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 15790

Title: NMR STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN OF THE ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN   PubMed: 18687679

Authors: Wang, Yu; Boudreaux, Daniel; Estrada, David; Egan, Chet; St. Jeor, Stephen; De Guzman, Roberto

Citation: Wang, Yu; Boudreaux, Daniel; Estrada, David; Egan, Chet; St. Jeor, Stephen; De Guzman, Roberto. "NMR STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN OF THE ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN"  J. Biol. Chem. 283, 28297-28304 (2008).

Assembly members:
ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN, polymer, 107 residues, 12071.731 Da.

Natural source:   Common Name: Andes Hantavirus   Taxonomy ID: 46607   Superkingdom: Viruses   Kingdom: not available   Genus/species: Hantavirus Andes virus

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

Entity Sequences (FASTA):
ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN: MHHHHHHGKPIPNPLLGLDS TENLYFQGIDPFTMSTLQEL QENITAHEQQLVTARQKLKD AEKAVEVDPDDVNKSTLQNR RAAVSTLETKLGELKRQLAD LVAAQKL

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts96
1H chemical shifts670

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN1

Entities:

Entity 1, ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN 107 residues - 12071.731 Da.

1   METHISHISHISHISHISHISGLYLYSPRO
2   ILEPROASNPROLEULEUGLYLEUASPSER
3   THRGLUASNLEUTYRPHEGLNGLYILEASP
4   PROPHETHRMETSERTHRLEUGLNGLULEU
5   GLNGLUASNILETHRALAHISGLUGLNGLN
6   LEUVALTHRALAARGGLNLYSLEULYSASP
7   ALAGLULYSALAVALGLUVALASPPROASP
8   ASPVALASNLYSSERTHRLEUGLNASNARG
9   ARGALAALAVALSERTHRLEUGLUTHRLYS
10   LEUGLYGLULEULYSARGGLNLEUALAASP
11   LEUVALALAALAGLNLYSLEU

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; D2O 100%

sample_3: entity, [U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.028 M; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

CYANA v1.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

AMBER v7, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAB69170 AAB69181 AAB69182 AAC55018 AAG22531
REF NP_604471