BMRB Entry 25810

Name: NMR structure of the N-domain of troponin C bound to the switch region of troponin I and the covalent levosimendan analog i9.
Published: 2016-07-20

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PDB ID: 2n7l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25810
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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:

NMR structure of the N-domain of troponin C bound to the switch region of troponin I and the covalent levosimendan analog i9.

Deposition date:

2015-09-14

Original release date:

2016-07-20

Authors:

Pineda Sanabria, Sandra; Sykes, Brian; Robertson, Ian

Citation:

Citation: Pineda Sanabria, Sandra; Robertson, Ian; Sun, Yin-Biao; Irving, Malcolm; Sykes, Brian. "Troponin C with covalently bound levosimendan analog i9 enhances contraction in cardiac muscle fibers" .

Assembly members:

Assembly members:
entity_1, polymer, 141 residues, 1702.936 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHGGLVPRGSMDDIY KAAVEQLTEEQKNEFKAAFD IFVLGAEDGSISTKELGKVM RMLGQNPTPEELQEMIDEVD EDGSGTVDFDEFLVMMVRXM KDDSENLYFQGRRVRISADA MMQALLGARAKESLDLRAHL K

Data sets:

assigned_chemical_shifts
- cChimera-i9

Data type	Count
13C chemical shifts	352
15N chemical shifts	116
19F chemical shifts	2
1H chemical shifts	675

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	CALCIUM ION	2

Entities:

Entity 1, entity_1 141 residues - 1702.936 Da.

MHHHHHHGGLVPRGSMDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGSISTKELGKVMRMLGQNPTPEELQEMIDEVD EDGSGTVDFDEFLVMMVR(4J4)MKDDSENLYFQGRRVRISADAMMQALLGARAKESLDLRAHLK Residues 1 to 7 are the His tag (Auth_seq_ID -15 to -9). Residues 8 to 15 are the thrombin cleavage site (Auth_seq_ID -8 to -1). Residues 16 to 104 are the N-domain of troponin C residues 1-89 (Auth_seq_ID 1 to 89). Residues 105 to 111 are the TEV cleavage site (Auth_seq_ID 90 to 96). Residues 112 to 141 are residues 144-173 of troponin I (Auth_seq_ID 97 to 126).

1

MET

HIS

GLY

LEU

2

VAL

PRO

ARG

GLY

SER

MET

ASP

ILE

TYR

3

LYS

ALA

VAL

GLU

GLN

LEU

THR

GLU

4

GLN

LYS

ASN

GLU

PHE

LYS

ALA

PHE

ASP

5

ILE

PHE

VAL

LEU

GLY

ALA

GLU

ASP

GLY

SER

6

ILE

SER

THR

LYS

GLU

LEU

GLY

LYS

VAL

MET

7

ARG

MET

LEU

GLY

GLN

ASN

PRO

THR

PRO

GLU

8

GLU

LEU

GLN

GLU

MET

ILE

ASP

GLU

VAL

ASP

9

GLU

ASP

GLY

SER

GLY

THR

VAL

ASP

PHE

ASP

10

GLU

PHE

LEU

VAL

MET

VAL

ARG

4J4

MET

11

LYS

ASP

SER

GLU

ASN

LEU

TYR

PHE

GLN

12

GLY

ARG

VAL

ARG

ILE

SER

ALA

ASP

ALA

13

MET

GLN

ALA

LEU

GLY

ALA

ARG

ALA

14

LYS

GLU

SER

LEU

ASP

LEU

ARG

ALA

HIS

LEU

15

LYS

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1

CA

Samples:

sample_1: entity_1, [U-15N], 0.65 mM; entity_2, [U-15N], 0.65 mM; potassium chloride 100 mM; imidazole 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM

sample_2: entity_1, [U-13C; U-15N], 0.65 mM; entity_2, [U-13C; U-15N], 0.65 mM; potassium chloride 100 mM; imidazole 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM

sample_3: entity_1, [U-13C; U-15N], 0.65 mM; entity_2, [U-13C; U-15N], 0.65 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM

sample_conditions_1: pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
gnoesyChsqc_CNfilt	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY CN filtered	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-19F HMQC	sample_3	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

TALOS, Cornilescu, Delaglio and Bax - Prediction of phi and psi dihedral angles

X-PLOR_NIH v2.35, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

PRODRG, A. W. Sch ttelkopf and D. M. F. van Aalten - Generation of topology and parameter files for non-standard aminoacid Ci9

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

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