BMRB Entry 4757

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:
Data typeCount
1H chemical shifts309
13C chemical shifts137
15N chemical shifts44

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA subunit 11

Entities:

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

1   GLYSERGLNGLULYSGLUALAILEGLUARG
2   LEULYSALALEUGLYPHEPROGLUSERLEU
3   VALILEGLNALATYRPHEALACYSGLULYS
4   ASNGLUASNLEUALAALAASNPHELEULEU
5   SERGLNASNPHEASPASPGLU

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:

NameSampleSample stateSample conditions
3D 1H-1H-15N NOESYnot availablenot availableEx-cond_1
3D 1H-1H-15N TOCSYnot availablenot availableEx-cond_1
3D 15N-1H-15N HSQC-NOE-HSQCnot availablenot availableEx-cond_1
3D CBCA(CO)NHnot availablenot availableEx-cond_1
3D CBCANHnot availablenot availableEx-cond_1
3D HBHA(CO)NHnot availablenot availableEx-cond_1
3D 1H-13C-1H HCCH-COSYnot availablenot availableEx-cond_1
3D 1H-13C-1H HCCH-TOCSYnot availablenot availableEx-cond_1
3D 1H-13C-1H NOESYnot availablenot availableEx-cond_1
2D NOESYnot availablenot availableEx-cond_1
2D DQF-COSYnot availablenot availableEx-cond_1
2D TOCSYnot availablenot availableEx-cond_1

Software:

XWINNMR v2.6 - processing

AURELIA v2.7.1 - assignment, peak integration

XEASY v1.5 - assignment

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB
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

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