GenomeNet

Database: PDB
Entry: 2VDR
LinkDB: 2VDR
Original site: 2VDR 
HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDR              
TITLE     INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A CHIMERIC                  
TITLE    2 FIBRINOGEN GAMMA CHAIN PEPTIDE, LGGAKQRGDV                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HEADPIECE, RESIDUES 32-483;                                
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6  INTEGRIN ALPHA-IIB HEAVY CHAIN;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: HEADPIECE, RESIDUES 27-487;                                
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  16 CHAIN: H;                                                            
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  19 CHAIN: L;                                                            
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: FIBRINOGEN;                                                
COMPND  22 CHAIN: C;                                                            
COMPND  23 FRAGMENT: GAMMA CHAIN C-TERMINAL PEPTIDE, RESIDUES 428-437;          
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  19 ORGANISM_COMMON: MOUSE;                                              
SOURCE  20 ORGANISM_TAXID: 10090;                                               
SOURCE  21 STRAIN: BALB/C;                                                      
SOURCE  22 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: MOUSE;                                              
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 STRAIN: BALB/C;                                                      
SOURCE  28 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 SYNTHETIC: YES;                                                      
SOURCE  31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  32 ORGANISM_COMMON: HUMAN;                                              
SOURCE  33 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, PLATELET     
KEYWDS   2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,       
KEYWDS   3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE  
KEYWDS   4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,   
KEYWDS   5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM      
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDR    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDR    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDR    0                                                
JRNL        AUTH   T.A.SPRINGER,J.ZHU,T.XIAO                                    
JRNL        TITL   STRUCTURAL BASIS FOR DISTINCTIVE RECOGNITION OF FIBRINOGEN   
JRNL        TITL 2 GAMMAC PEPTIDE BY THE PLATELET INTEGRIN ALPHAIIBBETA3.       
JRNL        REF    J.CELL BIOL.                  V. 182   791 2008              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   18710925                                                     
JRNL        DOI    10.1083/JCB.200801146                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER            
REMARK   1  TITL   STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO   
REMARK   1  TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS                              
REMARK   1  REF    NATURE                        V. 432    59 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15378069                                                     
REMARK   1  DOI    10.1038/NATURE02976                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 80277                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4276                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5145                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 297                          
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10537                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 1142                                    
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) : 43.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : -0.13000                                             
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : -0.06000                                             
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): 0.220         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.183         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.822         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11037 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7400 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15084 ; 1.043 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18022 ; 0.790 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1398 ; 5.725 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   482 ;34.156 ;24.315       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1739 ;12.173 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;14.711 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1698 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12324 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2184 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1991 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7668 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5312 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5756 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   925 ; 0.154 ; 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):    22 ; 0.116 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    77 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    40 ; 0.162 ; 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):  7058 ; 1.901 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11025 ; 2.897 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4619 ; 2.019 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4036 ; 2.975 ;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  : 26                                         
