BMRB Entry 34154

Name: NMR spatial structure of HER2 TM domain dimer in DPC micelles
Published: 2017-11-17

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PDB ID: 5ob4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34154
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR spatial structure of HER2 TM domain dimer in DPC micelles

Deposition date:

2017-06-26

Original release date:

2017-11-17

Authors:

Mineev, K.; Arseniev, A.

Citation:

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).
PubMed: 29063258

Assembly members:

Assembly members:
entity_1, polymer, 44 residues, 4734.805 Da.

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: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GCPAEQRASPLTSIISAVVG ILLVVVLGVVFGILIKRRQQ KIRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	202
15N chemical shifts	47
1H chemical shifts	339

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

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

1

GLY

CYS

PRO

ALA

GLU

GLN

ARG

ALA

SER

PRO

2

LEU

THR

SER

ILE

SER

ALA

VAL

GLY

3

ILE

LEU

VAL

LEU

GLY

VAL

4

PHE

GLY

ILE

LEU

ILE

LYS

ARG

GLN

5

LYS

ILE

ARG

LYS

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:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-filtered NOESY	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks