BMRB Entry 18084

Name: SOLUTION NMR-DERIVED STRUCTURE OF CALMODULIN C-LOBE BOUND WITH ER ALPHA PEPTIDE
Published: 2012-01-30

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PDB ID: 2llq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18084
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SOLUTION NMR-DERIVED STRUCTURE OF CALMODULIN C-LOBE BOUND WITH ER ALPHA PEPTIDE

Deposition date:

2011-11-15

Original release date:

2012-01-30

Authors:

Zhang, Yonghong

Citation:

Citation: Zhang, Yonghong; Li, Zhigang; Sacks, David; Ames, James. "Structural basis for Ca2+-induced activation and dimerization of estrogen receptor by calmodulin." J. Biol. Chem. 287, 9336-9344 (2012).
PubMed: 22275375

Assembly members:

Assembly members:
Calmodulin C-Lobe, polymer, 67 residues, 7737.527 Da.
ER alpha peptide, polymer, 19 residues, 2202.663 Da.
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin C-Lobe: EEEIREAFRVFDKDGNGYIS AAELRHVMTNLGEKLTDEEV DEMIREADIDGDGQVNYEEF VQMMTAK
ER alpha peptide: RAANLWPSPLMIKRSKKNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	129
15N chemical shifts	67
1H chemical shifts	254

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin C-Lobe	1
2	ER alpha peptide	2
3	CA2_1	3
4	CA2_2	3

Entities:

Entity 1, Calmodulin C-Lobe 67 residues - 7737.527 Da.

1

GLU

ILE

ARG

GLU

ALA

PHE

ARG

VAL

2

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

ILE

SER

3

ALA

GLU

LEU

ARG

HIS

VAL

MET

THR

ASN

4

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

VAL

5

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

ILE

ASP

6

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

PHE

7

VAL

GLN

MET

THR

ALA

LYS

Entity 2, ER alpha peptide 19 residues - 2202.663 Da.

1

ARG

ALA

ASN

LEU

TRP

PRO

SER

PRO

LEU

2

MET

ILE

LYS

ARG

SER

LYS

ASN

SER

Entity 3, CA2_1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: Cal_C, [U-100% 13C; U-100% 15N], 1 mM; H2O 93%; D2O 7%; Tris-d11 20 mM; sodium chloride 50 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	11440 16994 17881 17981 17982 17983 18323 19376 25344
PDB	1CMF 1CMG 1F71 1FW4 1J7P 1YRT 1YRU 1ZOT 2COL 2K3S 2KUH 2KZ2 2LLQ 2LQP 2RRT 4BYA 4RJD
DBJ	BAC39089 BAF45809 BAI66109 BAI66110 BAI66111
EMBL	CAB51566
GB	AAB25484 AAH10730 AAO17827 AAQ14324 AAX61134
REF	XP_001687795 XP_001869425 XP_007442524 XP_009577260 XP_010190430
AlphaFold	Q9UIS7