BMRB Entry 11311

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PDB ID: 1x3b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11311
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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 FAS1 domain of human transforming growth factor-beta induced protein IG-H3

Deposition date:

2010-08-10

Original release date:

2011-08-19

Authors:

Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Yoneyama, M.; Tomizawa, T.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the FAS1 domain of human transforming growth factor-beta induced protein IG-H3" .

Assembly members:

Assembly members:
FAS1 domain, polymer, 146 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: P040524-06

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FAS1 domain: GSSGSSGMGTVMDVLKGDNR FSMLVAAIQSAGLTETLNRE GVYTVFAPTNEAFRALPPRE RSRLLGDAKELANILKYHIG DEILVSGGIGALVRLKSLQG DKLEVSLKNNVVSVNKEPVA EPDIMATNGVVHVITNVLQP SGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	608
15N chemical shifts	142
1H chemical shifts	988

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FAS1 domain	1

Entities:

Entity 1, FAS1 domain 146 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

GLY

THR

2

VAL

MET

ASP

VAL

LEU

LYS

GLY

ASP

ASN

ARG

3

PHE

SER

MET

LEU

VAL

ALA

ILE

GLN

SER

4

ALA

GLY

LEU

THR

GLU

THR

LEU

ASN

ARG

GLU

5

GLY

VAL

TYR

THR

VAL

PHE

ALA

PRO

THR

ASN

6

GLU

ALA

PHE

ARG

ALA

LEU

PRO

ARG

GLU

7

ARG

SER

ARG

LEU

GLY

ASP

ALA

LYS

GLU

8

LEU

ALA

ASN

ILE

LEU

LYS

TYR

HIS

ILE

GLY

9

ASP

GLU

ILE

LEU

VAL

SER

GLY

ILE

GLY

10

ALA

LEU

VAL

ARG

LEU

LYS

SER

LEU

GLN

GLY

11

ASP

LYS

LEU

GLU

VAL

SER

LEU

LYS

ASN

12

VAL

SER

VAL

ASN

LYS

GLU

PRO

VAL

ALA

13

GLU

PRO

ASP

ILE

MET

ALA

THR

ASN

GLY

VAL

14

VAL

HIS

VAL

ILE

THR

ASN

VAL

LEU

GLN

PRO

15

SER

GLY

PRO

SER

GLY

Samples:

sample_1: FAS1 domain, [U-13C; U-15N], 0.39 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 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

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

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

BMRB	18466 18467 25425
PDB	1X3B 2LTB 2LTC 2VXP
GB	AAC24944