BMRB Entry 18676

Title:
Regulation of a potassium channel by the pro-domain of a matrix metalloprotease
Deposition date:
2012-08-21
Original release date:
2012-09-17
Authors:
Galea, Charles; Nguyen, Hai; Schmunk, Galina; Smith, Brian; Edwards, Robert; Norton, Raymond; Chandy, K
Citation:

Citation: Nguyen, Hai; Galea, Charles; Schmunk, Galina; Smith, Brian; Edwards, Robert; Norton, Raymond; Chandy, K. George. "Intracellular trafficking of the KV1.3 potassium channel is regulated by the prodomain of a matrix metalloprotease."  J. Biol. Chem. 288, 6451-6464 (2013).
PubMed: 23300077

Assembly members:

Assembly members:
MMP23_pro-domain_polypeptide, polymer, 80 residues, 8048.5 Da.

Natural source:

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MMP23_pro-domain_polypeptide: GPMGRGARVPSEAPGAGVER RWLGAALVALCLLPALVLLA RLGAPAVPAWSAAQGDVAAL GLSAVPPTRVPGPLAPRRRR

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts67
1H chemical shifts144

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MMP23_pro-domain_polypeptide1

Entities:

Entity 1, MMP23_pro-domain_polypeptide 80 residues - 8048.5 Da.

Residues -1 and 0 represent N-termianl residues remaining following cleavage with 3C protease.

1   GLYPROMETGLYARGGLYALAARGVALPRO
2   SERGLUALAPROGLYALAGLYVALGLUARG
3   ARGTRPLEUGLYALAALALEUVALALALEU
4   CYSLEULEUPROALALEUVALLEULEUALA
5   ARGLEUGLYALAPROALAVALPROALATRP
6   SERALAALAGLNGLYASPVALALAALALEU
7   GLYLEUSERALAVALPROPROTHRARGVAL
8   PROGLYPROLEUALAPROARGARGARGARG

Samples:

sample_1: MMP23 pro-domain, [U-99% 15N], 0.5 mM; sodium citrate 20 mM; TCEP 20 mM; DPC, [U-100% 2H], 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 10%; H2O 90%

sample_2: MMP23 pro-domain, [U-99% 13C; U-99% 15N], 0.7 mM; sodium citrate 20 mM; TCEP 20 mM; DPC, [U-100% 2H], 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 303 K

sample_conditions_2: pH: 5.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_2isotropicsample_conditions_2

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

NMRView v8.2.33, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis, peak picking

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMRJ, Varian - collection

MICS, Yang, Bax - data analysis

qMDD v2.4, Jaravine, Kazimierczuk, Mayzel, Orekhov - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PIR O75900
DBJ BAA24833 BAA24834 BAA92769 BAG60058
EMBL CAB38176
GB AAC62616 AAC63527 AAH25719 AAX36150 AAX42573
REF NP_008914 XP_008957633
SP O75900
AlphaFold O75900

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