BMRB Entry 15785

Name: C2A domain of synaptototagmin I solution structure in the FGF-1-C2A binary complex: key component in the fibroblast growthfactor non-classical pathway
Published: 2009-10-12

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PDB ID: 2k45
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15785
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:

C2A domain of synaptototagmin I solution structure in the FGF-1-C2A binary complex: key component in the fibroblast growthfactor non-classical pathway

Deposition date:

2008-05-28

Original release date:

2009-10-12

Authors:

Mohan, Sepuru; Yu, Chin

Citation:

Citation: Anbazhagan, Veerappan; Wang, Han-Min; Lu, Ching-Song; Yu, Chin. "A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1." Arch. Biochem. Biophys. 490, 158-162 (2009).
PubMed: 19723500

Assembly members:

Assembly members:
C2A, polymer, 128 residues, 14784.028 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 Host organism: Escherichia coli Vector: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C2A: EKLGKLQYSLDYDFQNNQLL VGIIQAAELPALDMGGTSDP YVKVFLLPDKKKKFETKVHR KTLNPVFNEQFTFKVPYSEL GGKTLVMAVYDFDRFSKHDI IGEFKVPMNTVDFGHVTEEW RDLQSAEK

Data sets:

assigned_chemical_shifts
- chemical_shift_set

Data type	Count
13C chemical shifts	531
15N chemical shifts	134
1H chemical shifts	870

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2A	1

Entities:

Entity 1, C2A 128 residues - 14784.028 Da.

1

GLU

LYS

LEU

GLY

LYS

LEU

GLN

TYR

SER

LEU

2

ASP

TYR

ASP

PHE

GLN

ASN

GLN

LEU

3

VAL

GLY

ILE

GLN

ALA

GLU

LEU

PRO

4

ALA

LEU

ASP

MET

GLY

THR

SER

ASP

PRO

5

TYR

VAL

LYS

VAL

PHE

LEU

PRO

ASP

LYS

6

LYS

PHE

GLU

THR

LYS

VAL

HIS

ARG

7

LYS

THR

LEU

ASN

PRO

VAL

PHE

ASN

GLU

GLN

8

PHE

THR

PHE

LYS

VAL

PRO

TYR

SER

GLU

LEU

9

GLY

LYS

THR

LEU

VAL

MET

ALA

VAL

TYR

10

ASP

PHE

ASP

ARG

PHE

SER

LYS

HIS

ASP

ILE

11

ILE

GLY

GLU

PHE

LYS

VAL

PRO

MET

ASN

THR

12

VAL

ASP

PHE

GLY

HIS

VAL

THR

GLU

TRP

13

ARG

ASP

LEU

GLN

SER

ALA

GLU

LYS

Samples:

sample_1: C2A, [U-100% 13C; U-100% 15N], 1.0 mM; Phosphate buffer 25 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker AV600 600 MHz
Bruker AV800 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks