BMRB Entry 10052

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR10052

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Title:
characterization of PCP-0SH in the D1 state was examined by using H/D exchange experiments.
Deposition date:
2006-11-20
Original release date:
2007-06-13
Authors:
Iimura, Satoshi; Umezaki, Taro; Takeuchi, Makoto; Mizuguchi, Mineyuki; Ogasahara, Kyoko; Yagi, Hiromasa; Akutsu, Hideo; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide
Citation:

Citation: Iimura, Satoshi; Umezaki, Taro; Takeuchi, Makoto; Mizuguchi, Mineyuki; Yagi, Hiromasa; Ogasahara, Kyoko; Akutsu, Hideo; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide. "Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under non-denaturing conditions: Role of the C-terminal a-helix of the protein in folding and stability"  Biochemistry 46, 3664-3672 (2007).
PubMed: 17309236

Assembly members:

Assembly members:
pyrrolidone carboxyl peptidase cys-free mutant, polymer, 208 residues, 22800 Da.

Natural source:

Natural source:   Common Name: P. furiosus   Taxonomy ID: 2261   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus furiosus

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pPCP3022

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pyrrolidone carboxyl peptidase cys-free mutant: MKVLVTGFEPFGGEKINPTE RIAKDLDGIKIGDAQVFGRV LPVVFGKAKEVLEKTLEEIK PDIAIHVGLAPGRSAISIER IAVNAIDARIPDNEGKKIED EPIVPGAPTAYFSTLPIKKI MKKLHERGIPAYISNSAGLY LSNYVMYLSLHHSATKGYPK MSGFIHVPYIPEQIIDKIGK GQVPPSMSYEMELEAVKVAI EVALEELL

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts296
1H chemical shifts296

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PCP homo tetramer subunit 11
2PCP homo tetramer subunit 21
3PCP homo tetramer subunit 31
4PCP homo tetramer subunit 41

Entities:

Entity 1, PCP homo tetramer subunit 1 208 residues - 22800 Da.

1   METLYSVALLEUVALTHRGLYPHEGLUPRO
2   PHEGLYGLYGLULYSILEASNPROTHRGLU
3   ARGILEALALYSASPLEUASPGLYILELYS
4   ILEGLYASPALAGLNVALPHEGLYARGVAL
5   LEUPROVALVALPHEGLYLYSALALYSGLU
6   VALLEUGLULYSTHRLEUGLUGLUILELYS
7   PROASPILEALAILEHISVALGLYLEUALA
8   PROGLYARGSERALAILESERILEGLUARG
9   ILEALAVALASNALAILEASPALAARGILE
10   PROASPASNGLUGLYLYSLYSILEGLUASP
11   GLUPROILEVALPROGLYALAPROTHRALA
12   TYRPHESERTHRLEUPROILELYSLYSILE
13   METLYSLYSLEUHISGLUARGGLYILEPRO
14   ALATYRILESERASNSERALAGLYLEUTYR
15   LEUSERASNTYRVALMETTYRLEUSERLEU
16   HISHISSERALATHRLYSGLYTYRPROLYS
17   METSERGLYPHEILEHISVALPROTYRILE
18   PROGLUGLNILEILEASPLYSILEGLYLYS
19   GLYGLNVALPROPROSERMETSERTYRGLU
20   METGLULEUGLUALAVALLYSVALALAILE
21   GLUVALALALEUGLUGLULEULEU

Samples:

sample_1: PCP, [U-13C; U-15N], 0.4 mM; Glycine 20 mM

sample_2: PCP, [U-15N], 0.4 mM; Glycine 20 mM

condition_1: pH: 2.5; temperature: 303 K

condition_2: pH: 3.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablecondition_1
HNCACBsample_1not availablecondition_1
HN(CO)CACBsample_1not availablecondition_1
HNCOsample_1not availablecondition_1
HN(CA)COsample_1not availablecondition_1
HSQC-NOESY-HSQCsample_2not availablecondition_2

Software:

XWIN-NMR, Bruker - collection

SPARKY v3.110, University of California - peak assignments

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAA32989
GB AAL81423 AFN04083
REF WP_011012443
SP O73944
AlphaFold O73944

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