BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15785

Title: C2A domain of synaptototagmin I solution structure in the FGF-1-C2A binary complex: key component in the fibroblast growthfactor non-classical pathway   PubMed: 19723500

Authors: Mohan, Sepuru; Yu, Chin

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).

Assembly members:
C2A, polymer, 128 residues, 14784.028 Da.

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

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

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

Data sets:
Data typeCount
15N chemical shifts134
13C chemical shifts531
1H chemical shifts870

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2A1

Entities:

Entity 1, C2A 128 residues - 14784.028 Da.

1   GLULYSLEUGLYLYSLEUGLNTYRSERLEU
2   ASPTYRASPPHEGLNASNASNGLNLEULEU
3   VALGLYILEILEGLNALAALAGLULEUPRO
4   ALALEUASPMETGLYGLYTHRSERASPPRO
5   TYRVALLYSVALPHELEULEUPROASPLYS
6   LYSLYSLYSPHEGLUTHRLYSVALHISARG
7   LYSTHRLEUASNPROVALPHEASNGLUGLN
8   PHETHRPHELYSVALPROTYRSERGLULEU
9   GLYGLYLYSTHRLEUVALMETALAVALTYR
10   ASPPHEASPARGPHESERLYSHISASPILE
11   ILEGLYGLUPHELYSVALPROMETASNTHR
12   VALASPPHEGLYHISVALTHRGLUGLUTRP
13   ARGASPLEUGLNSERALAGLULYS

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:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker AV600 600 MHz
  • Bruker AV800 800 MHz

Related Database Links:

BMRB 15952 17102 4039 4041 4166 4167
PDB
GB AAK15077 ELW70522 EPY85163 KFO26677 KFP32561
REF XP_005976391 XP_010164835 XP_010202276 XP_010211789