GenomeNet

Database: PDB
Entry: 2VDM
LinkDB: 2VDM
Original site: 2VDM 
HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDM              
TITLE     RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO            
TITLE    2 ANTAGONIST TIROFIBAN                                                 
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_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  19 ORGANISM_COMMON: MOUSE;                                              
SOURCE  20 ORGANISM_TAXID: 10090;                                               
SOURCE  21 STRAIN: BALB/C;                                                      
SOURCE  22 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: MOUSE;                                              
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 STRAIN: BALB/C;                                                      
SOURCE  28 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, PLATELET     
KEYWDS   2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,       
KEYWDS   3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE  
KEYWDS   4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,   
KEYWDS   5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM      
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDM    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDM    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDM    0                                                
SPRSDE     02-SEP-08 2VDM      1TY5                                             
JRNL        AUTH   T.A.SPRINGER,J.ZHU,T.XIAO                                    
JRNL        TITL   STRUCTURAL BASIS FOR DISTINCTIVE RECOGNITION OF FIBRINOGEN   
JRNL        TITL 2 GAMMAC PEPTIDE BY THE PLATELET INTEGRIN ALPHAIIBBETA3.       
JRNL        REF    J.CELL BIOL.                  V. 182   791 2008              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   18710925                                                     
JRNL        DOI    10.1083/JCB.200801146                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER            
REMARK   1  TITL   STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO   
REMARK   1  TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS                              
REMARK   1  REF    NATURE                        V. 432    59 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15378069                                                     
REMARK   1  DOI    10.1038/NATURE02976                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 46776                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2464                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3089                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10363                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 355                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.21000                                              
REMARK   3    B22 (A**2) : 1.21000                                              
REMARK   3    B33 (A**2) : -1.81000                                             
REMARK   3    B12 (A**2) : 0.60000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.958         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.213         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.955        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10871 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7295 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14826 ; 0.925 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17675 ; 0.759 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1353 ; 5.267 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   469 ;31.665 ;24.307       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1688 ;11.839 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;13.904 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1666 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12068 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2138 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2008 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7548 ; 0.169 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5311 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5649 ; 0.080 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   453 ; 0.122 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.099 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    60 ; 0.148 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.113 ; 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):  6968 ; 1.244 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10842 ; 2.056 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4547 ; 1.154 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3979 ; 1.907 ;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): 133.1640  12.3590  78.5150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0426 T22:   0.1742                                     
REMARK   3      T33:   0.0229 T12:   0.1713                                     
REMARK   3      T13:   0.0326 T23:   0.3886                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9623 L22:   6.1541                                     
REMARK   3      L33:   2.9042 L12:  -3.3784                                     
REMARK   3      L13:   1.0282 L23:  -1.7570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2017 S12:   0.0139 S13:  -0.6761                       
REMARK   3      S21:   0.8316 S22:  -0.2202 S23:  -1.4399                       
REMARK   3      S31:   0.5505 S32:   0.8926 S33:   0.4220                       
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): 129.1830  21.8950  69.1370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1461 T22:   0.1027                                     
REMARK   3      T33:  -0.1593 T12:   0.0585                                     
REMARK   3      T13:   0.0379 T23:   0.2725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1853 L22:   4.9013                                     
REMARK   3      L33:   1.5567 L12:   1.4397                                     
REMARK   3      L13:   0.4301 L23:  -0.8645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0813 S12:   0.0068 S13:  -0.2166                       
REMARK   3      S21:  -0.0961 S22:  -0.1640 S23:  -0.4528                       
REMARK   3      S31:   0.3996 S32:   0.4212 S33:   0.2453                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    63        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 118.6840  33.6410  64.5700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2020 T22:  -0.0917                                     
REMARK   3      T33:  -0.2080 T12:  -0.0562                                     
REMARK   3      T13:  -0.0519 T23:   0.1530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2918 L22:   2.4491                                     
REMARK   3      L33:   1.8113 L12:  -0.3883                                     
REMARK   3      L13:  -0.5044 L23:  -0.6760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0771 S12:  -0.0585 S13:  -0.0452                       
REMARK   3      S21:   0.2667 S22:  -0.1352 S23:  -0.4412                       
REMARK   3      S31:   0.0308 S32:   0.4716 S33:   0.2123                       
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): 107.0400  36.1120  63.9220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1657 T22:  -0.1398                                     
REMARK   3      T33:  -0.3337 T12:  -0.0891                                     
REMARK   3      T13:  -0.0587 T23:   0.0761                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6967 L22:   1.9635                                     
REMARK   3      L33:   2.7361 L12:  -0.7261                                     
REMARK   3      L13:  -1.7064 L23:  -0.2838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:   0.1301 S13:  -0.2687                       
REMARK   3      S21:   0.1513 S22:  -0.3274 S23:   0.1088                       
REMARK   3      S31:   0.1070 S32:  -0.0594 S33:   0.2725                       
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): 106.1000  24.4980  64.1590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1738 T22:  -0.1885                                     
REMARK   3      T33:  -0.2559 T12:  -0.0437                                     
REMARK   3      T13:   0.0008 T23:   0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9343 L22:   1.7002                                     
REMARK   3      L33:   2.3463 L12:  -0.0784                                     
REMARK   3      L13:  -0.7169 L23:  -1.0432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:   0.1575 S13:  -0.2321                       
REMARK   3      S21:  -0.0494 S22:  -0.1396 S23:   0.0029                       
REMARK   3      S31:   0.2176 S32:  -0.1401 S33:   0.1355                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  99.8230  13.0670  72.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0049 T22:  -0.2317                                     
REMARK   3      T33:  -0.1685 T12:  -0.1348                                     
REMARK   3      T13:   0.0662 T23:   0.0830                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7500 L22:   2.0947                                     
REMARK   3      L33:   3.7555 L12:  -0.5960                                     
REMARK   3      L13:   0.0849 L23:   0.4358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0990 S12:   0.1378 S13:  -0.4223                       
REMARK   3      S21:  -0.0801 S22:  -0.0930 S23:  -0.0359                       
REMARK   3      S31:   0.4405 S32:  -0.0801 S33:  -0.0060                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   291        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.9160   7.2120  84.5800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0920 T22:  -0.1666                                     
REMARK   3      T33:  -0.1034 T12:  -0.0212                                     
REMARK   3      T13:   0.0797 T23:   0.2129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3487 L22:   6.0947                                     
REMARK   3      L33:   6.8095 L12:  -0.6427                                     
REMARK   3      L13:  -1.4262 L23:   4.5242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2663 S12:  -0.3986 S13:  -0.5138                       
REMARK   3      S21:   0.4917 S22:  -0.0307 S23:   0.1057                       
REMARK   3      S31:   0.6801 S32:   0.1495 S33:   0.2970                       
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): 110.6190   2.9410  78.9130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:  -0.1732                                     
REMARK   3      T33:  -0.0876 T12:  -0.0145                                     
REMARK   3      T13:   0.0930 T23:   0.2434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7385 L22:   4.3235                                     
REMARK   3      L33:   4.8754 L12:  -0.9384                                     
REMARK   3      L13:  -1.1997 L23:   1.3342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1540 S12:   0.0756 S13:  -0.3235                       
REMARK   3      S21:  -0.0880 S22:  -0.2533 S23:   0.0402                       
REMARK   3      S31:   0.8708 S32:  -0.1205 S33:   0.4073                       
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): 124.4500   7.5290  80.2210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0932 T22:   0.0063                                     
REMARK   3      T33:   0.0159 T12:   0.1323                                     
REMARK   3      T13:   0.0518 T23:   0.3060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6329 L22:   3.3332                                     
REMARK   3      L33:   2.7348 L12:  -0.1035                                     
REMARK   3      L13:  -0.7219 L23:  -0.0563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1290 S12:  -0.1483 S13:  -0.4486                       
REMARK   3      S21:   0.0701 S22:  -0.2113 S23:  -0.3182                       
REMARK   3      S31:   0.6129 S32:   0.4612 S33:   0.3403                       
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): 106.5340  21.2800 169.6670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0333 T22:   0.1420                                     
REMARK   3      T33:   0.0702 T12:   0.0899                                     
REMARK   3      T13:  -0.1958 T23:  -0.1354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4228 L22:   4.4598                                     
REMARK   3      L33:   8.5569 L12:  -2.1058                                     
REMARK   3      L13:   2.9560 L23:  -3.6053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2967 S12:  -0.6181 S13:   0.0380                       
REMARK   3      S21:   1.4206 S22:   0.4282 S23:  -0.2532                       
REMARK   3      S31:  -1.0628 S32:  -0.9177 S33:  -0.1315                       
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    78        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.3390  29.8270 150.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7990 T22:   0.0967                                     
REMARK   3      T33:   0.0161 T12:   0.1627                                     
REMARK   3      T13:   0.0243 T23:  -0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9463 L22:   9.0368                                     
REMARK   3      L33:  43.3190 L12:  -5.4465                                     
REMARK   3      L13:  19.4668 L23: -17.1049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5629 S12:  -0.8826 S13:   0.5269                       
REMARK   3      S21:   1.1936 S22:   0.3049 S23:  -0.5801                       
REMARK   3      S31:  -2.3939 S32:  -2.2572 S33:   0.2581                       
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):  97.6030  38.2510 104.6010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1970 T22:  -0.0067                                     
REMARK   3      T33:  -0.2168 T12:  -0.2150                                     
REMARK   3      T13:   0.0066 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2053 L22:   0.7393                                     
REMARK   3      L33:   2.9255 L12:  -0.3104                                     
REMARK   3      L13:   0.2147 L23:  -1.1787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0140 S12:  -0.3212 S13:  -0.0586                       
REMARK   3      S21:   0.5553 S22:  -0.0301 S23:   0.1005                       
REMARK   3      S31:  -0.6181 S32:   0.0781 S33:   0.0161                       
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): 103.0920  34.3460  96.3200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0199 T22:  -0.0769                                     
REMARK   3      T33:  -0.2783 T12:  -0.1510                                     
REMARK   3      T13:  -0.0181 T23:   0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9689 L22:   1.2632                                     
REMARK   3      L33:   2.2414 L12:  -0.5951                                     
REMARK   3      L13:  -1.0307 L23:   0.2150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:  -0.3510 S13:   0.0774                       
REMARK   3      S21:   0.4131 S22:  -0.0953 S23:  -0.1755                       
REMARK   3      S31:  -0.1418 S32:   0.2027 S33:   0.0847                       
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): 100.3330  22.6260 131.3020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3260 T22:   0.1693                                     
REMARK   3      T33:   0.0074 T12:  -0.0447                                     
REMARK   3      T13:   0.0539 T23:   0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7377 L22:   2.7689                                     
REMARK   3      L33:  23.4941 L12:  -2.0258                                     
REMARK   3      L13:   8.0171 L23:  -5.7854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6779 S12:   0.5086 S13:  -0.8712                       
REMARK   3      S21:   0.0008 S22:   0.3372 S23:  -0.1800                       
REMARK   3      S31:   1.2913 S32:   0.5944 S33:  -1.0152                       
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): 109.4720  28.1270 149.7170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7095 T22:   0.1061                                     
REMARK   3      T33:   0.1305 T12:  -0.0481                                     
REMARK   3      T13:  -0.1040 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1437 L22:   2.0877                                     
REMARK   3      L33:  13.2447 L12:  -1.4581                                     
REMARK   3      L13:   4.3235 L23:  -2.6944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2974 S12:   0.4587 S13:   0.1675                       
REMARK   3      S21:   0.7784 S22:   0.4134 S23:  -0.7168                       
REMARK   3      S31:  -1.6823 S32:   1.2319 S33:  -0.1160                       
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): 119.2510  31.1760 183.8100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3534 T22:   1.1338                                     
REMARK   3      T33:   1.0922 T12:  -0.1422                                     
REMARK   3      T13:  -1.0368 T23:   0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3907 S12:  -1.4030 S13:   0.1351                       
REMARK   3      S21:  -0.1435 S22:   0.3542 S23:  -0.3330                       
REMARK   3      S31:  -1.2221 S32:   3.1313 S33:   0.0366                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H    13                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.7100  36.7560  33.5380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1793 T22:  -0.0775                                     
REMARK   3      T33:  -0.2307 T12:  -0.2355                                     
REMARK   3      T13:   0.0060 T23:   0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1816 L22:  17.3548                                     
REMARK   3      L33:  15.6083 L12: -10.7108                                     
REMARK   3      L13:   7.9651 L23: -11.7933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5947 S12:   0.5126 S13:  -0.5792                       
REMARK   3      S21:  -0.9268 S22:  -0.6716 S23:   0.0908                       
REMARK   3      S31:   1.3108 S32:  -0.0166 S33:   0.0769                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    14        H    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9500  42.1740  41.4690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2707 T22:  -0.1826                                     
REMARK   3      T33:  -0.2838 T12:  -0.0586                                     
REMARK   3      T13:  -0.0066 T23:   0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0201 L22:   0.5460                                     
REMARK   3      L33:   2.4272 L12:  -0.6723                                     
REMARK   3      L13:   1.6012 L23:   0.5885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0598 S12:  -0.0241 S13:   0.0918                       
REMARK   3      S21:   0.0104 S22:   0.0496 S23:   0.2428                       
REMARK   3      S31:   0.3504 S32:  -0.2838 S33:  -0.1094                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    55        H   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.7500  42.9750  43.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2510 T22:  -0.1151                                     
REMARK   3      T33:  -0.2512 T12:  -0.0554                                     
REMARK   3      T13:   0.0136 T23:   0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3041 L22:   0.3230                                     
REMARK   3      L33:   3.3734 L12:  -0.5822                                     
REMARK   3      L13:   1.8702 L23:  -1.0438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0852 S12:   0.0687 S13:   0.1227                       
REMARK   3      S21:  -0.0281 S22:   0.0130 S23:   0.0479                       
REMARK   3      S31:   0.1463 S32:  -0.3266 S33:   0.0722                       
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):  86.1230  47.6040  13.2300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2031 T22:  -0.0078                                     
REMARK   3      T33:  -0.1247 T12:  -0.1126                                     
REMARK   3      T13:  -0.0713 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5317 L22:   1.4237                                     
REMARK   3      L33:   3.3323 L12:  -1.6794                                     
REMARK   3      L13:  -0.3464 L23:   1.2385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3246 S12:   0.3220 S13:  -0.2627                       
REMARK   3      S21:  -0.3160 S22:   0.0736 S23:   0.3332                       
REMARK   3      S31:  -0.4413 S32:  -0.7710 S33:  -0.3982                       
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):  92.0910  44.5370   5.2110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0054 T22:   0.0508                                     
REMARK   3      T33:  -0.0683 T12:   0.1119                                     
REMARK   3      T13:  -0.1651 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7051 L22:   2.4121                                     
REMARK   3      L33:  13.0263 L12:   0.0259                                     
REMARK   3      L13:  -6.4447 L23:   1.2276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1441 S12:   0.5591 S13:  -0.1245                       
REMARK   3      S21:  -0.3715 S22:   0.1636 S23:  -0.2930                       
REMARK   3      S31:   1.1826 S32:  -0.0728 S33:  -0.3077                       
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):  94.2550  47.4110   9.4840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0471 T22:  -0.1098                                     
REMARK   3      T33:  -0.1829 T12:   0.0869                                     
REMARK   3      T13:  -0.0635 T23:   0.0474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0081 L22:   1.2575                                     
REMARK   3      L33:  17.7681 L12:   1.9584                                     
REMARK   3      L13:  -0.3067 L23:  -3.4153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2738 S12:  -0.0017 S13:   0.3364                       
REMARK   3      S21:  -0.5594 S22:  -0.2928 S23:   0.1853                       
REMARK   3      S31:   0.2544 S32:   0.7185 S33:   0.0190                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   190        H   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.6550  40.4600  -3.3680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5256 T22:   0.2778                                     
REMARK   3      T33:  -0.0238 T12:   0.2891                                     
REMARK   3      T13:   0.0261 T23:  -0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.2833 L22:   2.6581                                     
REMARK   3      L33:   3.2375 L12:   0.1457                                     
REMARK   3      L13:  -4.8146 L23:   1.7105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3197 S12:   0.0149 S13:  -1.3704                       
REMARK   3      S21:  -0.9467 S22:  -0.5993 S23:  -0.2013                       
REMARK   3      S31:   0.4162 S32:   1.2192 S33:   0.2797                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   207        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.7150  43.6710  -1.7230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0462 T22:   0.3491                                     
REMARK   3      T33:  -0.0350 T12:  -0.0228                                     
REMARK   3      T13:  -0.1806 T23:  -0.0857                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9914 L22:   6.2193                                     
REMARK   3      L33:  22.8893 L12:   4.4986                                     
REMARK   3      L13: -14.4984 L23:  -3.8509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0924 S12:   0.6505 S13:   0.2201                       
REMARK   3      S21:  -1.2402 S22:   0.5047 S23:   1.1632                       
REMARK   3      S31:   1.5531 S32:  -1.0156 S33:  -0.4123                       
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): 114.1160  50.1220  35.4450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2215 T22:  -0.0965                                     
