BMRB Entry 10315

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PDB ID: 2dhj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10315
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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 Rho GTPase activating protein 21 from human

Deposition date:

2009-03-11

Original release date:

2010-03-11

Authors:

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

Citation:

Citation: Li, H.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of Rho GTPase activating protein 21 from human" .

Assembly members:

Assembly members:
PH domain, polymer, 125 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: P051017-10

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGDAAKEGWLHFRPL VTDKGKRVGGSIRPWKQMYV VLRGHSLYLYKDKREQTTPS EEEQPISVNACLIDISYSET KRKNVFRLTTSDCECLFQAE DRDDMLAWIKTIQESSNLNS GPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	524
15N chemical shifts	119
1H chemical shifts	816

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 125 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ASP

ALA

2

LYS

GLU

GLY

TRP

LEU

HIS

PHE

ARG

PRO

LEU

3

VAL

THR

ASP

LYS

GLY

LYS

ARG

VAL

GLY

4

SER

ILE

ARG

PRO

TRP

LYS

GLN

MET

TYR

VAL

5

VAL

LEU

ARG

GLY

HIS

SER

LEU

TYR

LEU

TYR

6

LYS

ASP

LYS

ARG

GLU

GLN

THR

PRO

SER

7

GLU

GLN

PRO

ILE

SER

VAL

ASN

ALA

8

CYS

LEU

ILE

ASP

ILE

SER

TYR

SER

GLU

THR

9

LYS

ARG

LYS

ASN

VAL

PHE

ARG

LEU

THR

10

SER

ASP

CYS

GLU

CYS

LEU

PHE

GLN

ALA

GLU

11

ASP

ARG

ASP

MET

LEU

ALA

TRP

ILE

LYS

12

THR

ILE

GLN

GLU

SER

ASN

LEU

ASN

SER

13

GLY

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.01 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 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-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 900 MHz

PDB	2DHJ 2J59
DBJ	BAA92662 BAG59749
EMBL	CAD39153 CAD97787
GB	AAM22955 EAW86122 EDL78791 EDL78792 EHH18940
REF	NP_001178622 NP_001248214 NP_065875 XP_002806993 XP_003269414
SP	Q5T5U3
TPG	DAA23594
AlphaFold	Q5T5U3