BMRB Entry 25880

Name: Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus
Published: 2016-01-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25880

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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:

Backbone assignment of N-terminal fragment of F2-TnC from Lethocerus

Deposition date:

2015-11-05

Original release date:

2016-01-29

Authors:

Sanfelice, Domenico; Pastore, Annalisa; Bullard, Belinda; Adrover, Miguel

Citation:

Citation: Sanfelice, Domenico; Pastore, Annalisa; Bullard, Belinda; Adrover, Miguel. "Towards Understanding the Molecular Bases of Stretch Activation: A Structural comparison of the Two Troponin C Isoforms of Lethocerus" J. Biol. Chem. 291, 16090-16099 (2016).
PubMed: 27226601

Assembly members:

Assembly members:
Apo_N-term, polymer, 88 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Lethocerus Indicus Taxonomy ID: 212017 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lethocerus Indicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Apo_N-term: MVAMDDLDKDQIALLKRAFE AFAQEKSYIEANMVGTILQM LGHEVSDKQLTEIIVEVDAD GSGQLEFEEFVTLAARFLTE DNEEDSAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	252
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminus F2 TnC	1

Entities:

Entity 1, N-terminus F2 TnC 88 residues - Formula weight is not available

1

MET

VAL

ALA

MET

ASP

LEU

ASP

LYS

ASP

2

GLN

ILE

ALA

LEU

LYS

ARG

ALA

PHE

GLU

3

ALA

PHE

ALA

GLN

GLU

LYS

SER

TYR

ILE

GLU

4

ALA

ASN

MET

VAL

GLY

THR

ILE

LEU

GLN

MET

5

LEU

GLY

HIS

GLU

VAL

SER

ASP

LYS

GLN

LEU

6

THR

GLU

ILE

VAL

GLU

VAL

ASP

ALA

ASP

7

GLY

SER

GLY

GLN

LEU

GLU

PHE

GLU

PHE

8

VAL

THR

LEU

ALA

ARG

PHE

LEU

THR

GLU

9

ASP

ASN

GLU

ASP

SER

ALA

Samples:

sample_1: Apo N-term, [U-98% 13C; U-98% 15N], 0.5 – 1.0 mM; TRIS, [U-2H], 20 mM; KCl 100 mM; DTT, [U-2H], 2 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker Avance 800 MHz

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