BMRB Entry 30285

Name: Solution-state NMR structural ensemble of human Tsg101 UEV in complex with tenatoprazole
Published: 2017-11-10

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PDB ID: 5vkg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30285
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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-state NMR structural ensemble of human Tsg101 UEV in complex with tenatoprazole

Deposition date:

2017-04-21

Original release date:

2017-11-10

Authors:

Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol

Citation:

Citation: Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol. "Tsg101 chaperone function revealed by HIV-1 assembly inhibitors." Nat. Commun. 8, 1391-1391 (2017).
PubMed: 29123089

Assembly members:

Assembly members:
entity_1, polymer, 145 residues, 16559.207 Da.
entity_4N1, non-polymer, 331.413 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAVSESQLKKMVSKYKYRDL TVRETVNVITLYKDLKPVLD SYVFNDGSSRELMNLTGTIP VPYRGNTYNIPICLWLLDTY PYNPPICFVKPTSSMTIKTG KHVDANGKIYLPYLHEWKHP QSDLLGLIQVMIVVFGDEPP VFSRP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	521
15N chemical shifts	143
1H chemical shifts	1078

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 145 residues - 16559.207 Da.

1

GLY

ALA

VAL

SER

GLU

SER

GLN

LEU

LYS

2

MET

VAL

SER

LYS

TYR

LYS

TYR

ARG

ASP

LEU

3

THR

VAL

ARG

GLU

THR

VAL

ASN

VAL

ILE

THR

4

LEU

TYR

LYS

ASP

LEU

LYS

PRO

VAL

LEU

ASP

5

SER

TYR

VAL

PHE

ASN

ASP

GLY

SER

ARG

6

GLU

LEU

MET

ASN

LEU

THR

GLY

THR

ILE

PRO

7

VAL

PRO

TYR

ARG

GLY

ASN

THR

TYR

ASN

ILE

8

PRO

ILE

CYS

LEU

TRP

LEU

ASP

THR

TYR

9

PRO

TYR

ASN

PRO

ILE

CYS

PHE

VAL

LYS

10

PRO

THR

SER

MET

THR

ILE

LYS

THR

GLY

11

LYS

HIS

VAL

ASP

ALA

ASN

GLY

LYS

ILE

TYR

12

LEU

PRO

TYR

LEU

HIS

GLU

TRP

LYS

HIS

PRO

13

GLN

SER

ASP

LEU

GLY

LEU

ILE

GLN

VAL

14

MET

ILE

VAL

PHE

GLY

ASP

GLU

PRO

15

VAL

PHE

SER

ARG

PRO

Entity 2, entity_2 - C16 H19 N4 O2 S - 331.413 Da.

1

4N1

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_2
3D 1H-13C-12C filtered NOESY aliphatic	sample_1	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 30285

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: