BMRB Entry 30801

Name: NMR solution structures of tirasemtiv drug bound to a fast skeletal troponin C-troponin I complex
Published: 2021-03-19

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PDB ID: 7kaa
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30801
MolProbity Validation Chart

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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 solution structures of tirasemtiv drug bound to a fast skeletal troponin C-troponin I complex

Deposition date:

2020-09-30

Original release date:

2021-03-19

Authors:

Mercier, P.; Li, M.; Hartman, J.; Sykes, B.

Citation:

Citation: Li, M.; Mercier, P.; Hartman, J.; Sykes, B.. "Structural Basis of Tirasemtiv Activation of Fast Skeletal Muscle" J. Med. Chem. 64, 3026-3034 (2021).
PubMed: 33703886

Assembly members:

Assembly members:
entity_1, polymer, 152 residues, 17096.639 Da.
entity_CA, non-polymer, 40.078 Da.
entity_W97, non-polymer, 230.266 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASMTDQQAEARSYLSEEMI AEFKAAFDMFDADGGGDISV KELGTVMRMLGQTPTKEELD AIIEEVDEDGSGTIDFEEFL VMMVRQMKEDAGGAGGKLFD LRGKFKRPPLRRVRMSADAM LKALLGSKHKVCMDLRANLK QVKKEDHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	440
15N chemical shifts	145
1H chemical shifts	887

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2
3	unit_3	3

Entities:

Entity 1, unit_1 152 residues - 17096.639 Da.

1

MET

ALA

SER

MET

THR

ASP

GLN

ALA

GLU

2

ALA

ARG

SER

TYR

LEU

SER

GLU

MET

ILE

3

ALA

GLU

PHE

LYS

ALA

PHE

ASP

MET

PHE

4

ASP

ALA

ASP

GLY

ASP

ILE

SER

VAL

5

LYS

GLU

LEU

GLY

THR

VAL

MET

ARG

MET

LEU

6

GLY

GLN

THR

PRO

THR

LYS

GLU

LEU

ASP

7

ALA

ILE

GLU

VAL

ASP

GLU

ASP

GLY

8

SER

GLY

THR

ILE

ASP

PHE

GLU

PHE

LEU

9

VAL

MET

VAL

ARG

GLN

MET

LYS

GLU

ASP

10

ALA

GLY

ALA

GLY

LYS

LEU

PHE

ASP

11

LEU

ARG

GLY

LYS

PHE

LYS

ARG

PRO

LEU

12

ARG

VAL

ARG

MET

SER

ALA

ASP

ALA

MET

13

LEU

LYS

ALA

LEU

GLY

SER

LYS

HIS

LYS

14

VAL

CYS

MET

ASP

LEU

ARG

ALA

ASN

LEU

LYS

15

GLN

VAL

LYS

GLU

ASP

HIS

16

HIS

Entity 2, unit_2 - Ca - 40.078 Da.

1

CA

Entity 3, unit_3 - C12 H14 N4 O - 230.266 Da.

1

W97

Samples:

sample_1: TroponinC-Troponin I chimera, [U-13C; U-15N], 0.5 mM; Imidazole 10 mM; KCl 100 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC NH2 only	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY CNfiltered	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC CNfiltered	sample_1	isotropic	sample_conditions_1

Software:

VnmrJ v3.2, Varian - collection

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

NMRViewJ, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

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