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- PDB-1ps2: HIGH RESOLUTION NMR SOLUTION STRUCTURE OF HUMAN PS2, 19 STRUCTURES -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ps2 | ||||||
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Title | HIGH RESOLUTION NMR SOLUTION STRUCTURE OF HUMAN PS2, 19 STRUCTURES | ||||||
![]() | PS2 | ||||||
![]() | GROWTH FACTOR / CELL MOTILITY / TUMOR SUPPRESSOR / TREFOIL DOMAIN | ||||||
Function / homology | ![]() maintenance of gastrointestinal epithelium / response to iron ion / response to immobilization stress / growth factor activity / response to peptide hormone / Estrogen-dependent gene expression / cell population proliferation / carbohydrate metabolic process / cell differentiation / negative regulation of cell population proliferation ...maintenance of gastrointestinal epithelium / response to iron ion / response to immobilization stress / growth factor activity / response to peptide hormone / Estrogen-dependent gene expression / cell population proliferation / carbohydrate metabolic process / cell differentiation / negative regulation of cell population proliferation / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Williams, M.A. / Polshakov, V.I. / Gargaro, A.R. / Feeney, J. | ||||||
![]() | ![]() Title: High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. Authors: Polshakov, V.I. / Williams, M.A. / Gargaro, A.R. / Frenkiel, T.A. / Westley, B.R. / Chadwick, M.P. / May, F.E. / Feeney, J. #1: ![]() Title: Production and Comparison of Mature Single-Domain 'Trefoil' Peptides Pnr-2/Ps2 Cys58 and Pnr-2/Ps2 Ser58 Authors: Chadwick, M.P. / May, F.E. / Westley, B.R. #2: ![]() Title: NMR-Based Structural Studies of the Pnr-2/Ps2 Single Domain Trefoil Peptide. Similarities to Porcine Spasmolytic Peptide and Evidence for a Monomeric Structure Authors: Polshakov, V.I. / Frenkiel, T.A. / Westley, B. / Chadwick, M. / May, F. / Carr, M.D. / Feeney, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 324.1 KB | Display | ![]() |
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PDB format | ![]() | 280.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 340.2 KB | Display | ![]() |
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Full document | ![]() | 453.2 KB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 30.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 6662.300 Da / Num. of mol.: 1 / Mutation: C58S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: TOTAL NOE CONSTRAINT VIOLATIONS < 1.0 A Conformers calculated total number: 20 / Conformers submitted total number: 19 |