BMRB Entry 5801

Title:
Structural analysis of an EGF/TGF-alpha chimera with unique ErbB binding specificity
Deposition date:
2003-05-19
Original release date:
2003-10-13
Authors:
Wingens, Miriam; Walma, Tine; van Ingen, Hugo; Stortelers, Catelijne; van Leeuwen, Jeroen; van Zoelen, Everardus; Vuister, Geerten
Citation:

Citation: Wingens, Miriam; Walma, Tine; van Ingen, Hugo; Stortelers, Catelijne; van Leeuwen, Jeroen; van Zoelen, Everardus; Vuister, Geerten. "Structural Analysis of an Epidermal Growth Factor/Transforming Growth Factor-alpha Chimera with Unique ErbB Binding Specificity specificity"  J. Biol. Chem. 278, 39114-39123 (2003).
PubMed: 12869572

Assembly members:

Assembly members:
T1E, polymer, 54 residues, Formula weight is not available

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: Pichia pastoris   Vector: pPICZalphaA

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts56
1H chemical shifts346
coupling constants51
T1 relaxation values52

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1T1E1

Entities:

Entity 1, T1E 54 residues - Formula weight is not available

1   VALVALSERHISPHEASNASPCYSPROLEU
2   SERHISASPGLYTYRCYSLEUHISASPGLY
3   VALCYSMETTYRILEGLUALALEUASPLYS
4   TYRALACYSASNCYSVALVALGLYTYRILE
5   GLYGLUARGCYSGLNTYRARGASPLEULYS
6   TRPTRPGLULEU

Samples:

sample_1: T1E, [U-15N], 0.8 mM; K2HPO4/KH2PO4 50 mM

cond_set_1: pH: 6.3; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1not availablecond_set_1
3D 1H-15N TOCSYsample_1not availablecond_set_1
2D NOESYsample_1not availablecond_set_1
3D HNHAsample_1not availablecond_set_1
3D HNHBsample_1not availablecond_set_1

Software:

NMRPipe v1.8 - spectral processing

XEASY v1.2 - assignment, peak integration

X-PLOR v3.851 - restrained molecular dynamics

NMR spectrometers:

  • Varian UnityPlus 800 MHz
  • Varian UnityInova 600 MHz

Related Database Links:

PDB
REF XP_001088957

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