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 15618

Title: NMR ASSIGNMENT OF THE DOMAIN 527-651 OF THE SARS-COV NONSTRUCTURAL PROTEIN NSP3   PubMed: 19052085

Authors: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Saikatendu, Kumar; Neuman, Benjamin; Stevens, Raymond; Wilson, Ian; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt

Citation: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Neuman, Benjamin; Saikatendu, Kumar; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt. "Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold"  J. Virol. 83, 1823-1836 (2009).

Assembly members:
nsp3(527-651), polymer, 129 residues, Formula weight is not available

Natural source:   Common Name: SARS coronavirus   Taxonomy ID: 227859   Superkingdom: not available   Kingdom: Viruses   Genus/species: not available Coronavirus

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

Entity Sequences (FASTA):
nsp3(527-651): GSHMGTVSWNLREMLAHAEE TRKLMPICMDVRAIMATIQR KYKGIKIQEGIVDYGVRFFF YTSKEPVASIITKLNSLNEP LVTMPIGYVTHGFNLEEAAR CMRSLKAPAVVSVSSPDAVT TYNGYLTSS

Data sets:
Data typeCount
13C chemical shifts481
15N chemical shifts130
1H chemical shifts925

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nsp3(527-651)1

Entities:

Entity 1, nsp3(527-651) 129 residues - Formula weight is not available

1   GLYSERHISMETGLYTHRVALSERTRPASN
2   LEUARGGLUMETLEUALAHISALAGLUGLU
3   THRARGLYSLEUMETPROILECYSMETASP
4   VALARGALAILEMETALATHRILEGLNARG
5   LYSTYRLYSGLYILELYSILEGLNGLUGLY
6   ILEVALASPTYRGLYVALARGPHEPHEPHE
7   TYRTHRSERLYSGLUPROVALALASERILE
8   ILETHRLYSLEUASNSERLEUASNGLUPRO
9   LEUVALTHRMETPROILEGLYTYRVALTHR
10   HISGLYPHEASNLEUGLUGLUALAALAARG
11   CYSMETARGSERLEULYSALAPROALAVAL
12   VALSERVALSERSERPROASPALAVALTHR
13   THRTYRASNGLYTYRLEUTHRSERSER

Samples:

sample_13C15N: nsp3(527-651), [U-99% 13C; U-98% 15N], 1.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; D2O 10%

sample_conditions_1: ionic strength: 0.227 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_13C15Nisotropicsample_conditions_1
2D 1H-13C HSQCsample_13C15Nisotropicsample_conditions_1
3D HCCH-TOCSYsample_13C15Nisotropicsample_conditions_1
3D 1H-15N TOCSYsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic regionsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromatic regionsample_13C15Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_13C15Nisotropicsample_conditions_1
4D APSY-HNCOCAsample_13C15Nisotropicsample_conditions_1
4D APSY-HACANHsample_13C15Nisotropicsample_conditions_1
5D APSY-CBCACONHsample_13C15Nisotropicsample_conditions_1
5D APSY-HACACONHsample_13C15Nisotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

CARA v1.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - Creating Chemical Shift List, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker DRX 700 MHz

Related Database Links:

BMRB 15469 16613
PDB
DBJ BAC81346 BAC81347 BAC81360 BAC81361 BAC81374
GB AAP13439 AAP13442 AAP13566 AAP13575 AAP30028
REF NP_828849 NP_828850 NP_828862
SP P0C6T7 P0C6U8 P0C6W6 P0C6X7