REMARK   3      T33:  -0.1972 T12:   0.0119                                     
REMARK   3      T13:   0.0297 T23:   0.1222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5417 L22:   0.9300                                     
REMARK   3      L33:   0.8988 L12:  -0.0735                                     
REMARK   3      L13:  -0.4865 L23:   0.2195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0885 S12:   0.2293 S13:   0.0792                       
REMARK   3      S21:  -0.1718 S22:  -0.0168 S23:  -0.0873                       
REMARK   3      S31:  -0.3125 S32:   0.0307 S33:  -0.0718                       
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): 113.3910  39.1540  36.4690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2520 T22:  -0.1628                                     
REMARK   3      T33:  -0.2684 T12:   0.0695                                     
REMARK   3      T13:   0.0014 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5522 L22:   2.9398                                     
REMARK   3      L33:   2.6791 L12:   1.5928                                     
REMARK   3      L13:  -2.0217 L23:  -1.8266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1147 S12:   0.4019 S13:  -0.4701                       
REMARK   3      S21:  -0.1858 S22:   0.0051 S23:  -0.1938                       
REMARK   3      S31:   0.5192 S32:   0.1627 S33:  -0.1198                       
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): 112.1560  45.7340  35.9360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2388 T22:  -0.1602                                     
REMARK   3      T33:  -0.2579 T12:   0.0128                                     
REMARK   3      T13:  -0.0384 T23:   0.0771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1283 L22:   0.6033                                     
REMARK   3      L33:   3.0316 L12:   0.8981                                     
REMARK   3      L13:  -2.0588 L23:  -1.3523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0883 S12:   0.2990 S13:   0.0348                       
REMARK   3      S21:  -0.0327 S22:   0.0652 S23:  -0.0341                       
REMARK   3      S31:   0.3772 S32:   0.1340 S33:   0.0232                       
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): 100.2520  53.0350   8.4270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1953 T22:   0.1394                                     
REMARK   3      T33:  -0.2383 T12:   0.0251                                     
REMARK   3      T13:   0.0047 T23:   0.0856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7660 L22:   2.9411                                     
REMARK   3      L33:   5.2173 L12:  -1.5009                                     
REMARK   3      L13:   1.3547 L23:  -2.6727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5295 S12:   0.2929 S13:  -0.1838                       
REMARK   3      S21:  -0.4829 S22:  -0.3074 S23:   0.1587                       
REMARK   3      S31:   0.6646 S32:   0.2299 S33:  -0.2221                       
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): 101.4510  59.6550   9.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2381 T22:   0.1879                                     
REMARK   3      T33:  -0.2675 T12:   0.0085                                     
REMARK   3      T13:  -0.0086 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3505 L22:   5.3999                                     
REMARK   3      L33:   4.6282 L12:  -3.1331                                     
REMARK   3      L13:   3.0704 L23:  -2.8094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0607 S12:  -0.2293 S13:   0.4613                       
REMARK   3      S21:   0.3239 S22:  -0.1691 S23:  -0.1658                       
REMARK   3      S31:  -0.0545 S32:   0.2802 S33:   0.2298                       
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):  95.0700  59.9320   3.1960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2355 T22:   0.0884                                     
REMARK   3      T33:  -0.2127 T12:  -0.0190                                     
REMARK   3      T13:   0.0513 T23:   0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2964 L22:   3.7263                                     
REMARK   3      L33:   4.8336 L12:  -4.4909                                     
REMARK   3      L13:   3.9596 L23:  -1.2337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0154 S12:   0.2544 S13:  -0.0390                       
REMARK   3      S21:  -0.4880 S22:  -0.0491 S23:  -0.1207                       
REMARK   3      S31:   0.0183 S32:   0.2025 S33:   0.0337                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   198        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.8900  62.3000  -1.8740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0746 T22:   0.1750                                     
REMARK   3      T33:  -0.1636 T12:   0.0868                                     
REMARK   3      T13:   0.1183 T23:   0.1123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.3494 L22:   7.9082                                     
REMARK   3      L33:   9.2264 L12:  -8.1549                                     
REMARK   3      L13:   5.9917 L23:  -6.5288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1642 S12:   1.6823 S13:  -1.0121                       
REMARK   3      S21:  -0.5470 S22:   0.0535 S23:   0.1836                       
REMARK   3      S31:  -0.3750 S32:   1.0167 S33:  -0.2176                       
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. THESE ARE RE-REFINED COORDINATES OF THE           
REMARK   3  PREVIOUS WWPDB SUBMISSION 1TY5. THE STARTING MODEL WAS A 2.4        
REMARK   3  ANGSTROM STRUCTURE WITH A DIFFERENT BOUND LIGAND. THE MODEL IS      
REMARK   3  REFINED TO LOWER RFREE. ONE SEQUENCE MISTAKE IN THE AIIB            
REMARK   3  SUBUNIT IS CORRECTED. MORE OF BETA SUBUNIT DOMAIN I-EGF1 IS         
REMARK   3  BUILT. THE ARRANGEMENT OF ATOMS AT CENTERS IN THE LIGAND THAT       
REMARK   3  ARE FREE TO REARRANGE IN SOLVENT IS CHANGED. MISTAKES IN            
REMARK   3  CARBOHYDRATE ANOMERIC LINKAGES ARE ALSO CORRECTED.                  
