BMRB Entry 17829

Name: FVIII C2 Domain
Published: 2012-03-01

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17829

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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:

FVIII C2 Domain

Deposition date:

2011-08-03

Original release date:

2012-03-01

Authors:

Nuzzio, Kristin; Cullinan, David; Novakovic, Valerie; Boettcher, John; Rienstra, Chad; Gilbert, Gary; Baleja, James

Citation:

Citation: Nuzzio, Kristin; Cullinan, David; Novakovic, Valerie; Boettcher, John; Rienstra, Chad; Gilbert, Gary; Baleja, James. "Backbone resonance assignments of the C2 domain of coagulation factor VIII." Biomol. NMR Assignments 7, 31-34 (2013).
PubMed: 22392338

Assembly members:

Assembly members:
C2_Domain, polymer, 163 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C2_Domain: GSHMCSMPLGMESKAISDAQ ITASSYFTNMFATWSPSKAR LHLQGRSNAWRPQVNNPKEW LQVDFQKTMKVTGVTTQGVK SLLTSMYVKEFLISSSQDGH QWTLFFQNGKVKVFQGNQDS FTPVVNSLDPPLLTRYLRIH PQSWVHQIALRMEVLGCEAQ DLY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	440
15N chemical shifts	145
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2_Domain	1

Entities:

Entity 1, C2_Domain 163 residues - Formula weight is not available

1

GLY

SER

HIS

MET

CYS

SER

MET

PRO

LEU

GLY

2

MET

GLU

SER

LYS

ALA

ILE

SER

ASP

ALA

GLN

3

ILE

THR

ALA

SER

TYR

PHE

THR

ASN

MET

4

PHE

ALA

THR

TRP

SER

PRO

SER

LYS

ALA

ARG

5

LEU

HIS

LEU

GLN

GLY

ARG

SER

ASN

ALA

TRP

6

ARG

PRO

GLN

VAL

ASN

PRO

LYS

GLU

TRP

7

LEU

GLN

VAL

ASP

PHE

GLN

LYS

THR

MET

LYS

8

VAL

THR

GLY

VAL

THR

GLN

GLY

VAL

LYS

9

SER

LEU

THR

SER

MET

TYR

VAL

LYS

GLU

10

PHE

LEU

ILE

SER

GLN

ASP

GLY

HIS

11

GLN

TRP

THR

LEU

PHE

GLN

ASN

GLY

LYS

12

VAL

LYS

VAL

PHE

GLN

GLY

ASN

GLN

ASP

SER

13

PHE

THR

PRO

VAL

ASN

SER

LEU

ASP

PRO

14

PRO

LEU

THR

ARG

TYR

LEU

ARG

ILE

HIS

15

PRO

GLN

SER

TRP

VAL

HIS

GLN

ILE

ALA

LEU

16

ARG

MET

GLU

VAL

LEU

GLY

CYS

GLU

ALA

GLN

17

ASP

LEU

TYR

Samples:

sample_1: C2 Domain 0.8 mM; H2O 90%; D2O 10%; sodium chloride 50 mM; EDTA 50 uM; NaN3 0.01%; DSS 20 uM; imidazole 10 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker AMX 600 MHz