BMRB Entry 18323

Name: Solution structure of the calcium-bound CaM C-terminal domain in a complex
Published: 2012-05-08

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PDB ID: 2lqp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18323
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the calcium-bound CaM C-terminal domain in a complex

Deposition date:

2012-03-10

Original release date:

2012-05-08

Authors:

Liu, Zhihong

Citation:

Citation: Liu, Zhihong; Vogel, Hans. "Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin." Front. Mol. Neurosci. 5, 38-38 (2012).
PubMed: 22518098

Assembly members:

Assembly members:
entity, polymer, 71 residues, 8155.886 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 Vector: pET30b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: DTDSEEEIREAFRVFDKDGN GYISAAELRHVMTNLGEKLT DEEVDEMIREADIDGDGQVN YEEFVQMMTAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	261
15N chemical shifts	68
1H chemical shifts	250

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calcium-bound CaM C-terminal domain in a complex	1

Entities:

Entity 1, calcium-bound CaM C-terminal domain in a complex 71 residues - 8155.886 Da.

1

ASP

THR

ASP

SER

GLU

ILE

ARG

GLU

2

ALA

PHE

ARG

VAL

PHE

ASP

LYS

ASP

GLY

ASN

3

GLY

TYR

ILE

SER

ALA

GLU

LEU

ARG

HIS

4

VAL

MET

THR

ASN

LEU

GLY

GLU

LYS

LEU

THR

5

ASP

GLU

VAL

ASP

GLU

MET

ILE

ARG

GLU

6

ALA

ASP

ILE

ASP

GLY

ASP

GLY

GLN

VAL

ASN

7

TYR

GLU

PHE

VAL

GLN

MET

THR

ALA

8

LYS

Samples:

sample_1: CaM 1.0 mM; TRIS 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	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 HCACO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 500 MHz

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