BMRB Entry 36731

Name: NMR Structure of Mouse Keratin 17 Tail Domain (G390 - R433) in solution
Published: 2025-12-12

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PDB ID: 9m1y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36731
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of Mouse Keratin 17 Tail Domain (G390 - R433) in solution

Deposition date:

2025-02-26

Original release date:

2025-12-12

Authors:

Yeom, J.; Lee, C.; Kim, J.

Citation:

Citation: Yeom, J.; Lee, C.; Kim, J.. "NMR Structure of Mouse Keratin 17 Tail Domain (G390 - R433) in solution" .

Assembly members:

Assembly members:
Keratin, type I cytoskeletal 17, polymer, 47 residues, 5329.866 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10088 Superkingdom: not available Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Keratin, type I cytoskeletal 17: GSTGEDAHLTQYKPKEPVTT RQVRTIVEEVQDGKVISSRE QVHQTTR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	150
15N chemical shifts	42
1H chemical shifts	380

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 47 residues - 5329.866 Da.

1

GLY

SER

THR

GLY

GLU

ASP

ALA

HIS

LEU

THR

2

GLN

TYR

LYS

PRO

LYS

GLU

PRO

VAL

THR

3

ARG

GLN

VAL

ARG

THR

ILE

VAL

GLU

VAL

4

GLN

ASP

GLY

LYS

VAL

ILE

SER

ARG

GLU

5

GLN

VAL

HIS

GLN

THR

ARG

Samples:

sample_1: Keratin 17 (G390-R433), [U-13C; U-15N], 0.34 mg/mL; sodium phosphate 50 mM; D2O, [U-2H], 7%; H2O 93%

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

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

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - chemical shift assignment

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - peak picking

NMR spectrometers:

Bruker AVANCE III HD 850 MHz

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