BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17074

Click here to enlarge.

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/BMR17074
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: An arsenate reductase   PubMed: 20960080

Deposition date: 2010-07-23 Original release date: 2010-10-22

Authors: Yu, Caifang; Xia, Bin; Jin, Changwen

Citation: Yu, Caifang; Xia, Bin; Jin, Changwen. "(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803."  Biomol. NMR Assignments 5, 85-87 (2011).

Assembly members:
SynArsC, polymer, 134 residues, Formula weight is not available

Natural source:   Common Name: Synechocystis sp. PCC 6803   Taxonomy ID: 1148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis not available

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

Entity Sequences (FASTA):
SynArsC: GSHMKKVMFVCKRNSCRSQM AEGFAKTLGAGKIAVTSCGL ESSRVHPTAIAMMEEVGIDI SGQTSDPIENFNADDYDVVI SLCGCGVNLPPEWVTQEIFE DWQLEDPDGQSLEVFRTVRG QVKERVENLIAKIS

Data sets:
Data typeCount
13C chemical shifts541
15N chemical shifts137
1H chemical shifts845

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SynArsC1

Entities:

Entity 1, SynArsC 134 residues - Formula weight is not available

1   GLYSERHISMETLYSLYSVALMETPHEVAL
2   CYSLYSARGASNSERCYSARGSERGLNMET
3   ALAGLUGLYPHEALALYSTHRLEUGLYALA
4   GLYLYSILEALAVALTHRSERCYSGLYLEU
5   GLUSERSERARGVALHISPROTHRALAILE
6   ALAMETMETGLUGLUVALGLYILEASPILE
7   SERGLYGLNTHRSERASPPROILEGLUASN
8   PHEASNALAASPASPTYRASPVALVALILE
9   SERLEUCYSGLYCYSGLYVALASNLEUPRO
10   PROGLUTRPVALTHRGLNGLUILEPHEGLU
11   ASPTRPGLNLEUGLUASPPROASPGLYGLN
12   SERLEUGLUVALPHEARGTHRVALARGGLY
13   GLNVALLYSGLUARGVALGLUASNLEUILE
14   ALALYSILESER

Samples:

sample_1: SynArsC, [U-15N], 1 mM; DSS 0.01%; sodium azide 0.01%; sodium chloride 50 mM; sodium phosphate 50 mM; DTT 40 mM; D2O 10%; H2O 90%

sample_2: SynArsC, [U-13C; U-15N], 1 mM; DSS 0.01%; sodium azide 0.01%; sodium chloride 50 mM; sodium phosphate 50 mM; DTT 40 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17076 17077 25243
PDB
DBJ BAA18407 BAK50581 BAL29580 BAL32749 BAL35918
GB AGF52095 ALJ68053
REF WP_010873028
SP P74313

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