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BMRB Entry 17151

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17151
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Title: Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with 1-{[(4-methylphenyl)thio]acetyl}piperidine. Seattle Structure Genomics Center for Infectious Disease (SSGCID)

Deposition date: 2010-08-27 Original release date: 2010-11-01

Authors: Zheng, Suxin; Barnwal, Ravi Pratap; Leeper, Thomas; Varani, Gabriele

Citation: Zheng, Suxin; Barnwal, Ravi Pratap; Leeper, Thomas; Varani, Gabriele. "Null"  To be Published ., .-..

Assembly members:
FKBP, polymer, 117 residues, 13472.467 Da.
1-{[(4-methylphenyl)thio]acetyl}piperidine, non-polymer, 331.279 Da.

Natural source:   Common Name: Burkholderia pseudomallei   Taxonomy ID: 28450   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia pseudomallei

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

Entity Sequences (FASTA):
FKBP: GPGSMTVVTTESGLKYEDLT EGSGAEARAGQTVSVHYTGW LTDGQKFDSSKDRNDPFAFV LGGGMVIKGWDEGVQGMKVG GVRRLTIPPQLGYGARGAGG VIPPNATLVFEVELLDV

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts116
1H chemical shifts771

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FKBP1
21-{[(4-methylphenyl)thio]acetyl}piperidine2

Entities:

Entity 1, FKBP 117 residues - 13472.467 Da.

1   GLYPROGLYSERMETTHRVALVALTHRTHR
2   GLUSERGLYLEULYSTYRGLUASPLEUTHR
3   GLUGLYSERGLYALAGLUALAARGALAGLY
4   GLNTHRVALSERVALHISTYRTHRGLYTRP
5   LEUTHRASPGLYGLNLYSPHEASPSERSER
6   LYSASPARGASNASPPROPHEALAPHEVAL
7   LEUGLYGLYGLYMETVALILELYSGLYTRP
8   ASPGLUGLYVALGLNGLYMETLYSVALGLY
9   GLYVALARGARGLEUTHRILEPROPROGLN
10   LEUGLYTYRGLYALAARGGLYALAGLYGLY
11   VALILEPROPROASNALATHRLEUVALPHE
12   GLUVALGLULEULEUASPVAL

Entity 2, 1-{[(4-methylphenyl)thio]acetyl}piperidine - C14H19SNO - 331.279 Da.

1   F191

Samples:

sample_1: isomerase, [U-99% 13C; U-99% 15N], 0.6 – 1.5 mM; H2O 95%; D2O 5%; KCl 100 mM; potassium phosphate 20 mM; DTT 1 mM

sample_2: isomerase, [U-99% 13C; U-99% 15N], 0.6 – 1.5 mM; D2O 100%; KCl 100 mM; potassium phosphate 20 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16406 16491
PDB
EMBL CAH39299 CDU31864 CFB51428 CFD89802 CFD92609
GB ABA51599 ABC34056 ABN85861 ABN94560 AFI70186
REF WP_004525093 WP_004537279 WP_009895623 WP_010110204 WP_010120234

Download simulated HSQC data in one of the following formats:
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