BMRB Entry 25796

Name: NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin
Published: 2016-11-28

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PDB ID: 2n77
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR25796
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin

Deposition date:

2015-09-04

Original release date:

2016-11-28

Authors:

Wang, Xu; Putkey, John

Citation:

Citation: Wang, Xu; Putkey, John. "PEP-19 Modulates Calcium Binding to Calmodulin by Electrostatic Steering" Nat. Commun. 7, 13583-13583 (2016).
PubMed: 27876793

Assembly members:

Assembly members:
C-CaM, polymer, 73 residues, 8416.260 Da.
PEP-19, polymer, 62 residues, 6775.41 Da.

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: pET23d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C-CaM: MKDTDSEEEIREAFRVFDKD GNGYISAAELRHVMTNLGEK LTDEEVDEMIREADIDGDGQ VNYEEFVQMMTAK
PEP-19: MAERQGAGATNGKDKTSGEN DGQKKVQEEFDIDMDAPETE RAAVAIQSQFRKFQKKKAGS QS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- Assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	430
15N chemical shifts	112
1H chemical shifts	716

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 73 residues - 8416.260 Da.

Isolated C-domain of calmodulin from residue M76 to K148

1

MET

LYS

ASP

THR

ASP

SER

GLU

ILE

2

ARG

GLU

ALA

PHE

ARG

VAL

PHE

ASP

LYS

ASP

3

GLY

ASN

GLY

TYR

ILE

SER

ALA

GLU

LEU

4

ARG

HIS

VAL

MET

THR

ASN

LEU

GLY

GLU

LYS

5

LEU

THR

ASP

GLU

VAL

ASP

GLU

MET

ILE

6

ARG

GLU

ALA

ASP

ILE

ASP

GLY

ASP

GLY

GLN

7

VAL

ASN

TYR

GLU

PHE

VAL

GLN

MET

8

THR

ALA

LYS

Entity 2, entity_2 62 residues - 6775.41 Da.

1

MET

ALA

GLU

ARG

GLN

GLY

ALA

GLY

ALA

THR

2

ASN

GLY

LYS

ASP

LYS

THR

SER

GLY

GLU

ASN

3

ASP

GLY

GLN

LYS

VAL

GLN

GLU

PHE

4

ASP

ILE

ASP

MET

ASP

ALA

PRO

GLU

THR

GLU

5

ARG

ALA

VAL

ALA

ILE

GLN

SER

GLN

PHE

6

ARG

LYS

PHE

GLN

LYS

ALA

GLY

SER

7

GLN

SER

Samples:

sample_1: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%

sample_2: PEP_19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; H2O 95%; D2O 5%

sample_3: C-CaM, [U-100% 13C; U-100% 15N], 0.8 mM; PEP_19 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%

sample_4: PEP-19, [U-100% 13C; U-100% 15N], 0.8 mM; C-CaM 1.0 mM; potassium chloride 100 mM; EDTA, [U-2H], 5 mM; DSS, [U-2H], 10 uM; imidazole, [U-2H], 10 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.3; 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 HN(CO)CA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D F1--filtered, F3-edited NOESY-HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
3D HCCH-COSY	sample_4	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_4	isotropic	sample_conditions_1
D F1--filtered, F3-edited NOESY-HSQC	sample_4	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Felix_2007, Accelrys Software Inc. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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