Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18676
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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:
MMP23_pro-domain_polypeptide, polymer, 80 residues, 8048.5 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32a
Entity Sequences (FASTA):
MMP23_pro-domain_polypeptide: GPMGRGARVPSEAPGAGVER
RWLGAALVALCLLPALVLLA
RLGAPAVPAWSAAQGDVAAL
GLSAVPPTRVPGPLAPRRRR
Data type | Count |
13C chemical shifts | 161 |
15N chemical shifts | 67 |
1H chemical shifts | 144 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MMP23_pro-domain_polypeptide | 1 |
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 | GLY | PRO | MET | GLY | ARG | GLY | ALA | ARG | VAL | PRO | |
2 | SER | GLU | ALA | PRO | GLY | ALA | GLY | VAL | GLU | ARG | |
3 | ARG | TRP | LEU | GLY | ALA | ALA | LEU | VAL | ALA | LEU | |
4 | CYS | LEU | LEU | PRO | ALA | LEU | VAL | LEU | LEU | ALA | |
5 | ARG | LEU | GLY | ALA | PRO | ALA | VAL | PRO | ALA | TRP | |
6 | SER | ALA | ALA | GLN | GLY | ASP | VAL | ALA | ALA | LEU | |
7 | GLY | LEU | SER | ALA | VAL | PRO | PRO | THR | ARG | VAL | |
8 | PRO | GLY | PRO | LEU | ALA | PRO | ARG | ARG | ARG | ARG |
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
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
3D HNCO | sample_2 | isotropic | sample_conditions_2 |
3D HNCA | sample_2 | isotropic | sample_conditions_2 |
3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_2 |
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
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:
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or all simulated peaks
SPARKY: Backbone
or all simulated peaks