BMRB Entry 11127

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PDB ID: 1x4z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11127
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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 2nd fibronectin type III domain from mouse biregional cell adhesion molecule-related/down-regulated oncogenes (Cdon) binding protein

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

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

Citation:

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the 2nd fibronectin type III domain from mouse biregional cell adhesion molecule-related/down-regulated oncogenes (Cdon) binding protein" .

Assembly members:

Assembly members:
fibronectin type III (fn3) domain, polymer, 121 residues, Formula weight is not available

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryotase Kingdom: Metazoaouse Genus/species: Mus musculususe

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P040719-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fibronectin type III (fn3) domain: GSSGSSGSQPDHGRLSPPEA PDRPTISTASETSVYVTWIP RGNGGFPIQSFRVEYKKLKK VGDWILATSAIPPSRLSVEI TGLEKGISYKFRVRALNMLG ESEPSAPSRPYVVSGSGPSS G

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	506
15N chemical shifts	107
1H chemical shifts	787

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	fibronectin type III (fn3) domain	1

Entities:

Entity 1, fibronectin type III (fn3) domain 121 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

SER

GLN

PRO

2

ASP

HIS

GLY

ARG

LEU

SER

PRO

GLU

ALA

3

PRO

ASP

ARG

PRO

THR

ILE

SER

THR

ALA

SER

4

GLU

THR

SER

VAL

TYR

VAL

THR

TRP

ILE

PRO

5

ARG

GLY

ASN

GLY

PHE

PRO

ILE

GLN

SER

6

PHE

ARG

VAL

GLU

TYR

LYS

LEU

LYS

7

VAL

GLY

ASP

TRP

ILE

LEU

ALA

THR

SER

ALA

8

ILE

PRO

SER

ARG

LEU

SER

VAL

GLU

ILE

9

THR

GLY

LEU

GLU

LYS

GLY

ILE

SER

TYR

LYS

10

PHE

ARG

VAL

ARG

ALA

LEU

ASN

MET

LEU

GLY

11

GLU

SER

GLU

PRO

SER

ALA

PRO

SER

ARG

PRO

12

TYR

VAL

SER

GLY

SER

GLY

PRO

SER

13

GLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.43 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 v20030801, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz