BMRB Entry 4757

Name: 1H, 13C, 15N Chemical Shift Assignment for the UBA(2) Domain of HHR23A
Published: 2000-06-27

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PDB ID: 1dv0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4757
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, 15N Chemical Shift Assignment for the UBA(2) Domain of HHR23A

Deposition date:

2000-06-09

Original release date:

2000-06-27

Authors:

Withers-Ward, Elizabeth; Mueller, Thomas; Chen, Irvin; Feigon, Juli

Citation:

Citation: Withers-Ward, Elizabeth; Mueller, Thomas; Chen, Irvin; Feigon, Juli. "Biochemical and Structural Analysis of the Interaction Between the UBA(2) Domain of the DNA Repair Protein HHR23A and HIV-1 Vpr" Biochemistry 39, 14103-14112 (2000).

Assembly members:

Assembly members:
Ubiquitin associated domain, polymer, 47 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9696 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubiquitin associated domain: GSQEKEAIERLKALGFPESL VIQAYFACEKNENLAANFLL SQNFDDE

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	309
13C chemical shifts	137
15N chemical shifts	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA subunit 1	1

Entities:

Entity 1, UBA subunit 1 47 residues - Formula weight is not available

1

GLY

SER

GLN

GLU

LYS

GLU

ALA

ILE

GLU

ARG

2

LEU

LYS

ALA

LEU

GLY

PHE

PRO

GLU

SER

LEU

3

VAL

ILE

GLN

ALA

TYR

PHE

ALA

CYS

GLU

LYS

4

ASN

GLU

ASN

LEU

ALA

ASN

PHE

LEU

5

SER

GLN

ASN

PHE

ASP

GLU

Samples:

sample_1: Ubiquitin associated domain, [U-95% 13C; U-95% 15N], 2.5 mM

sample_2: Ubiquitin associated domain, [U-95% 15N], 2.5 mM

sample_3: Ubiquitin associated domain 2.5 mM

Ex-cond_1: pH: 6.5; temperature: 300 K; ionic strength: 0.2 M

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-1H-15N NOESY	not available	not available	Ex-cond_1
3D 1H-1H-15N TOCSY	not available	not available	Ex-cond_1
3D 15N-1H-15N HSQC-NOE-HSQC	not available	not available	Ex-cond_1
3D CBCA(CO)NH	not available	not available	Ex-cond_1
3D CBCANH	not available	not available	Ex-cond_1
3D HBHA(CO)NH	not available	not available	Ex-cond_1
3D 1H-13C-1H HCCH-COSY	not available	not available	Ex-cond_1
3D 1H-13C-1H HCCH-TOCSY	not available	not available	Ex-cond_1
3D 1H-13C-1H NOESY	not available	not available	Ex-cond_1
2D NOESY	not available	not available	Ex-cond_1
2D DQF-COSY	not available	not available	Ex-cond_1
2D TOCSY	not available	not available	Ex-cond_1

Software:

XWINNMR v2.6 - processing

AURELIA v2.7.1 - assignment, peak integration

XEASY v1.5 - assignment

NMR spectrometers:

Bruker DRX 500 MHz

PDB	1DV0 1F4I 1OQY 1QZE
DBJ	BAA04767 BAC29962 BAD92950 BAF82597 BAG56758
EMBL	CAA63145 CDQ99199
GB	AAB51177 AAH14026 AAH88364 AAI33283 AAI38685
PRF	2206377A
REF	NP_001076083 NP_001257291 NP_001284535 NP_005044 NP_033036
SP	A3KMV2 P54725 P54726
TPG	DAA28035
AlphaFold	A3KMV2 P54725 P54726