BMRB Entry 25965

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25965
MolProbity Validation Chart

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Title:
Solution structure of N-terminal extramembrane domain of SH protein
Deposition date:
2016-01-26
Original release date:
2016-02-15
Authors:
Li, Yan; To, Janet; Surya, Wahyu; Torres, Jaume
Citation:

Citation: Li, Yan; To, Janet; Verdia-Baguena, Carmina; Dossena, Silvia; Surya, Wahyu; Huang, Mei; Paulmichl, Markus; Liu, Ding Xiang; Aguilella, Vicente M; Torres, Jaume. "Inhibition of the Human Respiratory Syncytial Virus Small Hydrophobic Protein and Structural Variations in a Bicelle Environment"  J Virol. 88, 11899-11914 (2014).
PubMed: 25100835

Assembly members:

Assembly members:
entity, polymer, 14 residues, 1634.837 Da.

Natural source:

Natural source:   Common Name: Human respiratory syncytial virus   Taxonomy ID: 11250   Superkingdom: Viruses   Kingdom: not available   Genus/species: Pneumovirus not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MENTSITIEFSSKF

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts15
1H chemical shifts92

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 14 residues - 1634.837 Da.

1   METGLUASNTHRSERILETHRILEGLUPHE
2   SERSERLYSPHE

Samples:

sample_1: entity, [U-13C; U-15N], 0.7 mM; DHPC-DLPC 9.5%; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 70 mM; pH: 5.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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