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BMRB Entry 18804

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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/BMR18804
MolProbity Validation Chart

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Title: Homodimeric transmembrane domain of the human receptor tyrosine kinase ErbB1 (EGFR, HER1) in micelles

Deposition date: 2012-10-24 Original release date: 2013-10-22

Authors: Lesovoy, Dmitry; Bocharov, Eduard; Pustovalova, Yulia; Bocharova, Olga; Arseniev, Alexander

Citation: Bocharov, Eduard; Lesovoy, Dmitry; Pustovalova, Yulia; Bocharova, Olga; Arseniev, Alexander. "Homodimeric transmembrane domain of the human receptor tyrosine kinase ErbB1 (EGFR, HER1) in micelles"  To be Published ., .-..

Assembly members:
ErbB1tm, polymer, 44 residues, 4733.881 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: pGEMEX-1/(TRX-tmErbB1)

Entity Sequences (FASTA):
ErbB1tm: EGCPTNGPKIPSIATGMVGA LLLLLVVALGIGLFMRRRHI VRKR

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts46
1H chemical shifts346

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ErbB1 (EGFR, HER1), 11
2ErbB1 (EGFR, HER1), 21

Entities:

Entity 1, ErbB1 (EGFR, HER1), 1 44 residues - 4733.881 Da.

1   GLUGLYCYSPROTHRASNGLYPROLYSILE
2   PROSERILEALATHRGLYMETVALGLYALA
3   LEULEULEULEULEUVALVALALALEUGLY
4   ILEGLYLEUPHEMETARGARGARGHISILE
5   VALARGLYSARG

Samples:

sample_1: ErbB1tm, [U-99% 13C; U-99% 15N], 0.75 mM; ErbB1tm 0.75 mM; DPC, [U-99% 2H], 90 mM; sodium azide 0.3 mM; TCEP 6 mM; citric acid 10 mM; Na2HPO4 20 mM

sample_2: ErbB1tm, [U-99% 13C; U-99% 15N], 0.75 mM; ErbB1tm 0.75 mM; DPC, [U-99% 2H], 90 mM; sodium azide 0.3 mM; TCEP 6 mM; citric acid 10 mM; Na2HPO4 20 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C constant time HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C constant time HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N(TROSY) NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C(constant time) NOESY aliphaticsample_1isotropicsample_conditions_1
15N,13C-F1-filtered/F3-edited-NOESYsample_1isotropicsample_conditions_1
15N,13C-F1-filtered/F3-edited-NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CARA v1.8.4, Rochus Keller - chemical shift assignment

Mathematica, Wolfram Research - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16658 25729
PDB
DBJ BAD92679 BAF83041 BAH11869 BAI46646
EMBL CAA25240 CAA25282
GB AAG35789 AAG43243 AAH94761 AAS83109 AAT52212
PRF 1006266A
REF NP_005219 XP_004045514 XP_008967087 XP_519102
SP P00533
AlphaFold P00533

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