BMRB Entry 11148

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PDB ID: 2yrp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11148
MolProbity Validation Chart

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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 TIG domain from Human Nuclear factor of activated T-cells, cytoplasmic 4

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the TIG domain from Human Nuclear factor of activated T-cells, cytoplasmic 4" .

Assembly members:

Assembly members:
TIG domain, polymer, 114 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: P061030-04

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TIG domain: GSSGSSGLPQVEAYSPSACS VRGGEELVLTGSNFLPDSKV VFIERGPDGKLQWEEEATVN RLQSNEVTLTLTVPEYSNKR VSRPVQVYFYVSNGRRKRSP TQSFRFLPVICKEE

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	509
15N chemical shifts	119
1H chemical shifts	795

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TIG domain	1

Entities:

Entity 1, TIG domain 114 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

LEU

PRO

GLN

2

VAL

GLU

ALA

TYR

SER

PRO

SER

ALA

CYS

SER

3

VAL

ARG

GLY

GLU

LEU

VAL

LEU

THR

4

GLY

SER

ASN

PHE

LEU

PRO

ASP

SER

LYS

VAL

5

VAL

PHE

ILE

GLU

ARG

GLY

PRO

ASP

GLY

LYS

6

LEU

GLN

TRP

GLU

ALA

THR

VAL

ASN

7

ARG

LEU

GLN

SER

ASN

GLU

VAL

THR

LEU

THR

8

LEU

THR

VAL

PRO

GLU

TYR

SER

ASN

LYS

ARG

9

VAL

SER

ARG

PRO

VAL

GLN

VAL

TYR

PHE

TYR

10

VAL

SER

ASN

GLY

ARG

LYS

ARG

SER

PRO

11

THR

GLN

SER

PHE

ARG

PHE

LEU

PRO

VAL

ILE

12

CYS

LYS

GLU

Samples:

sample_1: TIG domain, [U-13C; U-15N], 0.94 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 K

Experiments:

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

Software:

TOPSPIN v1.3, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

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

Kujira v0.9823, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE II 900 MHz

PDB	2YRP
DBJ	BAG56726 BAG63617 BAI46039
GB	AAA79175 AAH08857 AAH53855 ABZ92167 ACG55652
REF	NP_001129494 NP_001185894 NP_001185895 NP_001185896 NP_001275731
SP	Q14934
AlphaFold	Q14934