BMRB Entry 10312

Name: Solution structure of the PH domain of Protein kinase C, nu type from human
Published: 2010-03-11

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PDB ID: 2d9z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10312
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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 the PH domain of Protein kinase C, nu type from human

Deposition date:

2009-03-11

Original release date:

2010-03-11

Authors:

Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of Protein kinase C, nu type from human" .

Assembly members:

Assembly members:
PH domain, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: Cell-free synthesis Vector: P050711-24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGMVKEGWMVHYTSR DNLRKRHYWRLDSKCLTLFQ NESGSKYYKEIPLSEILRIS SPRDFTNISQGSNPHCFEII TDTMVYFVGENNGDSSHNPV LAATGVGLDVAQSWEKAIRQ ALMSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	545
15N chemical shifts	131
1H chemical shifts	844

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PH domain	1

Entities:

Entity 1, PH domain 129 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

VAL

LYS

2

GLU

GLY

TRP

MET

VAL

HIS

TYR

THR

SER

ARG

3

ASP

ASN

LEU

ARG

LYS

ARG

HIS

TYR

TRP

ARG

4

LEU

ASP

SER

LYS

CYS

LEU

THR

LEU

PHE

GLN

5

ASN

GLU

SER

GLY

SER

LYS

TYR

LYS

GLU

6

ILE

PRO

LEU

SER

GLU

ILE

LEU

ARG

ILE

SER

7

SER

PRO

ARG

ASP

PHE

THR

ASN

ILE

SER

GLN

8

GLY

SER

ASN

PRO

HIS

CYS

PHE

GLU

ILE

9

THR

ASP

THR

MET

VAL

TYR

PHE

VAL

GLY

GLU

10

ASN

GLY

ASP

SER

HIS

ASN

PRO

VAL

11

LEU

ALA

THR

GLY

VAL

GLY

LEU

ASP

VAL

12

ALA

GLN

SER

TRP

GLU

LYS

ALA

ILE

ARG

GLN

13

ALA

LEU

MET

SER

GLY

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 0.42 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

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

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2D9Z
DBJ	BAA36514 BAG51354
GB	AAH30706 AAY14817 ADZ15743 AIC62718 EAX00398
REF	NP_001244477 NP_005804 XP_002757895 XP_002812168 XP_003125283
SP	O94806
AlphaFold	O94806