BMRB Entry 10250

Name: Solution structure of the PH domain of human Docking protein BRDG1
Published: 2009-11-20

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PDB ID: 1x1f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10250
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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 human Docking protein BRDG1

Deposition date:

2008-11-20

Original release date:

2009-11-20

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 human Docking protein BRDG1" .

Assembly members:

Assembly members:
PH domain, polymer, 149 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: P040301-57

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGQERLKITALPLYF EGFLLIKRSGYREYEHYWTE LRGTTLFFYTDKKSIIYVDK LDIVDLTCLTEQNSTEKNCA KFTLVLPKEEVQLKTENTES GEEWRGFILTVTELSVPQNV SLLPGQVIKLHEVLEREKKR RIESGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	673
15N chemical shifts	143
1H chemical shifts	1057

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 149 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

GLU

ARG

2

LEU

LYS

ILE

THR

ALA

LEU

PRO

LEU

TYR

PHE

3

GLU

GLY

PHE

LEU

ILE

LYS

ARG

SER

GLY

4

TYR

ARG

GLU

TYR

GLU

HIS

TYR

TRP

THR

GLU

5

LEU

ARG

GLY

THR

LEU

PHE

TYR

THR

6

ASP

LYS

SER

ILE

TYR

VAL

ASP

LYS

7

LEU

ASP

ILE

VAL

ASP

LEU

THR

CYS

LEU

THR

8

GLU

GLN

ASN

SER

THR

GLU

LYS

ASN

CYS

ALA

9

LYS

PHE

THR

LEU

VAL

LEU

PRO

LYS

GLU

10

VAL

GLN

LEU

LYS

THR

GLU

ASN

THR

GLU

SER

11

GLY

GLU

TRP

ARG

GLY

PHE

ILE

LEU

THR

12

VAL

THR

GLU

LEU

SER

VAL

PRO

GLN

ASN

VAL

13

SER

LEU

PRO

GLY

GLN

VAL

ILE

LYS

LEU

14

HIS

GLU

VAL

LEU

GLU

ARG

GLU

LYS

ARG

15

ARG

ILE

GLU

SER

GLY

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.00 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 v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.913, Kobayashi, N. - data analysis

CYANA v1.0.7, Guentert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz