BMRB Entry 11273

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PDB ID: 2dal
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11273
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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:

Solution Structure of the Novel Identified UBA-like Domain in the N-terminal of Human Fas Associated Factor 1 Protein

Deposition date:

2010-08-09

Original release date:

2011-08-18

Authors:

Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution Structure of the Novel Identified UBA-like Domain in the N-terminal of Human Fas Associated Factor 1 Protein" .

Assembly members:

Assembly members:
UBA-like domain, polymer, 62 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P050815-24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA-like domain: GSSGSSGGSAASSALKGLIQ QFTTITGASESVGKHMLEAC NNNLEMAVTMFLDGGGSGPS SG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	211
15N chemical shifts	54
1H chemical shifts	334

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA-like domain	1

Entities:

Entity 1, UBA-like domain 62 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

SER

ALA

2

ALA

SER

ALA

LEU

LYS

GLY

LEU

ILE

GLN

3

GLN

PHE

THR

ILE

THR

GLY

ALA

SER

GLU

4

SER

VAL

GLY

LYS

HIS

MET

LEU

GLU

ALA

CYS

5

ASN

LEU

GLU

MET

ALA

VAL

THR

MET

6

PHE

LEU

ASP

GLY

SER

GLY

PRO

SER

7

SER

GLY

Samples:

sample_1: UBA-like domain, [U-13C; U-15N], 0.26 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9321, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 700 MHz

PDB	2DAL
GB	EDM11425 EDM11426 EDM11427 KFM11413 KFO08321
REF	NP_001100556 XP_003477156 XP_004003056 XP_004644633 XP_004712317