BMRB Entry 19259

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19259
MolProbity Validation Chart

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Title:
Pin1 WW domain phospho-mimic S16E
Deposition date:
2013-05-22
Original release date:
2014-04-07
Authors:
Luh, Laura; Kirchner, Donata; Loehr, Frank; Haensel, Robert; Doetsch, Volker
Citation:

Citation: Luh, Laura; Hansel, Robert; Lohr, Frank; Kirchner, Donata; Krauskopf, Katharina; Pitzius, Susanne; Schafer, Birgit; Tufar, Peter; Corbeski, Ivan; Guntert, Peter; Dotsch, Volker. "Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition"  J. Am. Chem. Soc. 135, 13796-13803 (2013).
PubMed: 23968199

Assembly members:

Assembly members:
Pin1, polymer, 43 residues, 5085.650 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   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Pin1: GLEHMADEEKLPPGWEKRME RSSGRVYYFNHITNASQWER PSG

Data sets:
Data typeCount
13C chemical shifts182
15N chemical shifts39
1H chemical shifts275

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Pin11

Entities:

Entity 1, Pin1 43 residues - 5085.650 Da.

1   GLYLEUGLUHISMETALAASPGLUGLULYS
2   LEUPROPROGLYTRPGLULYSARGMETGLU
3   ARGSERSERGLYARGVALTYRTYRPHEASN
4   HISILETHRASNALASERGLNTRPGLUARG
5   PROSERGLY

Samples:

sample_1: Pin1 mM; HEPES 25 mM; sodium chloride 50 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 291 K

Experiments:

NameSampleSample stateSample conditions
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

TOPSPIN, Bruker Biospin - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16070 16088 17545 19258 25569
PDB
DBJ BAA87037 BAA87038 BAB22270 BAB22743 BAC35631
EMBL CAG28582
GB AAC50492 AAH02899 AAH38254 AAI12584 AAV38138
PRF 2209428A
REF NP_001029804 NP_001231300 NP_006212 NP_075860 XP_001099116
SP Q13526 Q5BIN5 Q9QUR7
TPG DAA28013
AlphaFold Q13526 Q5BIN5 Q9QUR7

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