BMRB Entry 18302

Name: Solution structure of the calcium-bound CaM N-terminal domain in a complex.
Published: 2012-06-04

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PDB ID: 2lqc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18302
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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 N-terminal domain in a complex.

Deposition date:

2012-02-29

Original release date:

2012-06-04

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:
CaM N-terminal domain, polymer, 77 residues, 8583.593 Da.
NSCaTE peptide, polymer, 24 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 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):
CaM N-terminal domain: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMK
NSCaTE peptide: GTGAALSWQAAIDAARQAKL MGSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	364
15N chemical shifts	95
1H chemical shifts	447

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CaM N-terminal domain	1
2	NSCaTE peptide	2
3	Calcium ion, 1	3
4	Calcium ion, 2	3

Entities:

Entity 1, CaM N-terminal domain 77 residues - 8583.593 Da.

1

ALA

ASP

GLN

LEU

THR

GLU

GLN

ILE

ALA

2

GLU

PHE

LYS

GLU

ALA

PHE

SER

LEU

PHE

ASP

3

LYS

ASP

GLY

ASP

GLY

THR

ILE

THR

LYS

4

GLU

LEU

GLY

THR

VAL

MET

ARG

SER

LEU

GLY

5

GLN

ASN

PRO

THR

GLU

ALA

GLU

LEU

GLN

ASP

6

MET

ILE

ASN

GLU

VAL

ASP

ALA

ASP

GLY

ASN

7

GLY

THR

ILE

ASP

PHE

PRO

GLU

PHE

LEU

THR

8

MET

ALA

ARG

LYS

MET

LYS

Entity 2, NSCaTE peptide 24 residues - Formula weight is not available

1

GLY

THR

GLY

ALA

LEU

SER

TRP

GLN

ALA

2

ALA

ILE

ASP

ALA

ARG

GLN

ALA

LYS

LEU

3

MET

GLY

SER

ALA

Entity 3, Calcium ion, 1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: calmodulin, [U-100% 13C; U-100% 15N], 1 mM; NSCaTE peptide 2 mM; H2O 55 M; D2O, [U-99% 2H], 5 M; DTT 10 mM; TRIS 20 mM

sample_2: NSCaTE peptide, [U-100% 13C; U-100% 15N], 1 mM; calmodulin 0.5 mM; H2O 55 M; D2O, [U-99% 2H], 5 M; DTT 10 mM; TRIS 20 mM

sample_3: calmodulin, [U-100% 13C; U-100% 15N], 1 mM; NSCaTE peptide 2 mM; Pf1 phage 7.5 mg

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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	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
2D 1H-15N HSQC	sample_3	anisotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 500 MHz

BMRB	18082 4174
PDB	1AK8 1F70 1J7O 1SW8 2KUG 2LLO 2LQC 2PQ3 3B32 3IFK 3UCT 3UCW 3UCY 4Q57 2LQC
EMBL	CAA29381 CAB65357 CCD82979 CUA69889 CAA12174 CAA33546 CAA39289 CAA43196 CAA84340
GB	AAH53790 ABW89042 ABW89043 ABW89044 ABW89045 AAA02501 AAA17030 AAA42016 AAA51899 AAA51900
REF	XP_001869424 XP_001995129 XP_002772218 XP_006032607 XP_006137175 NP_000710 NP_001123299 NP_001123301 NP_001123302 NP_001123303
DBJ	BAF03165
PRF	1512308A
SP	P15381 Q01815 Q13936
TPG	DAA29184
AlphaFold	P15381 Q01815 Q13936