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Open data
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Basic information
Entry | Database: PDB / ID: 2erl | |||||||||
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Title | PHEROMONE ER-1 FROM | |||||||||
![]() | MATING PHEROMONE ER-1 | |||||||||
![]() | PHEROMONE | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Anderson, D.H. / Weiss, M.S. / Eisenberg, D. | |||||||||
![]() | ![]() Title: A challenging case for protein crystal structure determination: the mating pheromone Er-1 from Euplotes raikovi. Authors: Anderson, D.H. / Weiss, M.S. / Eisenberg, D. #1: ![]() Title: A Cooperative Model for Receptor Recognition and Cell Adhesion: Evidence from the Molecular Packing in the 1.6-A Crystal Structure of the Pheromone Er-1 from the Ciliated Protozoan Euplotes Raikovi Authors: Weiss, M.S. / Anderson, D.H. / Raffioni, S. / Bradshaw, R.A. / Ortenzi, C. / Luporini, P. / Eisenberg, D. #2: ![]() Title: The NMR Solution Structure of the Pheromone Er-1 from the Ciliated Protozoan Euplotes Raikovi Authors: Mronga, S. / Luginbuhl, P. / Brown, L.R. / Ortenzi, C. / Luporini, P. / Bradshaw, R.A. / Wuthrich, K. #3: ![]() Title: Crystallization of the Euplotes Raikovi Mating Pheromone Er-1 Authors: Anderson, D. / Raffioni, S. / Luporini, P. / Bradshaw, R.A. / Eisenberg, D. #4: ![]() Title: Primary Structure of the Mating Pheromone Er-1 of the Ciliate Euplotes Raikovi Authors: Raffioni, S. / Luporini, P. / Chait, B.T. / Disper, S.S. / Bradshaw, R.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 38.5 KB | Display | ![]() |
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PDB format | ![]() | 27 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 416.4 KB | Display | ![]() |
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Full document | ![]() | 416.4 KB | Display | |
Data in XML | ![]() | 4.3 KB | Display | |
Data in CIF | ![]() | 5.1 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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Unit cell |
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Components
#1: Protein/peptide | Mass: 4417.881 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Chemical | ChemComp-EOH / |
#3: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.53 Å3/Da / Density % sol: 19.6 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 20 % | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 298-301 K / pH: 3.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 0.7107 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 20, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.7107 Å / Relative weight: 1 |
Reflection | Resolution: 1→25.26 Å / Num. obs: 13659 / % possible obs: 93.8 % / Observed criterion σ(I): 0 / Redundancy: 7.5 % / Rmerge(I) obs: 0.054 |
Reflection | *PLUS Lowest resolution: 8 Å / Num. obs: 13461 / % possible obs: 92.4 % / Num. measured all: 101188 |
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Processing
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Refinement | Resolution: 1→25.25 Å / Num. parameters: 3121 / Num. restraintsaints: 3883 / σ(F): 0 Stereochemistry target values: ENGH AND HUBER (1991) ACTA CRYST. A47, 392-400 Details: ANISOTROPIC TEMPERATURE FACTORS HAVE BEEN REFINED FOR THE NON-HYDROGEN ATOMS IN THIS ENTRY. HYDROGEN ATOMS HAVE ISOTROPIC U'S THAT ARE 1.2 TIMES THE ISOTROPIC U'S OF THE ATOMS ON WHICH THEY ...Details: ANISOTROPIC TEMPERATURE FACTORS HAVE BEEN REFINED FOR THE NON-HYDROGEN ATOMS IN THIS ENTRY. HYDROGEN ATOMS HAVE ISOTROPIC U'S THAT ARE 1.2 TIMES THE ISOTROPIC U'S OF THE ATOMS ON WHICH THEY RIDE. THE QUANTITIES ON THE ANISOU RECORD FOR EACH HYDROGEN ATOM ARE THE EQUIVALENT-TO-ISOTROPIC U'S.
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Solvent computation | Solvent model: DRIESSEN, ET AL., (1989) J.APPL.CRYST. 22, 510-516 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 4 / Occupancy sum non hydrogen: 1 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1→25.25 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 93 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.129 / Lowest resolution: 26 Å / % reflection Rfree: 10 % / Rfactor obs: 0.1292 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_plane_restr / Dev ideal: 0.206 |