BMRB Entry 16478

Title:
Solution structure of UBA domain of XIAP
Deposition date:
2009-09-04
Original release date:
2010-05-05
Authors:
Hui, Sin-Kam; Tse, Man-Kit; Sze, Kong-Hung
Citation:

Citation: Hui, Sin-Kam; Tse, Man-Kit; Yang, Yinhua; Wong, Benjamin Chun-Yu; Sze, Kong-Hung. "Backbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein."  Biomol. NMR Assignments 4, 13-15 (2010).
PubMed: 19916060

Assembly members:

Assembly members:
UBA, polymer, 104 residues, 11873.473 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32a

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts109
1H chemical shifts752

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA1

Entities:

Entity 1, UBA 104 residues - 11873.473 Da.

1   GLYSERALAMETALAASPILEGLYSERGLU
2   PHEGLULYSTHRPROSERLEUTHRARGARG
3   ILEASPASPTHRILEPHEGLNASNPROMET
4   VALGLNGLUALAILEARGMETGLYPHESER
5   PHELYSASPILELYSLYSILEMETGLUGLU
6   LYSILEGLNILESERGLYSERASNTYRLYS
7   SERLEUGLUVALLEUVALALAASPLEUVAL
8   ASNALAGLNLYSASPSERMETGLNASPGLU
9   SERSERGLNTHRSERLEUGLNLYSGLUILE
10   SERTHRGLUGLUGLNLEUARGARGLEUGLN
11   GLUGLULYSLEU

Samples:

sample_1: Bis-TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; PMSF 1 mM; UBA, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAG36609 BAI46620
GB AAC50373 AAC50518 AAH32729 AAW62257 AAX29953
REF NP_001158 NP_001191330 XP_001086574 XP_003262340 XP_003779771
SP P98170
AlphaFold P98170

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