BMRB Entry 26718

Name: Domain Swapped HIV RNase H
Published: 2016-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26718

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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:

Domain Swapped HIV RNase H

Deposition date:

2015-12-11

Original release date:

2016-02-12

Authors:

Mueller, Geoffrey; London, Robert; Zheng, Xunhai

Citation:

Citation: Zheng, Xunhai; Pedersen, Lars; Gabel, Scott; Mueller, Geoffrey; DeRose, Eugene; London, Robert. "Unfolding the HIV-1 reverse transcriptase RNase H domain - how to lose a molecular tug-of-war" Nucleic Acids Res. 44, 1776-1788 (2016).
PubMed: 26773054

Assembly members:

Assembly members:
RNase_H, polymer, 138 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNase_H: MNELYQLEKEPIVGAETFYV DGAANRETKLGKAGYVTNRG RQKVVTLTDTTNQKTELQAI YLALQDSGLEVNIVTDSQYA LGIIQAQPDQSESELVNQII EQLIKKEKVYLAWVPAHKGI GGNEQVDKLVSAGIRKVL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	239
15N chemical shifts	122
1H chemical shifts	122

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain Swapped HIV RNase H	1

Entities:

Entity 1, Domain Swapped HIV RNase H 138 residues - Formula weight is not available

Add 422 for correct numbering to HIV-1 Reverse Transcriptase

1

MET

ASN

GLU

LEU

TYR

GLN

LEU

GLU

LYS

GLU

2

PRO

ILE

VAL

GLY

ALA

GLU

THR

PHE

TYR

VAL

3

ASP

GLY

ALA

ASN

ARG

GLU

THR

LYS

LEU

4

GLY

LYS

ALA

GLY

TYR

VAL

THR

ASN

ARG

GLY

5

ARG

GLN

LYS

VAL

THR

LEU

THR

ASP

THR

6

THR

ASN

GLN

LYS

THR

GLU

LEU

GLN

ALA

ILE

7

TYR

LEU

ALA

LEU

GLN

ASP

SER

GLY

LEU

GLU

8

VAL

ASN

ILE

VAL

THR

ASP

SER

GLN

TYR

ALA

9

LEU

GLY

ILE

GLN

ALA

GLN

PRO

ASP

GLN

10

SER

GLU

SER

GLU

LEU

VAL

ASN

GLN

ILE

11

GLU

GLN

LEU

ILE

LYS

GLU

LYS

VAL

TYR

12

LEU

ALA

TRP

VAL

PRO

ALA

HIS

LYS

GLY

ILE

13

GLY

ASN

GLU

GLN

VAL

ASP

LYS

LEU

VAL

14

SER

ALA

GLY

ILE

ARG

LYS

VAL

LEU

Samples:

sample_1: RNase H, [U-99% 13C; U-99% 15N], 444 uM; TRIS, [U-2H], 25 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.002 M; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

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