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Yorodumi- PDB-2yhm: Structure of respiratory syncytial virus nucleocapsid protein, P2... -
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Basic information
| Entry | Database: PDB / ID: 2yhm | ||||||
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| Title | Structure of respiratory syncytial virus nucleocapsid protein, P212121 crystal form | ||||||
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Keywords | VIRAL PROTEIN/RNA / VIRAL PROTEIN-RNA COMPLEX | ||||||
| Function / homology | Function and homology informationRespiratory syncytial virus genome transcription / Translation of respiratory syncytial virus mRNAs / symbiont-mediated suppression of host PKR/eIFalpha signaling / helical viral capsid / Respiratory syncytial virus genome replication / RSV-host interactions / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry / protein serine/threonine kinase inhibitor activity ...Respiratory syncytial virus genome transcription / Translation of respiratory syncytial virus mRNAs / symbiont-mediated suppression of host PKR/eIFalpha signaling / helical viral capsid / Respiratory syncytial virus genome replication / RSV-host interactions / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry / protein serine/threonine kinase inhibitor activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / PKR-mediated signaling / Evasion by RSV of host interferon responses / viral capsid / viral nucleocapsid / symbiont-mediated suppression of host NF-kappaB cascade / host cell cytoplasm / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ribonucleoprotein complex / RNA binding Similarity search - Function | ||||||
| Biological species | HUMAN RESPIRATORY SYNCYTIAL VIRUS![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.6 Å | ||||||
Authors | El Omari, K. / Dhaliwal, B. / Ren, J. / Abrescia, N.G.A. / Lockyer, M. / Powell, K.L. / Hawkins, A.R. / Stammers, D.K. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2011Title: Structures of Respiratory Syncytial Virus Nucleocapsid Protein from Two Crystal Forms: Details of Potential Packing Interactions in the Native Helical Form. Authors: El Omari, K. / Dhaliwal, B. / Ren, J. / Abrescia, N.G.A. / Lockyer, M. / Powell, K.L. / Hawkins, A.R. / Stammers, D.K. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2yhm.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb2yhm.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 2yhm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2yhm_validation.pdf.gz | 537.2 KB | Display | wwPDB validaton report |
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| Full document | 2yhm_full_validation.pdf.gz | 618.1 KB | Display | |
| Data in XML | 2yhm_validation.xml.gz | 127.6 KB | Display | |
| Data in CIF | 2yhm_validation.cif.gz | 172.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yh/2yhm ftp://data.pdbj.org/pub/pdb/validation_reports/yh/2yhm | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4v5vC ![]() 2wj8S S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 1 / Auth seq-ID: 1 - 375 / Label seq-ID: 1 - 375
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Components
| #1: Protein | Mass: 41659.820 Da / Num. of mol.: 10 / Fragment: RESIDUES 1-375 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HUMAN RESPIRATORY SYNCYTIAL VIRUS / Strain: A2 / Production host: ![]() #2: RNA chain | | Mass: 21317.777 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() Sequence details | NON SPECIFIC RNA FROM CELLULAR ORIGIN BOUND TO THE NUCLEOPROT | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.08 Å3/Da / Density % sol: 60 % / Description: NONE |
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| Crystal grow | pH: 7 Details: 10% (W/V) PEG 400, 0.1 M KCL, 0.05 M HEPES PH 7.0, 0.01 M CACL2 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9785 |
| Detector | Type: MARRESEARCH / Detector: CCD |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 |
| Reflection | Resolution: 3.6→30 Å / Num. obs: 53027 / % possible obs: 81.7 % / Observed criterion σ(I): 2.5 / Redundancy: 11.2 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 14.1 |
| Reflection shell | Resolution: 3.6→3.73 Å / Redundancy: 10.9 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 2.5 / % possible all: 66.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 2WJ8 Resolution: 3.6→50 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.927 / SU B: 72.231 / SU ML: 0.464 / Cross valid method: THROUGHOUT / ESU R Free: 0.698 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT.
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 102.754 Å2
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| Refinement step | Cycle: LAST / Resolution: 3.6→50 Å
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| Refine LS restraints |
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HUMAN RESPIRATORY SYNCYTIAL VIRUS
X-RAY DIFFRACTION
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