BMRB Entry 30196

Name: Solution structure of the CaM34 with the iNOS CaM binding domain peptide
Published: 2017-09-25

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PDB ID: 5tp6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30196
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the CaM34 with the iNOS CaM binding domain peptide PubMed: 28121131

Deposition date: 2016-10-19 Original release date: 2017-09-25

Authors: Piazza, M.; Dieckmann, T.; Guillemette, J.

Citation: Piazza, Michael; Taiakina, Valentina; Dieckmann, Thorsten; Guillemette, J Guy. "Structural Consequences of Calmodulin EF Hand Mutations." Biochemistry 56, 944-956 (2017).

Assembly members:
Calmodulin, polymer, 148 residues, 16633.330 Da.
Nitric oxide synthase, inducible, polymer, 29 residues, 3402.371 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFAKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREAAIDGDGQVNYEE FVQMMTAK
Nitric oxide synthase, inducible: AGHMRPKRREIPLKVLVKAV LFACMLMRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	438
15N chemical shifts	161
1H chemical shifts	1010

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 148 residues - 16633.330 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

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, entity_2 29 residues - 3402.371 Da.

1

ALA

GLY

HIS

MET

ARG

PRO

LYS

ARG

GLU

2

ILE

PRO

LEU

LYS

VAL

LEU

VAL

LYS

ALA

VAL

3

LEU

PHE

ALA

CYS

MET

LEU

MET

ARG

LYS

Samples:

sample_1: CaM34, [U-99% 13C; U-99% 15N], 1 mM; Calcium chloride 10 mM; iNOS CaM binding domain peptide 1 mM; potassium chloride 100 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
3D HNCA	sample_1	anisotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-15N double filtered NOESY	sample_1	anisotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMR spectrometers:

Bruker DRX 600 MHz

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