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Entry: 2VDP
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HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDP              
TITLE     INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA            
TITLE    2 CHAIN PEPTIDE,LGGAKQAGDV                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HEADPIECE, RESIDUES 32-483;                                
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6  INTEGRIN ALPHA-IIB HEAVY CHAIN;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: HEADPIECE, RESIDUES 27-487;                                
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  16 CHAIN: H;                                                            
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  19 CHAIN: L;                                                            
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: FIBRINOGEN;                                                
COMPND  22 CHAIN: C;                                                            
COMPND  23 FRAGMENT: GAMMA CHAIN C-TERMINAL PEPTIDE, RESIDUES 428-437           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  19 ORGANISM_COMMON: MOUSE;                                              
SOURCE  20 ORGANISM_TAXID: 10090;                                               
SOURCE  21 STRAIN: BALB/C;                                                      
SOURCE  22 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: MOUSE;                                              
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 STRAIN: BALB/C;                                                      
SOURCE  28 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 SYNTHETIC: YES;                                                      
SOURCE  31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  32 ORGANISM_COMMON: HUMAN;                                              
SOURCE  33 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, PLATELET     
KEYWDS   2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,       
KEYWDS   3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE  
KEYWDS   4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,   
KEYWDS   5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM      
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDP    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDP    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDP    0                                                
JRNL        AUTH   T.A.SPRINGER,J.ZHU,T.XIAO                                    
JRNL        TITL   STRUCTURAL BASIS FOR DISTINCTIVE RECOGNITION OF FIBRINOGEN   
JRNL        TITL 2 GAMMAC PEPTIDE BY THE PLATELET INTEGRIN ALPHAIIBBETA3.       
JRNL        REF    J.CELL BIOL.                  V. 182   791 2008              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   18710925                                                     
JRNL        DOI    10.1083/JCB.200801146                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER            
REMARK   1  TITL   STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO   
REMARK   1  TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS                              
REMARK   1  REF    NATURE                        V. 432    59 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15378069                                                     
REMARK   1  DOI    10.1038/NATURE02976                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 51563                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2747                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3556                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 190                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10446                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 557                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.32000                                              
REMARK   3    B22 (A**2) : 1.32000                                              
REMARK   3    B33 (A**2) : -1.99000                                             
REMARK   3    B12 (A**2) : 0.66000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.579         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.274         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.036        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10930 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7321 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14918 ; 0.988 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17798 ; 0.770 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1375 ; 5.468 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   474 ;33.450 ;24.367       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1709 ;12.317 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;13.921 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1680 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12178 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2152 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2025 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7483 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5356 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5726 ; 0.080 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   521 ; 0.127 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    16 ; 0.104 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    53 ; 0.165 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7014 ; 1.677 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10928 ; 2.702 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4553 ; 1.567 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3977 ; 2.486 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    17                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.0690  12.1600  78.4970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1785 T22:   0.0504                                     
REMARK   3      T33:   0.0360 T12:   0.1509                                     
REMARK   3      T13:  -0.0454 T23:   0.3930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3750 L22:   8.6483                                     
REMARK   3      L33:   2.8785 L12:  -2.3624                                     
REMARK   3      L13:   0.0495 L23:   2.2085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1002 S12:   0.0363 S13:  -0.6719                       
REMARK   3      S21:   0.9044 S22:  -0.4605 S23:  -1.2706                       
REMARK   3      S31:   0.5267 S32:   0.8482 S33:   0.3604                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A    62                          
REMARK   3    ORIGIN FOR THE GROUP (A): 129.1270  21.5830  69.0850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1859 T22:   0.0273                                     
REMARK   3      T33:  -0.1243 T12:   0.0441                                     
REMARK   3      T13:   0.0150 T23:   0.2365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8674 L22:   3.5417                                     
REMARK   3      L33:   3.3466 L12:   0.5323                                     
REMARK   3      L13:  -0.4977 L23:   0.4667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0923 S12:  -0.0516 S13:  -0.1278                       
REMARK   3      S21:  -0.0728 S22:  -0.1415 S23:  -0.4017                       
REMARK   3      S31:   0.1215 S32:   0.3962 S33:   0.2338                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    63        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 118.6240  33.4510  64.5290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1027 T22:  -0.0203                                     
REMARK   3      T33:  -0.0304 T12:  -0.0561                                     
REMARK   3      T13:  -0.0160 T23:   0.1459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4535 L22:   1.3791                                     
REMARK   3      L33:   1.7087 L12:  -0.6441                                     
REMARK   3      L13:  -0.1526 L23:  -1.0647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0081 S12:  -0.0792 S13:   0.0914                       
REMARK   3      S21:   0.0890 S22:  -0.1625 S23:  -0.3784                       
REMARK   3      S31:   0.0419 S32:   0.3297 S33:   0.1706                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   116        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.0350  35.9960  63.7770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0843 T22:  -0.0087                                     
REMARK   3      T33:  -0.1198 T12:  -0.1092                                     
REMARK   3      T13:  -0.0308 T23:   0.0871                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4836 L22:   1.4638                                     
REMARK   3      L33:   2.6104 L12:  -0.1897                                     
REMARK   3      L13:  -2.0972 L23:  -0.2311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0740 S12:  -0.0332 S13:  -0.1254                       
REMARK   3      S21:   0.0758 S22:  -0.2023 S23:   0.2321                       
REMARK   3      S31:  -0.0665 S32:  -0.0686 S33:   0.1284                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   168        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.0020  24.3650  64.1220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0762 T22:  -0.0475                                     
REMARK   3      T33:  -0.0419 T12:  -0.0889                                     
REMARK   3      T13:   0.0044 T23:   0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6330 L22:   1.5137                                     
REMARK   3      L33:   2.9932 L12:  -0.2184                                     
REMARK   3      L13:  -0.6197 L23:  -1.0092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0352 S12:   0.2279 S13:  -0.1223                       
REMARK   3      S21:   0.0101 S22:  -0.1510 S23:   0.0540                       
REMARK   3      S31:   0.2412 S32:  -0.2279 S33:   0.1158                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  99.6470  13.0030  72.5440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0044 T22:  -0.1718                                     
REMARK   3      T33:  -0.0534 T12:  -0.1685                                     
REMARK   3      T13:   0.0695 T23:   0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4465 L22:   3.7954                                     
REMARK   3      L33:   5.1675 L12:  -0.9347                                     
REMARK   3      L13:  -0.3058 L23:   0.9602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0557 S12:   0.1869 S13:  -0.3731                       
REMARK   3      S21:  -0.0922 S22:  -0.1533 S23:   0.0995                       
REMARK   3      S31:   0.1491 S32:  -0.2706 S33:   0.2090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   291        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.7370   7.0990  84.5640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0223 T22:  -0.2859                                     
REMARK   3      T33:  -0.0845 T12:  -0.1026                                     
REMARK   3      T13:   0.0496 T23:   0.1900                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9057 L22:   5.2681                                     
REMARK   3      L33:   4.9168 L12:  -1.2266                                     
REMARK   3      L13:  -2.0852 L23:   2.4653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1696 S12:  -0.2839 S13:  -0.4264                       
REMARK   3      S21:   0.5635 S22:  -0.0600 S23:   0.1427                       
REMARK   3      S31:   0.8740 S32:   0.0499 S33:   0.2296                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   327        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A): 110.4340   2.8120  78.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1553 T22:  -0.2789                                     
REMARK   3      T33:  -0.0902 T12:  -0.0379                                     
REMARK   3      T13:   0.0800 T23:   0.1978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1275 L22:   2.5921                                     
REMARK   3      L33:   3.4108 L12:   0.4209                                     
REMARK   3      L13:   0.1007 L23:   0.3809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1837 S12:   0.0120 S13:  -0.3648                       
REMARK   3      S21:   0.0170 S22:  -0.2326 S23:   0.0377                       
REMARK   3      S31:   0.9074 S32:  -0.0394 S33:   0.4163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   373        A   452                          
REMARK   3    ORIGIN FOR THE GROUP (A): 124.3120   7.3840  80.2290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0044 T22:  -0.1094                                     
REMARK   3      T33:  -0.0525 T12:   0.0789                                     
REMARK   3      T13:   0.0232 T23:   0.2756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1197 L22:   2.3491                                     
REMARK   3      L33:   2.8387 L12:   0.1586                                     
REMARK   3      L13:  -0.1203 L23:  -0.5055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0731 S12:  -0.2664 S13:  -0.4662                       
REMARK   3      S21:   0.2293 S22:  -0.2609 S23:  -0.4038                       
REMARK   3      S31:   0.5759 S32:   0.5983 S33:   0.3339                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    72                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.4150  21.3850 169.6260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3264 T22:  -0.3717                                     
REMARK   3      T33:  -0.3740 T12:   0.1316                                     
REMARK   3      T13:  -0.1370 T23:  -0.1472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1347 L22:   3.1839                                     
REMARK   3      L33:   6.3418 L12:  -1.6565                                     
REMARK   3      L13:   2.1691 L23:  -1.5740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1645 S12:  -0.9077 S13:  -0.0482                       
REMARK   3      S21:   1.0447 S22:   0.4577 S23:  -0.2323                       
REMARK   3      S31:  -0.6025 S32:  -0.7964 S33:  -0.2932                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    79        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.8490  30.3390 149.4660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5938 T22:  -0.1017                                     
REMARK   3      T33:  -0.2527 T12:   0.3005                                     
REMARK   3      T13:   0.0271 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4990 L22:  10.5134                                     
REMARK   3      L33:  38.3639 L12:  -5.0049                                     
REMARK   3      L13:  16.4455 L23: -16.7198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7776 S12:  -0.7572 S13:   0.3265                       
REMARK   3      S21:   1.1927 S22:   0.6227 S23:  -0.6324                       
REMARK   3      S31:  -2.8502 S32:  -1.5784 S33:   0.1549                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    99        B   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  97.4680  38.1930 104.5680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2698 T22:  -0.0311                                     
REMARK   3      T33:  -0.1119 T12:  -0.1916                                     
REMARK   3      T13:   0.0765 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2858 L22:   0.3609                                     
REMARK   3      L33:   1.9942 L12:  -0.2502                                     
REMARK   3      L13:   0.2527 L23:  -0.7224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:  -0.1443 S13:   0.0050                       
REMARK   3      S21:   0.4069 S22:   0.0092 S23:  -0.0162                       
REMARK   3      S31:  -0.4653 S32:   0.0500 S33:   0.0102                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   173        B   338                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.9420  34.2690  96.2710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0616 T22:  -0.0771                                     
REMARK   3      T33:  -0.1866 T12:  -0.1855                                     
REMARK   3      T13:   0.0258 T23:   0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6648 L22:   1.6436                                     
REMARK   3      L33:   2.3486 L12:  -0.5337                                     
REMARK   3      L13:  -0.9118 L23:   0.0623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0554 S12:  -0.3395 S13:   0.0796                       
REMARK   3      S21:   0.4529 S22:  -0.0567 S23:  -0.0784                       
REMARK   3      S31:  -0.1301 S32:   0.2086 S33:   0.0012                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   339        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.1960  22.6550 131.2830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1223 T22:  -0.0895                                     
REMARK   3      T33:  -0.1368 T12:  -0.0782                                     
REMARK   3      T13:   0.1566 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7817 L22:   3.2226                                     
REMARK   3      L33:  21.2278 L12:  -1.8031                                     
REMARK   3      L13:   7.6309 L23:  -4.1690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6376 S12:   0.6941 S13:  -0.5921                       
REMARK   3      S21:  -0.1773 S22:   0.3031 S23:  -0.0403                       
REMARK   3      S31:   1.0732 S32:   0.7841 S33:  -0.9407                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   394        B   437                          
REMARK   3    ORIGIN FOR THE GROUP (A): 109.3310  28.2480 149.4790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2681 T22:  -0.4009                                     
REMARK   3      T33:  -0.2949 T12:  -0.0832                                     
REMARK   3      T13:  -0.0198 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1708 L22:   2.1877                                     
REMARK   3      L33:  20.4062 L12:  -1.8739                                     
REMARK   3      L13:   7.3523 L23:  -2.0611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4202 S12:   0.8589 S13:   0.2560                       
REMARK   3      S21:   0.7676 S22:   0.4524 S23:  -0.5348                       
REMARK   3      S31:  -1.8752 S32:   1.6414 S33:  -0.0322                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   438        B   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): 119.2080  31.4000 183.5950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6845 T22:   0.7793                                     
REMARK   3      T33:   0.6585 T12:  -0.0647                                     
REMARK   3      T13:  -0.7679 T23:  -0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3604 L22:   0.0157                                     
REMARK   3      L33:   6.2798 L12:  -0.2296                                     
REMARK   3      L13:  -4.5938 L23:   0.3138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.5493 S12:  -1.8097 S13:   0.5720                       
REMARK   3      S21:  -0.1441 S22:  -0.2731 S23:  -0.6768                       
REMARK   3      S31:  -2.6711 S32:   3.2783 S33:   1.8223                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H    13                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.7310  36.5670  33.4360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0172 T22:   0.0501                                     
REMARK   3      T33:  -0.1278 T12:  -0.1955                                     
REMARK   3      T13:  -0.1387 T23:   0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3175 L22:   8.3579                                     
REMARK   3      L33:  10.4725 L12:  -4.7524                                     
REMARK   3      L13:   6.0528 L23:  -8.2046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1507 S12:   0.4785 S13:  -0.6326                       
REMARK   3      S21:  -0.6786 S22:  -0.0684 S23:   0.3654                       
REMARK   3      S31:   1.0500 S32:  -0.2618 S33:  -0.0823                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    14        H    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9370  41.9070  41.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1957 T22:  -0.0093                                     
REMARK   3      T33:  -0.0769 T12:  -0.0497                                     
REMARK   3      T13:  -0.0161 T23:   0.0877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6793 L22:   2.3880                                     
REMARK   3      L33:   2.8221 L12:  -0.6181                                     
REMARK   3      L13:   0.5816 L23:  -0.0642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:  -0.0921 S13:  -0.0013                       
REMARK   3      S21:   0.0963 S22:   0.1119 S23:   0.2024                       
REMARK   3      S31:   0.2083 S32:  -0.3511 S33:  -0.1003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    55        H   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.7630  42.7960  43.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1959 T22:   0.0085                                     
REMARK   3      T33:  -0.0572 T12:  -0.0615                                     
REMARK   3      T13:   0.0169 T23:   0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4141 L22:   1.5081                                     
REMARK   3      L33:   3.6057 L12:  -0.5171                                     
REMARK   3      L13:   1.6828 L23:  -1.1660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0835 S12:  -0.1248 S13:   0.1779                       
REMARK   3      S21:  -0.0378 S22:   0.0488 S23:   0.0974                       
REMARK   3      S31:   0.1721 S32:  -0.1946 S33:   0.0347                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   111        H   134                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.1570  47.4620  13.1750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2719 T22:   0.1291                                     
REMARK   3      T33:  -0.0047 T12:  -0.1559                                     
REMARK   3      T13:  -0.1212 T23:   0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7787 L22:   1.9303                                     
REMARK   3      L33:   3.4840 L12:  -2.0125                                     
REMARK   3      L13:  -0.9340 L23:   1.9006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1384 S12:   0.1929 S13:  -0.4538                       
REMARK   3      S21:   0.0418 S22:   0.0025 S23:   0.0133                       
REMARK   3      S31:  -0.5796 S32:  -1.0782 S33:  -0.1409                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   137        H   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.2880  44.5370   4.8800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1725 T22:  -0.1351                                     
REMARK   3      T33:  -0.1671 T12:   0.0780                                     
REMARK   3      T13:  -0.1611 T23:   0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1673 L22:   1.5066                                     
REMARK   3      L33:  14.9147 L12:   0.7462                                     
REMARK   3      L13:  -6.6127 L23:   0.8251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2405 S12:   0.1712 S13:  -0.4571                       
REMARK   3      S21:  -0.1950 S22:   0.0166 S23:  -0.1318                       
REMARK   3      S31:   1.3225 S32:  -0.2606 S33:  -0.2571                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   165        H   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  94.3030  47.3030   9.4270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1524 T22:  -0.1546                                     
REMARK   3      T33:  -0.2672 T12:   0.0947                                     
REMARK   3      T13:  -0.0659 T23:   0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5770 L22:   1.3309                                     
REMARK   3      L33:  14.6915 L12:   1.1195                                     
REMARK   3      L13:  -2.0782 L23:   0.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3327 S12:  -0.3330 S13:   0.1400                       
REMARK   3      S21:  -0.4781 S22:   0.0059 S23:   0.1540                       
REMARK   3      S31:   0.5629 S32:   0.3316 S33:  -0.3386                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   190        H   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.6610  40.3190  -3.5120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4975 T22:   0.0628                                     
REMARK   3      T33:  -0.0634 T12:   0.3075                                     
REMARK   3      T13:  -0.1417 T23:  -0.1007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5970 L22:   1.3351                                     
REMARK   3      L33:   4.3298 L12:  -0.1422                                     
REMARK   3      L13:  -1.6085 L23:   1.2356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6915 S12:   0.0794 S13:  -1.5153                       
REMARK   3      S21:  -0.7848 S22:  -0.5788 S23:   0.0704                       
REMARK   3      S31:   0.8112 S32:   1.2039 S33:  -0.1127                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   207        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.9060  43.9930  -2.2810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2611 T22:   0.1164                                     
REMARK   3      T33:  -0.1512 T12:  -0.0110                                     
REMARK   3      T13:  -0.3487 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9463 L22:  11.0363                                     
REMARK   3      L33:  26.3478 L12:   6.4023                                     
REMARK   3      L13: -17.4415 L23:  -6.7556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6070 S12:   0.6738 S13:  -0.6419                       
REMARK   3      S21:  -1.4601 S22:   0.4788 S23:   0.5999                       
REMARK   3      S31:   2.1393 S32:  -1.7296 S33:   0.1282                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L    38                          
REMARK   3    ORIGIN FOR THE GROUP (A): 114.1110  49.9240  35.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1448 T22:   0.0275                                     
REMARK   3      T33:   0.0038 T12:   0.0487                                     
REMARK   3      T13:   0.0484 T23:   0.1657                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6173 L22:   0.7314                                     
REMARK   3      L33:   2.4751 L12:   0.5313                                     
REMARK   3      L13:  -0.1080 L23:   0.4539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1224 S12:   0.1503 S13:   0.2079                       
REMARK   3      S21:  -0.0825 S22:  -0.0736 S23:  -0.0461                       
REMARK   3      S31:  -0.2068 S32:   0.2741 S33:  -0.0488                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    39        L    69                          
REMARK   3    ORIGIN FOR THE GROUP (A): 113.3850  38.9760  36.4110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1109 T22:  -0.0153                                     
REMARK   3      T33:  -0.0673 T12:   0.0530                                     
REMARK   3      T13:   0.0000 T23:   0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7369 L22:   2.2959                                     
REMARK   3      L33:   4.0459 L12:   1.4300                                     
REMARK   3      L13:   0.0299 L23:  -1.5042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0381 S12:   0.3908 S13:  -0.3509                       
REMARK   3      S21:  -0.1819 S22:   0.0470 S23:  -0.0521                       
REMARK   3      S31:   0.7805 S32:   0.2280 S33:  -0.0851                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    70        L    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): 112.2070  45.4970  35.8190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1484 T22:  -0.0428                                     
REMARK   3      T33:  -0.0533 T12:   0.0151                                     
REMARK   3      T13:  -0.0583 T23:   0.1187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6233 L22:   1.8136                                     
REMARK   3      L33:   6.5969 L12:  -0.5726                                     
REMARK   3      L13:  -2.2635 L23:   0.4388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0520 S12:   0.3054 S13:  -0.0968                       
REMARK   3      S21:  -0.0765 S22:  -0.0371 S23:   0.0860                       
REMARK   3      S31:   0.3511 S32:  -0.0137 S33:   0.0891                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    98        L   135                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.2590  52.9530   8.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1465 T22:   0.2390                                     
REMARK   3      T33:  -0.0864 T12:   0.0824                                     
REMARK   3      T13:   0.0171 T23:   0.0899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8825 L22:   3.0048                                     
REMARK   3      L33:   6.5979 L12:  -2.0081                                     
REMARK   3      L13:   3.3815 L23:  -2.9352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5267 S12:   0.2634 S13:  -0.3226                       
REMARK   3      S21:  -0.4485 S22:  -0.2840 S23:   0.1670                       
REMARK   3      S31:   0.7147 S32:   0.2319 S33:  -0.2426                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   136        L   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.4740  59.5600   9.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2253 T22:   0.2441                                     
REMARK   3      T33:  -0.2343 T12:   0.0376                                     
REMARK   3      T13:  -0.0148 T23:   0.0669                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7928 L22:   7.7301                                     
REMARK   3      L33:   2.4874 L12:  -4.7425                                     
REMARK   3      L13:   2.8914 L23:  -2.1068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:  -0.2065 S13:   0.5781                       
REMARK   3      S21:   0.0780 S22:  -0.2879 S23:  -0.4460                       
REMARK   3      S31:  -0.0240 S32:   0.2947 S33:   0.2849                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   168        L   197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  95.0250  59.9230   3.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2568 T22:   0.1091                                     
REMARK   3      T33:  -0.1990 T12:   0.0406                                     
REMARK   3      T13:   0.0296 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0169 L22:   3.7924                                     
REMARK   3      L33:   5.9187 L12:  -3.6192                                     
REMARK   3      L13:   4.4036 L23:  -2.1424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:   0.2426 S13:   0.2185                       
REMARK   3      S21:  -0.2741 S22:  -0.1478 S23:  -0.0086                       
REMARK   3      S31:  -0.0331 S32:   0.1472 S33:   0.1577                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   198        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.9160  62.2880  -1.9010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2516 T22:   0.2085                                     
REMARK   3      T33:  -0.2139 T12:   0.1333                                     
REMARK   3      T13:   0.0801 T23:   0.1488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.6041 L22:   6.7983                                     
REMARK   3      L33:   5.6105 L12:  -6.6274                                     
REMARK   3      L13:   6.1128 L23:  -4.5203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5004 S12:   1.4644 S13:  -0.1356                       
REMARK   3      S21:  -0.5864 S22:  -0.5404 S23:  -0.1399                       
REMARK   3      S31:  -0.0577 S32:   1.0525 S33:   0.0400                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34116.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07223                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM (SBC2 3K)                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55536                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.5                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM            
REMARK 280  ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      118.10667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.05333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.05333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      118.10667            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, L                         
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     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     LEU C   402                                                      
REMARK 465     GLY C   403                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  4054     O    HOH A  4138              2.09            
