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- PDB-1go9: Monitoring the structural Consequences of Phe12-->D-Phe12 and Leu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1go9 | ||||||
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Title | Monitoring the structural Consequences of Phe12-->D-Phe12 and Leu15-->Aib15 substitution in h/r Corticotropin Releasing Hormone: Implications for Design of CRH antagonists. | ||||||
![]() | CORTICOTROPIN RELEASING HORMONE | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
Model type details | MINIMIZED AVERAGE | ||||||
![]() | Spyroulias, G.A. / Papazacharias, S. / Pairas, G. / Cordopatis, P. | ||||||
![]() | ![]() Title: Monitoring the Structural Consequences of Phe12-->D-Phe and Leu15-->Aib Substitution in Human/Rat Corticotropin Releasing Hormone. Implications for Design of Crh Antagonists. Authors: Spyroulias, G.A. / Papazacharias, S. / Pairas, G. / Cordopatis, P. #1: Journal: Protein Eng. / Year: 1993 Title: Solution Structure of Human Corticotropin Releasing Factor by 1H NMR and Distance Geometry with Restrained Molecular Dynamics. Authors: Romier, C. / Bernassau, J.M. / Cambillau, C. / Darbon, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 19.3 KB | Display | ![]() |
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PDB format | ![]() | 14.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4734.436 Da / Num. of mol.: 1 / Mutation: YES / Source method: obtained synthetically Details: SYNTHETIC ANALOGUE SYNTHESIZED THROUGH SOLID PHASE SYNTHESIS USING FMOC/TBU SYNTHETIC PROTOCOLS. NATIVE PHE12 AND LEU15 HAS BEEN SUBSTITUTED BY D-PHE AND ALPHA-AMINOISOBUTYRIC ACID Source: (synth.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||
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NMR experiment |
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NMR details | Text: MEAN STRUCTURE. THE STRUCTURE WAS DETERMINED USING 1H-1H DOUBLE-RESONANCE NMR SPECTROSCOPY. NMR-DERRIVED DISTANCE RESTRAINTS AND 3JHAHN COUPLING CONSTANTS AS WELL AS H-BOND CONSTRAINTS USED IN ...Text: MEAN STRUCTURE. THE STRUCTURE WAS DETERMINED USING 1H-1H DOUBLE-RESONANCE NMR SPECTROSCOPY. NMR-DERRIVED DISTANCE RESTRAINTS AND 3JHAHN COUPLING CONSTANTS AS WELL AS H-BOND CONSTRAINTS USED IN STRUCTURAL CALCULATION AND REFIMENT PROCEEDURE. |
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Sample preparation
Details | Contents: 34% H2O / 66% TFE |
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Sample conditions | pH: 3.8 / Pressure: 1 atm / Temperature: 310 K |
Crystal grow![]() | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model![]() |
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Processing
NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY SIMULATED ANNEALING IN TORSION ANGLE SPACE Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 40 / Conformers submitted total number: 1 |