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    32                          
REMARK   3    ORIGIN FOR THE GROUP (A): 130.0750  14.1410  72.0520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1269 T22:   0.0924                                     
REMARK   3      T33:   0.0326 T12:   0.0875                                     
REMARK   3      T13:   0.0477 T23:   0.2903                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5064 L22:   4.3405                                     
REMARK   3      L33:   2.5191 L12:  -0.1934                                     
REMARK   3      L13:   1.0806 L23:  -0.6442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0069 S12:   0.3691 S13:  -0.2807                       
REMARK   3      S21:   0.0607 S22:  -0.4708 S23:  -0.6162                       
REMARK   3      S31:   0.4584 S32:   0.7992 S33:   0.4778                       
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    33        A    54                          
REMARK   3    ORIGIN FOR THE GROUP (A): 126.9940  29.3980  71.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1604 T22:  -0.0221                                     
REMARK   3      T33:  -0.0250 T12:   0.0015                                     
REMARK   3      T13:  -0.0655 T23:   0.1856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9709 L22:  13.8415                                     
REMARK   3      L33:   4.5553 L12:   0.4717                                     
REMARK   3      L13:  -1.3274 L23:   5.7691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1593 S12:  -0.3785 S13:   0.0876                       
REMARK   3      S21:   0.1558 S22:  -0.2124 S23:  -0.5255                       
REMARK   3      S31:  -0.1230 S32:   0.1724 S33:   0.0531                       
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    55        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 121.1530  30.7180  64.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1675 T22:   0.0085                                     
REMARK   3      T33:  -0.0365 T12:  -0.0736                                     
REMARK   3      T13:  -0.0323 T23:   0.1680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6748 L22:   1.4259                                     
REMARK   3      L33:   1.6692 L12:  -0.3487                                     
REMARK   3      L13:  -0.1723 L23:  -0.6809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:   0.0122 S13:  -0.0059                       
REMARK   3      S21:   0.1725 S22:  -0.2646 S23:  -0.3390                       
REMARK   3      S31:  -0.0246 S32:   0.4267 S33:   0.2819                       
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   164                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.2880  35.9960  63.0630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1368 T22:  -0.0888                                     
REMARK   3      T33:  -0.1041 T12:  -0.0828                                     
REMARK   3      T13:  -0.0358 T23:   0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4628 L22:   1.9926                                     
REMARK   3      L33:   2.6118 L12:  -0.4821                                     
REMARK   3      L13:  -1.9390 L23:   0.3968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:  -0.0157 S13:  -0.1175                       
REMARK   3      S21:   0.0287 S22:  -0.1446 S23:   0.1613                       
REMARK   3      S31:  -0.0388 S32:   0.0315 S33:   0.1594                       
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   165        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A): 105.7730  24.8560  64.2490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0889 T22:  -0.0820                                     
REMARK   3      T33:  -0.0649 T12:  -0.0745                                     
REMARK   3      T13:  -0.0015 T23:   0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1797 L22:   0.7734                                     
REMARK   3      L33:   1.1158 L12:   0.1430                                     
REMARK   3      L13:  -0.4173 L23:  -0.3648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0348 S12:   0.0918 S13:  -0.1344                       
REMARK   3      S21:  -0.0161 S22:  -0.1999 S23:   0.0099                       
REMARK   3      S31:   0.2506 S32:  -0.0894 S33:   0.1651                       
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   315                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.4170  10.6060  73.7810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0294 T22:  -0.2023                                     
REMARK   3      T33:  -0.0917 T12:  -0.1316                                     
REMARK   3      T13:   0.0710 T23:   0.0591                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5943 L22:   2.1065                                     
REMARK   3      L33:   2.0306 L12:  -0.0649                                     
REMARK   3      L13:  -0.0317 L23:   0.4859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1181 S12:   0.0774 S13:  -0.2662                       
REMARK   3      S21:  -0.0398 S22:  -0.1491 S23:   0.0824                       
REMARK   3      S31:   0.3749 S32:  -0.0648 S33:   0.2672                       
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   316        A   337                          
REMARK   3    ORIGIN FOR THE GROUP (A): 104.1410   4.7230  86.1710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1631 T22:  -0.1655                                     
REMARK   3      T33:  -0.0559 T12:  -0.1631                                     
REMARK   3      T13:   0.1289 T23:   0.1805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1531 L22:   8.1318                                     
