BMRB Entry 5786

Name: Solution Structure of Neural Cadherin Prodomain
Published: 2004-02-11

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PDB ID: 1op4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5786
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of Neural Cadherin Prodomain

Deposition date:

2003-04-28

Original release date:

2004-02-11

Authors:

Koch, A.; Farooq, A.; Shan, W.; Gruzglin, G.; Zeng, L.; Colman, D.; Zhou, M.-M.

Citation:

Citation: Koch, Alexander; Farooq, Amjad; Zeng, Lei; Colman, David; Zhou, M.-M.. "Letter to the Editor: 1H, 15N and 13C resonance assignments for the N-cadherin prodomain" J. Biomol. NMR 28, 87-88 (2004).
PubMed: 14739643

Assembly members:

Assembly members:
N-cadherin prodomain, polymer, 159 residues, Formula weight is not available

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-cadherin prodomain: GHHHHHHHHHHSSGHIDDDD KHMEASGEIALCKTGFPEDV YSAVLPKDVHEGQPLLNVKF SNCNRKRKVQYESSEPADFK VDEDGTVYAVRSFPLTAEQA KFLIYAQDKETQEKWQVAVN LSREPTLTEEPMKEPHEIEE IVFPRQLAKHSGALQRQKR

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	416
15N chemical shifts	118
1H chemical shifts	621

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-cadherin, prodomain	1

Entities:

Entity 1, N-cadherin, prodomain 159 residues - Formula weight is not available

1

GLY

HIS

2

HIS

SER

GLY

HIS

ILE

ASP

3

LYS

HIS

MET

GLU

ALA

SER

GLY

GLU

ILE

ALA

4

LEU

CYS

LYS

THR

GLY

PHE

PRO

GLU

ASP

VAL

5

TYR

SER

ALA

VAL

LEU

PRO

LYS

ASP

VAL

HIS

6

GLU

GLY

GLN

PRO

LEU

ASN

VAL

LYS

PHE

7

SER

ASN

CYS

ASN

ARG

LYS

ARG

LYS

VAL

GLN

8

TYR

GLU

SER

GLU

PRO

ALA

ASP

PHE

LYS

9

VAL

ASP

GLU

ASP

GLY

THR

VAL

TYR

ALA

VAL

10

ARG

SER

PHE

PRO

LEU

THR

ALA

GLU

GLN

ALA

11

LYS

PHE

LEU

ILE

TYR

ALA

GLN

ASP

LYS

GLU

12

THR

GLN

GLU

LYS

TRP

GLN

VAL

ALA

VAL

ASN

13

LEU

SER

ARG

GLU

PRO

THR

LEU

THR

GLU

14

PRO

MET

LYS

GLU

PRO

HIS

GLU

ILE

GLU

15

ILE

VAL

PHE

PRO

ARG

GLN

LEU

ALA

LYS

HIS

16

SER

GLY

ALA

LEU

GLN

ARG

GLN

LYS

ARG

Samples:

sample_1: N-cadherin prodomain, [U-13C; U-15N], 1 mM; Phosphate 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	not available	not available	not available
3D 15N-separated NOESY	not available	not available	not available
HNHA	not available	not available	not available

Software:

NMRPipe - processing

X-PLOR - structure solution

xwinnmr - collection

ARIA - refinement

NMR spectrometers:

Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks