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Yorodumi- PDB-2hcc: SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES -
+Open data
-Basic information
Entry | Database: PDB / ID: 2hcc | ||||||
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Title | SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES | ||||||
Components | HUMAN CHEMOKINE HCC-2 | ||||||
Keywords | CHEMOKINE / HUMAN / HCC-2 / MIP-5 / LEUKOTACTIN-1 / CHEMOTAXIS / CC-CHEMOKINE | ||||||
Function / homology | Function and homology information CCR chemokine receptor binding / lymphocyte chemotaxis / eosinophil chemotaxis / chemokine-mediated signaling pathway / chemokine activity / chemoattractant activity / monocyte chemotaxis / cellular response to interleukin-1 / neutrophil chemotaxis / cellular response to type II interferon ...CCR chemokine receptor binding / lymphocyte chemotaxis / eosinophil chemotaxis / chemokine-mediated signaling pathway / chemokine activity / chemoattractant activity / monocyte chemotaxis / cellular response to interleukin-1 / neutrophil chemotaxis / cellular response to type II interferon / intracellular calcium ion homeostasis / chemotaxis / cell-cell signaling / cellular response to tumor necrosis factor / heparin binding / positive regulation of ERK1 and ERK2 cascade / inflammatory response / G protein-coupled receptor signaling pathway / signaling receptor binding / signal transduction / extracellular space Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Sticht, H. / Escher, S.E. / Schweimer, K. / Forssmann, W.G. / Roesch, P. / Adermann, K. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype. Authors: Sticht, H. / Escher, S.E. / Schweimer, K. / Forssmann, W.G. / Rosch, P. / Adermann, K. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Hcc-2, a Human Chemokine: Gene Structure, Expression Pattern, and Biological Activity Authors: Pardigol, A. / Forssmann, U. / Zucht, H.D. / Loetscher, P. / Schulz-Knappe, P. / Baggiolini, M. / Forssmann, W.G. / Magert, H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hcc.cif.gz | 584.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hcc.ent.gz | 510.2 KB | Display | PDB format |
PDBx/mmJSON format | 2hcc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hc/2hcc ftp://data.pdbj.org/pub/pdb/validation_reports/hc/2hcc | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7222.473 Da / Num. of mol.: 1 / Fragment: RESIDUES 48-113 OF HCC-2 PRECURSOR Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Pichia pastoris (fungus) / References: UniProt: Q16663 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: TWO-DIMENSIONAL 1H-1H |
-Sample preparation
Details | Contents: H2O/D2O(9:1) OR D2O |
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Sample conditions | Ionic strength: 0mM / pH: 3.0 / Pressure: 10E+5 PA atm / Temperature: 298 K |
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, RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 / Details: EXPERIMENTAL RESTRAINTS FOR THE STRUCTURE: | ||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY, AGREEMENT WITH EXPERIMENTAL DATA Conformers calculated total number: 100 / Conformers submitted total number: 30 |