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Database: PDB
Entry: 2VDO
LinkDB: 2VDO
Original site: 2VDO 
HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDO              
TITLE     INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA            
TITLE    2 CHAIN PEPTIDE, HHLGGAKQAGDV                                          
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, GAMMA POLYPEPTIDE;                             
COMPND  22 CHAIN: C;                                                            
COMPND  23 FRAGMENT: GAMMA CHAIN C-TERMINAL PEPTIDE, RESIDUES 426-437           
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 2VDO    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDO    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDO    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.    2.51 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) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 71126                          
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) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3807                            
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) : 2.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4785                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 260                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10538                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 1043                                    
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) : 51.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.266         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.761        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11034 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7394 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15073 ; 1.046 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18001 ; 0.789 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1397 ; 5.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   481 ;33.588 ;24.324       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1735 ;12.148 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    61 ;13.892 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1698 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12310 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2178 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1982 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7585 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5314 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5775 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   868 ; 0.137 ; 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):    18 ; 0.103 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    67 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    34 ; 0.148 ; 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):  7079 ; 1.852 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11024 ; 2.876 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4606 ; 1.939 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4028 ; 2.908 ;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): 132.9320  12.1020  78.3570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1882 T22:   0.0993                                     
REMARK   3      T33:   0.0165 T12:   0.0713                                     
REMARK   3      T13:  -0.0553 T23:   0.4004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3390 L22:  13.4216                                     
REMARK   3      L33:   3.7125 L12:  -2.4833                                     
REMARK   3      L13:  -0.6286 L23:   0.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1973 S12:  -0.0949 S13:  -0.3419                       
REMARK   3      S21:   0.5329 S22:  -0.1952 S23:  -0.9466                       
REMARK   3      S31:   0.5544 S32:   0.8323 S33:   0.3925                       
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): 129.0170  21.6150  68.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2484 T22:  -0.0629                                     
REMARK   3      T33:  -0.0864 T12:   0.0313                                     
REMARK   3      T13:   0.0143 T23:   0.2485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1771 L22:   6.1405                                     
REMARK   3      L33:   3.3315 L12:   0.0302                                     
REMARK   3      L13:  -0.1408 L23:   1.7500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0547 S12:  -0.0095 S13:  -0.1112                       
REMARK   3      S21:  -0.1423 S22:  -0.2830 S23:  -0.5369                       
REMARK   3      S31:   0.1076 S32:   0.3626 S33:   0.2283                       
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): 118.5350  33.3710  64.2890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2743 T22:  -0.1151                                     
REMARK   3      T33:  -0.1125 T12:  -0.0931                                     
REMARK   3      T13:  -0.0503 T23:   0.1361                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0076 L22:   1.6247                                     
REMARK   3      L33:   2.1037 L12:  -0.4411                                     
REMARK   3      L13:  -0.3526 L23:  -0.6230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0394 S12:  -0.0131 S13:   0.0086                       
REMARK   3      S21:   0.2021 S22:  -0.2131 S23:  -0.2712                       
REMARK   3      S31:  -0.0583 S32:   0.3853 S33:   0.1737                       
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): 106.9730  35.9030  63.4940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2434 T22:  -0.1651                                     
REMARK   3      T33:  -0.1988 T12:  -0.0866                                     
REMARK   3      T13:  -0.0376 T23:   0.0904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8786 L22:   1.4552                                     
REMARK   3      L33:   2.5665 L12:   0.4195                                     
REMARK   3      L13:  -1.9370 L23:  -0.1162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0199 S12:   0.0112 S13:  -0.1160                       
REMARK   3      S21:   0.0517 S22:  -0.1345 S23:   0.2048                       
REMARK   3      S31:   0.0121 S32:  -0.0421 S33:   0.1545                       
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): 105.9430  24.3110  63.8110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1889 T22:  -0.1844                                     
REMARK   3      T33:  -0.1462 T12:  -0.0824                                     
REMARK   3      T13:  -0.0100 T23:   0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9301 L22:   0.9556                                     
REMARK   3      L33:   1.9082 L12:  -0.0965                                     
REMARK   3      L13:  -0.6960 L23:  -0.4877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0272 S12:   0.1340 S13:  -0.1451                       
REMARK   3      S21:   0.0620 S22:  -0.1453 S23:  -0.0107                       
REMARK   3      S31:   0.2669 S32:  -0.1252 S33:   0.1181                       
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):  99.5560  12.9550  72.2190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0511 T22:  -0.2704                                     
REMARK   3      T33:  -0.0903 T12:  -0.1386                                     
REMARK   3      T13:   0.0535 T23:   0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4651 L22:   2.1919                                     
REMARK   3      L33:   3.8818 L12:   0.0965                                     
REMARK   3      L13:  -0.3252 L23:   0.5447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0558 S12:   0.1083 S13:  -0.2652                       
REMARK   3      S21:  -0.0325 S22:  -0.1912 S23:   0.1392                       
REMARK   3      S31:   0.4367 S32:  -0.2824 S33:   0.2470                       
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): 107.6080   7.0420  84.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0178 T22:  -0.2870                                     
REMARK   3      T33:  -0.0417 T12:  -0.0921                                     
REMARK   3      T13:   0.1011 T23:   0.2083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1282 L22:   5.3829                                     
REMARK   3      L33:   4.2387 L12:  -0.3323                                     
REMARK   3      L13:  -0.8189 L23:   2.9501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1844 S12:  -0.2593 S13:  -0.4108                       
REMARK   3      S21:   0.5516 S22:  -0.0453 S23:   0.1828                       
REMARK   3      S31:   0.9945 S32:   0.0143 S33:   0.2297                       
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): 110.1110   2.6630  78.4070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1302 T22:  -0.2959                                     
REMARK   3      T33:  -0.0399 T12:  -0.0369                                     
REMARK   3      T13:   0.1245 T23:   0.1794                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1018 L22:   3.3161                                     
REMARK   3      L33:   3.5102 L12:   0.4561                                     
REMARK   3      L13:  -0.0668 L23:   1.5637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1560 S12:  -0.0510 S13:  -0.4472                       
REMARK   3      S21:  -0.0115 S22:  -0.3381 S23:  -0.0598                       
REMARK   3      S31:   0.7308 S32:  -0.0741 S33:   0.4941                       
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): 124.1760   7.3280  79.9870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0488 T22:  -0.1037                                     
REMARK   3      T33:   0.0185 T12:   0.1029                                     
REMARK   3      T13:   0.0088 T23:   0.3095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9989 L22:   3.1486                                     
REMARK   3      L33:   3.0821 L12:   0.7461                                     
REMARK   3      L13:  -0.5003 L23:   0.0210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1362 S12:  -0.2629 S13:  -0.4431                       
REMARK   3      S21:   0.2734 S22:  -0.2923 S23:  -0.3881                       
REMARK   3      S31:   0.5990 S32:   0.6262 S33:   0.4285                       
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): 106.2680  21.3490 169.1560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4446 T22:  -0.3282                                     
REMARK   3      T33:  -0.3172 T12:   0.2057                                     
REMARK   3      T13:  -0.1188 T23:  -0.0935                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1423 L22:   4.0518                                     
REMARK   3      L33:  12.2091 L12:  -1.8839                                     
REMARK   3      L13:   5.5295 L23:  -2.9334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2719 S12:  -0.7559 S13:  -0.1586                       
REMARK   3      S21:   1.1934 S22:   0.3932 S23:  -0.4537                       
REMARK   3      S31:  -1.3284 S32:  -1.1794 S33:  -0.1213                       
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): 103.3770  29.3140 150.3420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6342 T22:  -0.0747                                     
REMARK   3      T33:  -0.0889 T12:   0.2407                                     
REMARK   3      T13:   0.0477 T23:  -0.0627                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6249 L22:  10.9980                                     
REMARK   3      L33:  39.4491 L12:  -4.3203                                     
REMARK   3      L13:  18.1102 L23: -15.1056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8897 S12:  -0.1758 S13:   0.7367                       
REMARK   3      S21:   1.1894 S22:   0.2821 S23:  -0.3446                       
REMARK   3      S31:  -3.5011 S32:  -1.1316 S33:   0.6077                       
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):  97.2700  38.1520 104.2390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1489 T22:  -0.0805                                     
REMARK   3      T33:  -0.1421 T12:  -0.2200                                     
REMARK   3      T13:   0.0447 T23:   0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2900 L22:   0.6087                                     
REMARK   3      L33:   1.4657 L12:  -0.3639                                     
REMARK   3      L13:   0.1069 L23:  -0.6001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:  -0.1666 S13:   0.0278                       
REMARK   3      S21:   0.4045 S22:   0.0270 S23:  -0.0117                       
REMARK   3      S31:  -0.4364 S32:   0.0948 S33:   0.0025                       
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): 102.7660  34.2180  95.9670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0421 T22:  -0.1583                                     
REMARK   3      T33:  -0.1993 T12:  -0.1953                                     
REMARK   3      T13:  -0.0108 T23:   0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4144 L22:   1.5802                                     
REMARK   3      L33:   2.1419 L12:  -0.2922                                     
REMARK   3      L13:  -0.7488 L23:   0.1298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0546 S12:  -0.2660 S13:   0.0958                       
REMARK   3      S21:   0.4302 S22:  -0.0990 S23:  -0.1348                       
REMARK   3      S31:  -0.0602 S32:   0.2247 S33:   0.0444                       
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):  99.9420  22.6510 130.8710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2490 T22:  -0.1016                                     
REMARK   3      T33:  -0.1234 T12:  -0.1048                                     
REMARK   3      T13:   0.0497 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7877 L22:   2.6048                                     
REMARK   3      L33:  26.1509 L12:  -2.7908                                     
REMARK   3      L13:   9.7730 L23:  -6.4844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6859 S12:   0.6576 S13:  -0.4734                       
REMARK   3      S21:  -0.3428 S22:   0.1939 S23:   0.1621                       
REMARK   3      S31:   1.4197 S32:   0.8471 S33:  -0.8798                       
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): 109.1530  28.2510 149.0690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4274 T22:  -0.3109                                     
REMARK   3      T33:  -0.1764 T12:  -0.1030                                     
REMARK   3      T13:  -0.0343 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1854 L22:   2.3089                                     
REMARK   3      L33:  23.1613 L12:  -1.4769                                     
REMARK   3      L13:   8.9390 L23:  -1.7802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4599 S12:   0.6106 S13:   0.1900                       
REMARK   3      S21:   0.6233 S22:   0.4505 S23:  -0.6388                       
REMARK   3      S31:  -2.2981 S32:   1.6894 S33:   0.0094                       
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): 119.0870  31.3350 183.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9511 T22:   0.8137                                     
REMARK   3      T33:   0.6802 T12:  -0.1471                                     
REMARK   3      T13:  -0.8658 T23:  -0.1889                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7646 L22:   5.4692                                     
REMARK   3      L33:  18.1237 L12:   4.5045                                     
REMARK   3      L13:  -6.9758 L23:  -8.9896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2075 S12:  -0.8478 S13:   1.0823                       
REMARK   3      S21:   2.1226 S22:  -0.1486 S23:  -1.9113                       
REMARK   3      S31:  -4.3227 S32:   3.7870 S33:   0.3561                       
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):  89.7690  36.5350  33.1670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2245 T22:  -0.0696                                     
REMARK   3      T33:  -0.0902 T12:  -0.1700                                     
REMARK   3      T13:  -0.0138 T23:   0.0502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.0138 L22:  17.6137                                     
REMARK   3      L33:  11.8823 L12: -12.1686                                     
REMARK   3      L13:   8.8313 L23:  -9.6293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3507 S12:   0.3005 S13:  -1.1269                       