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    SER A 101     -124.95     57.37                                   
REMARK 500    LYS A 118     -120.64     54.01                                   
REMARK 500    GLU A 123      131.39     95.90                                   
REMARK 500    LEU A 212      -47.91     70.94                                   
REMARK 500    SER A 261       73.01     52.65                                   
REMARK 500    THR A 296      138.86   -171.68                                   
REMARK 500    THR B   7       44.43    -97.90                                   
REMARK 500    ASP B  47       33.83    -97.44                                   
REMARK 500    VAL B  80       96.25     67.48                                   
REMARK 500    ASP B  95       -2.36     62.04                                   
REMARK 500    ASN B 148       30.72    -91.73                                   
REMARK 500    VAL B 157      -82.97   -127.51                                   
REMARK 500    SER B 213     -154.33   -116.15                                   
REMARK 500    LEU B 258       -8.34     82.77                                   
REMARK 500    VAL B 275      -79.59    -99.04                                   
REMARK 500    ALA B 309       79.01   -106.93                                   
REMARK 500    CYS B 374     -155.17    -92.48                                   
REMARK 500    LYS B 410      -23.84     73.48                                   
REMARK 500    GLU B 442       81.99     60.40                                   
REMARK 500    HIS B 446      -61.38     70.66                                   
REMARK 500    THR B 454      164.32     69.90                                   
REMARK 500    GLN C 407       76.95   -118.96                                   
REMARK 500    ASP H 179       -6.23     72.94                                   
REMARK 500    SER L  30       57.70     34.59                                   
REMARK 500    SER L  77       74.38     52.02                                   
REMARK 500    ASN L 212       77.51     51.55                                   
REMARK 500    GLU L 213       77.21   -153.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  51.7                                              
REMARK 620 3 ASP A 245   OD2 124.0  72.7                                        
REMARK 620 4 ASP A 247   O    79.4  76.1  95.7                                  
REMARK 620 5 THR A 250   O    72.0 121.8 163.1  80.9                            
REMARK 620 6 THR A 250   OG1 143.1 143.1  86.1  76.4  77.0                      
REMARK 620 7 GLU A 252   OE1  81.6  86.4  88.8 159.6 100.1 123.8                
REMARK 620 8 GLU A 252   OE2 128.4 129.9  80.0 149.0  94.3  72.7  51.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  79.3                                              
REMARK 620 3 ASP A 297   OD1  84.0  76.7                                        
REMARK 620 4 ARG A 303   O   164.6  92.3  81.4                                  
REMARK 620 5 ASP A 305   OD1 113.2 150.3 129.7  80.3                            
REMARK 620 6 ASP A 305   OD2  85.5 159.2  87.8  99.0  49.9                      
REMARK 620 7 HOH A4187   O   102.3  77.9 152.1  88.4  73.2 119.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 369   OD1  80.7                                              
REMARK 620 3 TYR A 371   O    79.1  80.7                                        
REMARK 620 4 ASP A 367   OD1  94.1  99.9 173.0                                  
REMARK 620 5 HOH A4200   O   148.2  69.2  86.1 100.8                            
REMARK 620 6 ASP A 373   OD1  99.9 177.5 101.8  77.6 110.7                      
REMARK 620 7 ASP A 373   OD2 134.7 132.1  77.6 106.6  67.1  49.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 432   O                                                      
REMARK 620 2 ASN A 430   OD1  87.8                                              
REMARK 620 3 ASP A 426   OD1  73.4  78.0                                        
REMARK 620 4 ASP A 428   OD1 146.5  84.9  73.1                                  
REMARK 620 5 ASP A 434   OD1 106.8 160.9  94.0  76.1                            
REMARK 620 6 ASP A 434   OD2  89.4 142.6 136.2 115.5  52.1                      
REMARK 620 7 HOH A4218   O   140.3  84.4 141.5  71.4  91.5  74.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1462   O2                                                     
REMARK 620 2 HOH C4006   O    96.3                                              
REMARK 620 3 ASP B 251   OD2 123.6 106.0                                        
REMARK 620 4 GOL B1462   O1   63.6  74.2  73.7                                  
REMARK 620 5 SER B 123   O   158.7  87.0  75.0 136.9                            
REMARK 620 6 ASP B 126   OD1  83.4  94.1 142.9 142.8  75.4                      
REMARK 620 7 ASP B 127   OD1  81.4 169.7  83.5 113.1  91.7  75.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1 100.0                                              
REMARK 620 3 ASP B 217   O   158.7  96.5                                        
REMARK 620 4 ASP B 217   OD1  90.7  91.6  75.4                                  
REMARK 620 5 PRO B 219   O    80.4 173.8  84.7  94.6                            
REMARK 620 6 GLU B 220   OE2 101.4  87.0  92.7 167.8  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B4046   O                                                      
REMARK 620 2 SER B 123   OG   90.3                                              
REMARK 620 3 GLU B 220   OE1  83.7 166.2                                        
REMARK 620 4 HOH B4012   O    94.7  86.9 105.9                                  
REMARK 620 5 ASP C 410   OD1  91.3  77.5  90.1 163.4                            
REMARK 620 6 SER B 121   OG  174.6  94.7  91.0  87.7  87.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1462                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514.                                                  
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN C SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 70906437 WHICH CORRESPONDS TO             
REMARK 999 THE UNIPROT ENTRY Q53Y18                                             
DBREF  2VDP A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDP B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDP C  402   411  UNP    Q53Y18   Q53Y18_HUMAN   428    437             
DBREF  2VDP H    1   221  PDB    2VDP     2VDP             1    221             
DBREF  2VDP L    1   214  PDB    2VDP     2VDP             1    214             
SEQADV 2VDP GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 C   10  LEU GLY GLY ALA LYS GLN ALA GLY ASP VAL                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HET    GOL  A1453       6                                                       
