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 16658

Title: Heterodimeric association of Transmembrane domains of ErbB1 and ErbB2 receptors Enabling Kinase Activation   PubMed: 20471394

Authors: MIneev, Konstantin; Bocharov, Eduard; Pustovalova, Yulia; Bocharova, Olga; Chupin, Vladimir; Arseniev, Alexander

Citation: Mineev, Konstantin; Bocharov, Eduard; Pustovalova, Yulia; Bocharova, Olga; Chupin, Vladimir; Arseniev, Alexander. "Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases."  J. Mol. Biol. 400, 231-243 (2010).

Assembly members:
ErbB1TM, polymer, 44 residues, Formula weight is not available
ErbB2TM, polymer, 44 residues, Formula weight is not available

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):
ErbB1TM: EGCPTNGPKIPSIATGMVGA LLLLLVVALGIGLFMRRRHI VRKR
ErbB2TM: GCPAEQRASPLTSIISAVVG ILLVVVLGVVFGILIKRRQQ KIRK

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts78
1H chemical shifts661

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EGFR TM segment1
2ErbB2 TM segment2

Entities:

Entity 1, EGFR TM segment 44 residues - Formula weight is not available

1   GLUGLYCYSPROTHRASNGLYPROLYSILE
2   PROSERILEALATHRGLYMETVALGLYALA
3   LEULEULEULEULEUVALVALALALEUGLY
4   ILEGLYLEUPHEMETARGARGARGHISILE
5   VALARGLYSARG

Entity 2, ErbB2 TM segment 44 residues - Formula weight is not available

1   GLYCYSPROALAGLUGLNARGALASERPRO
2   LEUTHRSERILEILESERALAVALVALGLY
3   ILELEULEUVALVALVALLEUGLYVALVAL
4   PHEGLYILELEUILELYSARGARGGLNGLN
5   LYSILEARGLYS

Samples:

sample_1: ErbB1TM, [U-100% 15N], 1 mM; ErbB2TM, [U-100% 15N], 1 mM; DMPC 12 mM; DHPC 48 mM; EDTA 3 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_2: ErbB1TM, [U-100% 13C; U-100% 15N], 1 mM; ErbB2TM 1 mM; DMPC, [U-2H], 12 mM; DHPC, [U-2H], 48 mM; EDTA 3 mM; TCEP 1 mM; D2O 100%

sample_4: ErbB1TM 1 mM; ErbB2TM, [U-100% 13C; U-100% 15N], 1 mM; DMPC, [U-2H], 12 mM; DHPC, [U-2H], 48 mM; EDTA 3 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_5: ErbB1TM, [U-100% 13C; U-100% 15N], 1 mM; ErbB2TM 1 mM; DMPC, [U-2H], 12 mM; DHPC, [U-2H], 48 mM; EDTA 3 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
3D 1H-15N TOCSYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3d-13Cfilt NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18804 25729 15231
PDB
DBJ BAD92679 BAF83041 BAH11869 BAI46646 BAG58195 BAG62073 BAJ17684
EMBL CAA25240 CAA25282 CAA27060
GB AAG35789 AAG43243 AAH94761 AAS83109 AAT52212 AAA75493 AAI56756 AAI67147 AAO18082 AAX40997
PRF 1006266A 1202345A
REF NP_005219 XP_004045514 XP_008967087 XP_519102 NP_001005862 NP_001276865 NP_001276866 NP_004439 XP_001090319
SP P00533 P04626