REMARK   3      S21:  -0.7807 S22:   0.1389 S23:   0.8024                       
REMARK   3      S31:   0.9651 S32:  -0.1217 S33:  -0.4896                       
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):  93.9400  41.8470  41.1790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2765 T22:  -0.1044                                     
REMARK   3      T33:  -0.1415 T12:  -0.0490                                     
REMARK   3      T13:  -0.0106 T23:   0.0860                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8415 L22:   1.8079                                     
REMARK   3      L33:   2.1204 L12:   0.2694                                     
REMARK   3      L13:   0.3730 L23:  -0.0486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0117 S12:   0.0100 S13:   0.0240                       
REMARK   3      S21:   0.0131 S22:   0.0321 S23:   0.1562                       
REMARK   3      S31:   0.2438 S32:  -0.2276 S33:  -0.0438                       
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):  93.7550  42.7160  43.4000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2598 T22:  -0.1033                                     
REMARK   3      T33:  -0.1137 T12:  -0.0739                                     
REMARK   3      T13:  -0.0109 T23:   0.0807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2994 L22:   0.4697                                     
REMARK   3      L33:   2.9323 L12:  -0.6681                                     
REMARK   3      L13:   1.2150 L23:  -0.8749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0618 S12:   0.0211 S13:   0.0989                       
REMARK   3      S21:  -0.0239 S22:   0.0014 S23:   0.0234                       
REMARK   3      S31:   0.1811 S32:  -0.3198 S33:   0.0604                       
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):  86.1990  47.5650  12.7000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3169 T22:   0.1195                                     
REMARK   3      T33:  -0.0732 T12:  -0.0740                                     
REMARK   3      T13:  -0.0794 T23:   0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2362 L22:   1.0957                                     
REMARK   3      L33:   3.7495 L12:  -1.1328                                     
REMARK   3      L13:   0.2121 L23:   0.2679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2808 S12:  -0.0405 S13:  -0.2693                       
REMARK   3      S21:  -0.0160 S22:  -0.1528 S23:   0.0973                       
REMARK   3      S31:  -0.0467 S32:  -0.6355 S33:  -0.1279                       
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):  92.2760  44.6200   4.6690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2932 T22:  -0.1692                                     
REMARK   3      T33:  -0.2078 T12:   0.0717                                     
REMARK   3      T13:  -0.1150 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9266 L22:   1.0004                                     
REMARK   3      L33:  14.2986 L12:  -2.4433                                     
REMARK   3      L13:  -4.7739 L23:   1.6041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4514 S12:   0.2063 S13:  -0.7114                       
REMARK   3      S21:  -0.2674 S22:  -0.3841 S23:   0.1243                       
REMARK   3      S31:   0.7970 S32:   0.2007 S33:  -0.0672                       
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):  94.3010  47.3970   9.1790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3257 T22:  -0.1987                                     
REMARK   3      T33:  -0.2788 T12:   0.1107                                     
REMARK   3      T13:  -0.0909 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.6160 L22:   1.9983                                     
REMARK   3      L33:  13.2310 L12:  -0.4580                                     
REMARK   3      L13:  -3.7996 L23:  -0.2035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4320 S12:  -0.4239 S13:   0.0020                       
REMARK   3      S21:  -0.3732 S22:  -0.1038 S23:  -0.0466                       
REMARK   3      S31:   0.6002 S32:   0.6535 S33:  -0.3282                       
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):  93.7780  40.4300  -3.6580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:  -0.0426                                     
REMARK   3      T33:  -0.1476 T12:   0.2758                                     
REMARK   3      T13:  -0.0960 T23:  -0.1315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7757 L22:   3.9136                                     
REMARK   3      L33:   6.2447 L12:   0.4237                                     
REMARK   3      L13:  -2.4523 L23:  -0.9758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6118 S12:   0.4813 S13:  -1.2766                       
REMARK   3      S21:  -0.8540 S22:  -0.7092 S23:  -0.0382                       
REMARK   3      S31:   0.5831 S32:   0.3961 S33:   0.0974                       
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):  85.8370  43.5500  -1.9310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1855 T22:   0.0345                                     
REMARK   3      T33:  -0.0956 T12:   0.0578                                     
REMARK   3      T13:  -0.2759 T23:  -0.0964                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9762 L22:   4.6661                                     
REMARK   3      L33:  15.7770 L12:   2.5961                                     
