BMRB Entry 26987

Name: HIV1 protease folded and cold-denatured
Published: 2021-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26987

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:

HIV1 protease folded and cold-denatured

Deposition date:

2017-01-03

Original release date:

2021-07-22

Authors:

Roesner, Heike; Kragelund, Birthe; Prestel, Andreas; Caldarini, Martina; Tiana, Guido; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro

Citation:

Citation: Roesner, Heike; Caldarini, Martina; Prestel, Andreas; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro; Tiana, Guido; Kragelund, Birthe. "Cold denaturation of the HIV-1 protease monomer" Biochemistry 56, 1029-1032 (2017).
PubMed: 28168877

Assembly members:

Assembly members:
HIV1_protease_monomer, polymer, 95 residues, Formula weight is not available

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 Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV1_protease_monomer: PQITLWKRPLVTIRIGGQLK EALLNTGADDTVLEEMNLPG KWKPKMIGGIGGFIKVRQYD QIPVEIAGHKAIGTVLVGPT PVNIIGRNLLTQIGA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	259
15N chemical shifts	158
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIV1 protease monomer, folded	1
2	HIV1 protease monomer, unfolded	1

Entities:

Entity 1, HIV1 protease monomer, folded 95 residues - Formula weight is not available

1

PRO

GLN

ILE

THR

LEU

TRP

LYS

ARG

PRO

LEU

2

VAL

THR

ILE

ARG

ILE

GLY

GLN

LEU

LYS

3

GLU

ALA

LEU

ASN

THR

GLY

ALA

ASP

4

THR

VAL

LEU

GLU

MET

ASN

LEU

PRO

GLY

5

LYS

TRP

LYS

PRO

LYS

MET

ILE

GLY

ILE

6

GLY

PHE

ILE

LYS

VAL

ARG

GLN

TYR

ASP

7

GLN

ILE

PRO

VAL

GLU

ILE

ALA

GLY

HIS

LYS

8

ALA

ILE

GLY

THR

VAL

LEU

VAL

GLY

PRO

THR

9

PRO

VAL

ASN

ILE

GLY

ARG

ASN

LEU

10

THR

GLN

ILE

GLY

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2

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

BMRB Entry 26987

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: