BMRB Entry 10268

Name: Solution structures of the CA domain of human protocadherin 9
Published: 2009-12-14

Click here to enlarge.

PDB ID: 2ee0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10268
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 structures of the CA domain of human protocadherin 9

Deposition date:

2008-12-15

Original release date:

2009-12-14

Authors:

Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structures of the CA domain of human protocadherin 9" .

Assembly members:

Assembly members:
CA domain, polymer, 114 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: P060417-18

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CA domain: GSSGSSGNDNRPVFKEGQVE VHIPENAPVGTSVIQLHATD ADIGSNAEIRYIFGAQVAPA TKRLFALNNTTGLITVQRSL DREETAIHKVTVLASDGSST PARATVTINVTDVN

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	469
15N chemical shifts	119
1H chemical shifts	753

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CA domain	1

Entities:

Entity 1, CA domain 114 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ASN

ASP

ASN

2

ARG

PRO

VAL

PHE

LYS

GLU

GLY

GLN

VAL

GLU

3

VAL

HIS

ILE

PRO

GLU

ASN

ALA

PRO

VAL

GLY

4

THR

SER

VAL

ILE

GLN

LEU

HIS

ALA

THR

ASP

5

ALA

ASP

ILE

GLY

SER

ASN

ALA

GLU

ILE

ARG

6

TYR

ILE

PHE

GLY

ALA

GLN

VAL

ALA

PRO

ALA

7

THR

LYS

ARG

LEU

PHE

ALA

LEU

ASN

THR

8

THR

GLY

LEU

ILE

THR

VAL

GLN

ARG

SER

LEU

9

ASP

ARG

GLU

THR

ALA

ILE

HIS

LYS

VAL

10

THR

VAL

LEU

ALA

SER

ASP

GLY

SER

THR

11

PRO

ALA

ARG

ALA

THR

VAL

THR

ILE

ASN

VAL

12

THR

ASP

VAL

ASN

Samples:

sample_1: CA domain, [U-13C; U-15N], 1 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 v20031121, Delaglio, F. - processing

NMRView v2.0.17, 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