REMARK   4                                                                      
REMARK   4 2VDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34060.                                       
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          : CUSTOM (SBC2 3K)                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.00                               
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) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.00                               
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   (%): 67.5                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG3350, 0.7 M MAGNESIUM          
REMARK 280  ACETATE, 0.1 M IMIDAZOLE, PH 6.5, VAPOR DIFFUSION,                  
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      118.15933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.07967            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.07967            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      118.15933            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 10970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.7 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     SER B    77                                                      
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  4035     O    HOH B  4037              2.20            
REMARK 500   O    HOH H  4020     O    HOH H  4022              2.17            
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       29.11   -140.09                                   
REMARK 500    SER A 101     -129.84     50.26                                   
REMARK 500    LYS A 118     -130.36     52.78                                   
REMARK 500    GLU A 123      129.73     99.33                                   
REMARK 500    LEU A 212      -52.09     77.55                                   
REMARK 500    SER A 261       70.65     48.18                                   
REMARK 500    THR B   7       54.79    -96.81                                   
REMARK 500    ARG B   8       66.56   -154.05                                   
REMARK 500    VAL B  10       73.90     43.29                                   
REMARK 500    ASP B  47       38.20    -99.88                                   
REMARK 500    ASP B  66       49.08   -142.48                                   
REMARK 500    VAL B  80       91.25     62.47                                   
REMARK 500    PRO B  94      121.59    -33.79                                   
REMARK 500    ASP B  95       -8.17     64.89                                   
REMARK 500    VAL B 157      -81.24   -125.69                                   
REMARK 500    SER B 213     -154.15   -117.99                                   
REMARK 500    LEU B 258       -3.08     87.71                                   
REMARK 500    VAL B 275      -75.46    -95.73                                   
REMARK 500    ASN B 303       60.95     61.46                                   
REMARK 500    CYS B 374     -158.88    -91.59                                   
REMARK 500    LYS B 410      -30.44     77.62                                   
REMARK 500    GLU B 442       76.08     57.35                                   
REMARK 500    HIS B 446      -59.26     70.85                                   
REMARK 500    THR B 454      153.28     67.52                                   
REMARK 500    ASP H 179      -13.54     70.49                                   
REMARK 500    SER L  30       67.08     24.91                                   
REMARK 500    SER L  77       81.64     59.56                                   
REMARK 500    ASN L 212       85.37     52.13                                   
REMARK 500    GLU L 213       57.88   -147.41                                   
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  47.0                                              
REMARK 620 3 ASP A 245   OD2 114.1  68.5                                        
REMARK 620 4 ASP A 247   O    79.8  69.2  90.7                                  
REMARK 620 5 THR A 250   C    92.4 135.8 153.2  89.8                            
REMARK 620 6 THR A 250   O    72.3 115.6 170.1  82.9  20.5                      
REMARK 620 7 THR A 250   OG1 144.3 143.5  94.8  79.3  59.0  76.7                
REMARK 620 8 GLU A 252   OE1  76.5  85.2  87.5 153.0 103.7 101.7 127.7          
REMARK 620 9 GLU A 252   OE2 123.1 130.9  86.6 155.8  82.1  96.2  77.0  50.9    
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  77.7                                              
REMARK 620 3 ASP A 297   OD1  81.3  76.4                                        
REMARK 620 4 ARG A 303   O   161.6  92.6  81.2                                  
REMARK 620 5 ASP A 305   OD1 106.9 152.9 130.4  88.9                            
REMARK 620 6 ASP A 305   OD2  81.1 155.4  88.1 104.0  47.4                      
REMARK 620 7 HOH A4120   O    97.2  76.1 152.1  95.5  76.9 119.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 369   OD1  79.8                                              
REMARK 620 3 TYR A 371   O    71.0  83.4                                        
REMARK 620 4 ASP A 367   OD1  78.3  98.7 148.3                                  
REMARK 620 5 ASP A 373   OD1  86.8 163.4 101.5  68.8                            
REMARK 620 6 ASP A 373   OD2 122.3 150.1  85.5 105.2  46.5                      
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  90.2                                              
REMARK 620 3 ASP A 426   OD1  77.5  83.6                                        
REMARK 620 4 ASP A 428   OD1 151.5  84.0  74.2                                  
REMARK 620 5 ASP A 434   OD1 107.1 160.8  92.1  76.9                            
REMARK 620 6 ASP A 434   OD2  91.1 142.3 133.3 110.4  48.0                      
REMARK 620 7 HOH A4134   O   138.3  84.6 142.2  69.0  87.6  69.9                
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 B1463   O2                                                     
REMARK 620 2 HOH B4009   O   102.1                                              
REMARK 620 3 ASP B 127   OD1  69.1 170.0                                        
REMARK 620 4 ASP B 251   OD2 116.5  95.2  85.1                                  
REMARK 620 5 GOL B1463   O1   63.4  74.9  96.4  63.5                            
REMARK 620 6 SER B 123   O   161.8  84.0 105.9  79.4 134.6                      
REMARK 620 7 ASP B 126   OD1  84.5 100.5  83.7 150.5 145.0  77.6                
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 162.4                                              
