BMRB Entry 30966

Name: cTnC-TnI chimera complexed with A2
Published: 2022-03-30

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PDB ID: 7swi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30966
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:

cTnC-TnI chimera complexed with A2

Deposition date:

2021-11-19

Original release date:

2022-03-30

Authors:

Poppe, L.; Hartman, J.; Romero, A.; Reagan, J.

Citation:

Citation: Poppe, L.; Hartman, J.; Romero, A.; Reagan, J.. "Structural and Thermodynamic Model for the Activation of Cardiac Troponin" Biochemistry 61, 741-748 (2022).
PubMed: 35349258

Assembly members:

Assembly members:
entity_1, polymer, 129 residues, 14222.121 Da.
entity_C9W, non-polymer, 462.495 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDDIYKAAVEQLTEEQKNEF KAAFDIFVLGAEDGCISTKE LGKVMRMLGQNPTPEELQEM IDEVDEDGSGTVDFDEFLVM MVRCMKDDSKGAGAGVRISA DAMMQALLGARAKESLDLRA HLKQVKKED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	555
15N chemical shifts	132
1H chemical shifts	912

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

Entities:

Entity 1, unit_1 129 residues - 14222.121 Da.

1

GLY

ASP

ILE

TYR

LYS

ALA

VAL

GLU

2

GLN

LEU

THR

GLU

GLN

LYS

ASN

GLU

PHE

3

LYS

ALA

PHE

ASP

ILE

PHE

VAL

LEU

GLY

4

ALA

GLU

ASP

GLY

CYS

ILE

SER

THR

LYS

GLU

5

LEU

GLY

LYS

VAL

MET

ARG

MET

LEU

GLY

GLN

6

ASN

PRO

THR

PRO

GLU

LEU

GLN

GLU

MET

7

ILE

ASP

GLU

VAL

ASP

GLU

ASP

GLY

SER

GLY

8

THR

VAL

ASP

PHE

ASP

GLU

PHE

LEU

VAL

MET

9

MET

VAL

ARG

CYS

MET

LYS

ASP

SER

LYS

10

GLY

ALA

GLY

ALA

GLY

VAL

ARG

ILE

SER

ALA

11

ASP

ALA

MET

GLN

ALA

LEU

GLY

ALA

12

ARG

ALA

LYS

GLU

SER

LEU

ASP

LEU

ARG

ALA

13

HIS

LEU

LYS

GLN

VAL

LYS

GLU

ASP

Entity 2, unit_2 - C21 H23 F N4 O5 S - 462.495 Da.

1

C9W

Samples:

sample_1: cTnC-TnI chimera, [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
X-filtered NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v3.0, Bruker Biospin - processing

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY v1.5.5, Bartels et al. - peak picking

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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