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Yorodumi- PDB-1hum: SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MUL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hum | ||||||
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Title | SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER | ||||||
Components | HUMAN MACROPHAGE INFLAMMATORY PROTEIN 1 BETA | ||||||
Keywords | CYTOKINE(CHEMOTACTIC) | ||||||
Function / homology | Function and homology information CCR1 chemokine receptor binding / positive regulation of natural killer cell chemotaxis / CCR5 chemokine receptor binding / CCR chemokine receptor binding / lymphocyte chemotaxis / positive regulation of calcium ion transport / eosinophil chemotaxis / chemokine-mediated signaling pathway / Chemokine receptors bind chemokines / chemokine activity ...CCR1 chemokine receptor binding / positive regulation of natural killer cell chemotaxis / CCR5 chemokine receptor binding / CCR chemokine receptor binding / lymphocyte chemotaxis / positive regulation of calcium ion transport / eosinophil chemotaxis / chemokine-mediated signaling pathway / Chemokine receptors bind chemokines / chemokine activity / establishment or maintenance of cell polarity / Interleukin-10 signaling / monocyte chemotaxis / negative regulation by host of viral transcription / cellular response to interleukin-1 / positive regulation of calcium-mediated signaling / neutrophil chemotaxis / cytokine activity / response to virus / response to toxic substance / cellular response to type II interferon / cell-cell signaling / cellular response to tumor necrosis factor / G alpha (i) signalling events / positive regulation of ERK1 and ERK2 cascade / cell adhesion / immune response / inflammatory response / G protein-coupled receptor signaling pathway / signal transduction / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Clore, G.M. / Lodi, P.J. / Garrett, D.S. / Gronenborn, A.M. | ||||||
Citation | Journal: Science / Year: 1994 Title: High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR. Authors: Lodi, P.J. / Garrett, D.S. / Kuszewski, J. / Tsang, M.L. / Weatherbee, J.A. / Leonard, W.J. / Gronenborn, A.M. / Clore, G.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hum.cif.gz | 53 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hum.ent.gz | 43.1 KB | Display | PDB format |
PDBx/mmJSON format | 1hum.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hu/1hum ftp://data.pdbj.org/pub/pdb/validation_reports/hu/1hum | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7824.742 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P13236 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Refinement | Software ordinal: 1 Details: RESTRAINED MINIMIZED AVERAGE STRUCTURE OVER 35 FILES AVE.RMS DIFF. TO MEAN FOR BACKBONE (4-69)= 0.304637 ANGSTROMS AVE.RMS DIFF. TO MEAN FOR ALL ORDERED NON-H-ATOMS (4-69)= 0.45 ANGSTROMS ...Details: RESTRAINED MINIMIZED AVERAGE STRUCTURE OVER 35 FILES AVE.RMS DIFF. TO MEAN FOR BACKBONE (4-69)= 0.304637 ANGSTROMS AVE.RMS DIFF. TO MEAN FOR ALL ORDERED NON-H-ATOMS (4-69)= 0.45 ANGSTROMS AVE.RMS DIFF. TO MEAN FOR ALL NON-H-ATOMS (4-69)= 0.706906 ANGSTROMS THE 3D STRUCTURE OF THE HMIP-1BETA DIMER IN SOLUTION BY NMR IS BASED ON 3586 EXPERIMENTAL RESTRAINTS COMPRISING: 3132 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS OF WHICH 228 ARE INTERSUBUNIT; 24 RESTRAINTS FOR 12 H-BONDS INVOLVING TIGHTLY BOUND WATER MOLECULES; 108 RESTRAINTS FOR 54 BACKBONE HYDROGEN BONDS INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 220 TORSION ANGLE RESTRAINTS (122 PHI, 10 PSI, 80 CHI1 AND 8 CHI2); AND 102 HN-HALPHA THREE-BOND COUPLING CONSTANTS. A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS AND 1H, 13C AND 15N ASSIGNMENTS ARE AVAILABLE FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. & GRONENBORN, A.M. (1988) FEBS LETT 229, 317-324. ALL STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE. THIS ENTRY CORRESPONDS TO THE RESTRAINED MINIMIZED AVERAGE STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 35 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES A 4 - A 69 (CHAIN A) AND B 4 - B 69 (CHAIN B), AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE FIELD THAT CONTAINS THE B VALUE IN X-RAY STRUCTURES (COLUMNS 61 - 66) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. |
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NMR ensemble | Conformers submitted total number: 1 |