REMARK 620 3 ASN B 215   OD1  89.6 100.8                                        
REMARK 620 4 ASP B 217   OD1  75.8  90.1  88.5                                  
REMARK 620 5 PRO B 219   O    88.3  82.8 173.7  96.8                            
REMARK 620 6 GLU B 220   OE2  89.7 105.4  83.7 163.7  90.3                      
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 B4028   O                                                      
REMARK 620 2 SER B 123   OG   90.9                                              
REMARK 620 3 GLU B 220   OE1  77.6 162.8                                        
REMARK 620 4 HOH B4008   O    97.1  88.2 105.7                                  
REMARK 620 5 AGG B1462   OXT  90.6  79.3  88.0 165.4                            
REMARK 620 6 SER B 121   OG  163.7  96.7  91.5  97.6  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGG B1462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1463                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514.                                                  
DBREF  2VDM A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDM B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDM H    1   221  PDB    2VDM     2VDM             1    221             
DBREF  2VDM L    1   214  PDB    2VDM     2VDM             1    214             
SEQADV 2VDM GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HET    AGG  B1462      30                                                       
HET    GOL  A1453       6                                                       
HET    GOL  B1463       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     AGG TIROFIBAN                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6   CA    6(CA 2+)                                                     
FORMUL   7  MAN    8(C6 H12 O6)                                                 
FORMUL   8  AGG    C22 H36 N2 O5 S                                              
FORMUL   9   MG    MG 2+                                                        
FORMUL  10  NAG    7(C8 H15 N O6)                                               
FORMUL  11  HOH   *355(H2 O)                                                    
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
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  GLU B  174  5                                   6    
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  ALA B  439  5                                   5    
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 4 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4  AB 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1  AC 4 GLU A  75  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 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AD 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AD 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AD 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AE 4 SER A 172  VAL A 175  0                                        
SHEET    2  AE 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AE 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AE 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AF 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AF 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AF 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AF 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AG 4 SER A 292  THR A 296  0                                        
SHEET    2  AG 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AG 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AG 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AH 2 MET A 314  ARG A 317  0                                        
SHEET    2  AH 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AI 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AI 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AI 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AI 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AJ 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AJ 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  LEU B  40  0                                        
SHEET    2  BA 3 CYS B  23  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BA 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BB 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 SER B 353  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  LEU B 389 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  LYS B 402 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 SER B 367  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 6 SER L  10  VAL L  13  0                                        
SHEET    2  LB 6 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 6 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 6 ILE L  33  GLN L  38 -1  O  GLY L  34   N  VAL L  89           
SHEET    5  LB 6 PHE L  44  TYR L  49 -1  O  MET L  45   N  GLN L  37           
SHEET    6  LB 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LC 4 SER L  10  VAL L  13  0                                        
SHEET    2  LC 4 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LC 4 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LC 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  LD 4 THR L 114  PHE L 118  0                                        
SHEET    2  LD 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LD 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LD 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LE 4 SER L 153  GLU L 154  0                                        
SHEET    2  LE 4 ASN L 145  ILE L 150 -1  O  ILE L 150   N  SER L 153           
SHEET    3  LE 4 SER L 191  THR L 197 -1  O  THR L 193   N  LYS L 149           
SHEET    4  LE 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.05  
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  2.03  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.05  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
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  2.03  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.03  
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  2.06  
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  1.45  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.39  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.38  
LINK        CA    CA A2004                 C   THR A 250     1555   1555  3.14  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.39  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.69  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.37  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.69  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.71  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.78  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.30  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.33  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.36  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.92  
LINK        CA    CA A2005                 O   HOH A4120     1555   1555  2.11  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.50  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.16  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.30  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.43  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.94  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.53  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.65  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.57  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.35  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.49  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.84  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.50  
LINK        CA    CA A2007                 O   HOH A4134     1555   1555  2.19  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.33  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.21  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK        MG    MG B2001                 O   HOH B4008     1555   1555  2.16  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.10  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.11  
LINK        MG    MG B2001                 OXT AGG B1462     1555   1555  2.36  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.08  
LINK        MG    MG B2001                 O   HOH B4028     1555   1555  2.12  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.43  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.27  
LINK        CA    CA B2002                 O1  GOL B1463     1555   1555  2.85  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.50  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.36  
LINK        CA    CA B2002                 O   HOH B4009     1555   1555  2.40  
LINK        CA    CA B2002                 O2  GOL B1463     1555   1555  2.43  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.32  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.27  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.28  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.20  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.37  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.39  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.44  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.45  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
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        -0.92                     
CISPEP   2 SER B  162    PRO B  163          0         5.64                     
CISPEP   3 SER B  168    PRO B  169          0        -9.63                     
CISPEP   4 PHE H  152    PRO H  153          0        -1.08                     
CISPEP   5 GLU H  154    PRO H  155          0         0.37                     
CISPEP   6 TRP H  194    PRO H  195          0         2.68                     
CISPEP   7 SER L    7    PRO L    8          0       -10.35                     
CISPEP   8 LEU L   94    PRO L   95          0        -1.94                     
CISPEP   9 TYR L  140    PRO L  141          0         3.74                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A4120                                          
SITE     1 AC3  5 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  5 ASP A 373                                                     
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4134                                          
SITE     1 AC5  2 ASN A  15  HOH A4139                                          
SITE     1 AC6  2 ASN A 249  HOH A4098                                          
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  AGG B1462                    
SITE     2 AC7  6 HOH B4008  HOH B4028                                          
SITE     1 AC8  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC8  6 GOL B1463  HOH B4009                                          
SITE     1 AC9  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC9  5 GLU B 220                                                     
SITE     1 BC1  5 ASN B  99  SER B 398  NAG B3371  HOH B4072                    
SITE     2 BC1  5 HOH B4073                                                     
SITE     1 BC2  4 LEU B 317  ASN B 320  NAG B3321  HOH B4074                    
SITE     1 BC3  4 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  2 ARG A 281  MAN B3322                                          
SITE     1 BC6  2 NAG B3321  MAN B3322                                          
SITE     1 BC7  5 ASN B 371  SER B 398  GLU B 400  NAG B3099                    
SITE     2 BC7  5 NAG B3372                                                     
SITE     1 BC8  4 NAG B3371  MAN B3373  MAN B3375  MAN B3376                    
SITE     1 BC9  5 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  5 MAN B3375                                                     
SITE     1 CC1  4 ASN A 299  SER A 396  GLU A 397  MAN B3373                    
SITE     1 CC2  6 ALA A 342  PRO A 343  NAG B3372  MAN B3373                    
SITE     2 CC2  6 MAN B3376  MAN B3377                                          
SITE     1 CC3  5 PRO A 343  SER A 344  LEU A 346  NAG B3372                    
SITE     2 CC3  5 MAN B3375                                                     
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5 17 ASP A 159  PHE A 160  TYR A 189  LEU A 192                    
SITE     2 CC5 17 ASP A 224  SER A 225  SER B 121  TYR B 122                    
SITE     3 CC5 17 SER B 123  ARG B 214  ASN B 215  ARG B 216                    
SITE     4 CC5 17 ASP B 217  ALA B 218  GLU B 220   MG B2001                    
SITE     5 CC5 17 HOH B4070                                                     
SITE     1 CC6  5 PHE A  87  ARG A  90  HIS A 112  LYS A 124                    
SITE     2 CC6  5 HOH A4037                                                     
SITE     1 CC7  6 ASP B 126  ASP B 127  ASP B 251  THR B 311                    
SITE     2 CC7  6  CA B2002  HOH B4031                                          
CRYST1  148.577  148.577  177.239  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      0.006731  0.003886  0.000000        0.00000                         
SCALE2      0.000000  0.007772  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system