BMRB Entry 25511

Name: Structure and dynamics of the acidosis-resistant a162H mutant of the switch region of troponin I bound to the regulatory domain of troponin C
Published: 2016-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25511

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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:

Structure and dynamics of the acidosis-resistant a162H mutant of the switch region of troponin I bound to the regulatory domain of troponin C

Deposition date:

2015-03-03

Original release date:

2016-06-30

Authors:

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

Citation:

Citation: Pineda Sanabria, Sandra; Robertson, Ian; Sykes, Brian. "Structure and Dynamics of the Acidosis-Resistant A162H Mutant of the Switch Region of Troponin I Bound to the Regulatory Domain of Troponin C" Biochemistry 54, 3583-3593 (2015).
PubMed: 25996354

Assembly members:

Assembly members:
cChimeraX-A162H, polymer, 141 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cChimeraX-A162H: MHHHHHHGGLVPRGSMDDIY KAAVEQLTEEQKNEFKAAFD IFVLGAEDGSISTKELGKVM RMLGQNPTPEELQEMIDEVD EDGSGTVDFDEFLVMMVRCM KDDSENLYFQGRRVRISADA MMQALLGARHKESLDLRAHL K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
- heteronuclear_T1_list_2
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
- heteronuclear_T2_list_2

Data type	Count
15N chemical shifts	91
1H chemical shifts	91
T1 relaxation values	176
T2 relaxation values	168

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cChimeraX-A162H	1
2	CALCIUM ION	2

Entities:

Entity 1, cChimeraX-A162H 141 residues - Formula weight is not available

Residues -15 to -7 correspond to the His tag. Residues -6 to -1 correspond to the thrombin cleavage site. Residues 1 to 89 correspond to residues 1 to 89 of cNTnC. Residues 90 to 96 correspond to the thrombin cleavage site. Residues 144 to 173 correspond to 144 to 173 of cTnI.

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

CYS

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

HIS

14

LYS

GLU

SER

LEU

ASP

LEU

ARG

ALA

HIS

LEU

15

LYS

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1

CA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2

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

BMRB Entry 25511

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: