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Database: PDB
Entry: 4A5W
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Original site: 4A5W 
HEADER    IMMUNE SYSTEM                           28-OCT-11   4A5W              
TITLE     CRYSTAL STRUCTURE OF C5B6                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C5;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   5 PROTEIN 4, COMPLEMENT C5 BETA CHAIN, COMPLEMENT C5 ALPHA CHAIN, C5A  
COMPND   6 ANAPHYLATOXIN, COMPLEMENT C5 ALPHA' CHAIN, C5B;                      
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COMPLEMENT COMPONENT C6;                                   
COMPND   9 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD                                                        
KEYWDS    IMMUNE SYSTEM, IMMUNITY, MEMBRANE ATTACK COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.HADDERS,D.BUBECK,F.FORNERIS,M.PANGBURN,O.LLORCA,S.M.LEA,P.GROS    
REVDAT   5   29-JUL-20 4A5W    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   13-NOV-19 4A5W    1       REMARK LINK                              
REVDAT   3   31-OCT-12 4A5W    1       JRNL                                     
REVDAT   2   09-MAY-12 4A5W    1       JRNL                                     
REVDAT   1   14-MAR-12 4A5W    0                                                
JRNL        AUTH   M.A.HADDERS,D.BUBECK,P.ROVERSI,S.HAKOBYAN,F.FORNERIS,        
JRNL        AUTH 2 B.P.MORGAN,M.K.PANGBURN,O.LLORCA,S.M.LEA,P.GROS              
JRNL        TITL   ASSEMBLY AND REGULATION OF THE MEMBRANE ATTACK COMPLEX BASED 
JRNL        TITL 2 ON STRUCTURES OF C5B6 AND SC5B9.                             
JRNL        REF    CELL REP.                     V.   1   200 2012              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   22832194                                                     
JRNL        DOI    10.1016/J.CELREP.2012.02.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 59017                          
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)  : 0.256                          
REMARK   3   R VALUE            (WORKING SET)  : 0.256                          
REMARK   3   FREE R VALUE                      : 0.270                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1214                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.59                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4041                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2291                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3950                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2292                   
REMARK   3   BIN FREE R VALUE                        : 0.2248                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.25                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 91                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18928                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 98.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 157.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.83700                                             
REMARK   3    B22 (A**2) : 0.12980                                              
REMARK   3    B33 (A**2) : 8.70720                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 1.207               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.893                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 19482  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 26326  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 6788   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 518    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2781   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 19479  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 2587   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 22866  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.10                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 22 : 112                            
REMARK   3    ORIGIN FOR THE GROUP (A):   43.9731  -20.2155  -33.5936           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0054 T22:    0.2619                                    
REMARK   3     T33:   -0.0742 T12:    0.1278                                    
REMARK   3     T13:   -0.0435 T23:   -0.1206                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6383 L22:    4.5854                                    
REMARK   3     L33:    1.4223 L12:   -1.7070                                    
REMARK   3     L13:   -2.6673 L23:   -0.5438                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0286 S12:   -0.0422 S13:    0.0224                     
REMARK   3     S21:    0.1299 S22:    0.0936 S23:   -0.3029                     
REMARK   3     S31:    0.0743 S32:    0.4027 S33:   -0.1221                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 113 : 253                           
REMARK   3    ORIGIN FOR THE GROUP (A):    6.5370  -11.7245  -25.7475           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2981 T22:    0.1192                                    
REMARK   3     T33:   -0.0486 T12:    0.0599                                    
REMARK   3     T13:    0.0083 T23:   -0.0078                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6656 L22:    0.9620                                    
REMARK   3     L33:    0.5486 L12:    0.0065                                    
REMARK   3     L13:    0.2920 L23:    0.6113                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1858 S12:   -0.0517 S13:    0.1383                     
REMARK   3     S21:    0.1570 S22:   -0.1116 S23:    0.0891                     
REMARK   3     S31:    0.0380 S32:    0.1046 S33:   -0.0743                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 254 : 772                           
REMARK   3    ORIGIN FOR THE GROUP (A):   15.5645  -27.9654  -11.9654           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4349 T22:    0.1066                                    
REMARK   3     T33:   -0.3274 T12:   -0.0072                                    
REMARK   3     T13:   -0.1482 T23:   -0.0355                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1729 L22:    1.3273                                    
REMARK   3     L33:    1.1775 L12:   -0.7135                                    
REMARK   3     L13:   -0.2719 L23:    0.1553                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0944 S12:   -0.4127 S13:   -0.3866                     
REMARK   3     S21:    0.5156 S22:    0.0097 S23:    0.0741                     
REMARK   3     S31:    0.5274 S32:    0.3345 S33:   -0.1041                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 773 : 1234                          
REMARK   3    ORIGIN FOR THE GROUP (A):    0.2338  -11.9509  -52.9164           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0890 T22:   -0.1241                                    
REMARK   3     T33:   -0.3461 T12:    0.2149                                    
REMARK   3     T13:    0.0040 T23:    0.0929                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6398 L22:    0.9062                                    
REMARK   3     L33:    2.0096 L12:    0.0784                                    
REMARK   3     L13:   -0.3717 L23:    0.2930                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2272 S12:    0.4783 S13:    0.0997                     
REMARK   3     S21:   -0.0366 S22:   -0.0576 S23:   -0.0733                     
REMARK   3     S31:   -0.0887 S32:    0.0636 S33:   -0.1696                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1243 : 1375                         
REMARK   3    ORIGIN FOR THE GROUP (A):    4.4325  -14.2791  -59.1429           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0400 T22:    0.1210                                    
REMARK   3     T33:   -0.3019 T12:    0.2062                                    
REMARK   3     T13:    0.0072 T23:    0.0333                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6907 L22:    2.0819                                    
REMARK   3     L33:    5.6595 L12:   -1.0969                                    
REMARK   3     L13:   -2.1578 L23:    2.5948                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0364 S12:    0.3940 S13:    0.3316                     
REMARK   3     S21:   -0.0172 S22:    0.2352 S23:   -0.2041                     
REMARK   3     S31:   -0.1399 S32:    0.6574 S33:   -0.2717                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND RESSEQ 1376 : 1676                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -45.0158    1.5810  -23.9480           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1575 T22:    0.2415                                    
REMARK   3     T33:   -0.1035 T12:   -0.0939                                    
REMARK   3     T13:    0.2326 T23:    0.1935                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6849 L22:    3.8131                                    
REMARK   3     L33:    0.0070 L12:   -3.4460                                    
REMARK   3     L13:   -0.2827 L23:    0.5193                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0266 S12:    0.4484 S13:    0.1180                     
REMARK   3     S21:    0.0700 S22:    0.2195 S23:   -0.1831                     
REMARK   3     S31:   -0.1381 S32:   -0.1283 S33:   -0.1929                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 22 : 79                             
REMARK   3    ORIGIN FOR THE GROUP (A):   84.2495  -53.8429 -102.2000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0732 T22:    0.1293                                    
REMARK   3     T33:    0.1346 T12:    0.3229                                    
REMARK   3     T13:    0.3337 T23:    0.1611                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    4.4683                                    
REMARK   3     L33:    0.2663 L12:   -1.3833                                    
REMARK   3     L13:   -0.4678 L23:   -0.2776                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0250 S12:    0.0269 S13:    0.0738                     
REMARK   3     S21:    0.1837 S22:   -0.1673 S23:    0.2845                     
REMARK   3     S31:    0.1770 S32:    0.1662 S33:    0.1423                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 80 : 304                            
REMARK   3    ORIGIN FOR THE GROUP (A):   41.3752  -58.3017  -50.9697           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1002 T22:   -0.0234                                    
REMARK   3     T33:   -0.0180 T12:    0.0877                                    
REMARK   3     T13:    0.0223 T23:   -0.0823                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7401 L22:    1.5019                                    
REMARK   3     L33:    1.6142 L12:    0.2599                                    
REMARK   3     L13:   -0.8494 L23:   -0.2077                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1649 S12:   -0.3195 S13:   -0.2321                     
REMARK   3     S21:    0.4201 S22:   -0.1187 S23:   -0.4572                     
REMARK   3     S31:    0.5997 S32:    0.0093 S33:   -0.0462                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND RESSEQ 305 : 642                           
REMARK   3    ORIGIN FOR THE GROUP (A):   46.5724  -60.5097  -66.5556           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2308 T22:   -0.1125                                    
REMARK   3     T33:    0.0308 T12:    0.1769                                    
REMARK   3     T13:    0.2342 T23:   -0.0468                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2187 L22:    2.2340                                    
REMARK   3     L33:    1.2089 L12:    0.0228                                    
REMARK   3     L13:   -0.6330 L23:   -0.1999                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2322 S12:   -0.1451 S13:   -0.1729                     
REMARK   3     S21:   -0.2449 S22:    0.0082 S23:   -0.4999                     
REMARK   3     S31:    0.3998 S32:   -0.1481 S33:    0.2240                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND RESSEQ 643 : 767                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -15.2354  -25.6086  -69.1830           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0356 T22:    0.2577                                    
REMARK   3     T33:   -0.0904 T12:    0.0190                                    
REMARK   3     T13:   -0.2622 T23:   -0.2091                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5212 L22:    1.9748                                    
REMARK   3     L33:    3.0125 L12:    0.5550                                    
REMARK   3     L13:    2.9197 L23:    0.6659                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0161 S12:    0.5601 S13:   -0.1772                     
REMARK   3     S21:   -0.0955 S22:    0.0366 S23:    0.7109                     
REMARK   3     S31:    0.3185 S32:   -0.1877 S33:   -0.0205                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND RESSEQ 768 : 934                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -43.2402  -49.1216 -110.4700           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1372 T22:   -0.2427                                    
REMARK   3     T33:    0.0940 T12:    0.2523                                    
REMARK   3     T13:   -0.1437 T23:    0.0770                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.4768 L22:    0.0331                                    
REMARK   3     L33:    3.1928 L12:    1.0606                                    
REMARK   3     L13:   -0.2979 L23:    0.5965                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0234 S12:    0.1916 S13:   -0.0374                     
REMARK   3     S21:    0.0366 S22:    0.3627 S23:   -0.3450                     
REMARK   3     S31:   -0.1246 S32:    0.1213 S33:   -0.3860                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3  RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NAG CA FUC BMA.     
REMARK   3  NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=18928. NUMBER WITH       
REMARK   3  APPROX DEFAULT CCP4 ATOM TYPE=99. NUMBER TREATED BY BAD NON-        
REMARK   3  BONDED CONTACTS=1.                                                  
REMARK   4                                                                      
REMARK   4 4A5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290050122.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97623                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59023                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
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     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3CU7, 3OJY, 2OK5                         
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 167 MM HEPES-NAOH PH7.8                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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 -1.000000  0.000000  0.000000       77.10850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      134.99150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      115.37350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      134.99150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       77.10850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      115.37350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       77.10850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      115.37350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      134.99150            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      115.37350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       77.10850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      134.99150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 127550 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     GLN A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     GLN A    21                                                      
REMARK 465     LEU A   673                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     HIS A   753                                                      
REMARK 465     MET A   754                                                      
REMARK 465     LYS A   755                                                      
REMARK 465     THR A   756                                                      
REMARK 465     LEU A   757                                                      
REMARK 465     LEU A   758                                                      
REMARK 465     PRO A   759                                                      
REMARK 465     VAL A   760                                                      
REMARK 465     SER A   761                                                      
REMARK 465     LYS A   762                                                      
REMARK 465     PRO A   763                                                      
REMARK 465     GLU A   764                                                      
REMARK 465     ILE A   765                                                      
REMARK 465     LEU A  1003                                                      
REMARK 465     PRO A  1004                                                      
REMARK 465     LYS A  1005                                                      
REMARK 465     GLY A  1006                                                      
REMARK 465     SER A  1007                                                      
REMARK 465     TYR A  1124                                                      
REMARK 465     GLN A  1125                                                      
REMARK 465     PRO A  1126                                                      
REMARK 465     ILE A  1127                                                      
REMARK 465     LYS A  1128                                                      
REMARK 465     LEU A  1129                                                      
REMARK 465     GLN A  1130                                                      
REMARK 465     GLY A  1131                                                      
REMARK 465     THR A  1132                                                      
REMARK 465     LYS A  1235                                                      
REMARK 465     ASP A  1236                                                      
REMARK 465     SER A  1237                                                      
REMARK 465     SER A  1238                                                      
REMARK 465     VAL A  1239                                                      
REMARK 465     PRO A  1240                                                      
REMARK 465     ASN A  1241                                                      
REMARK 465     THR A  1242                                                      
REMARK 465     GLU A  1387                                                      
REMARK 465     ALA A  1388                                                      
REMARK 465     SER A  1389                                                      
REMARK 465     HIS A  1390                                                      
REMARK 465     TYR A  1391                                                      
REMARK 465     ARG A  1392                                                      
REMARK 465     GLY A  1393                                                      
REMARK 465     TYR A  1394                                                      
REMARK 465     GLY A  1395                                                      
REMARK 465     ASN A  1396                                                      
REMARK 465     SER A  1397                                                      
REMARK 465     ASP A  1398                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     HIS B   263                                                      
REMARK 465     ASN B   264                                                      
REMARK 465     GLU B   265                                                      
REMARK 465     ASN B   266                                                      
REMARK 465     GLN B   267                                                      
REMARK 465     GLN B   268                                                      
REMARK 465     GLY B   269                                                      
REMARK 465     SER B   270                                                      
REMARK 465     PHE B   271                                                      
REMARK 465     SER B   272                                                      
REMARK 465     SER B   273                                                      
REMARK 465     LYS B   405                                                      
REMARK 465     LYS B   406                                                      
REMARK 465     ARG B   407                                                      
REMARK 465     VAL B   408                                                      
REMARK 465     LEU B   409                                                      
REMARK 465     PHE B   410                                                      
REMARK 465     ALA B   411                                                      
REMARK 465     LYS B   412                                                      
REMARK 465     LYS B   413                                                      
REMARK 465     THR B   414                                                      
REMARK 465     LYS B   415                                                      
REMARK 465     VAL B   416                                                      
REMARK 465     GLU B   417                                                      
REMARK 465     ARG B   448                                                      
