BMRB Entry 10026

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PDB ID: 1v5s
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10026
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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:

2006-09-25

Original release date:

2008-06-24

Authors:

Tochio, N.; Koshiba, S.; Inoue, M.; 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, 126 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: P020417-25

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Kinase associated domain 1 (KA1): MKDHLIHNVHKEEHAHAHNK DYDIPTTENLYFQGSSGSSG DMMREIRKVLGANNCDYEQR ERFLLFCVHGDGHAENLVQW EMEVCKLPRLSLNGVRFKRI SGTSIAFKNIASKIANELKL SGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	559
15N chemical shifts	141
1H chemical shifts	864

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MAP/microtubule affinity-regulating kinase 3	1

Entities:

Entity 1, MAP/microtubule affinity-regulating kinase 3 126 residues - Formula weight is not available

1

MET

LYS

ASP

HIS

LEU

ILE

HIS

ASN

VAL

HIS

2

LYS

GLU

HIS

ALA

HIS

ALA

HIS

ASN

LYS

3

ASP

TYR

ASP

ILE

PRO

THR

GLU

ASN

LEU

4

TYR

PHE

GLN

GLY

SER

GLY

SER

GLY

5

ASP

MET

ARG

GLU

ILE

ARG

LYS

VAL

LEU

6

GLY

ALA

ASN

CYS

ASP

TYR

GLU

GLN

ARG

7

GLU

ARG

PHE

LEU

PHE

CYS

VAL

HIS

GLY

8

ASP

GLY

HIS

ALA

GLU

ASN

LEU

VAL

GLN

TRP

9

GLU

MET

GLU

VAL

CYS

LYS

LEU

PRO

ARG

LEU

10

SER

LEU

ASN

GLY

VAL

ARG

PHE

LYS

ARG

ILE

11

SER

GLY

THR

SER

ILE

ALA

PHE

LYS

ASN

ILE

12

ALA

SER

LYS

ILE

ALA

ASN

GLU

LEU

LYS

LEU

13

SER

GLY

PRO

SER

GLY

Samples:

sample_1: KA1 domain, [U-13C; U-15N], 2.0 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	not available	condition_1
3D_15N-separated_NOESY	sample_1	not available	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425 - processing

NMRView v5.0.4 - data analysis

Kujira v0.853 - data analysis

CYANA v2.0.17 - structure solution & refinement

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1V5S
REF	XP_002696830 XP_005200933 XP_005200934 XP_005200936 XP_005200937
TPG	DAA17379