BMRB Entry 11075

Name: 1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain of kp60
Published: 2010-04-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11075

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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:

1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain of kp60

Deposition date:

2009-08-05

Original release date:

2010-04-07

Authors:

Iwaya, Naoko; Kuwahara, Yohta; Tenno, Takeshi; Tochio, Hidehito; Shirakawa, Masahiro; Hiroaki, Hidekazu

Citation:

Citation: Iwaya, Naoko; Kuwahara, Yohta; Fujiwara, Yoshie; Goda, Natsuko; Tenno, Takeshi; Akiyama, Kohei; Mase, Shogo; Tochio, Hidehito; Ikegami, Takahisa; Shirakawa, Masahiro; Hiroaki, Hidekazu. "A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization." J. Biol. Chem. 285, 16822-16829 (2010).
PubMed: 20339000

Assembly members:

Assembly members:
N-terminal domain of kp60, polymer, 78 residues, Formula weight is not available

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 Vector: pGEX-4T3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain of kp60: GSDHMTMSLQMIVENVKLAR EYALLGNYDSAMVYYQGVLD QMNKYLYSVKDTHLRQKWQQ VWQEINVEAKQVKDIMKT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	85
1H chemical shifts	574

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain of kp60	1

Entities:

Entity 1, N-terminal domain of kp60 78 residues - Formula weight is not available

1

GLY

SER

ASP

HIS

MET

THR

MET

SER

LEU

GLN

2

MET

ILE

VAL

GLU

ASN

VAL

LYS

LEU

ALA

ARG

3

GLU

TYR

ALA

LEU

GLY

ASN

TYR

ASP

SER

4

ALA

MET

VAL

TYR

GLN

GLY

VAL

LEU

ASP

5

GLN

MET

ASN

LYS

TYR

LEU

TYR

SER

VAL

LYS

6

ASP

THR

HIS

LEU

ARG

GLN

LYS

TRP

GLN

7

VAL

TRP

GLN

GLU

ILE

ASN

VAL

GLU

ALA

LYS

8

GLN

VAL

LYS

ASP

ILE

MET

LYS

THR

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

PDB	2RPA
GB	AAD42087 AAH09136 EDL03542
REF	NP_035965
SP	Q9WV86
AlphaFold	Q9WV86

BMRB Entry 11075

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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