BMRB Entry 25966

Name: Solution structure of C-terminal extramembrane domain of SH protein
Published: 2016-02-15

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PDB ID: 2nb8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25966
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of C-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, 27 residues, 3209.771 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: IAILNKLCEYNVFHNKTFEL PRARVNT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	112
15N chemical shifts	29
1H chemical shifts	190

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 27 residues - 3209.771 Da.

1

ILE

ALA

ILE

LEU

ASN

LYS

LEU

CYS

GLU

TYR

2

ASN

VAL

PHE

HIS

ASN

LYS

THR

PHE

GLU

LEU

3

PRO

ARG

ALA

ARG

VAL

ASN

THR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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