BMRB Entry 15783

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15783
MolProbity Validation Chart

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Title:
acidic fibroblast growth factor 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:
FGF-1, polymer, 133 residues, 15118.163 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET20

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FGF-1: YKKPKLLYCSNGGHFLRILP DGTVDGTRDRSDQHIQLQLS AESVGEVYIKSTETGQYLAM DTDGLLYGSQTPNEECLFLE RLEENHYNTYISKKHAEKNW FVGLKKNGSCKRGPRTHYGQ KAILFLPLPVSSD

Data sets:
Data typeCount
1H chemical shifts694
15N chemical shifts132
13C chemical shifts364

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FGF-11

Entities:

Entity 1, FGF-1 133 residues - 15118.163 Da.

1   TYRLYSLYSPROLYSLEULEUTYRCYSSER
2   ASNGLYGLYHISPHELEUARGILELEUPRO
3   ASPGLYTHRVALASPGLYTHRARGASPARG
4   SERASPGLNHISILEGLNLEUGLNLEUSER
5   ALAGLUSERVALGLYGLUVALTYRILELYS
6   SERTHRGLUTHRGLYGLNTYRLEUALAMET
7   ASPTHRASPGLYLEULEUTYRGLYSERGLN
8   THRPROASNGLUGLUCYSLEUPHELEUGLU
9   ARGLEUGLUGLUASNHISTYRASNTHRTYR
10   ILESERLYSLYSHISALAGLULYSASNTRP
11   PHEVALGLYLEULYSLYSASNGLYSERCYS
12   LYSARGGLYPROARGTHRHISTYRGLYGLN
13   LYSALAILELEUPHELEUPROLEUPROVAL
14   SERSERASP

Samples:

sample: FGF-1 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_NOESYsampleisotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AV600 600 MHz
  • Bruker AV800 800 MHz

Related Database Links:

BMRB 15960 16493 16494 16502 17464 17674
PDB
DBJ BAC29035 BAF82451 BAG35227 BAI46827
EMBL CAA32448 CAA36206 CAA42869 CAA46661 CAI29610
GB AAA37618 AAA52446 AAA52638 AAA79245 AAB29057
PRF 1605206A
REF NP_000791 NP_001127073 NP_001138364 NP_001138406 NP_001138407
SP P05230 P20002 P34004 P61148 P61149
AlphaFold P05230 P20002 P34004 P61148 P61149

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