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Yorodumi- PDB-6rlx: X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6rlx | |||||||||
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Title | X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS | |||||||||
Components |
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Keywords | HORMONE(MUSCLE RELAXANT) | |||||||||
Function / homology | Function and homology information Relaxin receptors / regulation of catalytic activity / female pregnancy / hormone activity / positive regulation of angiogenesis / G alpha (s) signalling events / positive regulation of gene expression / extracellular region Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.5 Å | |||||||||
Authors | Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 Title: X-ray structure of human relaxin at 1.5 A. Comparison to insulin and implications for receptor binding determinants. Authors: Eigenbrot, C. / Randal, M. / Quan, C. / Burnier, J. / O'Connell, L. / Rinderknecht, E. / Kossiakoff, A.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6rlx.cif.gz | 33.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6rlx.ent.gz | 23.4 KB | Display | PDB format |
PDBx/mmJSON format | 6rlx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6rlx_validation.pdf.gz | 438.2 KB | Display | wwPDB validaton report |
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Full document | 6rlx_full_validation.pdf.gz | 443 KB | Display | |
Data in XML | 6rlx_validation.xml.gz | 8.1 KB | Display | |
Data in CIF | 6rlx_validation.cif.gz | 10.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/6rlx ftp://data.pdbj.org/pub/pdb/validation_reports/rl/6rlx | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: WATERS 402, 404, 508, 509, AND 542 SHARE SOME DISTANCES TOO SHORT FOR INDEPENDENT MOLECULES. THEY MAY REPRESENT AN INCOMPLETELY RESOLVED CITRATE ION. FOR WATERS 403, 442, 502, 510, AND 541, THE ...1: WATERS 402, 404, 508, 509, AND 542 SHARE SOME DISTANCES TOO SHORT FOR INDEPENDENT MOLECULES. THEY MAY REPRESENT AN INCOMPLETELY RESOLVED CITRATE ION. FOR WATERS 403, 442, 502, 510, AND 541, THE SAME APPLIES. THESE PSEUDO-TWO-FOLD RELATED CLUSTERS ARE FOUND NEAR THE N-TERMINI OF THE A-CHAINS. | ||||||||
Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.830125, 0.207228, -0.517638), Vector: Details | PSEUDO TWO-FOLD CALCULATED FROM C ALPHA PORTIONS A 6 - A 20 AND B 7 - B 19 AND THE CORRESPONDING ATOMS OF MOLECULE 2. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAINS *C* AND *D* WHEN APPLIED TO CHAINS *A* AND *B*, RESPECTIVELY. | |
-Components
#1: Protein/peptide | Mass: 2661.178 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P04090 #2: Protein/peptide | Mass: 3200.797 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P04090 #3: Water | ChemComp-HOH / | Sequence details | NUMBERING OF THE RESIDUES IS BASED ON INSULIN (EG. 1INS OF PROTEIN DATA BANK). WEAK OR NONEXISTENT ...NUMBERING OF THE RESIDUES IS BASED ON INSULIN (EG. 1INS OF PROTEIN DATA BANK). WEAK OR NONEXISTEN | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.07 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.5 Å / Num. obs: 13471 / Num. measured all: 50106 / Rmerge(I) obs: 0.063 |
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-Processing
Software |
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Refinement | Rfactor Rwork: 0.187 / Rfactor obs: 0.187 / Highest resolution: 1.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 8 Å / Rfactor obs: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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