BMRB Entry 26687

Name: Chemical shifts of calcium saturated CaM34 (CaM D93A, D129A) with the iNOS CaM-binding domain peptide
Published: 2016-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26687

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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:

Chemical shifts of calcium saturated CaM34 (CaM D93A, D129A) with the iNOS CaM-binding domain peptide

Deposition date:

2015-10-07

Original release date:

2016-02-12

Authors:

Piazza, Michael; Dieckmann, Thorsten

Citation:

Citation: Piazza, Michael; Guillemette, Guy; Dieckmann, Thorsten. "Chemical shift assignments of calmodulin constructs with EF hand mutations" Biomol. NMR Assign. 10, 193-198 (2016).
PubMed: 26743203

Assembly members:

Assembly members:
CaM34, polymer, 148 residues, Formula weight is not available
iNOS, polymer, 17 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CaM34: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFAKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREAAIDGDGQVNYEE FVQMMTAK
iNOS: LKVLVKAVLFACMLMRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	419
15N chemical shifts	144
1H chemical shifts	882

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CaM34	1
2	iNOS	2

Entities:

Entity 1, CaM34 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

ALA

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

ILE

14

ASP

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

15

PHE

VAL

GLN

MET

THR

ALA

LYS

Entity 2, iNOS 17 residues - Formula weight is not available

1

LEU

LYS

VAL

LEU

VAL

LYS

ALA

VAL

LEU

PHE

2

ALA

CYS

MET

LEU

MET

ARG

LYS

Samples:

sample_1: CaM34, [U-99% 13C; U-99% 15N], 1 mM; potassium chloride 100 mM; iNOS 1 mM; sodium azide 0.2 mM; calcium chloride 1 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.5; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz

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