BMRB Entry 36014

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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/BMR36014
MolProbity Validation Chart

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Title:
Solution structure of the Pin1-PPIase (S138A) mutant
Deposition date:
2016-08-02
Original release date:
2017-08-07
Authors:
Tochio, N.; Wang, J.; Tate, S.
Citation:

Citation: Wang, Jing; Kawasaki, Ryosuke; Uewaki, Jun-Ichi; Rashid, Arif; Tochio, Naoya; Tate, Shin-Ichi. "Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1."  Molecules 22, E992-E992 (2017).
PubMed: 28617332

Assembly members:

Assembly members:
entity_1, polymer, 117 residues, 13105.732 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDCSSAKARGDLGAFS RGQMQKPFEDAAFALRTGEM SGPVFTDSGIHIILRTE

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts127
1H chemical shifts804

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 117 residues - 13105.732 Da.

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

Samples:

sample_1: Pin1 PPIase S138A mutant, [U-13C; U-15N], 1 mM; DTT 1 mM; EDTA 5 mM; sodium azide 0.03%; sodium phosphate 50 mM; sodium sulfate 100 mM; H2O 94%; D2O, [U-2H], 6%

sample_conditions_1: ionic strength: 250 mM; pH: 6.6; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

KUJIRA, Kobayashi, N. - data analysis

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AvanceII 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks