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Entry: 2VC2
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HEADER    CELL ADHESION/IMMUNE SYSTEM             18-SEP-07   2VC2              
TITLE     RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO            
TITLE    2 ANTAGONIST L-739758                                                  
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                                                             
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_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 STRAIN: BALB/C;                                                      
SOURCE  24 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  27 ORGANISM_COMMON: MOUSE;                                              
SOURCE  28 ORGANISM_TAXID: 10090;                                               
SOURCE  29 STRAIN: BALB/C;                                                      
SOURCE  30 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, HOST-VIRUS   
KEYWDS   2 INTERACTION, PYRROLIDONE CARBOXYLIC ACID, TRANSMEMBRANE,             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VC2    1       VERSN                                    
REVDAT   2   24-FEB-09 2VC2    1       VERSN                                    
REVDAT   1   02-SEP-08 2VC2    0                                                
SPRSDE     02-SEP-08 2VC2      1TY7                                             
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.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 38636                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2044                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2679                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10348                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 240                                     
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 3.21                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.04000                                              
REMARK   3    B22 (A**2) : 1.04000                                              
REMARK   3    B33 (A**2) : -1.56000                                             
REMARK   3    B12 (A**2) : 0.52000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.362         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.235        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10860 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7271 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14811 ; 1.001 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17626 ; 0.765 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1348 ; 5.376 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   466 ;33.205 ;24.292       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1682 ;13.057 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;14.475 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1664 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12050 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2134 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2083 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7418 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5297 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5762 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   310 ; 0.136 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.005 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    24 ; 0.113 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.103 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    45 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.110 ; 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):  6945 ; 0.826 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2727 ; 0.100 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10816 ; 1.274 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4563 ; 0.955 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3992 ; 1.692 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    17                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.5730  13.0120  78.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.1421                                     
REMARK   3      T33:   0.0197 T12:   0.1444                                     
REMARK   3      T13:  -0.0308 T23:   0.3019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7233 L22:   9.8242                                     
REMARK   3      L33:   4.7945 L12:  -7.8655                                     
REMARK   3      L13:   0.8507 L23:  -4.7303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0457 S12:   0.0475 S13:  -0.3473                       
REMARK   3      S21:   0.5761 S22:  -0.6331 S23:  -1.2072                       
REMARK   3      S31:   1.0696 S32:   0.9782 S33:   0.6789                       
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): 129.5560  22.2700  68.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1030 T22:   0.0917                                     
REMARK   3      T33:  -0.0742 T12:   0.0991                                     
REMARK   3      T13:   0.0537 T23:   0.2708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8477 L22:   3.4879                                     
REMARK   3      L33:   1.8232 L12:   1.3684                                     
REMARK   3      L13:  -0.2222 L23:  -0.9387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0212 S12:   0.0194 S13:  -0.3973                       
REMARK   3      S21:  -0.1557 S22:  -0.1482 S23:  -0.4809                       
REMARK   3      S31:   0.3790 S32:   0.1561 S33:   0.1271                       
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): 119.0040  33.9930  64.2150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1919 T22:  -0.1192                                     
REMARK   3      T33:  -0.1711 T12:  -0.0474                                     
REMARK   3      T13:   0.0058 T23:   0.1445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9567 L22:   3.1950                                     
REMARK   3      L33:   1.6406 L12:  -0.5012                                     
REMARK   3      L13:   0.0272 L23:  -0.8960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0842 S12:  -0.0768 S13:  -0.0439                       
REMARK   3      S21:   0.1416 S22:  -0.0189 S23:  -0.5303                       
REMARK   3      S31:   0.0429 S32:   0.3906 S33:   0.1031                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   116        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.4350  36.4570  63.5140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1325 T22:  -0.1544                                     
REMARK   3      T33:  -0.2854 T12:  -0.1121                                     
REMARK   3      T13:  -0.0522 T23:   0.1009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6353 L22:   2.0276                                     
REMARK   3      L33:   3.4132 L12:  -1.1640                                     
REMARK   3      L13:  -2.7311 L23:   0.1694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0299 S12:  -0.0699 S13:  -0.3453                       
REMARK   3      S21:  -0.0464 S22:  -0.1007 S23:   0.1070                       
REMARK   3      S31:   0.0081 S32:  -0.1374 S33:   0.1306                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   168        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.4540  24.8460  63.7150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0865 T22:  -0.2450                                     
REMARK   3      T33:  -0.2032 T12:  -0.0433                                     
REMARK   3      T13:   0.0069 T23:   0.0893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8596 L22:   1.5553                                     
REMARK   3      L33:   2.3250 L12:   0.3821                                     
REMARK   3      L13:  -0.7449 L23:  -1.0472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0033 S12:   0.0563 S13:  -0.2640                       
REMARK   3      S21:  -0.0753 S22:  -0.0986 S23:   0.0355                       
REMARK   3      S31:   0.1975 S32:  -0.2109 S33:   0.0953                       
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): 100.2240  13.4080  72.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0212 T22:  -0.1514                                     
REMARK   3      T33:  -0.1321 T12:  -0.1647                                     
REMARK   3      T13:   0.0524 T23:   0.0636                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9028 L22:   3.7926                                     
REMARK   3      L33:   4.2225 L12:   0.1094                                     
REMARK   3      L13:   0.5209 L23:  -0.1050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0504 S12:   0.1696 S13:  -0.4334                       
REMARK   3      S21:  -0.0438 S22:  -0.1123 S23:   0.0084                       
REMARK   3      S31:   0.2764 S32:  -0.1615 S33:   0.1627                       
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): 108.2260   7.5310  84.1150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0854 T22:  -0.1632                                     
REMARK   3      T33:  -0.0551 T12:  -0.0628                                     
REMARK   3      T13:   0.0531 T23:   0.2434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2237 L22:   6.0694                                     
REMARK   3      L33:   9.9055 L12:  -0.3869                                     
REMARK   3      L13:  -1.0962 L23:   3.7616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3077 S12:  -0.3149 S13:  -0.4480                       
REMARK   3      S21:   0.4591 S22:  -0.0723 S23:   0.1755                       
REMARK   3      S31:   0.4973 S32:  -0.3913 S33:   0.3800                       
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): 110.9950   3.2570  78.4320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2313 T22:  -0.2002                                     
REMARK   3      T33:  -0.0587 T12:  -0.0160                                     
REMARK   3      T13:   0.0364 T23:   0.2428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6463 L22:   4.9412                                     
REMARK   3      L33:   5.4110 L12:  -0.9434                                     
REMARK   3      L13:  -1.6576 L23:   1.7060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0747 S12:  -0.0630 S13:  -0.4393                       
REMARK   3      S21:  -0.0460 S22:  -0.3097 S23:   0.1195                       
REMARK   3      S31:   0.8004 S32:  -0.0954 S33:   0.3844                       
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): 124.7340   8.0010  79.9050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1271 T22:  -0.0060                                     
REMARK   3      T33:   0.0458 T12:   0.1278                                     
REMARK   3      T13:   0.0306 T23:   0.3077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9086 L22:   3.7805                                     
REMARK   3      L33:   2.8693 L12:   0.1687                                     
REMARK   3      L13:  -0.3903 L23:   0.6711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0591 S12:  -0.1427 S13:  -0.5477                       
REMARK   3      S21:   0.2430 S22:  -0.2263 S23:  -0.3451                       
REMARK   3      S31:   0.5283 S32:   0.4294 S33:   0.2853                       
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): 106.9090  20.9570 168.9110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0168 T22:   0.2120                                     
REMARK   3      T33:   0.2082 T12:   0.0805                                     
REMARK   3      T13:  -0.1474 T23:  -0.0599                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6266 L22:   2.1911                                     
REMARK   3      L33:   5.5584 L12:  -0.8147                                     
REMARK   3      L13:   0.8506 L23:  -1.3765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1874 S12:  -0.6527 S13:   0.0518                       
REMARK   3      S21:   1.1439 S22:   0.3860 S23:  -0.0331                       
