+Open data
-Basic information
Entry | Database: PDB / ID: 2hmx | |||||||||
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Title | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN | |||||||||
Components | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN | |||||||||
Keywords | MATRIX PROTEIN / HIV-1 P17 / HIV-1 MA | |||||||||
Function / homology | Function and homology information HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency ...HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA stem-loop binding / symbiont-mediated suppression of host gene expression / RNA-directed DNA polymerase activity / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral nucleocapsid / aspartic-type endopeptidase activity / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / symbiont entry into host cell / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / membrane Similarity search - Function | |||||||||
Biological species | Human immunodeficiency virus 1 | |||||||||
Method | SOLUTION NMR | |||||||||
Authors | Massiah, M.A. / Starich, M.R. / Paschall, C. / Christensen, A.M. / Sundquist, W.I. / Summers, M.F. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein. Authors: Massiah, M.A. / Starich, M.R. / Paschall, C. / Summers, M.F. / Christensen, A.M. / Sundquist, W.I. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hmx.cif.gz | 827.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hmx.ent.gz | 687.2 KB | Display | PDB format |
PDBx/mmJSON format | 2hmx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hmx_validation.pdf.gz | 355.7 KB | Display | wwPDB validaton report |
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Full document | 2hmx_full_validation.pdf.gz | 560.4 KB | Display | |
Data in XML | 2hmx_validation.xml.gz | 82 KB | Display | |
Data in CIF | 2hmx_validation.cif.gz | 107.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hm/2hmx ftp://data.pdbj.org/pub/pdb/validation_reports/hm/2hmx | 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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Atom site foot note | 1: VAL 8 - LEU 9 MODEL 14 OMEGA = 211.55 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: LEU 32 - LYS 33 MODEL 15 OMEGA = 148.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLN 29 - TYR 30 MODEL 16 OMEGA = 142.28 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: LYS 27 - LYS 28 MODEL 17 OMEGA = 149.30 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: GLN 29 - TYR 30 MODEL 18 OMEGA = 134.10 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: LYS 27 - LYS 28 MODEL 19 OMEGA = 148.11 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: GLN 29 - TYR 30 MODEL 19 OMEGA = 149.16 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 15003.958 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Cell line: BL21 / Plasmid: WISP93-93 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P12497 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other |
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-Processing
NMR software | Name: DSPACE / Developer: BIOSYM / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 20 |