REMARK 465     SER B   449                                                      
REMARK 465     GLU B   450                                                      
REMARK 465     TYR B   451                                                      
REMARK 465     GLY B   452                                                      
REMARK 465     ALA B   453                                                      
REMARK 465     ALA B   454                                                      
REMARK 465     LEU B   455                                                      
REMARK 465     ALA B   456                                                      
REMARK 465     TRP B   457                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     LYS B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     SER B   462                                                      
REMARK 465     GLY B   463                                                      
REMARK 465     LEU B   464                                                      
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     PHE B 736    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE B 818    CG   CD1  CD2  CE1  CE2  CZ                         
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 B  95   C   -  N   -  CD  ANGL. DEV. = -22.6 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    TYR A  23       71.11     43.14                                   
REMARK 500    PHE A  64      162.29    177.23                                   
REMARK 500    PRO A  89       63.47    -67.83                                   
REMARK 500    VAL A  99     -123.67     44.76                                   
REMARK 500    SER A 100       79.79     53.17                                   
REMARK 500    LEU A 152       -1.48     72.02                                   
REMARK 500    ALA A 155       73.43     54.10                                   
REMARK 500    VAL A 171      -65.71   -106.36                                   
REMARK 500    LYS A 206     -115.62     59.83                                   
REMARK 500    VAL A 223      -19.10     69.88                                   
REMARK 500    LEU A 224       76.07     57.85                                   
REMARK 500    ASN A 257       -4.72     79.23                                   
REMARK 500    THR A 261      -71.42    -58.08                                   
REMARK 500    GLN A 284       -1.70     81.45                                   
REMARK 500    THR A 285      -62.16   -129.04                                   
REMARK 500    MET A 287       38.49     71.01                                   
REMARK 500    ALA A 306      -72.01    -52.74                                   
REMARK 500    VAL A 307      -74.03    -57.02                                   
REMARK 500    LYS A 308     -126.79     41.40                                   
REMARK 500    TYR A 312       -9.17     70.48                                   
REMARK 500    LEU A 315      159.55    173.25                                   
REMARK 500    TYR A 352     -143.16     55.53                                   
REMARK 500    ASP A 377     -167.32    -79.16                                   
REMARK 500    ASP A 380       46.88     30.21                                   
REMARK 500    ASN A 398      -70.35    -61.37                                   
REMARK 500    GLN A 399     -169.47   -166.67                                   
REMARK 500    GLU A 400     -143.88     59.81                                   
REMARK 500    THR A 429      -73.50    -83.27                                   
REMARK 500    GLN A 462       -2.22     65.01                                   
REMARK 500    TRP A 469     -118.36     62.02                                   
REMARK 500    THR A 470       84.46     56.34                                   
REMARK 500    ASP A 471        2.73     82.36                                   
REMARK 500    ALA A 475     -145.99     59.95                                   
REMARK 500    PRO A 488       68.03   -102.01                                   
REMARK 500    THR A 497      -72.93    -50.48                                   
REMARK 500    GLN A 550      -74.88   -114.30                                   
REMARK 500    LYS A 617     -131.58     43.98                                   
REMARK 500    LEU A 620      -75.40   -133.74                                   
REMARK 500    GLU A 621      -21.27     65.06                                   
REMARK 500    VAL A 623      -61.33   -127.32                                   
REMARK 500    ASN A 641     -142.99     52.96                                   
REMARK 500    ALA A 657      -72.79    -56.38                                   
REMARK 500    GLU A 664     -145.02     57.12                                   
REMARK 500    LYS A 670      -76.61   -124.53                                   
REMARK 500    SER A 767     -156.41     58.16                                   
REMARK 500    ARG A 782     -111.17     49.12                                   
REMARK 500    ILE A 829       71.46     42.16                                   
REMARK 500    SER A 832      -18.89     76.15                                   
REMARK 500    VAL A 833       75.69     21.24                                   
REMARK 500    LEU A 841       70.84     47.09                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     228 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B   94     PRO B   95                 -147.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CFA   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT    
REMARK 900 PH 5.2, 303K, NMR, 20 STRUCTURES                                     
REMARK 900 RELATED ID: 1KJS   RELATED DB: PDB                                   
REMARK 900 NMR SOLUTION STRUCTURE OF C5A AT PH 5.2, 303K, 20 STRUCTURES         
REMARK 900 RELATED ID: 1XWE   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF C345C (NTR) DOMAIN OF C5 OF COMPLEMENT              
REMARK 900 RELATED ID: EMD-1991   RELATED DB: EMDB                              
DBREF  4A5W A   19   673  UNP    P01031   CO5_HUMAN       19    673             
DBREF  4A5W A  752  1676  UNP    P01031   CO5_HUMAN      752   1676             
DBREF  4A5W B   22   934  UNP    P13671   CO6_HUMAN       22    934             
SEQRES   1 A 1580  GLN GLU GLN THR TYR VAL ILE SER ALA PRO LYS ILE PHE          
SEQRES   2 A 1580  ARG VAL GLY ALA SER GLU ASN ILE VAL ILE GLN VAL TYR          
SEQRES   3 A 1580  GLY TYR THR GLU ALA PHE ASP ALA THR ILE SER ILE LYS          
SEQRES   4 A 1580  SER TYR PRO ASP LYS LYS PHE SER TYR SER SER GLY HIS          
SEQRES   5 A 1580  VAL HIS LEU SER SER GLU ASN LYS PHE GLN ASN SER ALA          
SEQRES   6 A 1580  ILE LEU THR ILE GLN PRO LYS GLN LEU PRO GLY GLY GLN          
SEQRES   7 A 1580  ASN PRO VAL SER TYR VAL TYR LEU GLU VAL VAL SER LYS          
SEQRES   8 A 1580  HIS PHE SER LYS SER LYS ARG MET PRO ILE THR TYR ASP          
SEQRES   9 A 1580  ASN GLY PHE LEU PHE ILE HIS THR ASP LYS PRO VAL TYR          
SEQRES  10 A 1580  THR PRO ASP GLN SER VAL LYS VAL ARG VAL TYR SER LEU          
SEQRES  11 A 1580  ASN ASP ASP LEU LYS PRO ALA LYS ARG GLU THR VAL LEU          
SEQRES  12 A 1580  THR PHE ILE ASP PRO GLU GLY SER GLU VAL ASP MET VAL          
SEQRES  13 A 1580  GLU GLU ILE ASP HIS ILE GLY ILE ILE SER PHE PRO ASP          
SEQRES  14 A 1580  PHE LYS ILE PRO SER ASN PRO ARG TYR GLY MET TRP THR          
SEQRES  15 A 1580  ILE LYS ALA LYS TYR LYS GLU ASP PHE SER THR THR GLY          
SEQRES  16 A 1580  THR ALA TYR PHE GLU VAL LYS GLU TYR VAL LEU PRO HIS          
SEQRES  17 A 1580  PHE SER VAL SER ILE GLU PRO GLU TYR ASN PHE ILE GLY          
SEQRES  18 A 1580  TYR LYS ASN PHE LYS ASN PHE GLU ILE THR ILE LYS ALA          
SEQRES  19 A 1580  ARG TYR PHE TYR ASN LYS VAL VAL THR GLU ALA ASP VAL          
SEQRES  20 A 1580  TYR ILE THR PHE GLY ILE ARG GLU ASP LEU LYS ASP ASP          
SEQRES  21 A 1580  GLN LYS GLU MET MET GLN THR ALA MET GLN ASN THR MET          
SEQRES  22 A 1580  LEU ILE ASN GLY ILE ALA GLN VAL THR PHE ASP SER GLU          
SEQRES  23 A 1580  THR ALA VAL LYS GLU LEU SER TYR TYR SER LEU GLU ASP          
SEQRES  24 A 1580  LEU ASN ASN LYS TYR LEU TYR ILE ALA VAL THR VAL ILE          
SEQRES  25 A 1580  GLU SER THR GLY GLY PHE SER GLU GLU ALA GLU ILE PRO          
SEQRES  26 A 1580  GLY ILE LYS TYR VAL LEU SER PRO TYR LYS LEU ASN LEU          
SEQRES  27 A 1580  VAL ALA THR PRO LEU PHE LEU LYS PRO GLY ILE PRO TYR          
SEQRES  28 A 1580  PRO ILE LYS VAL GLN VAL LYS ASP SER LEU ASP GLN LEU          
SEQRES  29 A 1580  VAL GLY GLY VAL PRO VAL THR LEU ASN ALA GLN THR ILE          
SEQRES  30 A 1580  ASP VAL ASN GLN GLU THR SER ASP LEU ASP PRO SER LYS          
SEQRES  31 A 1580  SER VAL THR ARG VAL ASP ASP GLY VAL ALA SER PHE VAL          
SEQRES  32 A 1580  LEU ASN LEU PRO SER GLY VAL THR VAL LEU GLU PHE ASN          
SEQRES  33 A 1580  VAL LYS THR ASP ALA PRO ASP LEU PRO GLU GLU ASN GLN          
SEQRES  34 A 1580  ALA ARG GLU GLY TYR ARG ALA ILE ALA TYR SER SER LEU          
SEQRES  35 A 1580  SER GLN SER TYR LEU TYR ILE ASP TRP THR ASP ASN HIS          
SEQRES  36 A 1580  LYS ALA LEU LEU VAL GLY GLU HIS LEU ASN ILE ILE VAL          
SEQRES  37 A 1580  THR PRO LYS SER PRO TYR ILE ASP LYS ILE THR HIS TYR          
SEQRES  38 A 1580  ASN TYR LEU ILE LEU SER LYS GLY LYS ILE ILE HIS PHE          
SEQRES  39 A 1580  GLY THR ARG GLU LYS PHE SER ASP ALA SER TYR GLN SER          
SEQRES  40 A 1580  ILE ASN ILE PRO VAL THR GLN ASN MET VAL PRO SER SER          
SEQRES  41 A 1580  ARG LEU LEU VAL TYR TYR ILE VAL THR GLY GLU GLN THR          
SEQRES  42 A 1580  ALA GLU LEU VAL SER ASP SER VAL TRP LEU ASN ILE GLU          
SEQRES  43 A 1580  GLU LYS CYS GLY ASN GLN LEU GLN VAL HIS LEU SER PRO          
SEQRES  44 A 1580  ASP ALA ASP ALA TYR SER PRO GLY GLN THR VAL SER LEU          
SEQRES  45 A 1580  ASN MET ALA THR GLY MET ASP SER TRP VAL ALA LEU ALA          
SEQRES  46 A 1580  ALA VAL ASP SER ALA VAL TYR GLY VAL GLN ARG GLY ALA          
SEQRES  47 A 1580  LYS LYS PRO LEU GLU ARG VAL PHE GLN PHE LEU GLU LYS          
SEQRES  48 A 1580  SER ASP LEU GLY CYS GLY ALA GLY GLY GLY LEU ASN ASN          
SEQRES  49 A 1580  ALA ASN VAL PHE HIS LEU ALA GLY LEU THR PHE LEU THR          
SEQRES  50 A 1580  ASN ALA ASN ALA ASP ASP SER GLN GLU ASN ASP GLU PRO          
SEQRES  51 A 1580  CYS LYS GLU ILE LEU LEU HIS MET LYS THR LEU LEU PRO          
SEQRES  52 A 1580  VAL SER LYS PRO GLU ILE ARG SER TYR PHE PRO GLU SER          
SEQRES  53 A 1580  TRP LEU TRP GLU VAL HIS LEU VAL PRO ARG ARG LYS GLN          
SEQRES  54 A 1580  LEU GLN PHE ALA LEU PRO ASP SER LEU THR THR TRP GLU          
SEQRES  55 A 1580  ILE GLN GLY VAL GLY ILE SER ASN THR GLY ILE CYS VAL          
SEQRES  56 A 1580  ALA ASP THR VAL LYS ALA LYS VAL PHE LYS ASP VAL PHE          
SEQRES  57 A 1580  LEU GLU MET ASN ILE PRO TYR SER VAL VAL ARG GLY GLU          
SEQRES  58 A 1580  GLN ILE GLN LEU LYS GLY THR VAL TYR ASN TYR ARG THR          
SEQRES  59 A 1580  SER GLY MET GLN PHE CYS VAL LYS MET SER ALA VAL GLU          
SEQRES  60 A 1580  GLY ILE CYS THR SER GLU SER PRO VAL ILE ASP HIS GLN          
SEQRES  61 A 1580  GLY THR LYS SER SER LYS CYS VAL ARG GLN LYS VAL GLU          
SEQRES  62 A 1580  GLY SER SER SER HIS LEU VAL THR PHE THR VAL LEU PRO          
SEQRES  63 A 1580  LEU GLU ILE GLY LEU HIS ASN ILE ASN PHE SER LEU GLU          
SEQRES  64 A 1580  THR TRP PHE GLY LYS GLU ILE LEU VAL LYS THR LEU ARG          
SEQRES  65 A 1580  VAL VAL PRO GLU GLY VAL LYS ARG GLU SER TYR SER GLY          
SEQRES  66 A 1580  VAL THR LEU ASP PRO ARG GLY ILE TYR GLY THR ILE SER          
SEQRES  67 A 1580  ARG ARG LYS GLU PHE PRO TYR ARG ILE PRO LEU ASP LEU          
SEQRES  68 A 1580  VAL PRO LYS THR GLU ILE LYS ARG ILE LEU SER VAL LYS          
SEQRES  69 A 1580  GLY LEU LEU VAL GLY GLU ILE LEU SER ALA VAL LEU SER          
SEQRES  70 A 1580  GLN GLU GLY ILE ASN ILE LEU THR HIS LEU PRO LYS GLY          
SEQRES  71 A 1580  SER ALA GLU ALA GLU LEU MET SER VAL VAL PRO VAL PHE          
SEQRES  72 A 1580  TYR VAL PHE HIS TYR LEU GLU THR GLY ASN HIS TRP ASN          
SEQRES  73 A 1580  ILE PHE HIS SER ASP PRO LEU ILE GLU LYS GLN LYS LEU          
SEQRES  74 A 1580  LYS LYS LYS LEU LYS GLU GLY MET LEU SER ILE MET SER          
SEQRES  75 A 1580  TYR ARG ASN ALA ASP TYR SER TYR SER VAL TRP LYS GLY          
SEQRES  76 A 1580  GLY SER ALA SER THR TRP LEU THR ALA PHE ALA LEU ARG          
SEQRES  77 A 1580  VAL LEU GLY GLN VAL ASN LYS TYR VAL GLU GLN ASN GLN          
SEQRES  78 A 1580  ASN SER ILE CYS ASN SER LEU LEU TRP LEU VAL GLU ASN          
SEQRES  79 A 1580  TYR GLN LEU ASP ASN GLY SER PHE LYS GLU ASN SER GLN          
SEQRES  80 A 1580  TYR GLN PRO ILE LYS LEU GLN GLY THR LEU PRO VAL GLU          
SEQRES  81 A 1580  ALA ARG GLU ASN SER LEU TYR LEU THR ALA PHE THR VAL          
SEQRES  82 A 1580  ILE GLY ILE ARG LYS ALA PHE ASP ILE CYS PRO LEU VAL          
SEQRES  83 A 1580  LYS ILE ASP THR ALA LEU ILE LYS ALA ASP ASN PHE LEU          
SEQRES  84 A 1580  LEU GLU ASN THR LEU PRO ALA GLN SER THR PHE THR LEU          
SEQRES  85 A 1580  ALA ILE SER ALA TYR ALA LEU SER LEU GLY ASP LYS THR          
SEQRES  86 A 1580  HIS PRO GLN PHE ARG SER ILE VAL SER ALA LEU LYS ARG          
SEQRES  87 A 1580  GLU ALA LEU VAL LYS GLY ASN PRO PRO ILE TYR ARG PHE          
SEQRES  88 A 1580  TRP LYS ASP ASN LEU GLN HIS LYS ASP SER SER VAL PRO          
SEQRES  89 A 1580  ASN THR GLY THR ALA ARG MET VAL GLU THR THR ALA TYR          
SEQRES  90 A 1580  ALA LEU LEU THR SER LEU ASN LEU LYS ASP ILE ASN TYR          
SEQRES  91 A 1580  VAL ASN PRO VAL ILE LYS TRP LEU SER GLU GLU GLN ARG          
SEQRES  92 A 1580  TYR GLY GLY GLY PHE TYR SER THR GLN ASP THR ILE ASN          
SEQRES  93 A 1580  ALA ILE GLU GLY LEU THR GLU TYR SER LEU LEU VAL LYS          
SEQRES  94 A 1580  GLN LEU ARG LEU SER MET ASP ILE ASP VAL SER TYR LYS          
SEQRES  95 A 1580  HIS LYS GLY ALA LEU HIS ASN TYR LYS MET THR ASP LYS          
SEQRES  96 A 1580  ASN PHE LEU GLY ARG PRO VAL GLU VAL LEU LEU ASN ASP          
SEQRES  97 A 1580  ASP LEU ILE VAL SER THR GLY PHE GLY SER GLY LEU ALA          
SEQRES  98 A 1580  THR VAL HIS VAL THR THR VAL VAL HIS LYS THR SER THR          
SEQRES  99 A 1580  SER GLU GLU VAL CYS SER PHE TYR LEU LYS ILE ASP THR          
SEQRES 100 A 1580  GLN ASP ILE GLU ALA SER HIS TYR ARG GLY TYR GLY ASN          
SEQRES 101 A 1580  SER ASP TYR LYS ARG ILE VAL ALA CYS ALA SER TYR LYS          
SEQRES 102 A 1580  PRO SER ARG GLU GLU SER SER SER GLY SER SER HIS ALA          
SEQRES 103 A 1580  VAL MET ASP ILE SER LEU PRO THR GLY ILE SER ALA ASN          
SEQRES 104 A 1580  GLU GLU ASP LEU LYS ALA LEU VAL GLU GLY VAL ASP GLN          
SEQRES 105 A 1580  LEU PHE THR ASP TYR GLN ILE LYS ASP GLY HIS VAL ILE          
SEQRES 106 A 1580  LEU GLN LEU ASN SER ILE PRO SER SER ASP PHE LEU CYS          
SEQRES 107 A 1580  VAL ARG PHE ARG ILE PHE GLU LEU PHE GLU VAL GLY PHE          
SEQRES 108 A 1580  LEU SER PRO ALA THR PHE THR VAL TYR GLU TYR HIS ARG          
SEQRES 109 A 1580  PRO ASP LYS GLN CYS THR MET PHE TYR SER THR SER ASN          
SEQRES 110 A 1580  ILE LYS ILE GLN LYS VAL CYS GLU GLY ALA ALA CYS LYS          
SEQRES 111 A 1580  CYS VAL GLU ALA ASP CYS GLY GLN MET GLN GLU GLU LEU          
SEQRES 112 A 1580  ASP LEU THR ILE SER ALA GLU THR ARG LYS GLN THR ALA          
SEQRES 113 A 1580  CYS LYS PRO GLU ILE ALA TYR ALA TYR LYS VAL SER ILE          
SEQRES 114 A 1580  THR SER ILE THR VAL GLU ASN VAL PHE VAL LYS TYR LYS          
SEQRES 115 A 1580  ALA THR LEU LEU ASP ILE TYR LYS THR GLY GLU ALA VAL          
SEQRES 116 A 1580  ALA GLU LYS ASP SER GLU ILE THR PHE ILE LYS LYS VAL          
SEQRES 117 A 1580  THR CYS THR ASN ALA GLU LEU VAL LYS GLY ARG GLN TYR          
SEQRES 118 A 1580  LEU ILE MET GLY LYS GLU ALA LEU GLN ILE LYS TYR ASN          
SEQRES 119 A 1580  PHE SER PHE ARG TYR ILE TYR PRO LEU ASP SER LEU THR          
SEQRES 120 A 1580  TRP ILE GLU TYR TRP PRO ARG ASP THR THR CYS SER SER          
SEQRES 121 A 1580  CYS GLN ALA PHE LEU ALA ASN LEU ASP GLU PHE ALA GLU          
SEQRES 122 A 1580  ASP ILE PHE LEU ASN GLY CYS                                  
SEQRES   1 B  913  CYS PHE CYS ASP HIS TYR ALA TRP THR GLN TRP THR SER          
SEQRES   2 B  913  CYS SER LYS THR CYS ASN SER GLY THR GLN SER ARG HIS          
SEQRES   3 B  913  ARG GLN ILE VAL VAL ASP LYS TYR TYR GLN GLU ASN PHE          
SEQRES   4 B  913  CYS GLU GLN ILE CYS SER LYS GLN GLU THR ARG GLU CYS          
SEQRES   5 B  913  ASN TRP GLN ARG CYS PRO ILE ASN CYS LEU LEU GLY ASP          
SEQRES   6 B  913  PHE GLY PRO TRP SER ASP CYS ASP PRO CYS ILE GLU LYS          
SEQRES   7 B  913  GLN SER LYS VAL ARG SER VAL LEU ARG PRO SER GLN PHE          
SEQRES   8 B  913  GLY GLY GLN PRO CYS THR ALA PRO LEU VAL ALA PHE GLN          
SEQRES   9 B  913  PRO CYS ILE PRO SER LYS LEU CYS LYS ILE GLU GLU ALA          
SEQRES  10 B  913  ASP CYS LYS ASN LYS PHE ARG CYS ASP SER GLY ARG CYS          
SEQRES  11 B  913  ILE ALA ARG LYS LEU GLU CYS ASN GLY GLU ASN ASP CYS          
SEQRES  12 B  913  GLY ASP ASN SER ASP GLU ARG ASP CYS GLY ARG THR LYS          
SEQRES  13 B  913  ALA VAL CYS THR ARG LYS TYR ASN PRO ILE PRO SER VAL          
SEQRES  14 B  913  GLN LEU MET GLY ASN GLY PHE HIS PHE LEU ALA GLY GLU          
SEQRES  15 B  913  PRO ARG GLY GLU VAL LEU ASP ASN SER PHE THR GLY GLY          
SEQRES  16 B  913  ILE CYS LYS THR VAL LYS SER SER ARG THR SER ASN PRO          
SEQRES  17 B  913  TYR ARG VAL PRO ALA ASN LEU GLU ASN VAL GLY PHE GLU          
SEQRES  18 B  913  VAL GLN THR ALA GLU ASP ASP LEU LYS THR ASP PHE TYR          
SEQRES  19 B  913  LYS ASP LEU THR SER LEU GLY HIS ASN GLU ASN GLN GLN          
SEQRES  20 B  913  GLY SER PHE SER SER GLN GLY GLY SER SER PHE SER VAL          
SEQRES  21 B  913  PRO ILE PHE TYR SER SER LYS ARG SER GLU ASN ILE ASN          
SEQRES  22 B  913  HIS ASN SER ALA PHE LYS GLN ALA ILE GLN ALA SER HIS          
SEQRES  23 B  913  LYS LYS ASP SER SER PHE ILE ARG ILE HIS LYS VAL MET          
SEQRES  24 B  913  LYS VAL LEU ASN PHE THR THR LYS ALA LYS ASP LEU HIS          
SEQRES  25 B  913  LEU SER ASP VAL PHE LEU LYS ALA LEU ASN HIS LEU PRO          
SEQRES  26 B  913  LEU GLU TYR ASN SER ALA LEU TYR SER ARG ILE PHE ASP          
SEQRES  27 B  913  ASP PHE GLY THR HIS TYR PHE THR SER GLY SER LEU GLY          
SEQRES  28 B  913  GLY VAL TYR ASP LEU LEU TYR GLN PHE SER SER GLU GLU          
SEQRES  29 B  913  LEU LYS ASN SER GLY LEU THR GLU GLU GLU ALA LYS HIS          
SEQRES  30 B  913  CYS VAL ARG ILE GLU THR LYS LYS ARG VAL LEU PHE ALA          
SEQRES  31 B  913  LYS LYS THR LYS VAL GLU HIS ARG CYS THR THR ASN LYS          
SEQRES  32 B  913  LEU SER GLU LYS HIS GLU GLY SER PHE ILE GLN GLY ALA          
SEQRES  33 B  913  GLU LYS SER ILE SER LEU ILE ARG GLY GLY ARG SER GLU          
SEQRES  34 B  913  TYR GLY ALA ALA LEU ALA TRP GLU LYS GLY SER SER GLY          
SEQRES  35 B  913  LEU GLU GLU LYS THR PHE SER GLU TRP LEU GLU SER VAL          
SEQRES  36 B  913  LYS GLU ASN PRO ALA VAL ILE ASP PHE GLU LEU ALA PRO          
SEQRES  37 B  913  ILE VAL ASP LEU VAL ARG ASN ILE PRO CYS ALA VAL THR          
SEQRES  38 B  913  LYS ARG ASN ASN LEU ARG LYS ALA LEU GLN GLU TYR ALA          
SEQRES  39 B  913  ALA LYS PHE ASP PRO CYS GLN CYS ALA PRO CYS PRO ASN          
SEQRES  40 B  913  ASN GLY ARG PRO THR LEU SER GLY THR GLU CYS LEU CYS          
SEQRES  41 B  913  VAL CYS GLN SER GLY THR TYR GLY GLU ASN CYS GLU LYS          
SEQRES  42 B  913  GLN SER PRO ASP TYR LYS SER ASN ALA VAL ASP GLY GLN          
SEQRES  43 B  913  TRP GLY CYS TRP SER SER TRP SER THR CYS ASP ALA THR          
SEQRES  44 B  913  TYR LYS ARG SER ARG THR ARG GLU CYS ASN ASN PRO ALA          
SEQRES  45 B  913  PRO GLN ARG GLY GLY LYS ARG CYS GLU GLY GLU LYS ARG          
SEQRES  46 B  913  GLN GLU GLU ASP CYS THR PHE SER ILE MET GLU ASN ASN          
SEQRES  47 B  913  GLY GLN PRO CYS ILE ASN ASP ASP GLU GLU MET LYS GLU          
SEQRES  48 B  913  VAL ASP LEU PRO GLU ILE GLU ALA ASP SER GLY CYS PRO          
SEQRES  49 B  913  GLN PRO VAL PRO PRO GLU ASN GLY PHE ILE ARG ASN GLU          
SEQRES  50 B  913  LYS GLN LEU TYR LEU VAL GLY GLU ASP VAL GLU ILE SER          
SEQRES  51 B  913  CYS LEU THR GLY PHE GLU THR VAL GLY TYR GLN TYR PHE          
SEQRES  52 B  913  ARG CYS LEU PRO ASP GLY THR TRP ARG GLN GLY ASP VAL          
SEQRES  53 B  913  GLU CYS GLN ARG THR GLU CYS ILE LYS PRO VAL VAL GLN          
SEQRES  54 B  913  GLU VAL LEU THR ILE THR PRO PHE GLN ARG LEU TYR ARG          
SEQRES  55 B  913  ILE GLY GLU SER ILE GLU LEU THR CYS PRO LYS GLY PHE          
SEQRES  56 B  913  VAL VAL ALA GLY PRO SER ARG TYR THR CYS GLN GLY ASN          
SEQRES  57 B  913  SER TRP THR PRO PRO ILE SER ASN SER LEU THR CYS GLU          
SEQRES  58 B  913  LYS ASP THR LEU THR LYS LEU LYS GLY HIS CYS GLN LEU          
SEQRES  59 B  913  GLY GLN LYS GLN SER GLY SER GLU CYS ILE CYS MET SER          
SEQRES  60 B  913  PRO GLU GLU ASP CYS SER HIS HIS SER GLU ASP LEU CYS          
SEQRES  61 B  913  VAL PHE ASP THR ASP SER ASN ASP TYR PHE THR SER PRO          
SEQRES  62 B  913  ALA CYS LYS PHE LEU ALA GLU LYS CYS LEU ASN ASN GLN          
SEQRES  63 B  913  GLN LEU HIS PHE LEU HIS ILE GLY SER CYS GLN ASP GLY          
SEQRES  64 B  913  ARG GLN LEU GLU TRP GLY LEU GLU ARG THR ARG LEU SER          
SEQRES  65 B  913  SER ASN SER THR LYS LYS GLU SER CYS GLY TYR ASP THR          
SEQRES  66 B  913  CYS TYR ASP TRP GLU LYS CYS SER ALA SER THR SER LYS          
SEQRES  67 B  913  CYS VAL CYS LEU LEU PRO PRO GLN CYS PHE LYS GLY GLY          
SEQRES  68 B  913  ASN GLN LEU TYR CYS VAL LYS MET GLY SER SER THR SER          
SEQRES  69 B  913  GLU LYS THR LEU ASN ILE CYS GLU VAL GLY THR ILE ARG          
SEQRES  70 B  913  CYS ALA ASN ARG LYS MET GLU ILE LEU HIS PRO GLY LYS          
SEQRES  71 B  913  CYS LEU ALA                                                  
MODRES 4A5W ASN A  911  ASN  GLYCOSYLATION SITE                                 
MODRES 4A5W ASN A 1630  ASN  GLYCOSYLATION SITE                                 
MODRES 4A5W ASN B  324  ASN  GLYCOSYLATION SITE                                 
MODRES 4A5W ASN B  855  ASN  GLYCOSYLATION SITE                                 
MODRES 4A5W THR B   38  THR  GLYCOSYLATION SITE                                 
HET    NAG  A1911      14                                                       
HET    NAG  A2630      14                                                       
HET     CA  B1000       1                                                       
HET    FUC  B1005      10                                                       
HET    NAG  B1324      14                                                       
HET    BMA  B1568      11                                                       
HET    BMA  B1571      11                                                       
HET    BMA  B1574      11                                                       
HET    NAG  B1855      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  FUC    C6 H12 O5                                                    
FORMUL   8  BMA    3(C6 H12 O6)                                                 
HELIX    1   1 ASP A  302  VAL A  307  1                                   6    
HELIX    2   2 THR A  531  VAL A  535  5                                   5    
HELIX    3   3 GLN A  613  LYS A  617  5                                   5    
HELIX    4   4 VAL A  623  GLU A  628  1                                   6    
HELIX    5   5 LYS A  629  ASP A  631  5                                   3    
HELIX    6   6 ASN A  642  GLY A  650  1                                   9    
HELIX    7   7 SER A  993  ILE A  999  1                                   7    
HELIX    8   8 ALA A 1010  GLY A 1028  1                                  19    
HELIX    9   9 ASP A 1037  SER A 1058  1                                  22    
HELIX   10  10 SER A 1075  ASN A 1090  1                                  16    
HELIX   11  11 ASN A 1096  ASN A 1110  1                                  15    
HELIX   12  12 VAL A 1135  ASP A 1157  1                                  23    
HELIX   13  13 LEU A 1161  THR A 1179  1                                  19    
HELIX   14  14 SER A 1184  LEU A 1197  1                                  14    
HELIX   15  15 HIS A 1202  GLU A 1215  1                                  14    
HELIX   16  16 ARG A 1246  ASN A 1260  1                                  15    
HELIX   17  17 ASP A 1263  GLU A 1276  1                                  14    
HELIX   18  18 ASP A 1289  LEU A 1307  1                                  19    
HELIX   19  19 SER A 1371  SER A 1376  1                                   6    
HELIX   20  20 ASN A 1435  GLY A 1445  1                                  11    
HELIX   21  21 ALA A 1545  CYS A 1553  1                                   9    
HELIX   22  22 GLN A 1658  ASN A 1674  1                                  17    
HELIX   23  23 PHE B   23  TYR B   27  5                                   5    
HELIX   24  24 ASP B   53  PHE B   60  1                                   8    
HELIX   25  25 PHE B  299  ALA B  305  1                                   7    
HELIX   26  26 SER B  335  HIS B  344  1                                  10    
HELIX   27  27 ASN B  350  GLY B  362  1                                  13    
HELIX   28  28 SER B  382  SER B  389  1                                   8    
HELIX   29  29 LYS B  428  PHE B  433  1                                   6    
HELIX   30  30 LYS B  467  ASN B  479  1                                  13    
HELIX   31  31 VAL B  491  ARG B  495  5                                   5    
HELIX   32  32 CYS B  499  ASP B  519  1                                  21    
HELIX   33  33 GLY B  549  GLU B  553  5                                   5    
HELIX   34  34 ALA B  815  LYS B  822  1                                   8    
HELIX   35  35 GLN B  842  GLU B  848  5                                   7    
HELIX   36  36 LEU B  884  GLY B  892  5                                   9    
HELIX   37  37 ILE B  911  ARG B  918  1                                   8    
SHEET    1  AA 4 GLN A  80  THR A  86  0                                        
SHEET    2  AA 4 SER A  36  GLN A  42 -1  O  GLU A  37   N  LEU A  85           
SHEET    3  AA 4 VAL A  24  PRO A  28 -1  O  VAL A  24   N  GLN A  42           
SHEET    4  AA 4 LEU A 651  LEU A 654 -1  O  THR A 652   N  ALA A  27           
SHEET    1  AB 2 PHE A  31  ARG A  32  0                                        
SHEET    2  AB 2 ILE A 119  THR A 120  1  N  THR A 120   O  PHE A  31           
SHEET    1  AC 4 SER A  67  VAL A  71  0                                        
SHEET    2  AC 4 ALA A  52  SER A  58 -1  O  ALA A  52   N  VAL A  71           
SHEET    3  AC 4 VAL A 102  SER A 108 -1  O  TYR A 103   N  LYS A  57           
SHEET    4  AC 4 SER A 112  MET A 117 -1  O  LYS A 113   N  VAL A 106           
SHEET    1  AD 3 PHE A 125  THR A 130  0                                        
SHEET    2  AD 3 SER A 140  LEU A 148 -1  O  ARG A 144   N  HIS A 129           
SHEET    3  AD 3 ILE A 182  LYS A 189 -1  O  ILE A 183   N  VAL A 145           
SHEET    1  AE 5 VAL A 134  TYR A 135  0                                        
SHEET    2  AE 5 THR A 212  VAL A 219  1  O  GLU A 218   N  TYR A 135           
SHEET    3  AE 5 GLY A 197  LYS A 204 -1  O  GLY A 197   N  VAL A 219           
SHEET    4  AE 5 THR A 159  ILE A 164 -1  O  VAL A 160   N  LYS A 204           
SHEET    5  AE 5 GLU A 170  GLU A 176 -1  N  VAL A 171   O  PHE A 163           
SHEET    1  AF 3 PHE A 227  PRO A 233  0                                        
SHEET    2  AF 3 GLU A 247  TYR A 254 -1  O  THR A 249   N  GLU A 232           
SHEET    3  AF 3 ALA A 297  THR A 300 -1  O  ALA A 297   N  ILE A 250           
SHEET    1  AG 4 ASN A 289  ILE A 293  0                                        
SHEET    2  AG 4 GLU A 262  ARG A 272 -1  O  ALA A 263   N  LEU A 292           
SHEET    3  AG 4 TYR A 322  GLU A 331 -1  O  TYR A 322   N  ARG A 272           
SHEET    4  AG 4 SER A 337  ILE A 342 -1  O  GLU A 338   N  VAL A 329           
SHEET    1  AH 3 LYS A 353  LEU A 356  0                                        
SHEET    2  AH 3 TYR A 369  LYS A 376 -1  O  GLN A 374   N  ASN A 355           
SHEET    3  AH 3 ALA A 418  LEU A 422 -1  O  ALA A 418   N  VAL A 373           
SHEET    1  AI 5 PHE A 362  LEU A 363  0                                        
SHEET    2  AI 5 ARG A 449  ALA A 456  1  O  ILE A 455   N  LEU A 363           
SHEET    3  AI 5 VAL A 428  THR A 437 -1  O  THR A 429   N  ALA A 456           
SHEET    4  AI 5 PRO A 387  ASP A 396 -1  O  THR A 389   N  LYS A 436           
SHEET    5  AI 5 SER A 402  VAL A 410 -1  O  SER A 402   N  THR A 394           
SHEET    1  AJ 3 TYR A 466  ILE A 467  0                                        
SHEET    2  AJ 3 HIS A 481  THR A 487 -1  O  THR A 487   N  TYR A 466           
SHEET    3  AJ 3 GLN A 524  PRO A 529 -1  O  GLN A 524   N  VAL A 486           
SHEET    1  AK 4 LYS A 508  GLU A 516  0                                        
SHEET    2  AK 4 HIS A 498  SER A 505 -1  O  TYR A 499   N  ARG A 515           
SHEET    3  AK 4 SER A 537  TYR A 544 -1  O  ARG A 539   N  LEU A 504           
SHEET    4  AK 4 VAL A 555  ASN A 562 -1  O  VAL A 555   N  TYR A 544           
SHEET    1  AL 3 GLN A 572  LEU A 575  0                                        
SHEET    2  AL 3 THR A 587  ALA A 593 -1  O  ASN A 591   N  HIS A 574           
SHEET    3  AL 3 ARG A 783  ALA A 789 -1  O  LYS A 784   N  MET A 592           
SHEET    1  AM 4 TRP A 773  VAL A 780  0                                        
SHEET    2  AM 4 SER A 598  ASP A 606 -1  O  SER A 598   N  VAL A 780           
SHEET    3  AM 4 THR A 796  SER A 805 -1  O  GLU A 798   N  VAL A 605           
SHEET    4  AM 4 GLY A 808  VAL A 811 -1  O  GLY A 808   N  SER A 805           
SHEET    1  AN 4 TRP A 773  VAL A 780  0                                        
SHEET    2  AN 4 SER A 598  ASP A 606 -1  O  SER A 598   N  VAL A 780           
SHEET    3  AN 4 THR A 796  SER A 805 -1  O  GLU A 798   N  VAL A 605           
SHEET    4  AN 4 VAL A 815  LYS A 818 -1  O  VAL A 815   N  ILE A 799           
SHEET    1  AO 2 GLY A 808  VAL A 811  0                                        
SHEET    2  AO 2 THR A 796  SER A 805 -1  O  GLY A 803   N  CYS A 810           
SHEET    1  AP 3 VAL A 823  MET A 827  0                                        
SHEET    2  AP 3 LYS A 842  ASN A 847 -1  O  THR A 844   N  GLU A 826           
SHEET    3  AP 3 SER A 892  THR A 897 -1  O  SER A 892   N  ASN A 847           
SHEET    1  AQ 4 GLN A 886  VAL A 888  0                                        
SHEET    2  AQ 4 MET A 853  ALA A 861 -1  O  MET A 853   N  VAL A 888           
SHEET    3  AQ 4 HIS A 908  THR A 916 -1  O  ASN A 911   N  SER A 860           
SHEET    4  AQ 4 GLU A 921  LEU A 927 -1  O  GLU A 921   N  LEU A 914           
SHEET    1  AR 2 ILE A 865  THR A 867  0                                        
SHEET    2  AR 2 VAL A 900  PRO A 902 -1  O  LEU A 901   N  CYS A 866           
SHEET    1  AS 4 LYS A 935  LEU A 944  0                                        
SHEET    2  AS 4 ALA A1357  VAL A1365 -1  O  ALA A1357   N  LEU A 944           
SHEET    3  AS 4 ILE A 973  LYS A 980 -1  O  LYS A 974   N  VAL A1364           
SHEET    4  AS 4 VAL A1338  VAL A1340 -1  O  VAL A1338   N  LEU A 977           
SHEET    1  AT 4 LYS A 957  PHE A 959  0                                        
SHEET    2  AT 4 LEU A1346  THR A1350 -1  O  LEU A1346   N  PHE A 959           
