BMRB Entry 15511

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15511
MolProbity Validation Chart

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Title:
1H,13C and 15N chemical shift assignments for stereo-array isotope labelled (SAIL) C-terminal dimerization domain of SARS coronavirus nucleocapsid protein
Deposition date:
2007-10-06
Original release date:
2008-06-26
Authors:
Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-lan; Huang, Tai-huang; Kainosho, Masatsune
Citation:

Citation: Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-lan; Huang, Tai-huang; Kainosho, Masatsune. "Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method"  J. Mol. Biol. 380, 608-622 (2008).
PubMed: 18561946

Assembly members:

Assembly members:
SARS_coronavirus_nucleocapsid_protein_residues_248-365, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 248485   Superkingdom: Viruses   Kingdom: not available   Genus/species: Coronavirus SARS coronavirus

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SARS_coronavirus_nucleocapsid_protein_residues_248-365: MHHHHHHAMGTKKSAAEASK KPRQKRTATKQYNVTQAFGR RGPEQTQGNFGDQDLIRQGT DYKHWPQIAQFAPSASAFFG MSRIGMEVTPSGTWLTYHGA IKLDDKDPQFKDNVILLNKH IDAYKTFP

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts123
1H chemical shifts575

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit11
2subunit21

Entities:

Entity 1, subunit1 128 residues - Formula weight is not available

1   METHISHISHISHISHISHISALAMETGLY
2   THRLYSLYSSERALAALAGLUALASERLYS
3   LYSPROARGGLNLYSARGTHRALATHRLYS
4   GLNTYRASNVALTHRGLNALAPHEGLYARG
5   ARGGLYPROGLUGLNTHRGLNGLYASNPHE
6   GLYASPGLNASPLEUILEARGGLNGLYTHR
7   ASPTYRLYSHISTRPPROGLNILEALAGLN
8   PHEALAPROSERALASERALAPHEPHEGLY
9   METSERARGILEGLYMETGLUVALTHRPRO
10   SERGLYTHRTRPLEUTHRTYRHISGLYALA
11   ILELYSLEUASPASPLYSASPPROGLNPHE
12   LYSASPASNVALILELEULEUASNLYSHIS
13   ILEASPALATYRLYSTHRPHEPRO

Samples:

sample_1: SARS coronavirus nucleocapsid protein residues 248-365, full SAIL isotope labeling, 0.5 ± 0.1 mM; D2O 10%; H2O 90 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 303 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Goddard - chemical shift assignment

CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks