BMRB Entry 34409

Name: Structure of HIV-1 CAcSP1NC mutant(W41A,M42A) interacting with maturation inhibitor EP39
Published: 2020-05-15

Click here to enlarge.

PDB ID: 6rwg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34409
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of HIV-1 CAcSP1NC mutant(W41A,M42A) interacting with maturation inhibitor EP39

Deposition date:

2019-06-05

Original release date:

2020-05-15

Authors:

Chen, X.; Coric, P.; Larue, V.; Nonin-Lecomte, S.; Bouaziz, S.; Structural Genomics Consortium (SGC), SGC

Citation:

Citation: Chen, Xiaowei; Coric, Pascale; Larue, Valery; Turcaud, Serge; Wang, Xiao; Nonin-Lecomte, Sylvie; Bouaziz, Serge. "Structure of HIV-1 CAcSP1NC mutant(W41A,M42A) interacting with maturation inhibitor EP39" Eur. J. Med. Chem. 204, 112634-112634 (2020).
PubMed: 32717487

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, 17446.146 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MYSPTSILDIRQGPKEPFRD YVDRFYKTLRAEQASQEVKN AATETLLVQNANPDCKTILK ALGPGATLEEMMTACQGVGG PGHKARVLAEAMSQVTNPAT IMIQKGNFRNQRKTVKCFNC GKEGHIAKNCRAPRKKGCWK CGKEGHQMKDCTERQAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
15N chemical shifts	153
1H chemical shifts	921

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

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

Entities:

Entity 1, entity_1 157 residues - 17446.146 Da.

1

MET

TYR

SER

PRO

THR

SER

ILE

LEU

ASP

ILE

2

ARG

GLN

GLY

PRO

LYS

GLU

PRO

PHE

ARG

ASP

3

TYR

VAL

ASP

ARG

PHE

TYR

LYS

THR

LEU

ARG

4

ALA

GLU

GLN

ALA

SER

GLN

GLU

VAL

LYS

ASN

5

ALA

THR

GLU

THR

LEU

VAL

GLN

ASN

6

ALA

ASN

PRO

ASP

CYS

LYS

THR

ILE

LEU

LYS

7

ALA

LEU

GLY

PRO

GLY

ALA

THR

LEU

GLU

8

MET

THR

ALA

CYS

GLN

GLY

VAL

GLY

9

PRO

GLY

HIS

LYS

ALA

ARG

VAL

LEU

ALA

GLU

10

ALA

MET

SER

GLN

VAL

THR

ASN

PRO

ALA

THR

11

ILE

MET

ILE

GLN

LYS

GLY

ASN

PHE

ARG

ASN

12

GLN

ARG

LYS

THR

VAL

LYS

CYS

PHE

ASN

CYS

13

GLY

LYS

GLU

GLY

HIS

ILE

ALA

LYS

ASN

CYS

14

ARG

ALA

PRO

ARG

LYS

GLY

CYS

TRP

LYS

15

CYS

GLY

LYS

GLU

GLY

HIS

GLN

MET

LYS

ASP

16

CYS

THR

GLU

ARG

GLN

ALA

ASN

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: HIV-1 CAcSP1NC, [U-15N], 300 uM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D TOCSY-HSQC	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v3.5 pl 7, Bruker Biospin - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation

TALOS, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz

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