BMRB Entry 10025

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PDB ID: 1ul7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10025
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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 structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3

Deposition date:

2006-09-07

Original release date:

2008-07-16

Authors:

Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tochio, N.; Koshiba, S.; Kobayashi, N.; Inoue, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Tomo, Y.; Motoda, Y.; Kobayashi, A.; Tanaka, A.; Hayashizaki, Y.; Terada, T.; Shirouzu, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3" Protein Sci. 15, 2534-2543 (2006).
PubMed: 17075132

Assembly members:

Assembly members:
kinase associated domain 1(KA1), polymer, 102 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: cell free synthesis Vector: P021202-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
kinase associated domain 1(KA1): GSSGSSGRFTWSMKTTSSMD PSDMMREIRKVLGANNCDYE QRERFLLFCVHGDGHAENLV QWEMEVCKLPRLSLNGVRFK RISGTSIAFKNIASKIANEL KL

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	436
15N chemical shifts	102
1H chemical shifts	696

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	kinase associated domain 1(KA1)	1

Entities:

Entity 1, kinase associated domain 1(KA1) 102 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ARG

PHE

THR

2

TRP

SER

MET

LYS

THR

SER

MET

ASP

3

PRO

SER

ASP

MET

ARG

GLU

ILE

ARG

LYS

4

VAL

LEU

GLY

ALA

ASN

CYS

ASP

TYR

GLU

5

GLN

ARG

GLU

ARG

PHE

LEU

PHE

CYS

VAL

6

HIS

GLY

ASP

GLY

HIS

ALA

GLU

ASN

LEU

VAL

7

GLN

TRP

GLU

MET

GLU

VAL

CYS

LYS

LEU

PRO

8

ARG

LEU

SER

LEU

ASN

GLY

VAL

ARG

PHE

LYS

9

ARG

ILE

SER

GLY

THR

SER

ILE

ALA

PHE

LYS

10

ASN

ILE

ALA

SER

LYS

ILE

ALA

ASN

GLU

LEU

11

LYS

LEU

Samples:

sample_1: KA1 domain, [U-13C; U-15N], 1.0 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.853, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1UL7
DBJ	BAC35922 BAD92779 BAE21056 BAE38602 BAG59243
EMBL	CAD61882 CAD62578
GB	AAA59991 AAC15093 AAD48007 AAD51631 AAF64455
REF	NP_001122390 NP_001122391 NP_001122392 NP_001122393 NP_002367
SP	P27448 Q03141
AlphaFold	P27448 Q03141