HET    GOL  B1462       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   7   CA    6(CA 2+)                                                     
FORMUL   8  MAN    8(C6 H12 O6)                                                 
FORMUL   9   MG    MG 2+                                                        
FORMUL  10  NAG    7(C8 H15 N O6)                                               
FORMUL  11  HOH   *557(H2 O)                                                    
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 SER B  121  LYS B  125  5                                   5    
HELIX   10  10 ASP B  127  THR B  146  1                                  20    
HELIX   11  11 PRO B  169  GLU B  174  5                                   6    
HELIX   12  12 CYS B  177  LYS B  181  5                                   5    
HELIX   13  13 GLN B  199  GLN B  210  1                                  12    
HELIX   14  14 GLY B  221  CYS B  232  1                                  12    
HELIX   15  15 CYS B  232  GLY B  237  1                                   6    
HELIX   16  16 LEU B  258  GLY B  264  5                                   7    
HELIX   17  17 SER B  291  LYS B  302  1                                  12    
HELIX   18  18 VAL B  314  ILE B  325  1                                  12    
HELIX   19  19 SER B  337  LYS B  350  1                                  14    
HELIX   20  20 CYS B  435  ALA B  439  5                                   5    
HELIX   21  21 ASN H   28  THR H   32  5                                   5    
HELIX   22  22 PRO H   62  PHE H   64  5                                   3    
HELIX   23  23 THR H   87  THR H   91  5                                   5    
HELIX   24  24 SER H  162  SER H  164  5                                   3    
HELIX   25  25 PRO H  206  SER H  209  5                                   4    
HELIX   26  26 ASP L   79  PHE L   83  5                                   5    
HELIX   27  27 SER L  121  GLY L  128  1                                   8    
HELIX   28  28 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 5 GLY A  63  GLN A  64  0                                        
SHEET    2  AA 5 LEU A   3  ALA A  12  1  O  PHE A  10   N  GLY A  63           
SHEET    3  AA 5 GLN A 444  ALA A 450 -1  O  VAL A 445   N  TYR A  11           
SHEET    4  AA 5 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    5  AA 5 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 3 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 3 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 3 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 THR A 125  PRO A 126 -1  N  THR A 125   O  TRP A 113           
SHEET    1  AD 4 THR A  76  VAL A  79  0                                        
SHEET    2  AD 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AD 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AD 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AE 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AE 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AE 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AE 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AF 4 SER A 172  VAL A 175  0                                        
SHEET    2  AF 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AF 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AF 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AG 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AG 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AG 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AG 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AH 4 VAL A 293  THR A 296  0                                        
SHEET    2  AH 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AH 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AH 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AI 2 MET A 314  ARG A 317  0                                        
SHEET    2  AI 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AJ 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AJ 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AJ 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AJ 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AK 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AK 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  LEU B  40  0                                        
SHEET    2  BA 3 CYS B  23  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BA 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BB 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 SER B 353  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  LEU B 389 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 9 SER L  10  VAL L  13  0                                        
SHEET    2  LB 9 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 9 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 9 ASN L  53  LEU L  54                                           
SHEET    5  LB 9 PHE L  44  TYR L  49 -1  O  TYR L  49   N  ASN L  53           
SHEET    6  LB 9 ILE L  33  GLN L  38 -1  O  TRP L  35   N  LEU L  47           
SHEET    7  LB 9 ASP L  85  GLN L  90 -1  O  ASP L  85   N  GLN L  38           
SHEET    8  LB 9 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    9  LB 9 ASP L  85  GLN L  90 -1  O  GLN L  90   N  THR L  97           
SHEET    1  LC 4 THR L 114  PHE L 118  0                                        
SHEET    2  LC 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LC 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LC 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LD 4 SER L 153  ARG L 155  0                                        
SHEET    2  LD 4 ASN L 145  ILE L 150 -1  O  TRP L 148   N  ARG L 155           
SHEET    3  LD 4 SER L 191  THR L 197 -1  O  THR L 193   N  LYS L 149           
SHEET    4  LD 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.08  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.05  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.05  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.07  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.06  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.05  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.04  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.09  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.45  
