BMRB Entry 26511

Name: Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields
Published: 2015-02-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26511

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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:

Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields

Deposition date:

2015-02-17

Original release date:

2015-02-24

Authors:

Tjandra, Nico; Wingfield, Paul; Stahl, Stephen; Bax, Ad

Citation:

Citation: Tjandra, Nico; Wingfield, Paul; Stahl, Stephen; Bax, Ad. "Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields" J. Biomol. NMR 8, 273-284 (1996).
PubMed: 8953218

Assembly members:

Assembly members:
protease, polymer, 97 residues, Formula weight is not available
[4-R-(-4-ALPHA,5-ALPHA,6-BETA,7-BETA)]-HEXAHYDRO-5,6-BIS(HYDROXY)-[1,3-BIS([4-HYDROXYMETHYL-PHENYL]METHYL)-4,7-BIS(PHENYLMETHYL)]-2H-1,3-DIAZEPINONE, non-polymer, 566.687 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protease: PQVTLWQRPLVTIKIGGQLK EALLDTGADDTVLEEMSLGR WKKMIGGIGGFIKVRQYDQI LIEIAGHKAIGTVLVGPTPV NIIGRNLLTQIGATLNF

Data sets:

heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
- heteronuclear_T1_list_2
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
- heteronuclear_T2_list_2
order_parameters

Data type	Count
heteronuclear NOE values	77
T1 relaxation values	156
T2 relaxation values	156
order parameters	462

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protease, 1	1
2	protease, 2	1
3	DMP323, 1	2
4	DMP323, 2	2

Entities:

Entity 1, protease, 1 97 residues - Formula weight is not available

1

PRO

GLN

VAL

THR

LEU

TRP

GLN

ARG

PRO

LEU

2

VAL

THR

ILE

LYS

ILE

GLY

GLN

LEU

LYS

3

GLU

ALA

LEU

ASP

THR

GLY

ALA

ASP

4

THR

VAL

LEU

GLU

MET

SER

LEU

GLY

ARG

5

TRP

LYS

MET

ILE

GLY

ILE

GLY

6

PHE

ILE

LYS

VAL

ARG

GLN

TYR

ASP

GLN

ILE

7

LEU

ILE

GLU

ILE

ALA

GLY

HIS

LYS

ALA

ILE

8

GLY

THR

VAL

LEU

VAL

GLY

PRO

THR

PRO

VAL

9

ASN

ILE

GLY

ARG

ASN

LEU

THR

GLN

10

ILE

GLY

ALA

THR

LEU

ASN

PHE

Entity 2, DMP323, 1 - C35 H38 N2 O5 - 566.687 Da.

1

DMP

Samples:

sample_1: protease, [U-100% 15N; >85% 2H], 1.5 mM; DMP323 1.5 mM; sodium acetate 50 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 300 K; pH: 5.2; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
15N-{1H} NOE	sample_1	isotropic	sample_conditions_1
15N-{1H} NOE	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection, data analysis

NMR spectrometers:

Bruker AMX 360 MHz
Bruker AMX 600 MHz