REMARK   3      L33:  16.7972 L12:  -0.1188                                     
REMARK   3      L13:  -0.2936 L23:  10.7464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2019 S12:  -0.3774 S13:  -0.4574                       
REMARK   3      S21:   0.6581 S22:  -0.6574 S23:   0.4486                       
REMARK   3      S31:   1.2820 S32:  -1.1033 S33:   0.8593                       
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   338        A   376                          
REMARK   3    ORIGIN FOR THE GROUP (A): 113.6150   3.5190  79.6680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0749 T22:  -0.2611                                     
REMARK   3      T33:  -0.0605 T12:   0.0068                                     
REMARK   3      T13:   0.0582 T23:   0.1902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6664 L22:   2.9922                                     
REMARK   3      L33:   2.0517 L12:   0.6866                                     
REMARK   3      L13:  -0.1091 L23:   0.9755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1760 S12:  -0.0346 S13:  -0.3178                       
REMARK   3      S21:  -0.1309 S22:  -0.1127 S23:  -0.0294                       
REMARK   3      S31:   0.5339 S32:   0.1794 S33:   0.2887                       
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   377        A   452                          
REMARK   3    ORIGIN FOR THE GROUP (A): 124.5220   7.5450  80.1950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0457 T22:  -0.0799                                     
REMARK   3      T33:  -0.0060 T12:   0.1004                                     
REMARK   3      T13:   0.0291 T23:   0.2788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1574 L22:   2.4891                                     
REMARK   3      L33:   2.9107 L12:   0.9162                                     
REMARK   3      L13:  -0.0147 L23:   0.2097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0909 S12:  -0.2130 S13:  -0.3615                       
REMARK   3      S21:   0.2477 S22:  -0.2637 S23:  -0.2917                       
REMARK   3      S31:   0.5424 S32:   0.6279 S33:   0.3546                       
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    28                          
REMARK   3    ORIGIN FOR THE GROUP (A): 113.7480  17.2440 172.2760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5332 T22:  -0.3366                                     
REMARK   3      T33:  -0.2075 T12:   0.0516                                     
REMARK   3      T13:  -0.3938 T23:  -0.0920                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9758 L22:  11.6676                                     
REMARK   3      L33:   5.5717 L12:  -1.3380                                     
REMARK   3      L13:   2.2247 L23:   0.9728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3184 S12:  -0.3658 S13:  -0.1020                       
REMARK   3      S21:   1.4565 S22:   0.5055 S23:  -0.8356                       
REMARK   3      S31:  -0.2894 S32:   0.4794 S33:  -0.1870                       
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    29        B    72                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.2570  23.7020 167.5800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5100 T22:  -0.0729                                     
REMARK   3      T33:  -0.4776 T12:   0.2875                                     
REMARK   3      T13:  -0.0447 T23:  -0.0942                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8787 L22:   3.2985                                     
REMARK   3      L33:  10.9136 L12:  -1.3853                                     
REMARK   3      L13:   3.2330 L23:  -2.3541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5732 S12:  -0.8802 S13:  -0.0411                       
REMARK   3      S21:   1.2774 S22:   0.7166 S23:  -0.2468                       
REMARK   3      S31:  -1.7546 S32:  -2.0912 S33:  -0.1434                       
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    79        B   100                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.3930  30.1130 148.4950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4310 T22:  -0.1569                                     
REMARK   3      T33:  -0.5200 T12:   0.2131                                     
REMARK   3      T13:   0.0115 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1355 L22:   8.2954                                     
REMARK   3      L33:  35.8670 L12:  -3.3482                                     
REMARK   3      L13:  16.5444 L23: -10.7296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9467 S12:  -0.5715 S13:   0.4243                       
REMARK   3      S21:   0.8436 S22:   0.2787 S23:  -0.9191                       
REMARK   3      S31:  -2.9333 S32:  -1.3429 S33:   0.6679                       
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   101        B   137                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9390  37.0620 108.1200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2266 T22:  -0.0377                                     
REMARK   3      T33:  -0.1198 T12:  -0.2305                                     
REMARK   3      T13:   0.0402 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0231 L22:   0.7196                                     
REMARK   3      L33:   4.3347 L12:  -0.6844                                     
REMARK   3      L13:   0.3406 L23:  -1.2790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1203 S12:  -0.2716 S13:   0.1423                       
REMARK   3      S21:   0.4935 S22:  -0.0394 S23:   0.0483                       
REMARK   3      S31:  -0.3848 S32:   0.1777 S33:   0.1596                       
