDVTIYHNPVCGTSRKVLG MIREAGIEPHVIEYMKTPLP RDMLVELLRQMAISPRALLR AKEARYAELGLDDPALSDEV LIDAMISNPVLMNRPVVVTP KGVRLCRPAETVQELL

Data sets:
Data typeCount
13C chemical shifts524
1H chemical shifts801
15N chemical shifts115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 136 residues - 15166.851 Da.

The 21 residues at the N-terminus are not natural.

1   METALAHISHISHISHISHISHISMETGLY
2   THRLEUGLUALAGLNTHRGLNGLYPROGLY
3   SERMETASPVALTHRILETYRHISASNPRO
4   VALCYSGLYTHRSERARGLYSVALLEUGLY
5   METILEARGGLUALAGLYILEGLUPROHIS
6   VALILEGLUTYRMETLYSTHRPROLEUPRO
7   ARGASPMETLEUVALGLULEULEUARGGLN
8   METALAILESERPROARGALALEULEUARG
9   ALALYSGLUALAARGTYRALAGLULEUGLY
10   LEUASPASPPROALALEUSERASPGLUVAL
11   LEUILEASPALAMETILESERASNPROVAL
12   LEUMETASNARGPROVALVALVALTHRPRO
13   LYSGLYVALARGLEUCYSARGPROALAGLU
14   THRVALGLNGLULEULEU

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 5 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; D2O 7%; H2O 93%

sample_2: entity, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 5 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; D2O 100%

sample_conditions_1: temperature: 293 K; pH: 7; pressure: 1 atm; ionic strength: 0.12 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
D2O exchangesample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY v3.115, Goddard - data analysis, peak picking

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
EMBL CAJ10964 CDL76386
GB AAL52173 AAN29912 AAX74345 ABQ61470 ABX62059
REF WP_002964107 WP_004683746 WP_004685628 WP_004691862 WP_006012423

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts