BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18246

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18246

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Title: Backbone assignment of porcine pepsin complex with pepstatin

Deposition date: 2012-02-08 Original release date: 2012-11-28

Authors: Wang, Shenlin; Horimoto, Yasumi; Dee, Derek; Yada, Rickey

Citation: Wang, Shenlin; Horimoto, Yasumi; Dee, Derek; Yada, Rickey. "Understanding of the nature of energy barrier of PS catalzed refolding by NMR spectroscopy"  Nat. Struct. Biol. ., .-..

Assembly members:
Pepsin, polymer, 326 residues, Formula weight is not available

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

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

Entity Sequences (FASTA):
Pepsin: IGDEPLENYLDTEYFGTIGI GTPAQDFTVIFDTGSSNLWV PSVYCSSLACSDHNQFNPDD SSTFEATSQELSITYGTGSM TGILGYDTVQVGGISDTNQI FGLSETEPGSFLYYAPFDGI LGLAYPSISASGATPVFDNL WDQGLVSQDLFSVYLSSNDD SGSVVLLGGIDSSYYTGSLN WVPVSVEGYWQITLDSITMD GETIACSGGCQAIVDTGTSL LTGPTSAIANIQSDIGASEN SDGEMVISCSSIDSLPDIVF TINGVQYPLSPSAYILQDDD SCTSGFEGMDVPTSSGELWI LGDVFIRQYYTVFDRANNKV GLAPVA

Data sets:
Data typeCount
13C chemical shifts928
15N chemical shifts303
1H chemical shifts303

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pepsin1

Entities:

Entity 1, Pepsin 326 residues - Formula weight is not available

1   ILEGLYASPGLUPROLEUGLUASNTYRLEU
2   ASPTHRGLUTYRPHEGLYTHRILEGLYILE
3   GLYTHRPROALAGLNASPPHETHRVALILE
4   PHEASPTHRGLYSERSERASNLEUTRPVAL
5   PROSERVALTYRCYSSERSERLEUALACYS
6   SERASPHISASNGLNPHEASNPROASPASP
7   SERSERTHRPHEGLUALATHRSERGLNGLU
8   LEUSERILETHRTYRGLYTHRGLYSERMET
9   THRGLYILELEUGLYTYRASPTHRVALGLN
10   VALGLYGLYILESERASPTHRASNGLNILE
11   PHEGLYLEUSERGLUTHRGLUPROGLYSER
12   PHELEUTYRTYRALAPROPHEASPGLYILE
13   LEUGLYLEUALATYRPROSERILESERALA
14   SERGLYALATHRPROVALPHEASPASNLEU
15   TRPASPGLNGLYLEUVALSERGLNASPLEU
16   PHESERVALTYRLEUSERSERASNASPASP
17   SERGLYSERVALVALLEULEUGLYGLYILE
18   ASPSERSERTYRTYRTHRGLYSERLEUASN
19   TRPVALPROVALSERVALGLUGLYTYRTRP
20   GLNILETHRLEUASPSERILETHRMETASP
21   GLYGLUTHRILEALACYSSERGLYGLYCYS
22   GLNALAILEVALASPTHRGLYTHRSERLEU
23   LEUTHRGLYPROTHRSERALAILEALAASN
24   ILEGLNSERASPILEGLYALASERGLUASN
25   SERASPGLYGLUMETVALILESERCYSSER
26   SERILEASPSERLEUPROASPILEVALPHE
27   THRILEASNGLYVALGLNTYRPROLEUSER
28   PROSERALATYRILELEUGLNASPASPASP
29   SERCYSTHRSERGLYPHEGLUGLYMETASP
30   VALPROTHRSERSERGLYGLULEUTRPILE
31   LEUGLYASPVALPHEILEARGGLNTYRTYR
32   THRVALPHEASPARGALAASNASNLYSVAL
33   GLYLEUALAPROVALALA

Samples:

sample_1: Pepsin, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2 mM; H2O 90%; D2O 10%; NaOAc 20 mM

sample_2: Pepsin, [U-100% 15N], 0.2 mM; H2O 90%; D2O 10%; NaOAc 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.3; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

BMRB 18245
PDB
GB AAA31095 AAA31096 ABM47074
REF NP_999038
SP P00791

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