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Open data
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Basic information
Entry | Database: PDB / ID: 2xrc | ||||||
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Title | Human complement factor I | ||||||
![]() | HUMAN COMPLEMENT FACTOR I | ||||||
![]() | IMMUNE SYSTEM / HYDROLASE / CONGLUTINOGEN ACTIVATING FACTOR / SERINE PROTEASE / COMPLEMENT SYSTEM | ||||||
Function / homology | ![]() complement factor I / complement activation, classical pathway / Regulation of Complement cascade / serine-type endopeptidase activity / innate immune response / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Roversi, P. / Johnson, S. / Lea, S.M. | ||||||
![]() | ![]() Title: Structural Basis for Complement Factor I Control and its Disease-Associated Sequence Polymorphisms. Authors: Roversi, P. / Johnson, S. / Caesar, J.J. / Mclean, F. / Leath, K.J. / Tsiftsoglou, S.A. / Morgan, B.P. / Harris, C.L. / Sim, R.B. / Lea, S.M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AI" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AI" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BH" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CI" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DI" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DJ" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 377.8 KB | Display | ![]() |
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PDB format | ![]() | 309.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 501.4 KB | Display | ![]() |
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Full document | ![]() | 538.5 KB | Display | |
Data in XML | ![]() | 66.6 KB | Display | |
Data in CIF | ![]() | 89.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 63537.355 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Chemical | ChemComp-CA / #3: Sugar | ChemComp-NAG / Nonpolymer details | N-ACETYLGLUC | Sequence details | THE PROTEIN IN THIS ENTRY IS THE MATURE FORM OF FACTOR I. THEREFORE THE SIGNAL PEPTIDE (FIRST 18 ...THE PROTEIN IN THIS ENTRY IS THE MATURE FORM OF FACTOR I. THEREFORE THE SIGNAL PEPTIDE (FIRST 18 RESIDUES) OF THE UNIPROT ENTRY IS MISSING FROM THE SAMPLE, AND SO IS THE SEQUENCE RRKR AT RESIDUE NUMBERS 336-339. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 54 % Description: THE CRYSTAL AND DATA WERE TETARTOHEDRALLY TWINNED. |
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Crystal grow | pH: 4 Details: 20.0-23.5% PEG 1500, 0.1M SODIUM SUCCINATE PH 4.0, 1MM CACL2 |
-Data collection
Diffraction | Mean temperature: 120 K | |||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 30, 2009 / Details: MIRRORS | |||||||||||||||||||||||||
Radiation | Monochromator: CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 | |||||||||||||||||||||||||
Reflection twin |
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Reflection | Resolution: 2.65→79 Å / Num. obs: 68978 / % possible obs: 90.8 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 53.4 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 10.5 | |||||||||||||||||||||||||
Reflection shell | Resolution: 2.65→2.79 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 2 / % possible all: 90.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1EKB, 1BY2, 1J8E AND 3B4V Resolution: 2.69→79 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.876 / SU B: 16.144 / SU ML: 0.318 / Cross valid method: THROUGHOUT / ESU R: 0.302 / ESU R Free: 0.07 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED BUT NOT DEPOSITED. TETARTOHEDRAL TWINNING
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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: 43.172 Å2
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Refinement step | Cycle: LAST / Resolution: 2.69→79 Å
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