BMRB Entry 30471

Name: Human Titin ZIg10
Published: 2019-08-16

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PDB ID: 6dl4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30471
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:

Human Titin ZIg10

Deposition date:

2018-05-31

Original release date:

2019-08-16

Authors:

Wright, N.

Citation:

Citation: Letourneau, A.; Wright, N.. "Structural Insights on the Obscurin-Binding Domains in Titin" Protein Pept. Lett. 25, 973-979 (2018).
PubMed: 30289063

Assembly members:

Assembly members:
Titin, polymer, 119 residues, 13965.898 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapienss

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Titin: RMAHEGALTGVTTDQKEKQK PDIVLYPEPVRVLEGETARF RCRVTGYPQPKVNWYLNGQL IRKSKRFRVRYDGIHYLDIV DCKSYDTGEVKVTAENPEGV IEHKVKLEIQQLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	94
1H chemical shifts	623

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 119 residues - 13965.898 Da.

1

ARG

MET

ALA

HIS

GLU

GLY

ALA

LEU

THR

GLY

2

VAL

THR

ASP

GLN

LYS

GLU

LYS

GLN

LYS

3

PRO

ASP

ILE

VAL

LEU

TYR

PRO

GLU

PRO

VAL

4

ARG

VAL

LEU

GLU

GLY

GLU

THR

ALA

ARG

PHE

5

ARG

CYS

ARG

VAL

THR

GLY

TYR

PRO

GLN

PRO

6

LYS

VAL

ASN

TRP

TYR

LEU

ASN

GLY

GLN

LEU

7

ILE

ARG

LYS

SER

LYS

ARG

PHE

ARG

VAL

ARG

8

TYR

ASP

GLY

ILE

HIS

TYR

LEU

ASP

ILE

VAL

9

ASP

CYS

LYS

SER

TYR

ASP

THR

GLY

GLU

VAL

10

LYS

VAL

THR

ALA

GLU

ASN

PRO

GLU

GLY

VAL

11

ILE

GLU

HIS

LYS

VAL

LYS

LEU

GLU

ILE

GLN

12

GLN

LEU

GLU

HIS

Samples:

sample_1: TRIS 20 mM; sodium chloride 50 mM; Human Titin ZIg10, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz

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