+Open data
-Basic information
Entry | Database: PDB / ID: 1bmo | |||||||||
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Title | BM-40, FS/EC DOMAIN PAIR | |||||||||
Components | BM-40 | |||||||||
Keywords | EXTRACELLULAR MODULE / GLYCOPROTEIN / ANTI-ADHESIVE PROTEIN | |||||||||
Function / homology | Function and homology information Scavenging by Class H Receptors / platelet alpha granule membrane / platelet alpha granule / anatomical structure development / extracellular matrix binding / regulation of cell morphogenesis / negative regulation of endothelial cell proliferation / basement membrane / ECM proteoglycans / Nuclear signaling by ERBB4 ...Scavenging by Class H Receptors / platelet alpha granule membrane / platelet alpha granule / anatomical structure development / extracellular matrix binding / regulation of cell morphogenesis / negative regulation of endothelial cell proliferation / basement membrane / ECM proteoglycans / Nuclear signaling by ERBB4 / endocytic vesicle lumen / collagen binding / negative regulation of angiogenesis / positive regulation of endothelial cell migration / platelet alpha granule lumen / nuclear matrix / Platelet degranulation / collagen-containing extracellular matrix / intracellular membrane-bounded organelle / calcium ion binding / cell surface / extracellular space / extracellular region / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT, 2-FOLD NCS AVERAGING / Resolution: 3.1 Å | |||||||||
Authors | Hohenester, E. / Maurer, P. / Timpl, R. | |||||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. Authors: Hohenester, E. / Maurer, P. / Timpl, R. #1: Journal: Nat.Struct.Biol. / Year: 1996 Title: Structure of a Novel Extracellular Ca(2+)-Binding Module in Bm-40 Authors: Hohenester, E. / Maurer, P. / Hohenadl, C. / Timpl, R. / Jansonius, J.N. / Engel, J. #2: Journal: J.Mol.Biol. / Year: 1995 Title: The C-Terminal Portion of Bm-40 (Sparc/Osteonectin) is an Autonomously Folding and Crystallisable Domain that Binds Calcium and Collagen Iv Authors: Maurer, P. / Hohenadl, C. / Hohenester, E. / Gohring, W. / Timpl, R. / Engel, J. #3: Journal: Faseb J. / Year: 1994 Title: The Biology of Sparc, a Protein that Modulates Cell-Matrix Interactions Authors: Lane, T.F. / Sage, E.H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bmo.cif.gz | 105.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bmo.ent.gz | 83.3 KB | Display | PDB format |
PDBx/mmJSON format | 1bmo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bm/1bmo ftp://data.pdbj.org/pub/pdb/validation_reports/bm/1bmo | HTTPS FTP |
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-Related structure data
Related structure data | 1sraS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS oper:
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-Components
#1: Protein | Mass: 27111.934 Da / Num. of mol.: 2 / Fragment: FS/EC DOMAIN PAIR, RESIDUES 53 - 286 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: 293 / Organ: KIDNEY / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P09486 #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-CA / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 65 % Description: THE R-FACTOR AFTER RIGID-BODY REFINEMENT OF THE TWO EC DOMAINS WAS 0.46 (8-3.1 A) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: HANGING DROP VAPOUR DIFFUSION AT 20 DEG C: 10 MG/ML PROTEIN IN 10 MM TRIS PH 7.5 + 2 MM CACL2; 0.1 M HEPES PH 7.5, 0.15 M NA-ACETATE, 15% PEG4K, vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→25 Å / Num. obs: 14328 / % possible obs: 90.7 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.267 / Mean I/σ(I) obs: 2.7 / % possible all: 85.1 |
Reflection | *PLUS Num. measured all: 47563 |
Reflection shell | *PLUS % possible obs: 85.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT, 2-FOLD NCS AVERAGING Starting model: BM-40 EC DOMAIN (PDB ENTRY 1SRA) Resolution: 3.1→8 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.01 Isotropic thermal model: RESTRAINED INDIVIDUAL WIT NCS RESTRAINTS Cross valid method: FREE R-FACTOR / σ(F): 0 Details: A BULK SOLVENT CORRECTION WAS USED (R=0.25, K=0.33, B=50A**2)
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Displacement parameters | Biso mean: 28 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.1→8 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell | Resolution: 3.1→3.23 Å / Total num. of bins used: 8
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Xplor file |
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