BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5238

Title: 1H and 15N chemical shift assignments for the heparin-binding domain of vascular endothelial growth factor   PubMed: 9634701

Deposition date: 2001-12-18 Original release date: 2002-02-08

Authors: Fairbrother, Wayne; Champe, Mark; Christinger, Hans; Keyt, Bruce; Starovasnik, Melissa

Citation: Fairbrother, Wayne; Champe, Mark; Christinger, Hans; Keyt, Bruce; Starovasnik, Melissa. "Solution structure of the heparin-binding domain of vascular endothelial growth factor"  Structure 6, 637-649 (1998).

Assembly members:
vascular endothelial growth factor, polymer, 55 residues, 6477 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):
vascular endothelial growth factor: ARQENPCGPCSERRKHLFVQ DPQTCKCSCKNTDSRCKARQ LELNERTCRCDKPRR

Data sets:
Data typeCount
15N chemical shifts55
1H chemical shifts359

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VEGF heparin-binding domain1

Entities:

Entity 1, VEGF heparin-binding domain 55 residues - 6477 Da.

1   ALAARGGLNGLUASNPROCYSGLYPROCYS
2   SERGLUARGARGLYSHISLEUPHEVALGLN
3   ASPPROGLNTHRCYSLYSCYSSERCYSLYS
4   ASNTHRASPSERARGCYSLYSALAARGGLN
5   LEUGLULEUASNGLUARGTHRCYSARGCYS
6   ASPLYSPROARGARG

Samples:

sample_1: vascular endothelial growth factor 1.0 mM

sample_2: vascular endothelial growth factor, [U-15N], 2.0 mM

condition_1: pH: 5.5; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2QF-COSYnot availablenot availablenot available
2Qnot availablenot availablenot available
TOCSYnot availablenot availablenot available
NOESYnot availablenot availablenot available
1H-15N HSQCnot availablenot availablenot available
1H-15N TOCSY-HSQCnot availablenot availablenot available
1H-15N NOESY-HSQCnot availablenot availablenot available
1H-15N ROESY-HSQCnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available

Software:

FELIX - analysis, processing

NMR spectrometers:

  • Bruker AMX 500 MHz

Related Database Links:

PDB
DBJ BAA78418 BAB20890 BAB68520
EMBL CAA09179 CAA44447 CAA57143 CAB82426 CAC19512
GenBank AAA30502 AAA30804 AAA35789 AAA36804 AAA36807
PRF 2105202A
REF NP_001003175 NP_001009854 NP_001020537 NP_001020538 NP_001020539
SWISS-PROT P15691 P15692 P26617 P49151 Q9GKR0

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts