+Open data
-Basic information
Entry | Database: PDB / ID: 1esk | ||||||
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Title | SOLUTION STRUCTURE OF NCP7 FROM HIV-1 | ||||||
Components | GAG POLYPROTEIN | ||||||
Keywords | VIRAL PROTEIN / (12-53)NCp7 / HIV-1 / PROTEIN | ||||||
Function / homology | Function and homology information integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / 2-LTR circle formation / Uncoating of the HIV Virion / Vpr-mediated nuclear import of PICs / Early Phase of HIV Life Cycle / Integration of provirus ...integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / 2-LTR circle formation / Uncoating of the HIV Virion / Vpr-mediated nuclear import of PICs / Early Phase of HIV Life Cycle / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / Binding and entry of HIV virion / viral life cycle / HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / Assembly Of The HIV Virion / retroviral ribonuclease H / exoribonuclease H / Budding and maturation of HIV virion / exoribonuclease H activity / protein processing / host multivesicular body / 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 / peptidase activity / 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 / DNA binding / zinc ion binding / identical protein binding / membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Morellet, N. / Demene, H. / Teilleux, V. / Huynh-Dinh, T. / de Rocquigny, H. / Fournie-Zaluski, M.-C. / Roques, B.P. | ||||||
Citation | Journal: To be Published Title: Solution Structure of (12-53)NCp7 of HIV-1 Authors: Morellet, N. / Demene, H. / Teilleux, V. / Huynh-Dinh, T. / de Rocquigny, H. / Fournie-Zaluski, M.-C. / Roques, B.P. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Conformational Behaviour of the Active and Inactive Forms of the Nucleocapsid NCp7 of HIV-1 Studied by 1H NMR. Authors: Morellet, N. / de Roquigny, H. / Mely, Y. / Jullian, N. / Demene, H. / Ottmann, M. / Gerard, D. / Darlix, J.L. / Fournie-Zaluski, M.C. / Roques, B.P. #2: Journal: J.Mol.Biol. / Year: 1998 Title: Structure of the Complex Between the HIV-1 Nucleocapsid Protein and the Single-stranded Pentanucleotide d(ACGCC). Authors: Morellet, N. / Demene, H. / Teilleux, V. / Huynh-Dinh, T. / de Roquigny, H. / Fournie-Zaluski, M.C. / Roques, B.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1esk.cif.gz | 125.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1esk.ent.gz | 101.9 KB | Display | PDB format |
PDBx/mmJSON format | 1esk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1esk_validation.pdf.gz | 351.1 KB | Display | wwPDB validaton report |
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Full document | 1esk_full_validation.pdf.gz | 391.5 KB | Display | |
Data in XML | 1esk_validation.xml.gz | 7.3 KB | Display | |
Data in CIF | 1esk_validation.cif.gz | 11.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/es/1esk ftp://data.pdbj.org/pub/pdb/validation_reports/es/1esk | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4837.642 Da / Num. of mol.: 1 / Fragment: RESIDUES 12-53 / Source method: obtained synthetically Details: The protein was chemically synthesized. The sequence is naturally found in human immunodeficiency virus type 1 (HIV-1). References: UniProt: P04585 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 2mM (12-53)NCp7, 90%H2O, 10% D2O, pH 6.0 / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: n.a. / pH: 6 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 444 NOE-derived distance constraints | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 9 |