SHEET    3  AT 4 ASP A1312  TYR A1317 -1  O  ASP A1314   N  SER A1349           
SHEET    4  AT 4 ALA A1322  LYS A1327 -1  N  LEU A1323   O  VAL A1315           
SHEET    1  AU 2 ALA A1216  LYS A1219  0                                        
SHEET    2  AU 2 TYR A1225  TRP A1228 -1  O  TYR A1225   N  LYS A1219           
SHEET    1  AV 2 PHE A1377  TYR A1378  0                                        
SHEET    2  AV 2 SER A1407  TYR A1408 -1  O  SER A1407   N  TYR A1378           
SHEET    1  AW 4 ASP A1382  GLN A1384  0                                        
SHEET    2  AW 4 LYS A1400  VAL A1403 -1  O  ARG A1401   N  GLN A1384           
SHEET    3  AW 4 PHE A1477  GLU A1481 -1  O  PHE A1477   N  ILE A1402           
SHEET    4  AW 4 ILE A1432  ALA A1434 -1  O  SER A1433   N  PHE A1480           
SHEET    1  AX 5 PHE A1450  LYS A1456  0                                        
SHEET    2  AX 5 HIS A1459  LEU A1464 -1  O  HIS A1459   N  LYS A1456           
SHEET    3  AX 5 ALA A1422  SER A1427 -1  O  ALA A1422   N  LEU A1464           
SHEET    4  AX 5 ALA A1491  GLU A1497 -1  O  THR A1492   N  SER A1427           
SHEET    5  AX 5 CYS A1505  TYR A1509 -1  O  CYS A1505   N  VAL A1495           
SHEET    1  AY 4 LEU A1581  THR A1587  0                                        
SHEET    2  AY 4 TYR A1559  SER A1564 -1  O  ALA A1560   N  LYS A1586           
SHEET    3  AY 4 GLN A1616  GLY A1621 -1  O  TYR A1617   N  VAL A1563           
SHEET    4  AY 4 TRP A1644  TYR A1647 -1  O  TRP A1644   N  MET A1620           
SHEET    1  BA 2 GLY B  42  HIS B  47  0                                        
SHEET    2  BA 2 GLN B  68  CYS B  73 -1  O  GLU B  69   N  ARG B  46           
SHEET    1  BB 2 GLN B 100  VAL B 103  0                                        
SHEET    2  BB 2 VAL B 122  GLN B 125 -1  O  ALA B 123   N  LYS B 102           
SHEET    1  BC 3 ASN B 185  PRO B 186  0                                        
SHEET    2  BC 3 TYR B 230  ARG B 231  1  N  ARG B 231   O  ASN B 185           
SHEET    3  BC 3 THR B 220  VAL B 221 -1  O  VAL B 221   N  TYR B 230           
SHEET    1  BD 2 LEU B 236  GLY B 240  0                                        
SHEET    2  BD 2 SER B 312  THR B 327 -1  O  ASN B 324   N  GLY B 240           
SHEET    1  BE 2 ASP B 257  THR B 259  0                                        
SHEET    2  BE 2 SER B 312  THR B 327  1  O  PHE B 313   N  THR B 259           
SHEET    1  BF 2 SER B 440  SER B 442  0                                        
SHEET    2  BF 2 SER B 370  PHE B 381  1  O  LEU B 378   N  ILE B 441           
SHEET    1  BG 2 ALA B 481  VAL B 482  0                                        
SHEET    2  BG 2 SER B 370  PHE B 381 -1  O  GLY B 372   N  ALA B 481           
SHEET    1  BH 2 HIS B 364  PHE B 366  0                                        
SHEET    2  BH 2 LEU B 487  PRO B 489 -1  O  ALA B 488   N  TYR B 365           
SHEET    1  BI 2 THR B 547  TYR B 548  0                                        
SHEET    2  BI 2 LYS B 554  GLN B 555 -1  O  LYS B 554   N  TYR B 548           
SHEET    1  BJ 2 GLY B 643  PRO B 645  0                                        
SHEET    2  BJ 2 LEU B 661  LEU B 663 -1  O  TYR B 662   N  CYS B 644           
SHEET    1  BK 2 ASP B 667  VAL B 668  0                                        
SHEET    2  BK 2 PHE B 684  ARG B 685 -1  O  PHE B 684   N  VAL B 668           
SHEET    1  BL 2 GLU B 677  GLY B 680  0                                        
SHEET    2  BL 2 VAL B 697  GLN B 700 -1  O  GLU B 698   N  VAL B 679           
SHEET    1  BM 2 GLU B 703  ILE B 705  0                                        
SHEET    2  BM 2 LEU B 721  ARG B 723 -1  O  TYR B 722   N  CYS B 704           
SHEET    1  BN 3 ILE B 715  THR B 716  0                                        
SHEET    2  BN 3 SER B 727  LEU B 730 -1  O  GLU B 729   N  THR B 716           
SHEET    3  BN 3 ARG B 743  THR B 745 -1  O  TYR B 744   N  ILE B 728           
SHEET    1  BO 2 ASP B 799  LEU B 800  0                                        
SHEET    2  BO 2 SER B 813  PRO B 814 -1  O  SER B 813   N  LEU B 800           
SSBOND   1 CYS A  567    CYS A  810                          1555   1555  2.03  
SSBOND   2 CYS A  634    CYS A  669                          1555   1555  2.03  
SSBOND   3 CYS A  856    CYS A  883                          1555   1555  2.04  
SSBOND   4 CYS A  866    CYS A 1527                          1555   1555  2.05  
SSBOND   5 CYS A 1101    CYS A 1159                          1555   1555  2.04  
SSBOND   6 CYS A 1375    CYS A 1505                          1555   1555  2.03  
SSBOND   7 CYS A 1405    CYS A 1474                          1555   1555  2.04  
SSBOND   8 CYS A 1520    CYS A 1525                          1555   1555  2.05  
SSBOND   9 CYS A 1532    CYS A 1606                          1555   1555  2.04  
SSBOND  10 CYS A 1553    CYS A 1676                          1555   1555  2.04  
SSBOND  11 CYS A 1654    CYS A 1657                          1555   1555  2.05  
SSBOND  12 CYS B   22    CYS B   61                          1555   1555  2.04  
SSBOND  13 CYS B   24    CYS B   65                          1555   1555  2.04  
SSBOND  14 CYS B   35    CYS B   73                          1555   1555  2.03  
SSBOND  15 CYS B   39    CYS B   78                          1555   1555  2.03  
SSBOND  16 CYS B   82    CYS B  117                          1555   1555  2.02  
SSBOND  17 CYS B   93    CYS B  127                          1555   1555  2.06  
SSBOND  18 CYS B   96    CYS B  133                          1555   1555  2.05  
SSBOND  19 CYS B  140    CYS B  151                          1555   1555  2.03  
SSBOND  20 CYS B  146    CYS B  164                          1555   1555  2.04  
SSBOND  21 CYS B  158    CYS B  173                          1555   1555  2.05  
SSBOND  22 CYS B  180    CYS B  218                          1555   1555  2.04  
SSBOND  23 CYS B  399    CYS B  420                          1555   1555  2.03  
SSBOND  24 CYS B  499    CYS B  623                          1555   1555  2.05  
SSBOND  25 CYS B  521    CYS B  570                          1555   1555  2.02  
SSBOND  26 CYS B  523    CYS B  539                          1555   1555  2.04  
SSBOND  27 CYS B  526    CYS B  541                          1555   1555  2.03  
SSBOND  28 CYS B  543    CYS B  552                          1555   1555  2.05  
SSBOND  29 CYS B  577    CYS B  611                          1555   1555  2.05  
SSBOND  30 CYS B  589    CYS B  601                          1555   1555  2.05  
SSBOND  31 CYS B  644    CYS B  686                          1555   1555  2.04  
SSBOND  32 CYS B  672    CYS B  699                          1555   1555  2.06  
SSBOND  33 CYS B  704    CYS B  746                          1555   1555  2.05  
SSBOND  34 CYS B  732    CYS B  761                          1555   1555  2.04  
SSBOND  35 CYS B  773    CYS B  784                          1555   1555  2.03  
SSBOND  36 CYS B  786    CYS B  823                          1555   1555  2.03  
SSBOND  37 CYS B  793    CYS B  816                          1555   1555  2.04  
SSBOND  38 CYS B  801    CYS B  837                          1555   1555  2.05  
SSBOND  39 CYS B  862    CYS B  880                          1555   1555  2.03  
SSBOND  40 CYS B  867    CYS B  873                          1555   1555  2.06  
SSBOND  41 CYS B  882    CYS B  919                          1555   1555  2.04  
SSBOND  42 CYS B  888    CYS B  912                          1555   1555  2.05  
SSBOND  43 CYS B  897    CYS B  932                          1555   1555  2.03  
LINK         ND2 ASN A 911                 C1  NAG A1911     1555   1555  1.50  
LINK         ND2 ASN A1630                 C1  NAG A2630     1555   1555  1.50  
LINK         CD1 TRP B  29                 C1  BMA B1574     1555   1555  1.55  
LINK         OG1 THR B  38                 C1  FUC B1005     1555   1555  1.43  
