BMRB Entry 17545

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17545
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structure of the first domain of human PIN1 in complex with a human Smad3 derived peptide.
Deposition date:
2011-03-22
Original release date:
2011-06-23
Authors:
Macias, Maria; Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan
Citation:

Citation: Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan; Macias, Maria. "A Smad action turnover switch operated by WW domain readers of a phosphoserine code."  Genes Dev. 25, 1275-1288 (2011).
PubMed: 21685363

Assembly members:

Assembly members:
first domain of human PIN1, polymer, 36 residues, 4231.730 Da.
human Smad3 derived peptide, polymer, 8 residues, 886.891 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
first domain of human PIN1: KLPPGWEKRMSRSSGRVYYF NHITNASQWERPSGNS
human Smad3 derived peptide: IPEXPPPG

Data sets:
Data typeCount
13C chemical shifts65
15N chemical shifts42
1H chemical shifts269

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PIN11
2Smad32

Entities:

Entity 1, PIN1 36 residues - 4231.730 Da.

1   LYSLEUPROPROGLYTRPGLULYSARGMET
2   SERARGSERSERGLYARGVALTYRTYRPHE
3   ASNHISILETHRASNALASERGLNTRPGLU
4   ARGPROSERGLYASNSER

Entity 2, Smad3 8 residues - 886.891 Da.

1   ILEPROGLUTPOPROPROPROGLY

Samples:

H: PIN1 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: PIN1, [U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: PIN1, [U-100% 13C; U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.420 M; pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYHisotropicsample_conditions_1
2D 1H-1H TOCSYHisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCACB15N13Cisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16070 16088 19258 19259 25569
PDB
DBJ BAA87037 BAA87038 BAB22270 BAB22743 BAC35631
EMBL CAG28582
GB AAC50492 AAH02899 AAH38254 AAI12584 AAV38138
PRF 2209428A
REF NP_001029804 NP_001231300 NP_001270625 NP_006212 NP_075860
SP Q13526 Q4R383 Q5BIN5 Q9QUR7
TPG DAA28013
AlphaFold Q13526 Q4R383 Q5BIN5 Q9QUR7 Q15796

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