BMRB Entry 10256

Click here to enlarge.

PDB ID: 2cof
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10256
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human

Deposition date:

2008-11-20

Original release date:

2009-11-20

Authors:

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

Citation:

Citation: Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human" .

Assembly members:

Assembly members:
PH domain, polymer, 107 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: P040921-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PH domain: GSSGSSGLETSSYLNVLVNS QWKSRWCSVRDNHLHFYQDR NRSKVAQQPLSLVGCEVVPD PSPDHLYSFRILHKGEELAK LEAKSSEEMGHWLGLLLSES GSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	432
15N chemical shifts	102
1H chemical shifts	679

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PH domain	1

Entities:

Entity 1, PH domain 107 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

LEU

GLU

THR

2

SER

TYR

LEU

ASN

VAL

LEU

VAL

ASN

SER

3

GLN

TRP

LYS

SER

ARG

TRP

CYS

SER

VAL

ARG

4

ASP

ASN

HIS

LEU

HIS

PHE

TYR

GLN

ASP

ARG

5

ASN

ARG

SER

LYS

VAL

ALA

GLN

PRO

LEU

6

SER

LEU

VAL

GLY

CYS

GLU

VAL

PRO

ASP

7

PRO

SER

PRO

ASP

HIS

LEU

TYR

SER

PHE

ARG

8

ILE

LEU

HIS

LYS

GLY

GLU

LEU

ALA

LYS

9

LEU

GLU

ALA

LYS

SER

GLU

MET

GLY

10

HIS

TRP

LEU

GLY

LEU

SER

GLU

SER

11

GLY

SER

GLY

PRO

SER

GLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.59 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: 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 v20031121, Delaglio, F - processing

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

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

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2COF
DBJ	BAB55135 BAF84401 BAG53870 BAH11936
GB	AAH24314 AAH33212 AAQ05765 EAW49470 EAW49471
REF	NP_001001936 NP_001248593 NP_001274753 NP_115939 XP_002821211
SP	Q8N4X5
AlphaFold	Q8N4X5