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Database: PDB
Entry: 3OED
LinkDB: 3OED
Original site: 3OED 
HEADER    IMMUNE SYSTEM                           12-AUG-10   3OED              
TITLE     THE STRUCTURE OF THE COMPLEX BETWEEN COMPLEMENT RECEPTOR CR2 AND ITS  
TITLE    2 LIGAND COMPLEMENT FRAGMENT C3D                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C3;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C3 (UNP RESIDUES 996-1303);                                
COMPND   5 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   6 PROTEIN 1;                                                           
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COMPLEMENT RECEPTOR TYPE 2;                                
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: CR2 (UNP RESIDUES 20-153);                                 
COMPND  13 SYNONYM: CR2, COMPLEMENT C3D RECEPTOR, EPSTEIN-BARR VIRUS RECEPTOR,  
COMPND  14 EBV RECEPTOR;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: C3, CPAMD1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: C3DR, CR2;                                                     
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B;                               
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PLASMID                                    
KEYWDS    COMPLEMENT RECEPTOR, COMPLEMENT FRAGMENT C3D, B CELL, IMMUNE SYSTEM   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.ISENMAN,J.M.H.VAN DEN ELSEN                                       
REVDAT   2   28-MAR-12 3OED    1       JRNL   VERSN                             
REVDAT   1   11-MAY-11 3OED    0                                                
JRNL        AUTH   J.M.VAN DEN ELSEN,D.E.ISENMAN                                
JRNL        TITL   A CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN COMPLEMENT  
JRNL        TITL 2 RECEPTOR 2 AND ITS LIGAND C3D.                               
JRNL        REF    SCIENCE                       V. 332   608 2011              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   21527715                                                     
JRNL        DOI    10.1126/SCIENCE.1201954                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17131                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 919                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.16                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1236                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6612                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 16                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.518         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.408         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.607        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6780 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9204 ; 1.446 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   844 ; 5.808 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   286 ;36.538 ;24.406       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1146 ;20.348 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;21.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1008 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5118 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5485 -21.6283 -57.6528              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0356 T22:    .0374                                     
REMARK   3      T33:    .0706 T12:   -.0249                                     
REMARK   3      T13:    .0058 T23:   -.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6733 L22:   1.1947                                     
REMARK   3      L33:   1.5979 L12:   -.1087                                     
REMARK   3      L13:   -.3750 L23:    .1621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0640 S12:   -.0224 S13:    .0424                       
REMARK   3      S21:    .0112 S22:    .0169 S23:   -.0768                       
REMARK   3      S31:   -.0471 S32:    .0299 S33:   -.0810                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   129                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.9277 -30.7946 -64.3885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0663 T22:    .0778                                     
REMARK   3      T33:    .0424 T12:   -.0124                                     
REMARK   3      T13:   -.0081 T23:   -.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .9914 L22:    .9521                                     
REMARK   3      L33:    .8644 L12:    .4032                                     
REMARK   3      L13:   -.0763 L23:    .1367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0150 S12:   -.0218 S13:    .0644                       
REMARK   3      S21:    .0360 S22:   -.0178 S23:    .0016                       
REMARK   3      S31:   -.0673 S32:   -.0343 S33:    .0028                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.2294 -71.6467 -68.5768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0343 T22:    .1026                                     
REMARK   3      T33:    .0466 T12:   -.0558                                     
REMARK   3      T13:   -.0160 T23:    .0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7974 L22:   1.3434                                     
REMARK   3      L33:   1.2472 L12:   -.0367                                     
REMARK   3      L13:    .0244 L23:    .0098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0613 S12:   -.1234 S13:   -.0323                       
REMARK   3      S21:    .0968 S22:   -.0475 S23:   -.1051                       
REMARK   3      S31:    .0135 S32:   -.0300 S33:   -.0138                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     0        D   129                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4993 -60.3752 -69.7465              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0368 T22:    .0657                                     
REMARK   3      T33:    .1770 T12:   -.0388                                     
REMARK   3      T13:   -.0443 T23:   -.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7430 L22:   2.2627                                     
REMARK   3      L33:    .6528 L12:    .1086                                     
REMARK   3      L13:    .3326 L23:    .4861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .1756 S12:   -.1093 S13:   -.3649                       
REMARK   3      S21:    .0161 S22:    .0865 S23:   -.2545                       
REMARK   3      S31:    .1116 S32:   -.0646 S33:   -.2620                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3OED COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061009.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.91000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.200                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1C3D                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 20% POLY ETHYLENE GLYCOL   
REMARK 280  6000, 200 MM CACL2, PH 7.0, VAPOR DIFFUSION, HANGING DROP           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       73.06000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.18121            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       84.35333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       73.06000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       42.18121            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       84.35333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       73.06000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       42.18121            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       84.35333            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       73.06000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       42.18121            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       84.35333            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       73.06000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       42.18121            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       84.35333            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       73.06000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       42.18121            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       84.35333            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       84.36242            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      168.70667            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       84.36242            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      168.70667            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       84.36242            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      168.70667            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       84.36242            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      168.70667            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       84.36242            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      168.70667            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       84.36242            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      168.70667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LEU A   299                                                      
REMARK 465     ASN A   300                                                      
REMARK 465     LEU A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     LEU A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     PRO A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     PHE C   130                                                      
REMARK 465     PRO C   131                                                      
REMARK 465     LEU C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     GLN B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     LEU B   299                                                      
REMARK 465     ASN B   300                                                      
REMARK 465     LEU B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     VAL B   303                                                      
REMARK 465     SER B   304                                                      
REMARK 465     LEU B   305                                                      
REMARK 465     GLN B   306                                                      
REMARK 465     LEU B   307                                                      
REMARK 465     PRO B   308                                                      
REMARK 465     SER B   309                                                      
REMARK 465     ARG B   310                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     PHE D   130                                                      
REMARK 465     PRO D   131                                                      
REMARK 465     LEU D   132                                                      
REMARK 465     GLU D   133                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE C   1    CG1  CG2  CD1                                       
REMARK 470     ILE D   1    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 230   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LEU D  44   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ASP D  52   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  39       -4.21     67.27                                   
REMARK 500    GLN A  40       24.30    -66.23                                   
REMARK 500    SER A  71       17.50     80.81                                   
REMARK 500    ASP A 181      -84.05    -43.59                                   
REMARK 500    ASP A 223       24.57     81.70                                   
REMARK 500    ASN A 225       -4.99   -160.92                                   
REMARK 500    PRO A 230       -6.60    -33.05                                   
REMARK 500    ALA A 293      105.90    -56.77                                   
REMARK 500    PRO C   7      138.99    -39.64                                   
REMARK 500    TYR C  17     -166.51   -111.74                                   
REMARK 500    GLU C  40      131.59    -39.95                                   
REMARK 500    VAL C  51      -53.29   -143.13                                   
REMARK 500    ILE C  82     -101.78    -88.56                                   
REMARK 500    THR C 100      137.92    -38.33                                   
REMARK 500    ASN C 115       30.26    -91.62                                   
REMARK 500    ASN C 116       14.34     51.09                                   
REMARK 500    GLU B  39       56.02     36.26                                   
REMARK 500    ILE B 115      -73.13    -49.90                                   
REMARK 500    HIS B 133       68.73    -64.14                                   
REMARK 500    LYS B 162      -74.58    -39.52                                   
REMARK 500    ASP B 163      -58.68    -14.16                                   
REMARK 500    GLU B 166      -75.77    -47.09                                   
REMARK 500    LYS B 224       44.50     30.43                                   
REMARK 500    PRO B 230       89.56    -63.39                                   
REMARK 500    LYS B 251       16.52     81.64                                   
REMARK 500    ASP B 252       84.02    -64.89                                   
REMARK 500    ARG B 267       62.46     35.16                                   
REMARK 500    ALA B 293      108.64    -58.84                                   
REMARK 500    SER D  32     -179.20    -69.56                                   
REMARK 500    VAL D  51      -60.33   -138.70                                   
REMARK 500    PRO D  72      176.60    -43.58                                   
REMARK 500    ILE D  82      -58.54   -126.18                                   
REMARK 500    ARG D  83       74.00   -106.56                                   
REMARK 500    ASN D 115       19.51    -61.66                                   
REMARK 500    ASN D 116       13.53     55.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C3D   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE COMPLEMENT FRAGMENT C3D                             
REMARK 900 RELATED ID: 1GHQ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE COMPLEX BETWEEN CR2 AND C3D WITH ANOTHER            
REMARK 900 (NON-PHYSIOLOGICALLY RELEVANT) BINDING MODE                          
DBREF  3OED A    3   310  UNP    P01024   CO3_HUMAN      996   1303             
DBREF  3OED C    0   133  UNP    P20023   CR2_HUMAN       20    153             
DBREF  3OED B    3   310  UNP    P01024   CO3_HUMAN      996   1303             
DBREF  3OED D    0   133  UNP    P20023   CR2_HUMAN       20    153             
SEQADV 3OED MET A    1  UNP  P01024              EXPRESSION TAG                 
SEQADV 3OED LEU A    2  UNP  P01024              EXPRESSION TAG                 
SEQADV 3OED ALA A   17  UNP  P01024    CYS  1010 ENGINEERED MUTATION            
SEQADV 3OED MET C   -1  UNP  P20023              INITIATING METHIONINE          
SEQADV 3OED MET B    1  UNP  P01024              EXPRESSION TAG                 
SEQADV 3OED LEU B    2  UNP  P01024              EXPRESSION TAG                 
SEQADV 3OED ALA B   17  UNP  P01024    CYS  1010 ENGINEERED MUTATION            
SEQADV 3OED MET D   -1  UNP  P20023              INITIATING METHIONINE          
SEQRES   1 A  310  MET LEU ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR          
SEQRES   2 A  310  PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR          
SEQRES   3 A  310  PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU          
SEQRES   4 A  310  GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA          
SEQRES   5 A  310  LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA          
SEQRES   6 A  310  PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS          
SEQRES   7 A  310  ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS          
SEQRES   8 A  310  VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER          
SEQRES   9 A  310  GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU          
SEQRES  10 A  310  LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO          
SEQRES  11 A  310  VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN          
SEQRES  12 A  310  ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE          
SEQRES  13 A  310  SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL          
SEQRES  14 A  310  ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE          
SEQRES  15 A  310  LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR          
SEQRES  16 A  310  VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG          
SEQRES  17 A  310  LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA          
SEQRES  18 A  310  LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU          
SEQRES  19 A  310  TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU          
SEQRES  20 A  310  LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL          
SEQRES  21 A  310  ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR          
SEQRES  22 A  310  GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU          
SEQRES  23 A  310  ALA GLN TYR GLN LYS ASP ALA PRO ASP HIS GLN GLU LEU          
SEQRES  24 A  310  ASN LEU ASP VAL SER LEU GLN LEU PRO SER ARG                  
SEQRES   1 C  135  MET GLY ILE SER CYS GLY SER PRO PRO PRO ILE LEU ASN          
SEQRES   2 C  135  GLY ARG ILE SER TYR TYR SER THR PRO ILE ALA VAL GLY          
SEQRES   3 C  135  THR VAL ILE ARG TYR SER CYS SER GLY THR PHE ARG LEU          
SEQRES   4 C  135  ILE GLY GLU LYS SER LEU LEU CYS ILE THR LYS ASP LYS          
SEQRES   5 C  135  VAL ASP GLY THR TRP ASP LYS PRO ALA PRO LYS CYS GLU          
SEQRES   6 C  135  TYR PHE ASN LYS TYR SER SER CYS PRO GLU PRO ILE VAL          
SEQRES   7 C  135  PRO GLY GLY TYR LYS ILE ARG GLY SER THR PRO TYR ARG          
SEQRES   8 C  135  HIS GLY ASP SER VAL THR PHE ALA CYS LYS THR ASN PHE          
SEQRES   9 C  135  SER MET ASN GLY ASN LYS SER VAL TRP CYS GLN ALA ASN          
SEQRES  10 C  135  ASN MET TRP GLY PRO THR ARG LEU PRO THR CYS VAL SER          
SEQRES  11 C  135  VAL PHE PRO LEU GLU                                          
SEQRES   1 B  310  MET LEU ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR          
SEQRES   2 B  310  PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR          
SEQRES   3 B  310  PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU          
SEQRES   4 B  310  GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA          
SEQRES   5 B  310  LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA          
SEQRES   6 B  310  PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS          
SEQRES   7 B  310  ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS          
SEQRES   8 B  310  VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER          
SEQRES   9 B  310  GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU          
SEQRES  10 B  310  LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO          
SEQRES  11 B  310  VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN          
SEQRES  12 B  310  ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE          
SEQRES  13 B  310  SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL          
SEQRES  14 B  310  ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE          
SEQRES  15 B  310  LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR          
SEQRES  16 B  310  VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG          
SEQRES  17 B  310  LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA          
SEQRES  18 B  310  LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU          
SEQRES  19 B  310  TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU          
SEQRES  20 B  310  LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL          
SEQRES  21 B  310  ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR          
SEQRES  22 B  310  GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU          
SEQRES  23 B  310  ALA GLN TYR GLN LYS ASP ALA PRO ASP HIS GLN GLU LEU          
SEQRES  24 B  310  ASN LEU ASP VAL SER LEU GLN LEU PRO SER ARG                  
SEQRES   1 D  135  MET GLY ILE SER CYS GLY SER PRO PRO PRO ILE LEU ASN          
SEQRES   2 D  135  GLY ARG ILE SER TYR TYR SER THR PRO ILE ALA VAL GLY          
SEQRES   3 D  135  THR VAL ILE ARG TYR SER CYS SER GLY THR PHE ARG LEU          
SEQRES   4 D  135  ILE GLY GLU LYS SER LEU LEU CYS ILE THR LYS ASP LYS          
SEQRES   5 D  135  VAL ASP GLY THR TRP ASP LYS PRO ALA PRO LYS CYS GLU          
SEQRES   6 D  135  TYR PHE ASN LYS TYR SER SER CYS PRO GLU PRO ILE VAL          
SEQRES   7 D  135  PRO GLY GLY TYR LYS ILE ARG GLY SER THR PRO TYR ARG          
SEQRES   8 D  135  HIS GLY ASP SER VAL THR PHE ALA CYS LYS THR ASN PHE          
SEQRES   9 D  135  SER MET ASN GLY ASN LYS SER VAL TRP CYS GLN ALA ASN          
SEQRES  10 D  135  ASN MET TRP GLY PRO THR ARG LEU PRO THR CYS VAL SER          
SEQRES  11 D  135  VAL PHE PRO LEU GLU                                          
FORMUL   5  HOH   *16(H2 O)                                                     
HELIX    1   1 ASP A    3  ILE A   11  5                                   9    
HELIX    2   2 GLU A   19  THR A   38  1                                  20    
HELIX    3   3 GLU A   47  ALA A   65  1                                  19    
HELIX    4   4 SER A   82  VAL A   97  1                                  16    
HELIX    5   5 SER A  104  GLN A  119  1                                  16    
HELIX    6   6 ILE A  137  ASN A  142  5                                   6    
HELIX    7   7 GLU A  145  GLU A  166  1                                  22    
HELIX    8   8 SER A  171  MET A  188  1                                  18    
HELIX    9   9 ARG A  192  MET A  206  1                                  15    
HELIX   10  10 LYS A  210  ALA A  221  1                                  12    
HELIX   11  11 LYS A  232  LYS A  251  1                                  20    
HELIX   12  12 VAL A  256  GLU A  265  1                                  10    
HELIX   13  13 GLY A  274  ALA A  293  1                                  20    
HELIX   14  14 ASP B    3  ILE B   11  5                                   9    
HELIX   15  15 GLU B   19  THR B   38  1                                  20    
HELIX   16  16 GLN B   40  GLY B   45  1                                   6    
HELIX   17  17 GLU B   47  ALA B   65  1                                  19    
HELIX   18  18 SER B   82  VAL B   97  1                                  16    
HELIX   19  19 SER B  104  GLN B  119  1                                  16    
HELIX   20  20 HIS B  133  ASN B  142  5                                  10    
HELIX   21  21 GLU B  145  GLU B  166  1                                  22    
HELIX   22  22 SER B  171  MET B  188  1                                  18    
HELIX   23  23 ARG B  192  MET B  206  1                                  15    
HELIX   24  24 GLY B  211  THR B  219  1                                   9    
HELIX   25  25 ALA B  221  ASN B  225  5                                   5    
HELIX   26  26 LYS B  232  LYS B  251  1                                  20    
HELIX   27  27 PHE B  255  GLN B  266  1                                  12    
HELIX   28  28 SER B  275  ALA B  293  1                                  19    
SHEET    1   A 3 ILE A 102  ASP A 103  0                                        
SHEET    2   A 3 THR C  25  CYS C  31 -1  O  VAL C  26   N  ILE A 102           
SHEET    3   A 3 GLY C  12  ILE C  14 -1  N  ARG C  13   O  SER C  30           
SHEET    1   B 4 ILE A 102  ASP A 103  0                                        
SHEET    2   B 4 THR C  25  CYS C  31 -1  O  VAL C  26   N  ILE A 102           
SHEET    3   B 4 SER C  42  ILE C  46 -1  O  LEU C  43   N  ILE C  27           
SHEET    4   B 4 THR C  54  TRP C  55 -1  O  THR C  54   N  ILE C  46           
SHEET    1   C 2 SER C   2  CYS C   3  0                                        
SHEET    2   C 2 ILE C  21  ALA C  22 -1  O  ILE C  21   N  CYS C   3           
SHEET    1   D 2 PHE C  35  ILE C  38  0                                        
SHEET    2   D 2 LYS C  61  TYR C  64 -1  O  GLU C  63   N  ARG C  36           
SHEET    1   E 4 GLY C  79  LYS C  81  0                                        
SHEET    2   E 4 SER C  93  CYS C  98 -1  O  ALA C  97   N  TYR C  80           
SHEET    3   E 4 SER C 109  CYS C 112 -1  O  VAL C 110   N  VAL C  94           
SHEET    4   E 4 TRP C 118  GLY C 119 -1  O  GLY C 119   N  TRP C 111           
SHEET    1   F 2 SER C 103  ASN C 105  0                                        
SHEET    2   F 2 THR C 125  VAL C 127 -1  O  THR C 125   N  ASN C 105           
SHEET    1   G 3 ILE B 102  ASP B 103  0                                        
SHEET    2   G 3 THR D  25  CYS D  31 -1  O  VAL D  26   N  ILE B 102           
SHEET    3   G 3 GLY D  12  ILE D  14 -1  N  ARG D  13   O  SER D  30           
SHEET    1   H 4 ILE B 102  ASP B 103  0                                        
SHEET    2   H 4 THR D  25  CYS D  31 -1  O  VAL D  26   N  ILE B 102           
SHEET    3   H 4 SER D  42  ILE D  46 -1  O  LEU D  43   N  ILE D  27           
SHEET    4   H 4 THR D  54  TRP D  55 -1  O  THR D  54   N  ILE D  46           
SHEET    1   I 2 SER D   2  CYS D   3  0                                        
SHEET    2   I 2 ILE D  21  ALA D  22 -1  O  ILE D  21   N  CYS D   3           
SHEET    1   J 2 PHE D  35  ILE D  38  0                                        
SHEET    2   J 2 LYS D  61  TYR D  64 -1  O  GLU D  63   N  ARG D  36           
SHEET    1   K 2 GLY D  79  LYS D  81  0                                        
SHEET    2   K 2 PHE D  96  CYS D  98 -1  O  ALA D  97   N  TYR D  80           
SHEET    1   L 2 PHE D 102  ASN D 105  0                                        
SHEET    2   L 2 THR D 125  SER D 128 -1  O  VAL D 127   N  SER D 103           
SHEET    1   M 2 TRP D 111  CYS D 112  0                                        
SHEET    2   M 2 TRP D 118  GLY D 119 -1  O  GLY D 119   N  TRP D 111           
SSBOND   1 CYS A  108    CYS A  165                          1555   1555  2.07  
SSBOND   2 CYS C    3    CYS C   45                          1555   1555  2.04  
SSBOND   3 CYS C   31    CYS C   62                          1555   1555  2.04  
SSBOND   4 CYS C   71    CYS C  112                          1555   1555  2.03  
SSBOND   5 CYS C   98    CYS C  126                          1555   1555  2.08  
SSBOND   6 CYS B  108    CYS B  165                          1555   1555  2.06  
SSBOND   7 CYS D    3    CYS D   45                          1555   1555  2.04  
SSBOND   8 CYS D   31    CYS D   62                          1555   1555  2.05  
SSBOND   9 CYS D   71    CYS D  112                          1555   1555  2.05  
SSBOND  10 CYS D   98    CYS D  126                          1555   1555  2.05  
CISPEP   1 THR C   19    PRO C   20          0         4.29                     
CISPEP   2 THR C   86    PRO C   87          0        13.53                     
CISPEP   3 GLY C  119    PRO C  120          0        -2.14                     
CISPEP   4 THR D   19    PRO D   20          0        -8.96                     
CISPEP   5 THR D   86    PRO D   87          0        -4.53                     
CISPEP   6 GLY D  119    PRO D  120          0        -2.61                     
CRYST1  146.120  146.120  253.060  90.00  90.00 120.00 H 3 2        36          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006844  0.003951  0.000000        0.00000                         
SCALE2      0.000000  0.007902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003952        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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