LINK         ND2 ASN A 249                 C1  NAG A3249     1555   1555  1.45  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.30  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.42  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.37  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.54  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.44  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.60  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.59  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.44  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.30  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.40  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.53  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.68  
LINK        CA    CA A2005                 O   HOH A4187     1555   1555  2.18  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.47  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.15  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.29  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.27  
LINK        CA    CA A2006                 O   HOH A4200     1555   1555  2.33  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.64  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.67  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.48  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.67  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.44  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.50  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.59  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.38  
LINK        CA    CA A2007                 O   HOH A4218     1555   1555  2.20  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.27  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.16  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.43  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.43  
LINK        MG    MG B2001                 O   HOH B4012     1555   1555  2.25  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.15  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.06  
LINK        MG    MG B2001                 OD1 ASP C 410     1555   1555  2.31  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.02  
LINK        MG    MG B2001                 O   HOH B4046     1555   1555  2.20  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.22  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.45  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.30  
LINK        CA    CA B2002                 O1  GOL B1462     1555   1555  2.79  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.31  
LINK        CA    CA B2002                 O   HOH C4006     1555   1555  2.32  
LINK        CA    CA B2002                 O2  GOL B1462     1555   1555  2.32  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.38  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.32  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.28  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.33  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.23  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.39  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.44  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.44  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.45  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
LINK         O3  MAN B3373                 C1  MAN B3374     1555   1555  1.45  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.45  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0         4.78                     
CISPEP   2 SER B  162    PRO B  163          0         3.91                     
CISPEP   3 SER B  168    PRO B  169          0       -10.12                     
CISPEP   4 PHE H  152    PRO H  153          0        -1.75                     
CISPEP   5 GLU H  154    PRO H  155          0        -2.36                     
CISPEP   6 TRP H  194    PRO H  195          0         6.45                     
CISPEP   7 SER L    7    PRO L    8          0        -9.26                     
CISPEP   8 LEU L   94    PRO L   95          0        -1.13                     
CISPEP   9 TYR L  140    PRO L  141          0         2.54                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A4187                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4200                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4218                                          
SITE     1 AC5  2 ASN A  15  HOH A4228                                          
SITE     1 AC6  1 ASN A 249                                                     
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  HOH B4012                    
SITE     2 AC7  6 HOH B4046  ASP C 410                                          
SITE     1 AC8  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC8  6 GOL B1462  HOH C4006                                          
SITE     1 AC9  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC9  5 GLU B 220                                                     
SITE     1 BC1  4 ASN B  99  SER B 398  HOH B4096  HOH B4097                    
SITE     1 BC2  4 MET A 285  LEU B 317  ASN B 320  NAG B3321                    
SITE     1 BC3  5 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     2 BC3  5 HOH B4099                                                     
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  2 ARG A 281  MAN B3322                                          
SITE     1 BC6  3 NAG B3321  MAN B3322  HOH B4100                               
SITE     1 BC7  5 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC7  5 NAG B3372                                                     
SITE     1 BC8  4 NAG B3371  MAN B3373  MAN B3375  MAN B3376                    
SITE     1 BC9  5 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  5 MAN B3375                                                     
SITE     1 CC1  4 ASN A 299  SER A 396  GLU A 397  MAN B3373                    
SITE     1 CC2  6 ALA A 342  PRO A 343  NAG B3372  MAN B3373                    
SITE     2 CC2  6 MAN B3376  MAN B3377                                          
SITE     1 CC3  7 PRO A 343  SER A 344  LEU A 346  NAG B3372                    
SITE     2 CC3  7 MAN B3375  HOH B4101  HOH B4102                               
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  3 ARG A  90  HIS A 112  HOH A4053                               
SITE     1 CC6  5 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 CC6  5  CA B2002                                                     
CRYST1  148.429  148.429  177.160  90.00  90.00 120.00 P 32 2 1      6          
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      0.006737  0.003890  0.000000        0.00000                         
SCALE2      0.000000  0.007779  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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