REMARK   3      S31:  -1.1070 S32:  -0.5534 S33:  -0.1986                       
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    77        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.1860  29.9910 148.8370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8430 T22:   0.1847                                     
REMARK   3      T33:   0.0081 T12:   0.1245                                     
REMARK   3      T13:   0.0110 T23:   0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.7237 L22:  13.2644                                     
REMARK   3      L33:  51.5541 L12:  -8.7802                                     
REMARK   3      L13:  24.8373 L23: -22.9964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0104 S12:  -0.5707 S13:   0.8636                       
REMARK   3      S21:   1.0820 S22:   0.4117 S23:  -0.6305                       
REMARK   3      S31:  -2.3692 S32:  -1.7584 S33:   0.5988                       
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):  97.8460  38.4080 104.1600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2278 T22:   0.0291                                     
REMARK   3      T33:  -0.1668 T12:  -0.2152                                     
REMARK   3      T13:   0.0546 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5819 L22:   1.2467                                     
REMARK   3      L33:   4.5437 L12:  -0.0224                                     
REMARK   3      L13:  -0.8880 L23:  -1.9589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0381 S12:  -0.3156 S13:  -0.0585                       
REMARK   3      S21:   0.6503 S22:  -0.1325 S23:   0.1323                       
REMARK   3      S31:  -0.8019 S32:   0.0002 S33:   0.0944                       
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): 103.3900  34.6080  95.9020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0580 T22:  -0.0636                                     
REMARK   3      T33:  -0.1926 T12:  -0.1628                                     
REMARK   3      T13:  -0.0154 T23:   0.1176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0073 L22:   1.2509                                     
REMARK   3      L33:   2.7756 L12:  -0.3685                                     
REMARK   3      L13:  -1.6745 L23:   0.3476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0685 S12:  -0.3889 S13:   0.0811                       
REMARK   3      S21:   0.4148 S22:  -0.0218 S23:  -0.0591                       
REMARK   3      S31:  -0.1479 S32:   0.1494 S33:  -0.0467                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   339        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.4480  22.5980 130.6160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5002 T22:   0.0555                                     
REMARK   3      T33:   0.1507 T12:  -0.0530                                     
REMARK   3      T13:   0.0692 T23:   0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5283 L22:   2.3465                                     
REMARK   3      L33:  23.1227 L12:  -1.9371                                     
REMARK   3      L13:   7.5971 L23:  -5.3163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6399 S12:   0.4877 S13:  -0.7756                       
REMARK   3      S21:   0.0116 S22:   0.2666 S23:  -0.0774                       
REMARK   3      S31:   1.3751 S32:   0.5835 S33:  -0.9065                       
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): 109.5880  27.9880 148.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8653 T22:   0.0843                                     
REMARK   3      T33:   0.2600 T12:  -0.0824                                     
REMARK   3      T13:  -0.0783 T23:   0.0791                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3730 L22:   1.7347                                     
REMARK   3      L33:  14.5426 L12:  -0.1485                                     
REMARK   3      L13:   5.5094 L23:   0.2158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1767 S12:   0.5676 S13:   0.2948                       
REMARK   3      S21:   1.0943 S22:   0.2611 S23:  -0.5232                       
REMARK   3      S31:  -1.2100 S32:   1.3723 S33:  -0.0844                       
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): 119.5790  31.0630 182.8940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8212 T22:   1.3637                                     
REMARK   3      T33:   1.0727 T12:  -0.0828                                     
REMARK   3      T13:  -0.5430 T23:  -0.1406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6357 L22:   0.6411                                     
REMARK   3      L33:   4.4959 L12:   0.6384                                     
REMARK   3      L13:  -1.6906 L23:  -1.6977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.4228 S12:  -1.8904 S13:   1.1246                       
REMARK   3      S21:  -0.1932 S22:   0.8610 S23:  -1.1110                       
REMARK   3      S31:  -1.0563 S32:   1.7807 S33:   0.5618                       
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):  90.3620  36.9200  33.2110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1189 T22:  -0.1249                                     
REMARK   3      T33:  -0.0849 T12:  -0.3076                                     
REMARK   3      T13:  -0.0191 T23:   0.0922                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.6157 L22:   3.7773                                     
REMARK   3      L33:  10.2503 L12:  -6.9231                                     
REMARK   3      L13:   4.0389 L23:   0.7624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3154 S12:   0.6752 S13:  -1.2006                       
REMARK   3      S21:  -0.6069 S22:  -0.2291 S23:   0.4775                       
REMARK   3      S31:   0.8967 S32:   0.0558 S33:  -0.0863                       
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):  94.3930  42.4780  41.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2340 T22:  -0.1544                                     
REMARK   3      T33:  -0.2586 T12:  -0.0319                                     
REMARK   3      T13:  -0.0294 T23:   0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2194 L22:   0.6976                                     
REMARK   3      L33:   2.1765 L12:  -0.4427                                     
REMARK   3      L13:   0.8341 L23:   1.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0398 S12:  -0.0652 S13:  -0.0167                       
REMARK   3      S21:   0.2409 S22:   0.1420 S23:   0.3545                       
REMARK   3      S31:   0.1822 S32:  -0.2283 S33:  -0.1818                       
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):  94.1990  43.2560  43.3680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2006 T22:  -0.1311                                     
REMARK   3      T33:  -0.1666 T12:  -0.0833                                     
REMARK   3      T13:  -0.0021 T23:   0.0852                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7901 L22:   1.1798                                     
REMARK   3      L33:   2.7387 L12:  -0.8617                                     
REMARK   3      L13:   1.4035 L23:  -0.3516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:  -0.1157 S13:   0.3006                       
REMARK   3      S21:  -0.1011 S22:   0.0216 S23:   0.0924                       
REMARK   3      S31:   0.2079 S32:  -0.2820 S33:   0.0838                       
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):  86.5420  47.8560  12.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1842 T22:   0.0386                                     
REMARK   3      T33:  -0.0562 T12:  -0.1326                                     
REMARK   3      T13:  -0.1222 T23:   0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7396 L22:   1.4694                                     
REMARK   3      L33:   3.1798 L12:  -0.9205                                     
REMARK   3      L13:  -0.0720 L23:   1.5262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0753 S12:   0.4461 S13:  -0.2291                       
REMARK   3      S21:  -0.2657 S22:   0.1350 S23:   0.3114                       
REMARK   3      S31:  -0.2434 S32:  -1.0382 S33:  -0.2103                       
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):  92.6920  45.0410   4.6570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1143 T22:   0.0222                                     
REMARK   3      T33:   0.0276 T12:   0.0048                                     
REMARK   3      T13:  -0.1524 T23:   0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1294 L22:   3.7238                                     
REMARK   3      L33:   9.2798 L12:  -0.7088                                     
REMARK   3      L13:  -4.8806 L23:   1.3913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0047 S12:   0.6207 S13:  -0.1050                       
REMARK   3      S21:  -0.3107 S22:   0.2086 S23:  -0.2041                       
REMARK   3      S31:   1.4446 S32:  -0.6714 S33:  -0.2039                       
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):  94.7300  47.7230   9.1520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0135 T22:  -0.0854                                     
REMARK   3      T33:  -0.1461 T12:  -0.0064                                     
REMARK   3      T13:  -0.0922 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0626 L22:   2.9704                                     
REMARK   3      L33:  12.5899 L12:   2.0444                                     
REMARK   3      L13:  -0.0379 L23:  -4.9632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3822 S12:   0.0532 S13:   0.1687                       
REMARK   3      S21:  -0.2039 S22:  -0.3684 S23:   0.1098                       
REMARK   3      S31:   0.5898 S32:   0.0894 S33:  -0.0138                       
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):  94.1900  40.8090  -3.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7315 T22:   0.1663                                     
REMARK   3      T33:   0.0508 T12:   0.1744                                     
REMARK   3      T13:   0.0128 T23:  -0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3736 L22:   1.7869                                     
REMARK   3      L33:   2.7151 L12:   0.9340                                     
REMARK   3      L13:   3.2775 L23:   1.3412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3938 S12:   0.2796 S13:  -1.3141                       
REMARK   3      S21:  -0.5929 S22:  -0.4154 S23:  -0.2270                       
REMARK   3      S31:   1.0547 S32:   0.8618 S33:   0.0216                       
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):  86.3360  44.3670  -2.5030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0010 T22:   0.3618                                     
REMARK   3      T33:   0.0811 T12:  -0.0702                                     
REMARK   3      T13:  -0.1904 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7952 L22:   6.2133                                     
REMARK   3      L33:  32.6049 L12:   5.8294                                     
REMARK   3      L13: -14.4785 L23:  -4.3254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5702 S12:   1.3446 S13:  -0.6410                       
REMARK   3      S21:  -0.8986 S22:   0.5851 S23:   0.2749                       
REMARK   3      S31:   1.4070 S32:  -2.0539 S33:  -0.0149                       
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): 114.4560  50.5550  35.1330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1884 T22:  -0.1083                                     
REMARK   3      T33:  -0.1098 T12:   0.0423                                     
REMARK   3      T13:   0.0295 T23:   0.1703                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6978 L22:   0.3574                                     
REMARK   3      L33:   2.9377 L12:   0.4710                                     
REMARK   3      L13:  -0.3573 L23:   0.0887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0911 S12:   0.1926 S13:   0.1162                       
REMARK   3      S21:  -0.2027 S22:   0.0378 S23:  -0.1679                       
REMARK   3      S31:  -0.3464 S32:   0.1982 S33:  -0.1290                       
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): 113.8320  39.6160  36.1270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2829 T22:  -0.1124                                     
REMARK   3      T33:  -0.2001 T12:   0.0902                                     
REMARK   3      T13:   0.0222 T23:   0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6082 L22:   3.7429                                     
REMARK   3      L33:   4.0307 L12:   1.3607                                     
REMARK   3      L13:  -1.6574 L23:  -3.6655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1565 S12:   0.3113 S13:  -0.4732                       
REMARK   3      S21:  -0.1702 S22:  -0.0498 S23:  -0.1436                       
REMARK   3      S31:   0.7711 S32:   0.2183 S33:  -0.1067                       
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): 112.5820  46.1410  35.5600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1940 T22:  -0.2109                                     
REMARK   3      T33:  -0.1760 T12:  -0.0120                                     
REMARK   3      T13:  -0.0262 T23:   0.0923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1547 L22:   1.4421                                     
REMARK   3      L33:   2.9263 L12:  -1.1239                                     
REMARK   3      L13:  -2.7280 L23:  -0.7374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1533 S12:   0.2545 S13:  -0.1397                       
REMARK   3      S21:  -0.0668 S22:   0.0076 S23:   0.0528                       
REMARK   3      S31:   0.3393 S32:   0.3336 S33:   0.1458                       
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): 100.6090  53.4350   8.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1981 T22:   0.2513                                     
REMARK   3      T33:  -0.1768 T12:   0.0042                                     
REMARK   3      T13:   0.0317 T23:   0.1328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2059 L22:   2.2758                                     
REMARK   3      L33:   5.6946 L12:  -1.4027                                     
REMARK   3      L13:   2.3516 L23:  -1.8903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5744 S12:   0.2390 S13:  -0.3818                       
REMARK   3      S21:  -0.4121 S22:  -0.2004 S23:   0.2705                       
REMARK   3      S31:   0.7065 S32:   0.1935 S33:  -0.3740                       
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): 101.6810  60.0070   8.8170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2038 T22:   0.2081                                     
REMARK   3      T33:  -0.2617 T12:  -0.0624                                     
REMARK   3      T13:   0.0266 T23:   0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7846 L22:   7.4661                                     
REMARK   3      L33:   6.0809 L12:  -6.2128                                     
REMARK   3      L13:   5.2356 L23:  -3.7835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1581 S12:  -0.4119 S13:   0.5810                       
REMARK   3      S21:   0.2693 S22:  -0.2019 S23:  -0.3453                       
REMARK   3      S31:  -0.0676 S32:   0.1376 S33:   0.3600                       
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):  95.2340  60.4010   2.9270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2156 T22:   0.0992                                     
REMARK   3      T33:  -0.1868 T12:  -0.0002                                     
REMARK   3      T13:   0.0136 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3176 L22:   3.5028                                     
REMARK   3      L33:   4.2091 L12:  -2.8159                                     
REMARK   3      L13:   3.1881 L23:  -0.5187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0192 S12:   0.4584 S13:   0.0094                       
REMARK   3      S21:  -0.3992 S22:  -0.2128 S23:  -0.1515                       
REMARK   3      S31:  -0.0987 S32:   0.0315 S33:   0.1936                       
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): 103.0900  62.8590  -2.0080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0357 T22:   0.1675                                     
REMARK   3      T33:  -0.2103 T12:   0.0375                                     
REMARK   3      T13:   0.0838 T23:   0.2321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3513 L22:   5.5826                                     
REMARK   3      L33:   3.0088 L12:  -5.6862                                     
REMARK   3      L13:   0.1143 L23:  -1.4314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0542 S12:   1.2485 S13:  -0.0894                       
REMARK   3      S21:  -0.3307 S22:  -0.1808 S23:   0.0457                       
REMARK   3      S31:  -0.3978 S32:   0.5631 S33:   0.2350                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2VC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33829.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-03                          
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               : CHESS                              
REMARK 200  BEAMLINE                       : A-1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9760                             
REMARK 200  MONOCHROMATOR                  : RH-COATED SI                       
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41563                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.10                               
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.0                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1TXV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG 3350, 0.7 M                   
REMARK 280  MAGNESIUM ACETATE, 0.1 M IMIDAZOLE, PH 6.5, VAPOR                   
REMARK 280  DIFFUSION, 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      117.47800            
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       58.73900            
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       58.73900            
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      117.47800            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     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  4005     O    HOH B  4023              2.10            
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    ASN A   2       28.36   -149.03                                   
REMARK 500    GLN A  47       18.25     58.57                                   
REMARK 500    SER A 101     -114.25     46.75                                   
REMARK 500    LYS A 118     -134.50     54.43                                   
REMARK 500    GLU A 123      129.92     91.47                                   
REMARK 500    LEU A 212      -61.32     69.98                                   
REMARK 500    SER A 261       72.36     44.97                                   
REMARK 500    THR B   7       39.28    -90.81                                   
REMARK 500    ARG B   8       72.41   -150.77                                   
REMARK 500    ASP B  47       42.43    -97.57                                   
REMARK 500    ASN B  48       15.40     59.46                                   
REMARK 500    PHE B  56       78.44   -151.84                                   
REMARK 500    VAL B  63       96.14    -64.13                                   
REMARK 500    ASP B  66       55.01   -140.39                                   
REMARK 500    SER B  78      -68.13   -151.36                                   
REMARK 500    VAL B  80       93.70     64.26                                   
REMARK 500    ASP B  95      -21.26     65.90                                   
REMARK 500    ASN B 148       40.13    -95.31                                   
REMARK 500    VAL B 157      -83.81   -127.14                                   
REMARK 500    LEU B 196      108.41    -48.47                                   
REMARK 500    SER B 213     -152.56   -112.60                                   
REMARK 500    LEU B 258       -6.23     86.33                                   
REMARK 500    ASN B 303       60.41     60.06                                   
REMARK 500    ALA B 309       75.10   -108.40                                   
REMARK 500    LYS B 410      -25.47     72.43                                   
REMARK 500    GLU B 442       70.16     53.05                                   
REMARK 500    HIS B 446      -54.43     74.06                                   
REMARK 500    THR B 454      150.11     70.31                                   
REMARK 500    THR H  91       96.68    -66.62                                   
REMARK 500    TYR H 101      -60.46   -124.83                                   
REMARK 500    SER L  30       71.65     17.14                                   
REMARK 500    SER L  43     -155.59    -84.60                                   
REMARK 500    SER L  77       78.56     54.16                                   
REMARK 500    ASN L 138       76.56     53.13                                   
REMARK 500    ASN L 212       72.98     50.97                                   
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  46.3                                              
REMARK 620 3 ASP A 245   OD2 111.0  65.8                                        
REMARK 620 4 ASP A 247   O    81.0  68.4  85.6                                  
REMARK 620 5 THR A 250   C    96.7 138.1 150.8  90.0                            
REMARK 620 6 THR A 250   O    75.2 116.5 165.5  82.5  22.0                      
REMARK 620 7 THR A 250   OG1 149.4 136.9  87.9  76.5  63.1  81.4                
REMARK 620 8 GLU A 252   OE1  76.1  85.4  89.3 153.0 106.7 105.1 129.8          
REMARK 620 9 GLU A 252   OE2 124.7 132.6  90.1 153.5  81.2  97.0  77.2  52.7    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  79.2                                              
REMARK 620 3 ARG A 303   O   150.1  86.1                                        
REMARK 620 4 ASP A 297   OD1  75.7  73.7  75.2                                  
REMARK 620 5 ASP A 305   OD1 107.2 163.8  94.2 122.1                            
REMARK 620 6 ASP A 305   OD2  76.3 147.5 105.2  79.8  47.7                      
REMARK 620 N                    1     2     3     4     5                       
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  76.8                                              
REMARK 620 3 TYR A 371   O    68.1  85.8                                        
REMARK 620 4 ASP A 367   OD1  81.1  95.6 148.1                                  
REMARK 620 5 ASP A 373   OD1  85.5 160.1  96.0  72.5                            
REMARK 620 6 ASP A 373   OD2 121.7 150.6  81.6 109.1  48.6                      
REMARK 620 N                    1     2     3     4     5                       
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  83.1                                              
REMARK 620 3 ASP A 426   OD1  75.1  86.4                                        
REMARK 620 4 ASP A 428   OD1 141.9  82.4  68.9                                  
REMARK 620 5 ASP A 434   OD1 112.1 164.1  93.2  82.7                            
REMARK 620 6 ASP A 434   OD2  94.9 138.1 133.7 119.0  48.2                      
REMARK 620 7 HOH A4029   O   133.9  83.6 147.3  78.9  88.3  67.8                
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 B1478   O2                                                     
REMARK 620 2 HOH B4025   O    93.9                                              
REMARK 620 3 ASP B 251   OD2 120.3 116.9                                        
REMARK 620 4 GOL B1478   O1   60.6  73.6  79.7                                  
REMARK 620 5 SER B 123   O   147.6 101.2  77.7 151.3                            
REMARK 620 6 ASP B 126   OD1  85.0  87.7 140.9 138.6  67.4                      
REMARK 620 7 ASP B 127   OD1  73.4 157.4  85.7 113.5  82.3  73.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 159.2                                              
REMARK 620 3 ASN B 215   OD1  87.6 109.0                                        
REMARK 620 4 ASP B 217   OD1  70.9  94.5  94.7                                  
