BMRB Entry 7127

Name: Fibronectin 2F3 chemical shift assignments
Published: 2007-05-29

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PDB ID: 2h41
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7127
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:

Fibronectin 2F3 chemical shift assignments

Deposition date:

2006-05-22

Original release date:

2007-05-29

Authors:

Vakonakis, Ioannis; Campbell, Iain

Citation:

Citation: Vakonakis, Ioannis; Staunton, David; Rooney, Luke; Campbell, Iain. "Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis." EMBO J. 26, 2575-2583 (2007).
PubMed: 17464288

Assembly members:

Assembly members:
2F3, polymer, 95 residues, 9833.7 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Vector: pGEX-6P-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
2F3: GPLGSHLVATSESVTEITAS SFVVSWVSASDTVSGFRVEY ELSEEGDEPQYLDLPSTATS VNIPDLLPGRKYIVNVYQIS EDGEQSLILSTSQTT

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	318
15N chemical shifts	97
1H chemical shifts	645

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	2F3	1

Entities:

Entity 1, 2F3 95 residues - 9833.7 Da.

The 2F3 sequence corresponds to that of the second type III domain of fibronectin with an additional 6 non-canonical amino-terminal residues from the expression system

1

GLY

PRO

LEU

GLY

SER

HIS

LEU

VAL

ALA

THR

2

SER

GLU

SER

VAL

THR

GLU

ILE

THR

ALA

SER

3

SER

PHE

VAL

SER

TRP

VAL

SER

ALA

SER

4

ASP

THR

VAL

SER

GLY

PHE

ARG

VAL

GLU

TYR

5

GLU

LEU

SER

GLU

GLY

ASP

GLU

PRO

GLN

6

TYR

LEU

ASP

LEU

PRO

SER

THR

ALA

THR

SER

7

VAL

ASN

ILE

PRO

ASP

LEU

PRO

GLY

ARG

8

LYS

TYR

ILE

VAL

ASN

VAL

TYR

GLN

ILE

SER

9

GLU

ASP

GLY

GLU

GLN

SER

LEU

ILE

LEU

SER

10

THR

SER

GLN

THR

Samples:

sample_1: 2F3, [U-15N], 2 ± 0.2 mM; NaCl 20 mM; NaPi 20 mM; D2O 5%; H2O 95%

sample_2: 2F3, [U-13C; U-15N], 1.5 ± 0.1 mM; NaCl 20 mM; NaPi 20 mM; D2O 5%; H2O 95%

conditions_1: ionic strength: 160 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

conditions_2: ionic strength: 160 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N HSQC	sample_1	not available	conditions_1
CBCA(CO)NH	sample_2	not available	conditions_1
CBCANH	sample_2	not available	conditions_1
C(CO)NH	sample_2	not available	conditions_1
H(CCO)NH	sample_2	not available	conditions_1
HC(C)H-COSY	sample_2	not available	conditions_2
HCHC 4D NOESY	sample_2	not available	conditions_2
HBHA(CO)NH	sample_2	not available	conditions_1
HNHA	sample_1	not available	conditions_1

Software:

Omega Spectrometer Operating Software vBeta 6.0.3b2, Bruker - Data collection

NMRPipe v2.3 Rev 2005.319.11.22, NIH - Data processing

PIPP v4.3.7, NIH - Data analysis

NMR spectrometers:

home built . 600 MHz
home built . 500 MHz