REMARK   3      L13:  -8.4835 L23:  -0.0704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3870 S12:   0.5271 S13:  -0.6436                       
REMARK   3      S21:  -1.3335 S22:   0.1229 S23:   0.8409                       
REMARK   3      S31:   1.9895 S32:  -0.8019 S33:   0.2641                       
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): 114.1070  49.9490  35.1290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2726 T22:  -0.0949                                     
REMARK   3      T33:  -0.0562 T12:   0.0350                                     
REMARK   3      T13:   0.0170 T23:   0.1437                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0134 L22:   0.7562                                     
REMARK   3      L33:   2.1007 L12:   0.7360                                     
REMARK   3      L13:  -0.5759 L23:   0.4119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1040 S12:   0.2783 S13:   0.2746                       
REMARK   3      S21:  -0.0646 S22:  -0.0411 S23:   0.0119                       
REMARK   3      S31:  -0.0664 S32:   0.0992 S33:  -0.0630                       
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): 113.4010  39.0080  36.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2137 T22:  -0.1133                                     
REMARK   3      T33:  -0.1353 T12:   0.0267                                     
REMARK   3      T13:  -0.0125 T23:   0.0945                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5345 L22:   1.8099                                     
REMARK   3      L33:   2.2669 L12:   0.3649                                     
REMARK   3      L13:  -0.0669 L23:  -0.8368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0157 S12:   0.3718 S13:  -0.2639                       
REMARK   3      S21:  -0.1599 S22:   0.1330 S23:  -0.0711                       
REMARK   3      S31:   0.5319 S32:   0.1353 S33:  -0.1174                       
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): 112.1810  45.5600  35.6380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2667 T22:  -0.1490                                     
REMARK   3      T33:  -0.1319 T12:  -0.0084                                     
REMARK   3      T13:  -0.0302 T23:   0.0966                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9213 L22:   0.9542                                     
REMARK   3      L33:   5.4599 L12:  -0.7525                                     
REMARK   3      L13:  -1.7655 L23:   0.0516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0217 S12:   0.3695 S13:  -0.0510                       
REMARK   3      S21:  -0.0058 S22:  -0.0539 S23:   0.1147                       
REMARK   3      S31:   0.3861 S32:  -0.1419 S33:   0.0755                       
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): 100.3050  52.9530   8.0760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2881 T22:   0.0465                                     
REMARK   3      T33:  -0.1507 T12:   0.0622                                     
REMARK   3      T13:   0.0160 T23:   0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2854 L22:   1.9437                                     
REMARK   3      L33:   5.8958 L12:  -1.9374                                     
REMARK   3      L13:   3.5235 L23:  -2.6131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4621 S12:   0.3527 S13:  -0.2704                       
REMARK   3      S21:  -0.2924 S22:  -0.3435 S23:   0.1354                       
REMARK   3      S31:   0.4835 S32:   0.3681 S33:  -0.1186                       
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): 101.4590  59.6270   8.7240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3834 T22:   0.1493                                     
REMARK   3      T33:  -0.2440 T12:   0.0510                                     
REMARK   3      T13:  -0.0031 T23:   0.0308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6961 L22:   5.2547                                     
REMARK   3      L33:   2.8572 L12:  -4.4602                                     
REMARK   3      L13:   2.9753 L23:  -2.3522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1208 S12:  -0.1972 S13:   0.5044                       
REMARK   3      S21:   0.1206 S22:  -0.1868 S23:  -0.4294                       
REMARK   3      S31:  -0.0663 S32:   0.3298 S33:   0.3076                       
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):  95.1880  59.8360   2.9730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3512 T22:  -0.0006                                     
REMARK   3      T33:  -0.2585 T12:   0.0468                                     
REMARK   3      T13:  -0.0067 T23:   0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7968 L22:   4.3387                                     
REMARK   3      L33:   4.7133 L12:  -5.0596                                     
REMARK   3      L13:   4.5306 L23:  -2.6858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0511 S12:   0.2758 S13:   0.0881                       
REMARK   3      S21:  -0.2341 S22:  -0.1424 S23:  -0.0250                       
REMARK   3      S31:   0.0375 S32:   0.2784 S33:   0.0913                       
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): 102.6600  62.2790  -2.3980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3440 T22:   0.1709                                     
REMARK   3      T33:  -0.1917 T12:   0.1622                                     
REMARK   3      T13:   0.0901 T23:   0.1440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.1961 L22:   5.2787                                     
REMARK   3      L33:  12.6441 L12:  -4.6242                                     
REMARK   3      L13:   9.7312 L23:  -5.3059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5371 S12:   1.5211 S13:   0.3215                       
REMARK   3      S21:  -0.5150 S22:  -0.7958 S23:  -0.3958                       
REMARK   3      S31:   0.2665 S32:   1.2939 S33:   0.2587                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VDO 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-34088.                                       
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   : 557015                             
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.2                                
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      117.71133            
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       58.85567            
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       58.85567            
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      117.71133            
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: 11960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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     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  4100     O    HOH A  4252              2.04            
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     -122.75     50.05                                   
REMARK 500    LYS A 118     -122.03     51.68                                   
REMARK 500    GLU A 123      134.43     99.29                                   
REMARK 500    LEU A 212      -46.37     71.52                                   
REMARK 500    SER A 222     -176.60    -68.49                                   
REMARK 500    SER A 261       70.41     53.50                                   
REMARK 500    PRO A 337       20.70    -78.97                                   
REMARK 500    VAL B  10       72.70     41.75                                   
REMARK 500    PHE B  56       79.46   -151.14                                   
REMARK 500    ASP B  71     -158.49   -114.49                                   
REMARK 500    VAL B  80      103.48     66.94                                   
REMARK 500    ASP B  95       15.65     59.99                                   
REMARK 500    VAL B 157      -87.56   -125.17                                   
REMARK 500    SER B 213     -156.57   -114.46                                   
REMARK 500    ASP B 241       51.69   -111.55                                   
REMARK 500    LEU B 258      -12.59     83.66                                   
REMARK 500    VAL B 275      -84.29    -91.16                                   
REMARK 500    CYS B 374     -158.98    -95.87                                   
REMARK 500    LYS B 410      -23.04     75.11                                   
REMARK 500    GLU B 442       82.06     55.65                                   
REMARK 500    HIS B 446      -63.52     67.44                                   
REMARK 500    ASN B 452      -60.71   -106.21                                   
REMARK 500    THR B 454      147.91     69.28                                   
REMARK 500    HIS C 401      -56.05   -145.80                                   
REMARK 500    LEU C 402      -11.91   -160.62                                   
REMARK 500    GLN C 407       70.24   -114.72                                   
REMARK 500    ASP H 179      -16.30     77.13                                   
REMARK 500    SER L  30       58.49     31.85                                   
REMARK 500    SER L  77       75.63     58.09                                   
REMARK 500    ASN L 212       70.10     51.30                                   
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  52.0                                              
REMARK 620 3 ASP A 245   OD2 122.3  70.3                                        
REMARK 620 4 ASP A 247   O    78.0  77.3  90.7                                  
REMARK 620 5 THR A 250   O    76.3 126.9 158.1  81.7                            
REMARK 620 6 THR A 250   OG1 145.2 139.5  80.4  75.7  77.8                      
REMARK 620 7 GLU A 252   OE1  88.8  81.6  82.5 158.9 111.4 122.3                
REMARK 620 8 GLU A 252   OE2 132.1 126.1  80.3 148.5  95.6  73.1  49.8          
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 HOH A4304   O                                                      
REMARK 620 2 ASN A 299   OD1  96.2                                              
REMARK 620 3 ASP A 301   OD1  82.8  81.5                                        
REMARK 620 4 ASP A 297   OD1 162.9  79.1  80.2                                  
REMARK 620 5 ARG A 303   O    98.6 161.9  90.1  83.7                            
REMARK 620 6 ASP A 305   OD1  69.0 112.9 149.1 128.0  82.3                      
REMARK 620 7 ASP A 305   OD2 113.0  85.7 160.7  83.2  97.9  50.0                
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  75.7                                              
REMARK 620 3 TYR A 371   O    75.6  87.2                                        
REMARK 620 4 ASP A 367   OD1  87.3  93.6 162.2                                  
REMARK 620 5 HOH A4342   O   151.4  76.2  97.8  99.6                            
REMARK 620 6 ASP A 373   OD1  93.6 164.0 101.7  73.8 115.1                      
REMARK 620 7 ASP A 373   OD2 129.0 147.5  80.7 106.9  75.7  48.3                
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  86.3                                              
REMARK 620 3 HOH A4381   O   134.6  88.6                                        
REMARK 620 4 ASP A 426   OD1  78.2  83.8 145.8                                  
REMARK 620 5 ASP A 428   OD1 157.6  93.8  67.8  79.5                            
REMARK 620 6 ASP A 434   OD1 100.4 170.8  91.2  91.2  77.6                      
REMARK 620 7 ASP A 434   OD2  82.1 138.2  72.2 131.9 111.4  50.0                
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   C2                                                     
REMARK 620 2 GOL B1462   O2   27.8                                              
REMARK 620 3 HOH C4014   O    95.7  81.6                                        
REMARK 620 4 ASP B 127   OD1  82.0  92.4 170.6                                  
REMARK 620 5 ASP B 251   OD2  99.2 126.0 104.6  84.7                            
REMARK 620 6 GOL B1462   O1   46.8  62.8  70.2 113.5  69.3                      
REMARK 620 7 SER B 123   O   177.1 155.0  86.0  96.8  78.0 132.1                
REMARK 620 8 ASP B 126   OD1 105.1  80.8  88.6  83.3 151.0 139.6  77.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 164.1                                              
REMARK 620 3 ASN B 215   OD1  96.3  95.5                                        
REMARK 620 4 ASP B 217   OD1  76.8  91.5  94.8                                  
REMARK 620 5 PRO B 219   O    89.1  81.8 166.7  98.3                            
REMARK 620 6 GLU B 220   OE2  92.4 100.0  81.4 168.1  86.2                      
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 ASP C 410   OD1                                                    
REMARK 620 2 HOH B4088   O    92.1                                              
REMARK 620 3 SER B 121   OG   90.3 176.5                                        
REMARK 620 4 SER B 123   OG   79.3  89.3  88.7                                  
REMARK 620 5 GLU B 220   OE1  93.6  90.9  91.5 172.9                            
REMARK 620 6 HOH B4022   O   154.7  98.7  78.1  78.1 108.9                      
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: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
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  2VDO A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDO B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDO C  400   411  UNP    Q53Y18   Q53Y18_HUMAN   426    437             
DBREF  2VDO H    1   221  PDB    2VDO     2VDO             1    221             
DBREF  2VDO L    1   214  PDB    2VDO     2VDO             1    214             
SEQADV 2VDO 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   12  HIS HIS 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   *1043(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  ASP B  126  5                                   6    
HELIX   10  10 ASP B  127  THR B  146  1                                  20    
HELIX   11  11 PRO B  169  LEU B  173  5                                   5    
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  GLU B  323  1                                  10    
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   74  SER H   76  5                                   3    
HELIX   24  24 THR H   87  THR H   91  5                                   5    
HELIX   25  25 SER H  162  SER H  164  5                                   3    
HELIX   26  26 PRO H  206  SER H  209  5                                   4    
HELIX   27  27 ASP L   79  PHE L   83  5                                   5    
HELIX   28  28 SER L  121  SER L  127  1                                   7    
HELIX   29  29 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 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  O  THR A 125   N  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  VAL B 310  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  VAL B 332  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  2.03  
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  2.09  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.07  
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  2.05  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.05  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.11  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN A  15                 C1 ANAG A3015     1555   1555  1.45  
LINK         ND2 ASN A 249                 C1 ANAG A3249     1555   1555  1.44  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.30  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.37  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.51  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.45  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.47  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.71  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.26  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.66  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.46  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.32  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.39  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.57  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.62  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.26  
LINK        CA    CA A2005                 O   HOH A4304     1555   1555  2.18  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.30  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.27  
LINK        CA    CA A2006                 O   HOH A4342     1555   1555  2.34  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.67  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.69  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.49  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.57  
LINK        CA    CA A2007                 O   HOH A4381     1555   1555  2.26  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.35  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.41  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.65  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.52  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.31  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.21  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.45  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.20  
LINK        MG    MG B2001                 OD1 ASP C 410     1555   1555  2.21  
LINK        MG    MG B2001                 O   HOH B4022     1555   1555  2.21  
LINK        MG    MG B2001                 O   HOH B4088     1555   1555  2.19  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  1.95  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.27  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.34  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.37  
LINK        CA    CA B2002                 O1  GOL B1462     1555   1555  2.98  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.24  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.24  
LINK        CA    CA B2002                 O   HOH C4014     1555   1555  2.39  
LINK        CA    CA B2002                 O2  GOL B1462     1555   1555  2.47  
LINK        CA    CA B2002                 C2  GOL B1462     1555   1555  2.99  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.35  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.29  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.23  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.32  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.36  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.33  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.45  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
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  1.44  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
LINK         O3  MAN B3373                 C1 AMAN B3374     1555   1555  1.44  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.44  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0        -0.41                     
CISPEP   2 SER B  162    PRO B  163          0         5.17                     
CISPEP   3 SER B  168    PRO B  169          0       -10.76                     
CISPEP   4 PHE H  152    PRO H  153          0        -2.06                     
CISPEP   5 GLU H  154    PRO H  155          0         1.44                     
CISPEP   6 TRP H  194    PRO H  195          0         3.25                     
CISPEP   7 SER L    7    PRO L    8          0       -10.16                     
CISPEP   8 LEU L   94    PRO L   95          0        -2.78                     
CISPEP   9 TYR L  140    PRO L  141          0        -0.99                     
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 A4304                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4342                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4381                                          
SITE     1 AC5  1 ASN A  15                                                     
SITE     1 AC6  1 ASN A 249                                                     
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  HOH B4022                    
SITE     2 AC7  6 HOH B4088  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 C4014                                          
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  NAG B3371  HOH B4197                    
SITE     1 BC2 10 MET A 285  LEU B 317  ASN B 320  NAG B3321                    
SITE     2 BC2 10 HOH B4198  HOH B4199  HOH B4200  HOH B4201                    
SITE     3 BC2 10 HOH B4202  HOH B4203                                          
SITE     1 BC3  6 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     2 BC3  6 HOH B4201  HOH B4204                                          
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  2 ARG A 281  MAN B3322                                          
SITE     1 BC6  2 NAG B3321  MAN B3322                                          
SITE     1 BC7  6 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC7  6 NAG B3099  NAG B3372                                          
SITE     1 BC8  4 NAG B3371  MAN B3373  MAN B3375  MAN B3376                    
SITE     1 BC9  6 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  6 MAN B3375  HOH B4205                                          
SITE     1 CC1  5 ASN A 299  LEU A 332  SER A 396  GLU A 397                    
SITE     2 CC1  5 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  6 SER A 344  LEU A 346  NAG B3372  MAN B3375                    
SITE     2 CC3  6 HOH B4206  HOH B4208                                          
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  3 ARG A  90  HOH A4391  HOH A4393                               
SITE     1 CC6  7 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 CC6  7  CA B2002  HOH B4196  HOH H4021                               
CRYST1  148.331  148.331  176.567  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      0.006742  0.003892  0.000000        0.00000                         
SCALE2      0.000000  0.007785  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005664        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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