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 4944

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4944

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Title: 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state.

Deposition date: 2001-01-22 Original release date: 2001-05-17

Authors: Jacobs, Doris; Messens, Joris; Wechselberger, Rainer; Brosens, Elke; Wyns, Lode; Willem, Rudolph; Martins, Jose

Citation: Jacobs, Doris; Messens, Joris; Wechselberger, Rainer; Brosens, Elke; Willem, Rudolph; Wyns, Lode; Martins, Jose. "Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state"  J. Biomol. NMR 20, 95-96 (2001).

Assembly members:
Arsenate reductase, polymer, 131 residues, 14812 Da.

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

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

Entity Sequences (FASTA):
Arsenate reductase: MDKKTIYFICTGNSCRSQMA EGWGKEILGEGWNVYSAGIE THGVNPKAIEAMKEVDIDIS NHTSDLIDNDILKQSDLVVT LCSDADNNCPILPPNVKKEH WGFDDPAGKEWSEFQRVRDE IKLAIEKFKLR

Data sets:
Data typeCount
1H chemical shifts244
13C chemical shifts358
15N chemical shifts122

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 - 14812 Da.

1   METASPLYSLYSTHRILETYRPHEILECYS
2   THRGLYASNSERCYSARGSERGLNMETALA
3   GLUGLYTRPGLYLYSGLUILELEUGLYGLU
4   GLYTRPASNVALTYRSERALAGLYILEGLU
5   THRHISGLYVALASNPROLYSALAILEGLU
6   ALAMETLYSGLUVALASPILEASPILESER
7   ASNHISTHRSERASPLEUILEASPASNASP
8   ILELEULYSGLNSERASPLEUVALVALTHR
9   LEUCYSSERASPALAASPASNASNCYSPRO
10   ILELEUPROPROASNVALLYSLYSGLUHIS
11   TRPGLYPHEASPASPPROALAGLYLYSGLU
12   TRPSERGLUPHEGLNARGVALARGASPGLU
13   ILELYSLEUALAILEGLULYSPHELYSLEU
14   ARG

Samples:

sample_1: Arsenate reductase, [U-95% 13C; U-98% 15N], 1.8 mM; DTT 1.0 mM; EDTA 0.1 mM; K2SO4 50 mM; potassium phosphate buffer 50 mM

sample_2: Arsenate reductase, [U-98% 15N], 1.8 mM; DTT 1.0 mM; EDTA 0.1 mM; K2SO4 50 mM; potassium phosphate buffer 50 mM

Ex-cond_1: pH: 6.7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
1H-15N HSQC-TOCSYnot availablenot availablenot available
1H-15N HSQC-NOESYnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCOnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
HN(CA)COnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HNCACBnot availablenot availablenot available

Software:

FELIX v97.0 - processing, manual peak picking, manual assignment

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker DRX 600 MHz
  • Varian Inova 750 MHz

Related Database Links:

PDB
DBJ BAB43887 BAC54538 BAE18778 BAE92851 BAG12261
EMBL CAG39708
GB AAA25638 ACZ58845 ACZ68457 ACZ68855 ACZ68904
REF NP_395554 WP_000358995 WP_002452591 WP_002508683 WP_003756625
SP P0A005 P0A006 Q49WS7 Q6GIZ3

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