BMRB Entry 30156

Name: Solution NMR-derived structure of calmodulin bound with ER alpha peptides
Published: 2017-02-09

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PDB ID: 5t0x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30156
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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:

Solution NMR-derived structure of calmodulin bound with ER alpha peptides

Deposition date:

2016-08-16

Original release date:

2017-02-09

Authors:

Zhang, Y.; Ames, J.

Citation:

Citation: Zhang, Y.; Ames, J.. "Solution NMR-derived structure of calmodulin bound with ER alpha peptides" .

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, 16721.350 Da.
Estrogen receptor peptide, polymer, 19 residues, 2202.645 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
Estrogen receptor peptide: RAANLWPSPLMIKRSKKNS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	437
15N chemical shifts	145
1H chemical shifts	600

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2, 1	2
3	entity_2, 2	2
4	CALCIUM ION, 1	3
5	CALCIUM ION, 2	3
6	CALCIUM ION, 3	3
7	CALCIUM ION, 4	3

Entities:

Entity 1, entity_1 148 residues - 16721.350 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

ASP

THR

ASP

9

SER

GLU

ILE

ARG

GLU

ALA

PHE

ARG

10

VAL

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

ILE

11

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

THR

12

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

13

VAL

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

ILE

14

ASP

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

15

PHE

VAL

GLN

MET

THR

ALA

LYS

Entity 2, entity_2, 1 19 residues - 2202.645 Da.

1

ARG

ALA

ASN

LEU

TRP

PRO

SER

PRO

LEU

2

MET

ILE

LYS

ARG

SER

LYS

ASN

SER

Entity 3, CALCIUM ION, 1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: 13C/15N-CaM/ERalpha, [U-99% 13C; U-99% 15N], 0.6 mM; 15N-labeled CaM/ERalpha, [U-99% 15N], 1 mM; H2O 90%; D2O 10%; Tris-d11 20 mM; CaCl2 5 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; 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 HNCO	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

HADDOCK, Bonvin - structure calculation

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker 1 800 MHz
Bruker 1 600 MHz

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