BMRB Entry 34981

Name: Solution NMR study of the titin I-band IgI domain I82 reveals conformational dynamics
Published: 2025-11-10

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PDB ID: 9ibk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34981
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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:

Solution NMR study of the titin I-band IgI domain I82 reveals conformational dynamics

Deposition date:

2025-02-12

Original release date:

2025-11-10

Authors:

Pfuhl, M.; Gage, M.

Citation:

Citation: Kelly, C.; Abukar, S.; Gage, M.; Pfuhl, M.. "Solution NMR study of the titin I-band IgI domain I82 reveals conformational dynamics" .

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, 11715.221 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21 Vector: pET-151dTOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GIDPFTIEPAWERHLQDVTL KEGQTCTMTCQFSVPNVKSE WFRNGRVLKPQGRVKTEVEH KVHKLTIADVRAEDQGQYTC KHEDLETSAELRIEKGELRS GC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	111
1H chemical shifts	717

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 102 residues - 11715.221 Da.

1

GLY

ILE

ASP

PRO

PHE

THR

ILE

GLU

PRO

ALA

2

TRP

GLU

ARG

HIS

LEU

GLN

ASP

VAL

THR

LEU

3

LYS

GLU

GLY

GLN

THR

CYS

THR

MET

THR

CYS

4

GLN

PHE

SER

VAL

PRO

ASN

VAL

LYS

SER

GLU

5

TRP

PHE

ARG

ASN

GLY

ARG

VAL

LEU

LYS

PRO

6

GLN

GLY

ARG

VAL

LYS

THR

GLU

VAL

GLU

HIS

7

LYS

VAL

HIS

LYS

LEU

THR

ILE

ALA

ASP

VAL

8

ARG

ALA

GLU

ASP

GLN

GLY

GLN

TYR

THR

CYS

9

LYS

HIS

GLU

ASP

LEU

GLU

THR

SER

ALA

GLU

10

LEU

ARG

ILE

GLU

LYS

GLY

GLU

LEU

ARG

SER

11

GLY

CYS

Samples:

sample_1: Titin, [U-95% 15N], 0.5 ± 0.05 mM; sodium chloride 50.0 ± 1.0 mM; HEPES 20.0 ± 0.5 mM; DTT 2.0 ± 0.1 mM; sodium azide 0.02 ± 0.001 % w/v

sample_2: Titin, [U-95% 13C; U-95% 15N], 0.5 ± 0.05 mM; sodium chloride 50.0 ± 1.0 mM; HEPES 20.0 ± 0.5 mM; DTT 2.0 ± 0.1 mM; sodium azide 0.02 ± 0.001 % w/v

sample_conditions_1: ionic strength: 50.0 mM; pH: 7.0; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C TROSY aromatic	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 HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(COC)C(H)	sample_2	isotropic	sample_conditions_1
3D HN(COCC)H	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v4.3.0, Bruker Biospin - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment

CcpNmr Analysis Assign v3.2.12, CCPN - chemical shift assignment

ARIA, Nilges and Bardiaux - structure calculation

NMR spectrometers:

Bruker AVANCE III HD 950 MHz
Bruker AVANCE NEO 800 MHz
Bruker AVANCE III 700 MHz

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