BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15723

Title: NMR assignment of the nonstructural protein nsp3(1066-1181) from SARS-CoV   PubMed: 19636888

Deposition date: 2008-04-09 Original release date: 2008-04-18

Authors: Wuthrich, Kurt; Serrano, Pedro; Johnson, Margaret; Chatterjee, Amarnath; Pedrini, Bill

Citation: Serrano, Pedro; Johnson, Margaret; Chatterjee, Amarnath; Pedrini, Bill; Wuthrich, Kurt. "NMR assignment of the nonstructural protein nsp3(1066-1181) from SARS-CoV"  Biomol. NMR Assignments 2, 135-138 (2008).

Assembly members:
nsp3(1066-1181), polymer, 116 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET25b

Entity Sequences (FASTA):
nsp3(1066-1181): MYTEQPIDLVPTQPLPNASF DNFKLTCSNTKFADDLNQMT GFTKPASRELSVTFFPDLNG DVVAIDYRHYSASFKKGAKL LHKPIVWHINQATTKTTFKP NTWCLRCLWSTKPVDT

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts114
1H chemical shifts817

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nsp3(1066-1181)1

Entities:

Entity 1, nsp3(1066-1181) 116 residues - Formula weight is not available

1   METTYRTHRGLUGLNPROILEASPLEUVAL
2   PROTHRGLNPROLEUPROASNALASERPHE
3   ASPASNPHELYSLEUTHRCYSSERASNTHR
4   LYSPHEALAASPASPLEUASNGLNMETTHR
5   GLYPHETHRLYSPROALASERARGGLULEU
6   SERVALTHRPHEPHEPROASPLEUASNGLY
7   ASPVALVALALAILEASPTYRARGHISTYR
8   SERALASERPHELYSLYSGLYALALYSLEU
9   LEUHISLYSPROILEVALTRPHISILEASN
10   GLNALATHRTHRLYSTHRTHRPHELYSPRO
11   ASNTHRTRPCYSLEUARGCYSLEUTRPSER
12   THRLYSPROVALASPTHR

Samples:

sample_1: nsp3(1066-1181), [U-99% 13C; U-99% 15N], 1.4 mM; sodium chloride 50 mM; sodium azide 2 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.302 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

CARA v1.7, Keller and Wuthrich - chemical shift assignment, peak picking

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - geometry optimization

NMR spectrometers:

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

Related Database Links:

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

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