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 34154

Title: NMR spatial structure of HER2 TM domain dimer in DPC micelles   PubMed: 29063258

Deposition date: 2017-06-26 Original release date: 2017-11-17

Authors: Mineev, K.; Arseniev, A.

Citation: Lesovoy, D.; Mineev, K.; Bragin, P.; Bocharova, O.; Bocharov, E.; Arseniev, A.. "NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins."  J. Biomol. NMR 69, 165-179 (2017).

Assembly members:
entity_1, polymer, 44 residues, 4734.805 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GCPAEQRASPLTSIISAVVG ILLVVVLGVVFGILIKRRQQ KIRK

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts47
1H chemical shifts339

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 44 residues - 4734.805 Da.

1   GLYCYSPROALAGLUGLNARGALASERPRO
2   LEUTHRSERILEILESERALAVALVALGLY
3   ILELEULEUVALVALVALLEUGLYVALVAL
4   PHEGLYILELEUILELYSARGARGGLNGLN
5   LYSILEARGLYS

Samples:

sample_1: DPC, [U-99% 2H], 200 mM; HER2TM 2.5 mM; HER2TM_label, [U-100% 13C; U-100% 15N], 2.5 mM; potassium phosphate 20 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 30 mM; pH: 6.0; pressure: 1 Pa; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 13C-filtered NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN, Bruker Biospin - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker av600 600 MHz

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