BMRB Entry 16478

Name: Solution structure of UBA domain of XIAP
Published: 2010-05-05

Click here to enlarge.

PDB ID: 2kna
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16478
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA: GSAMADIGSEFEKTPSLTRR IDDTIFQNPMVQEAIRMGFS FKDIKKIMEEKIQISGSNYK SLEVLVADLVNAQKDSMQDE SSQTSLQKEISTEEQLRRLQ EEKL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	445
15N chemical shifts	109
1H chemical shifts	752

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA	1

Entities:

Entity 1, UBA 104 residues - 11873.473 Da.

1

GLY

SER

ALA

MET

ALA

ASP

ILE

GLY

SER

GLU

2

PHE

GLU

LYS

THR

PRO

SER

LEU

THR

ARG

3

ILE

ASP

THR

ILE

PHE

GLN

ASN

PRO

MET

4

VAL

GLN

GLU

ALA

ILE

ARG

MET

GLY

PHE

SER

5

PHE

LYS

ASP

ILE

LYS

ILE

MET

GLU

6

LYS

ILE

GLN

ILE

SER

GLY

SER

ASN

TYR

LYS

7

SER

LEU

GLU

VAL

LEU

VAL

ALA

ASP

LEU

VAL

8

ASN

ALA

GLN

LYS

ASP

SER

MET

GLN

ASP

GLU

9

SER

GLN

THR

SER

LEU

GLN

LYS

GLU

ILE

10

SER

THR

GLU

GLN

LEU

ARG

LEU

GLN

11

GLU

LYS

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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

PDB	2KNA
DBJ	BAG36609 BAI46620
GB	AAC50373 AAC50518 AAH32729 AAW62257 AAX29953
REF	NP_001158 NP_001191330 XP_001086574 XP_003262340 XP_003779771
SP	P98170
AlphaFold	P98170