REMARK 620 5 PRO B 219   O    86.3  78.6 170.6  89.9                            
REMARK 620 6 GLU B 220   OE2  88.9 104.2  86.9 159.6  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B4024   O                                                      
REMARK 620 2 SER B 123   OG   78.1                                              
REMARK 620 3 GLU B 220   OE1 118.8 160.8                                        
REMARK 620 4 HOH B4006   O    89.9  78.9  91.4                                  
REMARK 620 5 180 B1477   O1  109.9  79.5 101.3 146.8                            
REMARK 620 6 SER B 121   OG  152.7  77.1  84.4  74.4  76.4                      
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  MG A1460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 180 B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF                        
REMARK 800  SUGAR BOUND TO ASN B 320 RESIDUES 3320 TO 3324                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF                        
REMARK 800  SUGAR BOUND TO ASN B 371 RESIDUES 3371 TO 3377                      
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 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.                                                  
DBREF  2VC2 A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VC2 B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VC2 H    1   221  PDB    2VC2     2VC2             1    221             
DBREF  2VC2 L    1   214  PDB    2VC2     2VC2             1    214             
SEQADV 2VC2 GLY A  282  UNP  P08514    ALA   313 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 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     MG  A1460       1                                                       
HET    GOL  A1461       6                                                       
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    180  B1477      34                                                       
HET    GOL  B1478       6                                                       
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                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     180 2-(S)-[N-(3-PYRIDYLSULFONYL)AMINO]-3-[[2-                        
HETNAM   2 180  CARBONYL-5-[2-(PIPERIDIN-4-YL)ETHYL]-THIENO[2,3-                
HETNAM   3 180  B]THIOPHENEYL]AMINO]-PROPIONIC ACID                             
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     GOL GLYCERIN                                                         
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6   CA    6(CA 2+)                                                     
FORMUL   7  MAN    8(C6 H12 O6)                                                 
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL   9  180    C22 H26 N4 O5 S3                                             
FORMUL  10  NAG    7(C8 H15 N O6)                                               
FORMUL  11  HOH   *98(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 ALA A  318  ARG A  320  5                                   3    
HELIX    7   7 TYR A  440  ALA A  442  5                                   3    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LYS B   41  ASP B   47  1                                   7    
HELIX   10  10 SER B  121  LYS B  125  5                                   5    
HELIX   11  11 ASP B  127  THR B  146  1                                  20    
HELIX   12  12 PRO B  169  LEU B  173  5                                   5    
HELIX   13  13 CYS B  177  LYS B  181  5                                   5    
HELIX   14  14 GLN B  199  GLN B  210  1                                  12    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 CYS B  232  GLY B  237  1                                   6    
HELIX   17  17 ASP B  259  GLY B  264  5                                   6    
HELIX   18  18 SER B  291  LYS B  302  1                                  12    
HELIX   19  19 VAL B  314  GLU B  323  1                                  10    
HELIX   20  20 SER B  337  LYS B  350  1                                  14    
HELIX   21  21 CYS B  435  GLN B  440  5                                   6    
HELIX   22  22 ASN H   28  THR H   32  5                                   5    
HELIX   23  23 PRO H   62  PHE H   64  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  GLY L  128  1                                   8    
HELIX   29  29 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 LEU A   3  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  ALA A 450 -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 VAL B  63  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 SER B 353  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  LEU B 389 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 159  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  HIS L 198 -1  O  THR L 193   N  LYS L 149           
SHEET    4  LD 4 SER L 201  ASN L 210 -1  O  SER L 201   N  HIS L 198           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.07  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.04  
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  2.05  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.06  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
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  2.03  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.07  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.44  
LINK         ND2 ASN A 249                 C1  NAG A3249     1555   1555  1.44  
LINK        MG    MG A1460                 O   HOH A4023     1555   1555  2.73  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.39  
