BMRB Entry 11451

Title:
NMR strucure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)
Deposition date:
2011-07-16
Original release date:
2015-06-26
Authors:
Takeda, Mitsuhiro; Jee, JunGoo; Ono, Akira; Okuma, Kosuke; Terauchi, Tsutomu; Kainosho, Masatsune
Citation:

Citation: Takeda, Mitsuhiro; Jee, JunGoo; Ono, Akira; Terauchi, Tsutomu; Kainosho, Masatsune. "Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups"  J. Am. Chem. Soc. 133, 17420-17427 (2011).
PubMed: 21955241

Assembly members:

Assembly members:
entity, polymer, 164 residues, 18174.578 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli   Vector: pET3a

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts173
1H chemical shifts858

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1peptidyl-prolyl cis-trans isomerase1

Entities:

Entity 1, peptidyl-prolyl cis-trans isomerase 164 residues - 18174.578 Da.

1   METVALTHRPHEHISTHRASNHISGLYASP
2   ILEVALILELYSTHRPHEASPASPLYSALA
3   PROGLUTHRVALLYSASNPHELEUASPTYR
4   CYSARGGLUGLYPHETYRASNASNTHRILE
5   PHEHISARGVALILEASNGLYPHEMETILE
6   GLNGLYGLYGLYPHEGLUPROGLYMETLYS
7   GLNLYSALATHRLYSGLUPROILELYSASN
8   GLUALAASNASNGLYLEULYSASNTHRARG
9   GLYTHRLEUALAMETALAARGTHRGLNALA
10   PROHISSERALATHRALAGLNPHEPHEILE
11   ASNVALVALASPASNASPPHELEUASNPHE
12   SERGLYGLUSERLEUGLNGLYTRPGLYTYR
13   CYSVALPHEALAGLUVALVALASPGLYMET
14   ASPVALVALASPLYSILELYSGLYVALALA
15   THRGLYARGSERGLYMETHISGLNASPVAL
16   PROLYSGLUASPVALILEILEGLUSERVAL
17   THRVALSERGLU

Samples:

sample_1: EPPIb, SAIL [e-SAIL Phe, e-SAIL Tyr], 0.3 mM; sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM

sample_2: EPPIb, SAIL [z-SAIL Phe, e-SAIL Tyr], 0.3 mM; sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM

sample_3: EPPIb, SAIL [d-SAIL Phe, d-SAIL Tyr], 0.3 mM; sodium phosphate 50 mM; DTT 1 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.4 M; pH: 6.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
2D HB(CBCG)HEsample_1isotropicsample_conditions_1
2D HB(CBCGCZ) HZsample_2isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAB34010 BAE76302 BAG76074 BAI23892 BAI29364
EMBL CAD05020 CAP75055 CAQ30997 CAQ88114 CAQ97399
GB AAA23453 AAC73627 AAG54882 AAL19490 AAN42110
PIR AB0569
REF NP_308614 NP_415058 NP_455128 NP_459531 NP_706403
SP P23869
AlphaFold P23869

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