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 16768

Title: EGF   PubMed: 21029725

Deposition date: 2010-03-08 Original release date: 2011-11-28

Authors: Hsiao Wen, Huang; Mohan, Sepuru; Chin, Yu

Citation: Huang, Hsiao Wen; Mohan, Sepuru; Yu, Chin. "The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin"  Biochem. Biophys. Res. Commun. 402, 705-710 (2010).

Assembly members:
hEGF, polymer, 53 residues, 6229.053 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   Vector: pET-32a

Entity Sequences (FASTA):
hEGF: NSDSECPLSHDGYCLHDGVC MYIEALDKYACNCVVGYIGE RCQYRDLKWWELR

Data sets:
Data typeCount
13C chemical shifts184
15N chemical shifts48
1H chemical shifts262

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hEGF1

Entities:

Entity 1, hEGF 53 residues - 6229.053 Da.

1   ASNSERASPSERGLUCYSPROLEUSERHIS
2   ASPGLYTYRCYSLEUHISASPGLYVALCYS
3   METTYRILEGLUALALEUASPLYSTYRALA
4   CYSASNCYSVALVALGLYTYRILEGLYGLU
5   ARGCYSGLNTYRARGASPLEULYSTRPTRP
6   GLULEUARG

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.07 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation

NMR spectrometers:

  • Varian Uniform NMR System 700 MHz

Related Database Links:

BMRB 1377 1378 2075 2076 2077 2078
PDB
DBJ BAG61319
EMBL CAA28240 CCA96179 CEK41095
GB AAA60744 AAA72173 AAA72241 AAA72506 AAA72563
REF NP_001171601 NP_001171602 NP_001954 XP_001088957 XP_002804220
SP P01133
AlphaFold P01133

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