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   138        B   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.2760  43.1080  94.9320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0956 T22:  -0.1204                                     
REMARK   3      T33:  -0.1042 T12:  -0.2048                                     
REMARK   3      T13:   0.0137 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2712 L22:   0.7980                                     
REMARK   3      L33:   4.2329 L12:   0.0412                                     
REMARK   3      L13:  -1.3445 L23:  -0.4346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1659 S12:  -0.2002 S13:   0.1686                       
REMARK   3      S21:   0.3609 S22:  -0.0854 S23:  -0.0598                       
REMARK   3      S31:  -0.5642 S32:   0.2230 S33:  -0.0805                       
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   202        B   342                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.4650  31.4470  97.1540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0599 T22:  -0.0974                                     
REMARK   3      T33:  -0.1573 T12:  -0.1865                                     
REMARK   3      T13:  -0.0210 T23:   0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5295 L22:   1.5569                                     
REMARK   3      L33:   1.9793 L12:  -0.7815                                     
REMARK   3      L13:  -0.6696 L23:   0.4022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0347 S12:  -0.2959 S13:   0.0719                       
REMARK   3      S21:   0.4684 S22:  -0.0655 S23:  -0.1139                       
REMARK   3      S31:   0.0011 S32:   0.2328 S33:   0.1002                       
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   343        B   390                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.5840  21.7460 133.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2415 T22:  -0.0509                                     
REMARK   3      T33:  -0.1708 T12:  -0.0519                                     
REMARK   3      T13:   0.0301 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5801 L22:   3.0602                                     
REMARK   3      L33:  24.4817 L12:  -1.9241                                     
REMARK   3      L13:   7.8241 L23:  -4.7267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7802 S12:   0.7670 S13:  -0.4658                       
REMARK   3      S21:  -0.3422 S22:   0.1905 S23:  -0.1241                       
REMARK   3      S31:   1.5879 S32:   1.0544 S33:  -0.9706                       
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 :   B   391        B   441                          
REMARK   3    ORIGIN FOR THE GROUP (A): 108.5290  28.6310 149.9560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4680 T22:  -0.3329                                     
REMARK   3      T33:  -0.1853 T12:  -0.0742                                     
REMARK   3      T13:  -0.0323 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4165 L22:   2.5646                                     
REMARK   3      L33:  22.3065 L12:  -1.4135                                     
REMARK   3      L13:   8.1958 L23:  -2.0718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5095 S12:   0.3702 S13:   0.1596                       
REMARK   3      S21:   0.7477 S22:   0.4255 S23:  -0.4918                       
REMARK   3      S31:  -2.2382 S32:   1.1673 S33:   0.0840                       
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 :   B   442        B   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): 120.0640  31.0660 184.4760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5715 T22:   1.5098                                     
REMARK   3      T33:   1.1120 T12:  -0.3991                                     
REMARK   3      T13:  -0.9833 T23:  -0.1423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9298 L22:  20.6503                                     
REMARK   3      L33:   2.2601 L12:  -9.0084                                     
REMARK   3      L13:   2.9802 L23:  -6.8316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0021 S12:  -1.2108 S13:   0.2598                       
REMARK   3      S21:   3.2835 S22:  -0.8862 S23:  -4.0040                       
REMARK   3      S31:  -1.2283 S32:   5.1978 S33:   1.8883                       
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     1        H    31                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.6610  36.1380  38.0710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1914 T22:  -0.0108                                     
REMARK   3      T33:  -0.0695 T12:  -0.1378                                     
REMARK   3      T13:  -0.0130 T23:   0.0532                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2002 L22:   5.3786                                     
REMARK   3      L33:   6.3577 L12:  -2.0402                                     
REMARK   3      L13:   3.7337 L23:  -3.5323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2521 S12:   0.1840 S13:  -0.3798                       
REMARK   3      S21:  -0.2607 S22:  -0.0368 S23:   0.2724                       
REMARK   3      S31:   0.6521 S32:  -0.1354 S33:  -0.2153                       
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    32        H   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.5780  43.8020  41.1100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1935 T22:  -0.0055                                     
REMARK   3      T33:  -0.0610 T12:  -0.0491                                     
REMARK   3      T13:  -0.0061 T23:   0.0749                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1847 L22:   0.6209                                     
REMARK   3      L33:   2.8509 L12:  -0.2202                                     
REMARK   3      L13:   0.9068 L23:  -0.4825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.1078 S13:   0.0779                       
REMARK   3      S21:   0.0097 S22:  -0.0627 S23:   0.0597                       
REMARK   3      S31:   0.0714 S32:  -0.2312 S33:   0.0495                       
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   123        H   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  91.8280  46.8260   5.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1922 T22:  -0.1133                                     
REMARK   3      T33:  -0.1513 T12:   0.0959                                     
REMARK   3      T13:  -0.0724 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3694 L22:   1.8655                                     
REMARK   3      L33:  11.1482 L12:  -0.7554                                     
REMARK   3      L13:  -1.4707 L23:  -0.1040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2059 S12:   0.2741 S13:  -0.2516                       
REMARK   3      S21:  -0.3223 S22:  -0.1127 S23:  -0.0020                       
REMARK   3      S31:   0.7386 S32:  -0.0914 S33:  -0.0932                       
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   186        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.7630  42.3920  -2.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1336 T22:  -0.0298                                     
REMARK   3      T33:  -0.2082 T12:   0.1508                                     
REMARK   3      T13:  -0.1592 T23:  -0.1394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7071 L22:   2.7947                                     
REMARK   3      L33:   8.7499 L12:  -1.0243                                     
REMARK   3      L13:  -2.6669 L23:   1.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1302 S12:   0.4186 S13:  -0.8154                       
REMARK   3      S21:  -0.9514 S22:  -0.3258 S23:   0.3098                       
REMARK   3      S31:   1.5176 S32:   0.1092 S33:   0.1957                       
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 :   L     1        L   104                          
REMARK   3    ORIGIN FOR THE GROUP (A): 112.9620  45.3290  35.3670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1844 T22:  -0.0069                                     
REMARK   3      T33:  -0.0566 T12:   0.0158                                     
REMARK   3      T13:  -0.0080 T23:   0.1042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1897 L22:   0.7050                                     
REMARK   3      L33:   2.2925 L12:   0.2270                                     
REMARK   3      L13:  -0.6823 L23:  -0.3964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0672 S12:   0.3263 S13:   0.0725                       
REMARK   3      S21:  -0.0973 S22:  -0.0077 S23:  -0.0337                       
REMARK   3      S31:   0.1397 S32:  -0.0045 S33:  -0.0595                       
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 :   L   105        L   160                          
REMARK   3    ORIGIN FOR THE GROUP (A):  99.6910  57.8230   5.3960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2449 T22:   0.1861                                     
REMARK   3      T33:  -0.1904 T12:   0.0720                                     
REMARK   3      T13:   0.0349 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8369 L22:   4.0411                                     
REMARK   3      L33:   4.0935 L12:  -3.7715                                     
REMARK   3      L13:   3.0199 L23:  -2.8696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1404 S12:   0.2287 S13:   0.2401                       
REMARK   3      S21:  -0.1237 S22:  -0.2792 S23:  -0.1870                       
REMARK   3      S31:   0.1924 S32:   0.4300 S33:   0.1389                       
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   161        L   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  95.7610  57.3740   5.3830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2702 T22:   0.0630                                     
REMARK   3      T33:  -0.2088 T12:   0.0479                                     
REMARK   3      T13:   0.0041 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7788 L22:   5.5380                                     
REMARK   3      L33:   5.1761 L12:  -5.5046                                     
REMARK   3      L13:   4.5810 L23:  -3.5699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1019 S12:   0.1531 S13:  -0.1716                       
REMARK   3      S21:  -0.0784 S22:  -0.0803 S23:   0.1474                       
REMARK   3      S31:   0.0835 S32:   0.2213 S33:  -0.0216                       
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   193        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.7210  62.5240  -1.3470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2592 T22:   0.2045                                     
REMARK   3      T33:  -0.1120 T12:   0.1302                                     
REMARK   3      T13:   0.0453 T23:   0.1559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.0175 L22:   4.2715                                     
REMARK   3      L33:   9.5348 L12:  -4.4939                                     
REMARK   3      L13:   7.5253 L23:  -5.1262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2547 S12:   1.2658 S13:   0.3870                       
REMARK   3      S21:  -0.3362 S22:  -0.6392 S23:  -0.4028                       
REMARK   3      S31:   0.0022 S32:   0.9662 S33:   0.3846                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VDR 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-34089.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07223                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM (SBC2 3K)                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 609049                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM            
REMARK 280  ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.86200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.93100            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.93100            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.86200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, H, L                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ALA 396 TO ARG                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     LEU C   402                                                      
REMARK 465     GLY C   403                                                      
REMARK 465     GLY C   404                                                      
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 A  4194     O    HOH A  4195              2.20            
REMARK 500   O    HOH B  4029     O    HOH A  4258              2.15            
REMARK 500   O    HOH B  4122     O    HOH A  4258              2.09            
REMARK 500   O    HOH L  4014     O    HOH L  4137              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -124.46     51.48                                   
REMARK 500    LYS A 118     -120.91     51.92                                   
REMARK 500    GLU A 123      134.02     98.17                                   
REMARK 500    LEU A 212      -48.68     72.16                                   
REMARK 500    THR A 296      143.95   -171.71                                   
REMARK 500    VAL B  10       75.08     40.69                                   
REMARK 500    PHE B  56       81.67   -153.35                                   
REMARK 500    ASP B  71     -157.00   -112.18                                   
REMARK 500    VAL B  80       97.55     68.35                                   
REMARK 500    VAL B 157      -87.45   -127.66                                   
REMARK 500    SER B 213     -154.96   -107.16                                   
REMARK 500    ASP B 241       48.86   -107.62                                   
REMARK 500    LEU B 258      -11.85     84.06                                   
REMARK 500    VAL B 275      -77.27    -87.01                                   
REMARK 500    LYS B 410      -25.51     72.80                                   
REMARK 500    GLN B 440       54.66   -105.22                                   
REMARK 500    GLU B 442       78.14     53.27                                   
REMARK 500    HIS B 446      -57.96     70.17                                   
REMARK 500    THR B 454      158.85     69.16                                   
REMARK 500    ASP H 179      -16.14     75.75                                   
REMARK 500    SER L  30       56.30     31.29                                   
REMARK 500    SER L  77       79.31     64.31                                   
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  50.9                                              
REMARK 620 3 ASP A 245   OD2 118.1  67.2                                        
REMARK 620 4 ASP A 247   O    79.2  77.8  85.5                                  
REMARK 620 5 THR A 250   O    75.7 125.5 159.8  82.7                            
REMARK 620 6 THR A 250   OG1 144.6 142.9  84.9  76.0  76.5                      
REMARK 620 7 GLU A 252   OE1  84.2  82.0  91.4 159.2 105.3 124.3                
REMARK 620 8 GLU A 252   OE2 128.6 129.3  91.4 148.6  90.2  72.6  51.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  80.0                                              
REMARK 620 3 ASP A 297   OD1  82.4  79.5                                        
REMARK 620 4 ARG A 303   O   160.9  86.2  82.2                                  
REMARK 620 5 ASP A 305   OD1 119.4 144.0 129.9  79.3                            
REMARK 620 6 ASP A 305   OD2  94.1 165.0  86.0  96.0  50.7                      
REMARK 620 7 HOH A4317   O    89.6  80.3 159.3 101.0  70.5 113.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 369   OD1  75.8                                              
REMARK 620 3 TYR A 371   O    77.1  89.5                                        
REMARK 620 4 ASP A 367   OD1  86.1  90.1 162.8                                  
REMARK 620 5 HOH A4361   O   149.7  73.9 102.2  94.3                            
REMARK 620 6 ASP A 373   OD1  94.1 161.6 103.3  73.7 115.2                      
REMARK 620 7 ASP A 373   OD2 133.9 147.5  86.4 102.9  75.5  48.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 432   O                                                      
REMARK 620 2 ASN A 430   OD1  87.0                                              
REMARK 620 3 ASP A 426   OD1  78.8  86.3                                        
REMARK 620 4 ASP A 428   OD1 156.7  88.6  78.1                                  
REMARK 620 5 ASP A 434   OD1  99.5 171.7  90.0  83.4                            
REMARK 620 6 ASP A 434   OD2  85.6 135.3 134.8 113.1  51.0                      
REMARK 620 7 HOH A4399   O   131.6  80.0 145.3  69.8  99.1  72.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1462   C2                                                     
REMARK 620 2 GOL B1462   O2   28.0                                              
REMARK 620 3 ASP B 251   OD2 100.4 127.7                                        
REMARK 620 4 GOL B1462   O1   46.4  64.8  67.9                                  
REMARK 620 5 HOH C4011   O   100.4  84.8 107.7  80.0                            
REMARK 620 6 SER B 123   O   178.6 152.8  79.0 134.1  80.9                      
REMARK 620 7 ASP B 126   OD1 104.6  79.5 151.0 141.0  81.9  75.6                
REMARK 620 8 ASP B 127   OD1  82.3  91.3  86.4 111.8 164.6  96.4  82.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 161.5                                              
REMARK 620 3 ASN B 215   OD1  94.4  98.5                                        
REMARK 620 4 ASP B 217   OD1  75.5  90.1  95.5                                  
REMARK 620 5 PRO B 219   O    89.2  80.0 171.1  93.3                            
REMARK 620 6 GLU B 220   OE2  91.1 103.0  85.5 166.6  86.3                      
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 B4112   O                                                      
REMARK 620 2 SER B 123   OG   95.5                                              
REMARK 620 3 GLU B 220   OE1  87.1 177.4                                        
REMARK 620 4 HOH B4041   O    99.5  80.5  99.2                                  
REMARK 620 5 ASP C 410   OD1  96.3  88.3  91.4 161.3                            
REMARK 620 6 SER B 121   OG  171.8  89.9  87.6  75.2  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1462                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 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. THERE IS A A408R  MUTATION                       
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN C SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 70906437 WHICH CORRESPONDS TO             
REMARK 999 THE UNIPROT ENTRY Q53Y18                                             
DBREF  2VDR A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDR B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDR H    1   221  PDB    2VDR     2VDR             1    221             
DBREF  2VDR L    1   214  PDB    2VDR     2VDR             1    214             
DBREF  2VDR C  402   411  UNP    Q53Y18   Q53Y18_HUMAN   428    437             
SEQADV 2VDR GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQADV 2VDR ARG C  408  UNP  Q53Y18    ALA   396 ENGINEERED MUTATION            
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 C   10  LEU GLY GLY ALA LYS GLN ARG GLY ASP VAL                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HET    GOL  A1453       6                                                       
HET    GOL  B1462       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   7   CA    6(CA 2+)                                                     
FORMUL   8  MAN    8(C6 H12 O6)                                                 
FORMUL   9   MG    MG 2+                                                        
FORMUL  10  NAG    7(C8 H15 N O6)                                               
FORMUL  11  HOH   *1142(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 SER B  121  ASP B  126  5                                   6    
HELIX   10  10 ASP B  127  THR B  146  1                                  20    
HELIX   11  11 PRO B  169  LEU B  173  5                                   5    
HELIX   12  12 CYS B  177  LYS B  181  5                                   5    
HELIX   13  13 GLN B  199  LYS B  209  1                                  11    
HELIX   14  14 GLY B  221  CYS B  232  1                                  12    
HELIX   15  15 CYS B  232  GLY B  237  1                                   6    
HELIX   16  16 LEU B  258  GLY B  264  5                                   7    
HELIX   17  17 SER B  291  LYS B  302  1                                  12    
HELIX   18  18 VAL B  314  GLU B  323  1                                  10    
HELIX   19  19 SER B  337  LYS B  350  1                                  14    
HELIX   20  20 CYS B  435  ALA B  441  5                                   7    
HELIX   21  21 ASN H   28  THR H   32  5                                   5    
HELIX   22  22 THR H   87  THR H   91  5                                   5    
HELIX   23  23 SER H  162  SER H  164  5                                   3    
HELIX   24  24 PRO H  206  SER H  209  5                                   4    
HELIX   25  25 ASP L   79  PHE L   83  5                                   5    
HELIX   26  26 SER L  121  GLY L  128  1                                   8    
HELIX   27  27 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 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 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 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 VAL A 293  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  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 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  2.08  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.06  
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  2.04  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.10  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.07  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.05  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.04  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.05  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.04  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.11  
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  2.34  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.40  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.41  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.42  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.44  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.55  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.32  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.71  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.28  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.41  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.52  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.60  
LINK        CA    CA A2005                 O   HOH A4317     1555   1555  2.25  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.56  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.27  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.19  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.30  
LINK        CA    CA A2006                 O   HOH A4361     1555   1555  2.41  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.70  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.66  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.55  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.46  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.37  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.64  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.43  
LINK        CA    CA A2007                 O   HOH A4399     1555   1555  2.34  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.31  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.22  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.45  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.43  
LINK        MG    MG B2001                 O   HOH B4041     1555   1555  2.31  
LINK        MG    MG B2001                 O   HOH B4112     1555   1555  2.20  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.34  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.16  
LINK        MG    MG B2001                 OD1 ASP C 410     1555   1555  2.13  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.08  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.28  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.38  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.40  
LINK        CA    CA B2002                 O   HOH C4011     1555   1555  2.30  
LINK        CA    CA B2002                 O1  GOL B1462     1555   1555  3.00  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.32  
LINK        CA    CA B2002                 O2  GOL B1462     1555   1555  2.62  
LINK        CA    CA B2002                 C2  GOL B1462     1555   1555  2.99  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.37  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.33  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.18  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.34  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.36  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.41  
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  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.44  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.43  
LINK         O3  MAN B3373                 C1  MAN B3374     1555   1555  1.44  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.44  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0         0.54                     
CISPEP   2 SER B  162    PRO B  163          0         4.09                     
CISPEP   3 SER B  168    PRO B  169          0       -11.30                     
CISPEP   4 PHE H  152    PRO H  153          0        -4.90                     
CISPEP   5 GLU H  154    PRO H  155          0        -0.27                     
CISPEP   6 TRP H  194    PRO H  195          0         6.04                     
CISPEP   7 SER L    7    PRO L    8          0        -9.55                     
CISPEP   8 LEU L   94    PRO L   95          0        -4.13                     
CISPEP   9 TYR L  140    PRO L  141          0         1.75                     
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 A4317                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4361                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4399                                          
SITE     1 AC5  1 ASN A  15                                                     
SITE     1 AC6  1 ASN A 249                                                     
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  HOH B4041                    
SITE     2 AC7  6 HOH B4112  ASP C 410                                          
SITE     1 AC8  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC8  6 GOL B1462  HOH C4011                                          
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  6 ASN B  99  SER B 398  NAG B3371  HOH B4032                    
SITE     2 BC1  6 HOH B4237  HOH B4238                                          
SITE     1 BC2  9 MET A 285  LEU B 317  ASN B 320  NAG B3321                    
SITE     2 BC2  9 HOH B4239  HOH B4240  HOH B4241  HOH B4242                    
SITE     3 BC2  9 HOH B4245                                                     
SITE     1 BC3  6 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     2 BC3  6 HOH B4244  HOH B4245                                          
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  4 ARG A 281  MAN B3322  HOH B4246  HOH B4247                    
SITE     1 BC6  2 NAG B3321  MAN B3322                                          
SITE     1 BC7  7 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC7  7 NAG B3099  NAG B3372  HOH B4238                               
SITE     1 BC8  5 NAG B3371  MAN B3373  MAN B3375  MAN B3376                    
SITE     2 BC8  5 HOH B4248                                                     
SITE     1 BC9  6 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  6 MAN B3375  HOH B4249                                          
SITE     1 CC1  5 ASN A 299  SER A 396  GLU A 397  MAN B3373                    
SITE     2 CC1  5 HOH B4250                                                     
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  8 PRO A 343  SER A 344  LEU A 346  NAG B3372                    
SITE     2 CC3  8 MAN B3375  HOH B4253  HOH B4254  HOH B4255                    
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  3 ARG A  90  HOH A4153  HOH A4412                               
SITE     1 CC6  8 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 CC6  8  CA B2002  HOH B4234  HOH B4235  HOH B4236                    
CRYST1  148.328  148.328  176.793  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006742  0.003892  0.000000        0.00000                         
SCALE2      0.000000  0.007785  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005656        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system