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BMRB Entry 18864

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18864
MolProbity Validation Chart

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Title: High resolution structure and dynamics of CsPinA parvulin at physiological temperature

Deposition date: 2012-11-28 Original release date: 2013-12-02

Authors: Jaremko, Lukasz; Jaremko, Mariusz; Zweckstetter, Markus; Bayer, Peter; Ejchart, Andrzej

Citation: Jaremko, Lukasz; Jaremko, Mariusz; Zweckstetter, Markus; Bayer, Peter; Ejchart, Andrzej. "High resolution structure and dynamics of CsPinA parvulin at physiological temperature"  Not known ., .-..

Assembly members:
CsPinA, polymer, 97 residues, 10516.343 Da.

Natural source:   Common Name: Cenarchaeum symbiosum   Taxonomy ID: 46770   Superkingdom: Archaea   Kingdom: not available   Genus/species: Cenarchaeum symbiosum

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

Entity Sequences (FASTA):
CsPinA: GPMGSMADKIKCSHILVKKQ GEALAVQERLKAGEKFGKLA KELSIDGGSAKRDGSLGYFG RGKMVKPFEDAAFRLQVGEV SEPVKSEFGYHVIKRLG

Data typeCount
13C chemical shifts332
15N chemical shifts90
1H chemical shifts668
heteronuclear NOE values521
T1 relaxation values344
T2 relaxation values344

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CsPinA1

Entities:

Entity 1, CsPinA 97 residues - 10516.343 Da.

1   GLYPROMETGLYSERMETALAASPLYSILE
2   LYSCYSSERHISILELEUVALLYSLYSGLN
3   GLYGLUALALEUALAVALGLNGLUARGLEU
4   LYSALAGLYGLULYSPHEGLYLYSLEUALA
5   LYSGLULEUSERILEASPGLYGLYSERALA
6   LYSARGASPGLYSERLEUGLYTYRPHEGLY
7   ARGGLYLYSMETVALLYSPROPHEGLUASP
8   ALAALAPHEARGLEUGLNVALGLYGLUVAL
9   SERGLUPROVALLYSSERGLUPHEGLYTYR
10   HISVALILELYSARGLEUGLY

Samples:

sample_1: CsPinA, [U-100% 15N], 0.9 mM; H20 93%; D2O 7%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NOE)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R1)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R1)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R1)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R1)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R2)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R2)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R2)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC (R2)sample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

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

NMR spectrometers:

  • Bruker Avance 400 MHz
  • Varian UnityPlus 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 11080
PDB
GB AAC62692 ABK77807

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