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 4037

Title: Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli

Deposition date: 1997-06-26 Original release date: 1998-07-05

Authors: Clubb, Robert; Thanabal, Venkataraman; Fejzo, Jasna; Ferguson, Stephen; Zydowsky, Lynne; Baker, C.; Walsh, Christopher; Wagner, Gerhard

Citation: Clubb, Robert; Thanabal, Venkataraman; Fejzo, Jasna; Ferguson, Stephen; Zydowsky, Lynne; Baker, C.; Walsh, Christopher; Wagner, Gerhard. "Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli "  Biochemistry 32, 6391-6401 (1993).

Assembly members:
periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, polymer, 167 residues, 18244 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase: AAKGDPHVLLTTSAGNIELE LDKQKAPVSVQNFVDYVNSG FYNNTTFHRVIPGFMIQGGG FTEQMQQKKPNPPIKNEADN GLRNTRGTIAMARTADKDSA TSQFFINVADNAFLDHGQRD FGYAVFGKVVKGMDVADKIS QVPTHDVGPYQNVPSKPVVI LSAKVLP

Data sets:
Data typeCount
1H chemical shifts323
13C chemical shifts328
15N chemical shifts153

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1eCyP1

Entities:

Entity 1, eCyP 167 residues - 18244 Da.

1   ALAALALYSGLYASPPROHISVALLEULEU
2   THRTHRSERALAGLYASNILEGLULEUGLU
3   LEUASPLYSGLNLYSALAPROVALSERVAL
4   GLNASNPHEVALASPTYRVALASNSERGLY
5   PHETYRASNASNTHRTHRPHEHISARGVAL
6   ILEPROGLYPHEMETILEGLNGLYGLYGLY
7   PHETHRGLUGLNMETGLNGLNLYSLYSPRO
8   ASNPROPROILELYSASNGLUALAASPASN
9   GLYLEUARGASNTHRARGGLYTHRILEALA
10   METALAARGTHRALAASPLYSASPSERALA
11   THRSERGLNPHEPHEILEASNVALALAASP
12   ASNALAPHELEUASPHISGLYGLNARGASP
13   PHEGLYTYRALAVALPHEGLYLYSVALVAL
14   LYSGLYMETASPVALALAASPLYSILESER
15   GLNVALPROTHRHISASPVALGLYPROTYR
16   GLNASNVALPROSERLYSPROVALVALILE
17   LEUSERALALYSVALLEUPRO

Samples:

sample_one: periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, [U-15N], 0.2 – 2.0 mM; phosphate_buffer 50 mM

sample_two: periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase, [U-13C;U-15N], 0.2 – 2.0 mM; phosphate_buffer 50 mM

sample_conditions_one: pH: 6.2; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions

Software:

No software information available

NMR spectrometers:

  • Bruker AMX500 500MHz MHz
  • Bruker AMX600 600MHz MHz

Related Database Links:

PDB
DBJ BAB37637 BAE77927 BAG79149 BAI27622 BAI32792
EMBL CAD08141 CAP77816 CAQ33683 CAQ90814 CAR00303
GB AAA23451 AAA23772 AAA24261 AAA58160 AAC76388
PIR AI1001
REF NP_312241 NP_417822 NP_458430 NP_462375 NP_709138
SP P0AFL3 P0AFL4 P0AFL5 P20753

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