BMRB Entry 30137

Name: Structure of the C-terminal transmembrane domain of scavenger receptor BI (SR-BI)
Published: 2017-03-02

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PDB ID: 5ktf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30137
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:

Structure of the C-terminal transmembrane domain of scavenger receptor BI (SR-BI)

Deposition date:

2016-07-11

Original release date:

2017-03-02

Authors:

Chadwick, A.; Peterson, F.; Volkman, B.; Sahoo, D.

Citation:

Citation: Chadwick, Alexandra; Jensen, Davin; Hanson, Paul; Lange, Philip; Proudfoot, Sarah; Peterson, Francis; Volkman, Brian; Sahoo, Daisy. "NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif" Structure 25, 446-457 (2017).
PubMed: 28162952

Assembly members:

Assembly members:
entity_1, polymer, 73 residues, 8185.792 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE30-SMT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSKIEPVVLPLLWFEQSGAM GGKPLSTFYTQLVLMPQVLH YAQYVLLGLGGLLLLVPIIC QLRSQEKCFLFWS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	284
15N chemical shifts	68
1H chemical shifts	496

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 73 residues - 8185.792 Da.

1

GLY

SER

LYS

ILE

GLU

PRO

VAL

LEU

PRO

2

LEU

TRP

PHE

GLU

GLN

SER

GLY

ALA

MET

3

GLY

LYS

PRO

LEU

SER

THR

PHE

TYR

THR

4

GLN

LEU

VAL

LEU

MET

PRO

GLN

VAL

LEU

HIS

5

TYR

ALA

GLN

TYR

VAL

LEU

GLY

LEU

GLY

6

GLY

LEU

VAL

PRO

ILE

CYS

7

GLN

LEU

ARG

SER

GLN

GLU

LYS

CYS

PHE

LEU

8

PHE

TRP

SER

Samples:

sample_1: LPPG, [U-2H], 5.0 w/v; scavenger receptor BI (SR-BI), [U-99% 13C; U-99% 15N], 1 mM; sodium azide 0.02 w/v

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

XEASY, Bartels et al. - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AvanceIII 500 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