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 17918

Title: Solution structure of the TbPIN1   PubMed: 22900083

Deposition date: 2011-09-06 Original release date: 2012-08-21

Authors: Sun, Lifang; Lin, Donghai; Zhao, Yufen

Citation: Sun, Lifang; Wu, Xueji; Peng, Yu; Goh, Jian-Yuan; Liou, Yih-Cherng; Lin, Donghai; Zhao, Yufen. "Solution Structural Analysis of the Single-Domain Parvulin TbPin1"  PLoS One 7, e43017-e43017 (2012).

Assembly members:
Prolyl_Cis/trans_Isomerase_TbPIN1, polymer, 115 residues, 12515.130 Da.

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
Prolyl_Cis/trans_Isomerase_TbPIN1: MSEKLRAAHLLVKFSGSRNP VSRRTGDSTADVTYEDAIKE LQKWSQRIASGEVSFEEAAS QRSDCGSYASGGDLGFFSSG EMMKPFEDAVRALKIGDISP IVQTDSGLHIIKRLA

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts122
1H chemical shifts801

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TbPIN11

Entities:

Entity 1, TbPIN1 115 residues - 12515.130 Da.

1   METSERGLULYSLEUARGALAALAHISLEU
2   LEUVALLYSPHESERGLYSERARGASNPRO
3   VALSERARGARGTHRGLYASPSERTHRALA
4   ASPVALTHRTYRGLUASPALAILELYSGLU
5   LEUGLNLYSTRPSERGLNARGILEALASER
6   GLYGLUVALSERPHEGLUGLUALAALASER
7   GLNARGSERASPCYSGLYSERTYRALASER
8   GLYGLYASPLEUGLYPHEPHESERSERGLY
9   GLUMETMETLYSPROPHEGLUASPALAVAL
10   ARGALALEULYSILEGLYASPILESERPRO
11   ILEVALGLNTHRASPSERGLYLEUHISILE
12   ILELYSARGLEUALA

Samples:

sample_1: Prolyl Cis/trans Isomerase TbPIN1, [U-99% 13C; U-99% 15N], 0.8 – 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 101325 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CBH13077
GB AAX69357 AAZ12840
REF XP_011775354 XP_846906

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