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 25243

Title: AN ARSENATE REDUCTASE IN OXIDIZED STATE   PubMed: 26224634

Deposition date: 2014-09-23 Original release date: 2015-08-03

Authors: Jin, Changwen; Hu, Cuiyun

Citation: Jin, Changwen; Hu, Cuiyun. "A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction"  J. Biol. Chem. 290, 22262-22273 (2015).

Assembly members:
entity, polymer, 131 residues, 14409.351 Da.

Natural source:   Common Name: Synechocystis   Taxonomy ID: 1142   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis not available

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

Entity Sequences (FASTA):
entity: MKKVMFVSKRNSSRSQMAEG FAKTLGAGKIAVTSSGLESS RVHPTAIAMMEEVGIDISGQ TSDPIENFNADDYDVVISLC GCGVNLPPEWVTQEIFEDWQ LEDPDGQSLEVFRTVRGQVK ERVENLIAKIS

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts138
1H chemical shifts875

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Arsenate Reductase1

Entities:

Entity 1, Arsenate Reductase 131 residues - 14409.351 Da.

1   METLYSLYSVALMETPHEVALSERLYSARG
2   ASNSERSERARGSERGLNMETALAGLUGLY
3   PHEALALYSTHRLEUGLYALAGLYLYSILE
4   ALAVALTHRSERSERGLYLEUGLUSERSER
5   ARGVALHISPROTHRALAILEALAMETMET
6   GLUGLUVALGLYILEASPILESERGLYGLN
7   THRSERASPPROILEGLUASNPHEASNALA
8   ASPASPTYRASPVALVALILESERLEUCYS
9   GLYCYSGLYVALASNLEUPROPROGLUTRP
10   VALTHRGLNGLUILEPHEGLUASPTRPGLN
11   LEUGLUASPPROASPGLYGLNSERLEUGLU
12   VALPHEARGTHRVALARGGLYGLNVALLYS
13   GLUARGVALGLUASNLEUILEALALYSILE
14   SER

Samples:

sample_1: protein, [U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_2: protein, [U-13C; U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

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