BMRB Entry 15900

Name: MMP23, a metalloprotease with a toxin-like potassium channel blocking domain and immunomodulatory role with relevance in prostate cancer
Published: 2009-12-11

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PDB ID: 2k72
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15900
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:

MMP23, a metalloprotease with a toxin-like potassium channel blocking domain and immunomodulatory role with relevance in prostate cancer

Deposition date:

2008-07-31

Original release date:

2009-12-11

Authors:

Khoo, Keith; Feng, Zhiping

Citation:

Citation: Rangaraju, Srikant; Khoo, Keith; Feng, Zhi-Ping; Crossley, George; Nugent, Daniel; Khaytin, Ilya; Chi, Victor; Pham, Cory; Calabresi, Peter; Pennington, Michael; Norton, Raymond; Chandy, K. George. "Potassium channel modulation by a toxin domain in matrix metalloprotease 23." J. Biol. Chem. 285, 9124-9136 (2010).
PubMed: 19965868

Assembly members:

Assembly members:
MMP23-BgK, polymer, 37 residues, 4442.344 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MMP23-BgK: YGCLDRIFVCTSWARKGFCD VRQRLMKRLCPRSCDFC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	270

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MMP23-BgK	1

Entities:

Entity 1, MMP23-BgK 37 residues - 4442.344 Da.

1

TYR

GLY

CYS

LEU

ASP

ARG

ILE

PHE

VAL

CYS

2

THR

SER

TRP

ALA

ARG

LYS

GLY

PHE

CYS

ASP

3

VAL

ARG

GLN

ARG

LEU

MET

LYS

ARG

LEU

CYS

4

PRO

ARG

SER

CYS

ASP

PHE

CYS

Samples:

94%H2O_6%D2O: MMP23-BgK 2.26 mM; H2O 94%; D2O, [U-100% 2H], 6%

100%D2O: MMP23-BgK 2.2-2.3 mM; D2O, [U-100% 2H], 100%

278K_pH5.00: pH: 5.00; pressure: 1 atm; temperature: 278 K

293K_pH5.00: pH: 5.00; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	94%H2O_6%D2O	isotropic	278K_pH5.00
2D 1H-1H NOESY	94%H2O_6%D2O	isotropic	278K_pH5.00
2D DQF-COSY	94%H2O_6%D2O	isotropic	293K_pH5.00
2D 1H-13C HSQC	94%H2O_6%D2O	isotropic	293K_pH5.00
2D 1H-15N HSQC	94%H2O_6%D2O	isotropic	293K_pH5.00
2D 1H-1H TOCSY	100%D2O	isotropic	278K_pH5.00
2D 1H-1H NOESY	100%D2O	isotropic	278K_pH5.00
2D 1H-1H TOCSY	94%H2O_6%D2O	isotropic	293K_pH5.00
2D 1H-1H NOESY	94%H2O_6%D2O	isotropic	293K_pH5.00

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

XEASY vv1.3.13, Bartels et al. - chemical shift assignment, peak picking

TOPSPIN vv1.3, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 500 MHz

PDB	2K72
DBJ	BAA24832 BAE27223
GB	AAC34886 AAH86586 AAI07358 AAI07359 EDL15021
REF	NP_036115 NP_446058 XP_006538942 XP_006538943 XP_006538944
SP	O88272 O88676
AlphaFold	O88272 O88676