BMRB Entry 7128

Name: Fibronecting 1F3-2F3 backbone chemical shift assignments
Published: 2007-05-29

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PDB ID: 2ha1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7128
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Fibronecting 1F3-2F3 backbone chemical shift assignments PubMed: 17464288

Deposition date: 2006-05-23 Original release date: 2007-05-29

Authors: Vakonakis, Ioannis; Campbell, Iain

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).

Assembly members:
1F3-2F3, polymer, 201 residues, 22097 Da.

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

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):
1F3-2F3: SGPVEVFITETPSQPNSHPI QWNAPQPSHISKYILRWRPK NSVGRWKEATIPGHLNSYTI KGLKPGVVYEGQLISIQQYG HQEVTRFDFTTTSTSTPVTS NTVTGETTPFSPLVATSESV TEITASSFVVSWVSASDTVS GFRVEYELSEEGDEPQYLDL PSTATSVNIPDLLPGRKYIV NVYQISEDGEQSLILSTSQT T

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	175
1H chemical shifts	175

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	1F3-2F3	1

Entities:

Entity 1, 1F3-2F3 201 residues - 22097 Da.

This sequence corresponds to the first two type III domain on human Fibronectin and the connecting amino acid linker

1

SER

GLY

PRO

VAL

GLU

VAL

PHE

ILE

THR

GLU

2

THR

PRO

SER

GLN

PRO

ASN

SER

HIS

PRO

ILE

3

GLN

TRP

ASN

ALA

PRO

GLN

PRO

SER

HIS

ILE

4

SER

LYS

TYR

ILE

LEU

ARG

TRP

ARG

PRO

LYS

5

ASN

SER

VAL

GLY

ARG

TRP

LYS

GLU

ALA

THR

6

ILE

PRO

GLY

HIS

LEU

ASN

SER

TYR

THR

ILE

7

LYS

GLY

LEU

LYS

PRO

GLY

VAL

TYR

GLU

8

GLY

GLN

LEU

ILE

SER

ILE

GLN

TYR

GLY

9

HIS

GLN

GLU

VAL

THR

ARG

PHE

ASP

PHE

THR

10

THR

SER

THR

SER

THR

PRO

VAL

THR

SER

11

ASN

THR

VAL

THR

GLY

GLU

THR

PRO

PHE

12

SER

PRO

LEU

VAL

ALA

THR

SER

GLU

SER

VAL

13

THR

GLU

ILE

THR

ALA

SER

PHE

VAL

14

SER

TRP

VAL

SER

ALA

SER

ASP

THR

VAL

SER

15

GLY

PHE

ARG

VAL

GLU

TYR

GLU

LEU

SER

GLU

16

GLU

GLY

ASP

GLU

PRO

GLN

TYR

LEU

ASP

LEU

17

PRO

SER

THR

ALA

THR

SER

VAL

ASN

ILE

PRO

18

ASP

LEU

PRO

GLY

ARG

LYS

TYR

ILE

VAL

19

ASN

VAL

TYR

GLN

ILE

SER

GLU

ASP

GLY

GLU

20

GLN

SER

LEU

ILE

LEU

SER

THR

SER

GLN

THR

21

THR

Samples:

sample_1: 1F3-2F3, [U-15N], 1.2 ± 0.2 mM; NaCl 150 mM; NaPi 20 mM; D2O 5%; H2O 95%

sample_2: 1F3-2F3, [U-13C; U-15N], 1 ± 0.1 ; NaCl 150 mM; NaPi 20 mM; D2O 5%; H2O 95%

conditions_1: ionic strength: 420 mM; pH: 7; 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
HNCA	sample_2	not available	conditions_1
HN(CO)CA	sample_2	not available	conditions_1

Software:

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

NMRPipe v2.3 Rev 2005.319.11.22, NIH/NIDDK - Data processing

PIPP v4.3.7, NIH - Data analysis

TOPSPIN v1.3, Bruker - Data collection

NMR spectrometers:

home build . 750 MHz
Bruker Avance II 500 MHz

Biological Magnetic Resonance Data Bank