+Open data
-Basic information
Entry | Database: PDB / ID: 1xqj | ||||||
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Title | 3.10 A Crystal structure of maspin, space group I 4 2 2 | ||||||
Components | Maspin | ||||||
Keywords | ANTITUMOR PROTEIN / SERPIN / MASPIN / TUMOR SUPPRESSION | ||||||
Function / homology | Function and homology information prostate gland morphogenesis / cornified envelope / regulation of epithelial cell proliferation / sarcoplasm / extracellular matrix organization / morphogenesis of an epithelium / serine-type endopeptidase inhibitor activity / extracellular space / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Al-Ayyoubi, M. / Gettins, P.G. / Volz, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Crystal Structure of Human Maspin, a Serpin with Antitumor Properties: Reactive Center Loop of Mapsin is Exposed but Constrained Authors: Al-Ayyoubi, M. / Gettins, P.G. / Volz, K. | ||||||
History |
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Remark 999 | SEQUENCE THE AUTHORS STATE THAT RESIDUES 66, 176, AND 187 WERE VAL, SER, AND VAL IN THE CONSTRUCT, ...SEQUENCE THE AUTHORS STATE THAT RESIDUES 66, 176, AND 187 WERE VAL, SER, AND VAL IN THE CONSTRUCT, WHICH CONFLICTS WITH SWS ENTRY P36952. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xqj.cif.gz | 87.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xqj.ent.gz | 65.6 KB | Display | PDB format |
PDBx/mmJSON format | 1xqj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xqj_validation.pdf.gz | 430.5 KB | Display | wwPDB validaton report |
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Full document | 1xqj_full_validation.pdf.gz | 441.7 KB | Display | |
Data in XML | 1xqj_validation.xml.gz | 17.1 KB | Display | |
Data in CIF | 1xqj_validation.cif.gz | 22.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xq/1xqj ftp://data.pdbj.org/pub/pdb/validation_reports/xq/1xqj | HTTPS FTP |
-Related structure data
Related structure data | 1xqgC 1by7S 1hleS 1ovaS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 43775.551 Da / Num. of mol.: 1 Mutation: C20S, C34A, C183S, C205S, C214S, C287S, C323S, C373S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SERPINB5, PI5 / Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / References: UniProt: P36952 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.9 Å3/Da / Density % sol: 68 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.2 Details: 45% PEG400, SODIUM CITRATE 0.2M, TRIS 0.1M, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 10, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. obs: 11544 / % possible obs: 96.1 % / Redundancy: 5.2 % / Biso Wilson estimate: 72.7 Å2 / Rmerge(I) obs: 0.121 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.64 / Mean I/σ(I) obs: 1.9 / % possible all: 98 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB IDS 1HLE, 1BY7, 1OVA Resolution: 3.1→38.9 Å / Rfactor Rfree error: 0.023 / Data cutoff high absF: 371724.29 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 39.4988 Å2 / ksol: 0.313919 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 74.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.1→38.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.1→3.29 Å / Rfactor Rfree error: 0.211 / Total num. of bins used: 6
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Xplor file |
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