BMRB Entry 11589

Name: A GB1-gp41 fusion protein containing hydrophobic pocket binding domain residues of gp41
Published: 2018-12-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11589

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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:

A GB1-gp41 fusion protein containing hydrophobic pocket binding domain residues of gp41

Deposition date:

2015-03-06

Original release date:

2018-12-11

Authors:

Walsh, Joseph; Chu, Shidong; Zhang, Shao-Qing; Gochin, Miriam

Citation:

Citation: Walsh, Joseph; Chu, Shidong; Zhang, Shao-Qing; Gochin, Miriam. "Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery." Protein Eng. Des. Sel. 28, 107-116 (2015).
PubMed: 25792539

Assembly members:

Assembly members:
GB1(i635), polymer, 96 residues, 10696.3 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRK603

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GB1(i635): MGSSHHHHHHSGGSMQYKLI LNGKTLKGETTTEAVDAATA EKVFKQYANDNGVDGEWTYD DATKTFTVTEGGSGGSNKSL EQKANHETWEAWDREI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gp41 hydrophobic pocket binding domain	1

Entities:

Entity 1, gp41 hydrophobic pocket binding domain 96 residues - 10696.3 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

SER

MET

GLN

TYR

LYS

LEU

ILE

3

LEU

ASN

GLY

LYS

THR

LEU

LYS

GLY

GLU

THR

4

THR

GLU

ALA

VAL

ASP

ALA

THR

ALA

5

GLU

LYS

VAL

PHE

LYS

GLN

TYR

ALA

ASN

ASP

6

ASN

GLY

VAL

ASP

GLY

GLU

TRP

THR

TYR

ASP

7

ASP

ALA

THR

LYS

THR

PHE

THR

VAL

THR

GLU

8

GLY

SER

GLY

SER

ASN

LYS

SER

LEU

9

GLU

GLN

LYS

ALA

ASN

HIS

GLU

THR

TRP

GLU

10

ALA

TRP

ASP

ARG

GLU

ILE

Samples:

sample_1: GB1(i635), [U-100% 13C; U-100% 15N], 1.3 – 2.1 mM; MES 10 mM; arginine 50 mM; glutamate 50 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 298 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

Software:

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

CARA, Swiss Federal Institute of Technology - chemical shift assignment

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 800 MHz

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