LINK         ND2 ASN B 324                 C1  NAG B1324     1555   1555  1.62  
LINK         CD1 TRP B 568                 C1  BMA B1568     1555   1555  1.54  
LINK         CD1 TRP B 571                 C1  BMA B1571     1555   1555  1.55  
LINK         ND2 ASN B 855                 C1  NAG B1855     1555   1555  1.61  
LINK         OD1 ASP B 172                CA    CA B1000     1555   1555  2.76  
CISPEP   1 ASP A   61    LYS A   62          0        14.69                     
CISPEP   2 LYS A   62    LYS A   63          0        -0.25                     
CISPEP   3 GLN A   96    ASN A   97          0         3.70                     
CISPEP   4 SER A  100    TYR A  101          0        15.71                     
CISPEP   5 GLU A  207    ASP A  208          0        -5.16                     
CISPEP   6 MET A  283    GLN A  284          0         5.31                     
CISPEP   7 ALA A  286    MET A  287          0         0.00                     
CISPEP   8 HIS A  473    LYS A  474          0         3.42                     
CISPEP   9 TYR A  610    GLY A  611          0        -7.56                     
CISPEP  10 VAL A  612    GLN A  613          0        -3.66                     
CISPEP  11 SER A  767    TYR A  768          0       -12.05                     
CISPEP  12 TYR A  768    PHE A  769          0         2.24                     
CISPEP  13 GLU A  771    SER A  772          0        -1.00                     
CISPEP  14 GLU A  863    GLY A  864          0         1.74                     
CISPEP  15 SER A  870    PRO A  871          0        -0.73                     
CISPEP  16 ILE A  873    ASP A  874          0        -1.60                     
CISPEP  17 GLY A  906    LEU A  907          0        -0.43                     
CISPEP  18 LEU A  992    SER A  993          0       -11.35                     
CISPEP  19 ASN A 1221    PRO A 1222          0         2.63                     
CISPEP  20 TYR A 1280    GLY A 1281          0         5.69                     
CISPEP  21 GLY A 1281    GLY A 1282          0         0.61                     
CISPEP  22 PHE A 1284    TYR A 1285          0        15.12                     
CISPEP  23 TYR A 1285    SER A 1286          0        -5.66                     
CISPEP  24 SER A 1286    THR A 1287          0         7.94                     
CISPEP  25 THR A 1368    SER A 1369          0        15.44                     
CISPEP  26 GLU A 1484    VAL A 1485          0       -14.45                     
CISPEP  27 CYS A 1525    LYS A 1526          0         8.67                     
CISPEP  28 CYS A 1527    VAL A 1528          0         5.25                     
CISPEP  29 ILE A 1543    SER A 1544          0         0.65                     
CISPEP  30 GLU A 1571    ASN A 1572          0       -18.19                     
CISPEP  31 ASN A 1572    VAL A 1573          0        -8.15                     
CISPEP  32 LYS A 1586    THR A 1587          0         2.27                     
CISPEP  33 GLU A 1589    ALA A 1590          0        -0.39                     
CISPEP  34 PHE A 1633    ARG A 1634          0        20.13                     
CISPEP  35 THR A 1652    THR A 1653          0         6.82                     
CISPEP  36 THR A 1653    CYS A 1654          0         6.99                     
CISPEP  37 SER A 1656    CYS A 1657          0        -1.92                     
CISPEP  38 LYS B  143    PHE B  144          0       -18.85                     
CISPEP  39 GLU B  157    CYS B  158          0        -5.20                     
CISPEP  40 ASN B  159    GLY B  160          0        -7.82                     
CISPEP  41 ASP B  166    ASN B  167          0        -3.53                     
CISPEP  42 ARG B  171    ASP B  172          0       -12.10                     
CISPEP  43 CYS B  173    GLY B  174          0         2.75                     
CISPEP  44 GLY B  174    ARG B  175          0        -3.71                     
CISPEP  45 LYS B  177    ALA B  178          0         0.55                     
CISPEP  46 THR B  226    SER B  227          0        -5.76                     
CISPEP  47 SER B  227    ASN B  228          0       -12.48                     
CISPEP  48 GLU B  247    ASP B  248          0        -3.81                     
CISPEP  49 GLN B  274    GLY B  275          0        -0.92                     
CISPEP  50 GLY B  275    GLY B  276          0         0.16                     
CISPEP  51 SER B  286    SER B  287          0        -1.02                     
CISPEP  52 GLU B  291    ASN B  292          0       -17.70                     
CISPEP  53 ASN B  294    HIS B  295          0       -11.19                     
CISPEP  54 GLU B  403    THR B  404          0         0.78                     
CISPEP  55 GLU B  427    LYS B  428          0        -2.09                     
CISPEP  56 ALA B  437    GLU B  438          0         0.08                     
CISPEP  57 TRP B  568    GLY B  569          0         5.89                     
CISPEP  58 THR B  580    TYR B  581          0       -12.89                     
CISPEP  59 PRO B  592    ALA B  593          0        14.01                     
CISPEP  60 PRO B  594    GLN B  595          0       -15.36                     
CISPEP  61 GLY B  598    LYS B  599          0       -12.29                     
CISPEP  62 GLN B  607    GLU B  608          0        22.28                     
CISPEP  63 ILE B  615    MET B  616          0        -8.02                     
CISPEP  64 ASN B  619    GLY B  620          0        -9.04                     
CISPEP  65 GLY B  620    GLN B  621          0        -8.65                     
CISPEP  66 GLN B  621    PRO B  622          0        -3.94                     
CISPEP  67 MET B  630    LYS B  631          0       -18.46                     
CISPEP  68 ASP B  634    LEU B  635          0         3.28                     
CISPEP  69 THR B  674    GLY B  675          0         0.79                     
CISPEP  70 LEU B  713    THR B  714          0         8.55                     
CISPEP  71 THR B  716    PRO B  717          0        -3.14                     
CISPEP  72 PRO B  733    LYS B  734          0        -7.88                     
CISPEP  73 GLY B  740    PRO B  741          0        -0.43                     
CISPEP  74 GLY B  748    ASN B  749          0         3.23                     
CISPEP  75 GLN B  777    LYS B  778          0        22.15                     
CISPEP  76 LYS B  778    GLN B  779          0        18.64                     
CISPEP  77 SER B  780    GLY B  781          0       -13.18                     
CISPEP  78 SER B  782    GLU B  783          0         2.29                     
CISPEP  79 SER B  788    PRO B  789          0        -9.46                     
CISPEP  80 LEU B  832    HIS B  833          0       -20.33                     
CISPEP  81 GLY B  835    SER B  836          0        -4.42                     
CISPEP  82 ASP B  839    GLY B  840          0         0.86                     
CISPEP  83 GLU B  848    ARG B  849          0        10.67                     
CISPEP  84 ASN B  855    SER B  856          0        -3.60                     
CISPEP  85 LYS B  872    CYS B  873          0        -6.11                     
CISPEP  86 SER B  876    THR B  877          0       -11.13                     
CISPEP  87 CYS B  880    VAL B  881          0         1.22                     
CISPEP  88 GLY B  930    LYS B  931          0       -14.22                     
CISPEP  89 CYS B  932    LEU B  933          0         8.12                     
CRYST1  154.217  230.747  269.983  90.00  90.00  90.00 I 21 21 21    8          
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      0.006484  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004334  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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