BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18338

Title: C-terminal propeptide (PPc) region of vibrio extracellular metalloprotease   PubMed: 23228665

Deposition date: 2012-03-20 Original release date: 2013-01-03

Authors: Yun, Ji-Hye

Citation: Yun, Ji-Hye; Kim, Heeyoun; Park, Jung Eun; Lee, Jung Sup; Lee, Weontae. "Solution structure and dynamics of C-terminal regulatory domain of Vibrio vulnificus extracellular metalloprotease."  Biochem. Biophys. Res. Commun. 430, 541-546 (2013).

Assembly members:
C-terminal_propeptide_(PPc)_region_of_vibrio_extracellular_metalloprotease, polymer, 101 residues, Formula weight is not available

Natural source:   Common Name: vibrio vulnificus   Taxonomy ID: 672   Superkingdom: Bacteria   Kingdom: not available   Genus/species: vibrio vulnificus

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

Entity Sequences (FASTA):
C-terminal_propeptide_(PPc)_region_of_vibrio_extracellular_metalloprotease: GNVLKNNTPVSNLTGNKGSE VFYTFTVDRNATAVVSISGG SGDADLYLKAGSKPTTSSWD CRPYRYGNNESCSVSAAPGT TYHVMIKGYSNYSGVTLKLQ Y

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts102
1H chemical shifts631

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PPc1

Entities:

Entity 1, PPc 101 residues - Formula weight is not available

1   GLYASNVALLEULYSASNASNTHRPROVAL
2   SERASNLEUTHRGLYASNLYSGLYSERGLU
3   VALPHETYRTHRPHETHRVALASPARGASN
4   ALATHRALAVALVALSERILESERGLYGLY
5   SERGLYASPALAASPLEUTYRLEULYSALA
6   GLYSERLYSPROTHRTHRSERSERTRPASP
7   CYSARGPROTYRARGTYRGLYASNASNGLU
8   SERCYSSERVALSERALAALAPROGLYTHR
9   THRTYRHISVALMETILELYSGLYTYRSER
10   ASNTYRSERGLYVALTHRLEULYSLEUGLN
11   TYR

Samples:

PPc_domain_of_vEP: PPc protein, [U-100% 15N], 0.6 mM; HEPES (pH 7.0) 20 mM; Sodium chloride 100 mM; DTT 10 mM; NaN3 0.01%; H2O 90%; D2O 10%

PPc_domain_of_vEP_2: PPc protein, [U-100% 13C; U-100% 15N], 0.6 mM; HEPES (pH 7.0) 20 mM; Sodium chloride 100 mM; DTT 10 mM; NaN3 0.01%; H2O 90%; D2O 10%

0.6mM_PPc_protein: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCPPc_domain_of_vEPisotropic0.6mM_PPc_protein
3D 1H-15N NOESYPPc_domain_of_vEPisotropic0.6mM_PPc_protein
3D 1H-13C NOESYPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HNCACBPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HBHA(CO)NHPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HNCAPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HNCOPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HBHA(CO)NHPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein
3D HCCH-TOCSYPPc_domain_of_vEP_2isotropic0.6mM_PPc_protein

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 900 MHz

Related Database Links:

PDB
DBJ BAC22940 BAC97491 BAI66359 BAI66360 BAI66361
EMBL CAM34546
GB AAC44789 AAC45343 AAC72410 AAO07886 ABI95803
REF WP_011081880 WP_015728348 WP_026050529 WP_026130953 WP_038940484

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