BMRB Entry 15466

Title:
STRUCTURE CHARACTERISATION OF PINA WW DOMAIN AND COMPARISON WITH OTHER GROUP IV WW DOMAINS, PIN1 AND ESS1   PubMed: 18503784
Deposition date:
2007-09-11
Original release date:
2008-06-25
Authors:
Ng, C.; Kato, Y.; Tanokura, M.; Brownlee, R.
Citation:

Citation: Ng, Chai; Kato, Yusuke; Tanokura, Masaru; Brownlee, Robert. "Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1"  Biochim. Biophys. Acta 1784, 1208-1214 (2008).

Assembly members:

Assembly members:
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE, polymer, 54 residues, 6262.056 Da.

Natural source:

Natural source:   Common Name: ASPERGILLUS NIDULANS   Taxonomy ID: 162425   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: ASPERGILLUS NIDULANS

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PLYSS

Experimental source:

Natural source:   Common Name: ASPERGILLUS NIDULANS   Taxonomy ID: 162425   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: ASPERGILLUS NIDULANS

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PLYSS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE: GSMVNTGLPAGWEVRHSNSK NLPYYFNPATRESRWEPPAD TDMETLKMYMATYH

Data sets:
Data typeCount
13C chemical shifts145
15N chemical shifts49
1H chemical shifts330

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 54 residues - 6262.056 Da.

1   GLYSERMETVALASNTHRGLYLEUPROALA
2   GLYTRPGLUVALARGHISSERASNSERLYS
3   ASNLEUPROTYRTYRPHEASNPROALATHR
4   ARGGLUSERARGTRPGLUPROPROALAASP
5   THRASPMETGLUTHRLEULYSMETTYRMET
6   ALATHRTYRHIS

Samples:

sample_1: PEPTIDYL-PROLYL CIS/TRANS ISOMERASE, [U-100% 13C; U-100% 15N], 1.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D HNHAsample_1isotropicsample_conditions_1
3D_13C- SEPARATED_ NOESYsample_1isotropicsample_conditions_1
3D_15N- SEPARATED_ NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HCCH -COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY v3, Goddard - chemical shift assignment, data analysis, peak picking

VNMR, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - Energy minimisation, refinement

NMR spectrometers:

  • VARIAN INOVA 500 MHz

Related Database Links:

BMRB 15003
PDB
GB AAC49984 EAA57931
REF XP_663749
TPE CBF70093

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