BMRB Entry 11266

Click here to enlarge.

PDB ID: 1wy8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11266
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 the N-terminal Ubiquitin-like Domain in Human Np95/ICBP90-like Ring Finger Protein (NIRF)

Deposition date:

2010-08-09

Original release date:

2011-08-18

Authors:

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

Citation:

Citation: Zhao, C.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ubiquitin-like Domain in Human Np95/ICBP90-like Ring Finger Protein (NIRF)" .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 89 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: P041101-10

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like domain: GSSGSSGMWIQVRTIDGSKT CTIEDVSRKATIEELRERVW ALFDVRPECQRLFYRGKQLE NGYTLFDYDVGLNDIIQLLV RPDSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	368
15N chemical shifts	86
1H chemical shifts	581

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

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

Entities:

Entity 1, ubiquitin-like domain 89 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

TRP

ILE

2

GLN

VAL

ARG

THR

ILE

ASP

GLY

SER

LYS

THR

3

CYS

THR

ILE

GLU

ASP

VAL

SER

ARG

LYS

ALA

4

THR

ILE

GLU

LEU

ARG

GLU

ARG

VAL

TRP

5

ALA

LEU

PHE

ASP

VAL

ARG

PRO

GLU

CYS

GLN

6

ARG

LEU

PHE

TYR

ARG

GLY

LYS

GLN

LEU

GLU

7

ASN

GLY

TYR

THR

LEU

PHE

ASP

TYR

ASP

VAL

8

GLY

LEU

ASN

ASP

ILE

GLN

LEU

VAL

9

ARG

PRO

ASP

SER

GLY

PRO

SER

GLY

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.91 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 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 v20020425, Delaglio, F. - processing

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

Kujira v0.921, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WY8
DBJ	BAB68317 BAC31223 BAC38081 BAC81739 BAE00280
GB	AAH28397 AAH60241 AAI48950 AAM33798 AAM33799
REF	NP_001095740 NP_659122 NP_690856 XP_001142916 XP_002742966
SP	Q7TMI3 Q96PU4
TPG	DAA26932
AlphaFold	Q7TMI3 Q96PU4