BMRB Entry 27782

Name: 1HN, 13C, and 15N Resonance Assignments of human Calmodulin bound to CaMBP2 peptide
Published: 2019-04-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27782

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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:

1HN, 13C, and 15N Resonance Assignments of human Calmodulin bound to CaMBP2 peptide

Deposition date:

2019-02-12

Original release date:

2019-04-12

Authors:

Varney, Kristen; Wilder, Paul; Raquel, Godoy-Ruiz; Mancia, Filippo; Weber, David

Citation:

Citation: Varney, Kristen; Wilder, Paul; Godoy-Ruiz, Raquel; Mancia, Filippo; Weber, David. "1HN, 13C, and 15N resonance assignments of human calmodulin bound to a peptide derived from the STRA6 vitamin A transporter (CaMBP2)" Biomol. NMR Assignments 13, 275-278 (2019).
PubMed: 30875027

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, Formula weight is not available
CaMBP2, polymer, 27 residues, Formula weight is not available

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: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
CaMBP2: VSNAKRARAHWQLLYTLVNN PSLVGSR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	131
1H chemical shifts	130

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin	1
2	CaMBP2	2

Entities:

Entity 1, Calmodulin 148 residues - Formula weight is not available

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, CaMBP2 27 residues - Formula weight is not available

1

VAL

SER

ASN

ALA

LYS

ARG

ALA

ARG

ALA

HIS

2

TRP

GLN

LEU

TYR

THR

LEU

VAL

ASN

3

PRO

SER

LEU

VAL

GLY

SER

ARG

Samples:

sample_1: Calmodulin, [U-13C; U-15N], 0.25 mM; CaMBP2 0.25 mM; sodium chloride 50 mM; calcium chloride 10 mM; magnesium chloride 5 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 80 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

NMR spectrometers:

Bruker Avance III 950 MHz

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