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 15469

Title: NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3   PubMed: 19636862

Deposition date: 2008-01-11 Original release date: 2008-02-05

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

Citation: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Wuthrich, Kurt. "NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3"  Biomol. NMR Assignments 1, 191-194 (2007).

Assembly members:
nsp3(513-651), polymer, 143 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):
nsp3(513-651): GSHMVLPSEAPNAKEEILGT VSWNLREMLAHAEETRKLMP ICMDVRAIMATIQRKYKGIK IQEGIVDYGVRFFFYTSKEP VASIITKLNSLNEPLVTMPI GYVTHGFNLEEAARCMRSLK APAVVSVSSPDAVTTYNGYL TSS

Data sets:
Data typeCount
15N chemical shifts143
1H chemical shifts967
13C chemical shifts615

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nsp3(513-651)1

Entities:

Entity 1, nsp3(513-651) 143 residues - Formula weight is not available

1   GLYSERHISMETVALLEUPROSERGLUALA
2   PROASNALALYSGLUGLUILELEUGLYTHR
3   VALSERTRPASNLEUARGGLUMETLEUALA
4   HISALAGLUGLUTHRARGLYSLEUMETPRO
5   ILECYSMETASPVALARGALAILEMETALA
6   THRILEGLNARGLYSTYRLYSGLYILELYS
7   ILEGLNGLUGLYILEVALASPTYRGLYVAL
8   ARGPHEPHEPHETYRTHRSERLYSGLUPRO
9   VALALASERILEILETHRLYSLEUASNSER
10   LEUASNGLUPROLEUVALTHRMETPROILE
11   GLYTYRVALTHRHISGLYPHEASNLEUGLU
12   GLUALAALAARGCYSMETARGSERLEULYS
13   ALAPROALAVALVALSERVALSERSERPRO
14   ASPALAVALTHRTHRTYRASNGLYTYRLEU
15   THRSERSER

Samples:

sample_13C15N: nsp3(513-651), [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; D2O 10%; H2O 90%

sample_15N: nsp3(513-651), [U-98% 15N], 1.2 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; D2O 10%; H2O 90%

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_15Nisotropicsample_conditions_1
2D 1H-13C HSQCsample_13C15Nisotropicsample_conditions_1
3D HNCAsample_13C15Nisotropicsample_conditions_1
3D HNCACBsample_13C15Nisotropicsample_conditions_1
3D CBCA(CO)NHsample_13C15Nisotropicsample_conditions_1
3D HNCOsample_13C15Nisotropicsample_conditions_1
3D HCCH-TOCSYsample_13C15Nisotropicsample_conditions_1
3D HCCH-COSYsample_13C15Nisotropicsample_conditions_1
3D C(CO)NHsample_13C15Nisotropicsample_conditions_1
3D H(CCO)NHsample_13C15Nisotropicsample_conditions_1
3D 1H-15N TOCSYsample_13C15Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic regionsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromatic regionsample_13C15Nisotropicsample_conditions_1

Software:

CYANA v1.3, Bruker Biospin - collection, processing

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

CYANA v1.2, Guntert, Mumenthaler and Wuthrich - Creating Chemical Shift List

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15618 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

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