LINK        CA    CA A2004                 C   THR A 250     1555   1555  3.09  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.45  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.52  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.34  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.57  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.35  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.91  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.64  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.52  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.39  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.89  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.43  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.32  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.35  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.36  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.82  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.46  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.37  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.62  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.33  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.46  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.76  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.56  
LINK        CA    CA A2007                 O   HOH A4029     1555   1555  2.35  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.38  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.61  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.43  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  1.89  
LINK        MG    MG B2001                 O   HOH B4006     1555   1555  1.87  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.18  
LINK        MG    MG B2001                 O1  180 B1477     1555   1555  2.14  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.36  
LINK        MG    MG B2001                 O   HOH B4024     1555   1555  2.48  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.30  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.65  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.36  
LINK        CA    CA B2002                 O1  GOL B1478     1555   1555  3.05  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.26  
LINK        CA    CA B2002                 O   HOH B4025     1555   1555  2.32  
LINK        CA    CA B2002                 O2  GOL B1478     1555   1555  2.30  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.24  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.27  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.23  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.17  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.31  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.51  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.43  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.43  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.45  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.45  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.43  
LINK         O3  MAN B3373                 C1  MAN 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  1.44  
CISPEP   1 SER B   84    PRO B   85          0         0.89                     
CISPEP   2 SER B  162    PRO B  163          0         3.43                     
CISPEP   3 SER B  168    PRO B  169          0        -7.81                     
CISPEP   4 PHE H  152    PRO H  153          0        -6.31                     
CISPEP   5 GLU H  154    PRO H  155          0         0.95                     
CISPEP   6 TRP H  194    PRO H  195          0         3.96                     
CISPEP   7 SER L    7    PRO L    8          0       -13.08                     
CISPEP   8 LEU L   94    PRO L   95          0         4.17                     
CISPEP   9 TYR L  140    PRO L  141          0         5.12                     
SITE     1 AC1  2 ASP A 232  HOH A4023                                          
SITE     1 AC2  4 ALA A  89  ARG A  90  HIS A 112  LYS A 124                    
SITE     1 AC3  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC3  5 GLU A 252                                                     
SITE     1 AC4  5 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC4  5 ASP A 305                                                     
SITE     1 AC5  5 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC5  5 ASP A 373                                                     
SITE     1 AC6  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC6  6 ASP A 434  HOH A4029                                          
SITE     1 AC7  1 ASN A  15                                                     
SITE     1 AC8  1 ASN A 249                                                     
SITE     1 AC9 17 ASP A 159  PHE A 160  TYR A 190  LEU A 192                    
SITE     2 AC9 17 ASP A 224  SER A 225  SER B 121  TYR B 122                    
SITE     3 AC9 17 SER B 123  ARG B 214  ASN B 215  ARG B 216                    
SITE     4 AC9 17 ASP B 217  ALA B 218  GLU B 220   MG B2001                    
SITE     5 AC9 17 HOH B4024                                                     
SITE     1 BC1  5 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 BC1  5  CA B2002                                                     
SITE     1 BC2  6 SER B 121  SER B 123  GLU B 220  180 B1477                    
SITE     2 BC2  6 HOH B4006  HOH B4024                                          
SITE     1 BC3  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 BC3  6 GOL B1478  HOH B4025                                          
SITE     1 BC4  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC4  5 GLU B 220                                                     
SITE     1 BC5  2 ASN B  99  SER B 398                                          
SITE     1 BC6  3 ARG A 281  LEU B 317  ASN B 320                               
SITE     1 BC7 13 ASN A 299  LEU A 332  ALA A 342  PRO A 343                    
SITE     2 BC7 13 SER A 344  LEU A 345  LEU A 346  SER A 396                    
SITE     3 BC7 13 GLU A 397  SER B 369  ASN B 371  SER B 398                    
SITE     4 BC7 13 GLU B 400                                                     
CRYST1  149.151  149.151  176.217  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      0.006705  0.003871  0.000000        0.00000                         
SCALE2      0.000000  0.007742  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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