BMRB Entry 50015

Name: Assignment of Titin domain I83
Published: 2021-04-11

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PDB ID: 6yj0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50015
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:

Assignment of Titin domain I83

Deposition date:

2019-09-12

Original release date:

2021-04-11

Authors:

Pfuhl, Mark

Citation:

Citation: Kelly, Colleen; Pace, Nicola; Gage, Matthew; Pfuhl, Mark. "Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions" J. Mol. Biol. 433, 166977-166977 (2021).
PubMed: 33811919

Assembly members:

Assembly members:
Titin, polymer, 106 residues, 11900 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 Vector: pET151/D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Titin: GIDPFTAEPIQFTKRIQNIV VSEHQSATFECEVSFDDAIV TWYKGPTELTESQKYNFRND GRCHYMTIHNVTPDDEGVYS VIARLEPRGEARSTAELKGE LRSGC*

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	452
15N chemical shifts	107
1H chemical shifts	711

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	I83	1

Entities:

Entity 1, I83 106 residues - 11900 Da.

1

GLY

ILE

ASP

PRO

PHE

THR

ALA

GLU

PRO

ILE

2

GLN

PHE

THR

LYS

ARG

ILE

GLN

ASN

ILE

VAL

3

VAL

SER

GLU

HIS

GLN

SER

ALA

THR

PHE

GLU

4

CYS

GLU

VAL

SER

PHE

ASP

ALA

ILE

VAL

5

THR

TRP

TYR

LYS

GLY

PRO

THR

GLU

LEU

THR

6

GLU

SER

GLN

LYS

TYR

ASN

PHE

ARG

ASN

ASP

7

GLY

ARG

CYS

HIS

TYR

MET

THR

ILE

HIS

ASN

8

VAL

THR

PRO

ASP

GLU

GLY

VAL

TYR

SER

9

VAL

ILE

ALA

ARG

LEU

GLU

PRO

ARG

GLY

GLU

10

ALA

ARG

SER

THR

ALA

GLU

LEU

LYS

GLY

GLU

11

LEU

ARG

SER

GLY

CYS

X

Samples:

sample_1: I83, [U-98% 15N], 0.6 mM

sample_2: I83, [U-95% 13C; U-95% 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.20; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.6, Bruker Biospin - collection, processing

CcpNMR v2.4, CCPN - data analysis, peak picking

NMR spectrometers:

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