BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 11588

Title: Solution structure of Human Pin1 PPIase C113S mutant   PubMed: 26226559

Authors: Jing, Wang; Tochio, Naoya; Tate, Shin-ichi

Citation: Wang, Jing; Tochio, Naoya; Kawasaki, Ryosuke; Tamari, Yu; Xu, Ning; Uewaki, Jun-ichi; Utsunomiya-Tate, Naoko; Tate, Shin-ichi. "Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase"  Biochemistry 54, 5242-5253 (2015).

Assembly members:
entity, polymer, 117 residues, 13105.775 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDSSSAKARGDLGAFS RGQMQKPFEDASFALRTGEM SGPVFTDSGIHIILRTE

Data sets:
Data typeCount
13C chemical shifts511
15N chemical shifts126
1H chemical shifts801

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 117 residues - 13105.775 Da.

1   GLYSERHISMETGLUPROALAARGVALARG
2   CYSSERHISLEULEUVALLYSHISSERGLN
3   SERARGARGPROSERSERTRPARGGLNGLU
4   LYSILETHRARGTHRLYSGLUGLUALALEU
5   GLULEUILEASNGLYTYRILEGLNLYSILE
6   LYSSERGLYGLUGLUASPPHEGLUSERLEU
7   ALASERGLNPHESERASPSERSERSERALA
8   LYSALAARGGLYASPLEUGLYALAPHESER
9   ARGGLYGLNMETGLNLYSPROPHEGLUASP
10   ALASERPHEALALEUARGTHRGLYGLUMET
11   SERGLYPROVALPHETHRASPSERGLYILE
12   HISILEILELEUARGTHRGLU

Samples:

sample_1: sodium sulfate 100 mM; sodium phosphate 50 mM; D2O, [U-2H], 6%; H2O 94%; EDTA 5 mM; DTT 1 mM; NaN3 0.03%

sample_conditions_1: ionic strength: 150 mM; pH: 6.6; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

MAGRO, Kobayashi N. - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - data analysis

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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