BMRB Entry 16406

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16406

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Title:
Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Deposition date:
2009-07-13
Original release date:
2009-07-23
Authors:
Zheng, Suxin; Leeper, Thomas; Varani, Gabriele
Citation:

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

Assembly members:

Assembly members:
peptidyl-prolyl cis-trans isomerase, polymer, 117 residues, 12239.810 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
peptidyl-prolyl cis-trans isomerase: GPGSMTVVTTESGLKYEDLT EGSGAEARAGQTVSVHYTGW LTDGQKFDSSKDRNDPFAFV LGGGMVIKGWDEGVQGMKVG GVRRLTIPPQLGYGARGAGG VIPPNATLVFEVELLDV

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts109
1H chemical shifts748

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 117 residues - 12239.810 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

Samples:

C13_N15-labeled: entity, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 20 mM; potassium chloride 100 mM; H2O 95%; D2O 5%

N15-labeled: entity, [U-100% 15N], 0.5 mM; potassium phosphate 20 mM; potassium chloride 100 mM; H2O 95%; D2O 5%

N15-labeled_2: entity, [U-100% 15N], 0.5 mM; potassium phosphate 20 mM; potassium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHC13_N15-labeledisotropicsample_conditions_1
3D HNCACBC13_N15-labeledisotropicsample_conditions_1
3D HNCAC13_N15-labeledisotropicsample_conditions_1
3D HN(CO)CAC13_N15-labeledisotropicsample_conditions_1
3D HCCH-TOCSYC13_N15-labeledisotropicsample_conditions_1
3D 1H-13C NOESYC13_N15-labeledisotropicsample_conditions_1
2D 1H-15N HSQCN15-labeledisotropicsample_conditions_1
3D 1H-15N NOESYN15-labeledisotropicsample_conditions_1
2D 1H-15N HSQCN15-labeled_2isotropicsample_conditions_1
2D 1H-1H TOCSYN15-labeled_2isotropicsample_conditions_1
2D 1H-1H NOESYN15-labeled_2isotropicsample_conditions_1
3D 1H-15N TOCSYN15-labeledisotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement, structure solution

ANALYSIS v1.0, CCPN - chemical shift assignment

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

NMR spectrometers:

  • Bruker AMX 600 MHz
  • Bruker AMX 750 MHz

Related Database Links:

BMRB 16491 17151
PDB
EMBL CAH39299 CDU31864 CFB51428 CFD89802 CFD92609
GB ABA51599 ABC34056 ABN85861 ABN94560 AFI70186
REF WP_004525093 WP_004537279 WP_009895623 WP_010110204 WP_010120234

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SPARKY: Backbone or all simulated peaks