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Database: PDB
Entry: 2VDQ
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HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDQ              
TITLE     INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A CHIMERIC                  
TITLE    2 FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQRGDV                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HEADPIECE, RESIDUES 32-483;                                
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6  INTEGRIN ALPHA-IIB HEAVY CHAIN;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: HEADPIECE, RESIDUES 27-487;                                
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  16 CHAIN: H;                                                            
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  19 CHAIN: L;                                                            
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: FIBRINOGEN, GAMMA POLYPEPTIDE;                             
COMPND  22 CHAIN: C;                                                            
COMPND  23 FRAGMENT: GAMMA CHAIN C-TERMINAL PEPTIDE, RESIDUES 426-437;          
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 2VDQ    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDQ    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDQ    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.    2.59 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) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 60283                          
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) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.141                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3207                            
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) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3171                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10515                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 1332                                    
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) : 41.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.21000                                             
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : 0.31000                                              
REMARK   3    B12 (A**2) : -0.10000                                             
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): 0.381         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.204        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11011 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7399 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15042 ; 1.043 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17995 ; 0.786 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1392 ; 5.666 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   480 ;34.024 ;24.250       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1734 ;12.618 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    63 ;14.186 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1694 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12275 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2182 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2167 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7952 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5357 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5803 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1064 ; 0.144 ; 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):    24 ; 0.109 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    93 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    43 ; 0.155 ; 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):  7028 ; 1.831 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10991 ; 2.920 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4613 ; 1.902 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4030 ; 2.953 ;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): 129.9990  14.2740  71.9790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1787 T22:   0.0578                                     
REMARK   3      T33:   0.0188 T12:   0.1115                                     
REMARK   3      T13:   0.0870 T23:   0.2906                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1519 L22:   5.0488                                     
REMARK   3      L33:   3.6863 L12:  -0.3678                                     
REMARK   3      L13:   1.1721 L23:  -0.3050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0385 S12:   0.4202 S13:  -0.4221                       
REMARK   3      S21:  -0.0407 S22:  -0.3412 S23:  -0.5086                       
REMARK   3      S31:   0.4757 S32:   0.8968 S33:   0.3797                       
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): 126.9090  29.6390  71.6850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1973 T22:  -0.0144                                     
REMARK   3      T33:  -0.1091 T12:   0.0036                                     
REMARK   3      T13:  -0.0214 T23:   0.1883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4012 L22:  13.1682                                     
REMARK   3      L33:   3.3830 L12:   0.3354                                     
REMARK   3      L13:  -0.8020 L23:   3.7316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1791 S12:  -0.3031 S13:   0.0000                       
REMARK   3      S21:  -0.0964 S22:  -0.3707 S23:  -0.1127                       
REMARK   3      S31:  -0.1689 S32:   0.0444 S33:   0.1915                       
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): 121.1170  30.8140  64.9070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1370 T22:   0.0192                                     
REMARK   3      T33:  -0.0122 T12:  -0.0652                                     
REMARK   3      T13:  -0.0353 T23:   0.1571                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2436 L22:   1.4073                                     
REMARK   3      L33:   1.7709 L12:  -0.5960                                     
REMARK   3      L13:  -0.4862 L23:  -0.7239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0851 S12:  -0.1345 S13:   0.0430                       
REMARK   3      S21:   0.1812 S22:  -0.1609 S23:  -0.3336                       
REMARK   3      S31:   0.0019 S32:   0.4327 S33:   0.2460                       
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): 107.2940  36.0800  63.0130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1120 T22:  -0.0383                                     
REMARK   3      T33:  -0.0803 T12:  -0.0791                                     
REMARK   3      T13:  -0.0354 T23:   0.0961                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4072 L22:   1.5037                                     
REMARK   3      L33:   2.5331 L12:   0.3592                                     
REMARK   3      L13:  -1.6436 L23:  -0.2923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0072 S12:   0.0379 S13:  -0.1503                       
REMARK   3      S21:  -0.0011 S22:  -0.2012 S23:   0.2352                       
REMARK   3      S31:  -0.0055 S32:   0.0328 S33:   0.1940                       
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): 105.7750  24.9610  64.1890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0788 T22:  -0.0583                                     
REMARK   3      T33:  -0.0321 T12:  -0.0571                                     
REMARK   3      T13:   0.0054 T23:   0.0660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0567 L22:   1.2248                                     
REMARK   3      L33:   2.1111 L12:   0.2732                                     
REMARK   3      L13:  -0.6243 L23:  -0.6772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0165 S12:   0.1411 S13:  -0.0951                       
REMARK   3      S21:   0.0331 S22:  -0.1469 S23:  -0.0012                       
REMARK   3      S31:   0.2090 S32:  -0.1146 S33:   0.1304                       
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): 102.4390  10.7280  73.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0473 T22:  -0.1845                                     
REMARK   3      T33:  -0.0614 T12:  -0.1151                                     
REMARK   3      T13:   0.0776 T23:   0.0796                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8569 L22:   2.1080                                     
REMARK   3      L33:   1.9814 L12:  -0.2102                                     
REMARK   3      L13:   0.1843 L23:   0.4512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1105 S12:   0.1435 S13:  -0.3214                       
REMARK   3      S21:  -0.0541 S22:  -0.1359 S23:   0.0494                       
REMARK   3      S31:   0.4135 S32:  -0.1282 S33:   0.2465                       
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): 104.1120   4.8050  86.1090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1279 T22:  -0.1388                                     
REMARK   3      T33:  -0.0602 T12:  -0.1425                                     
REMARK   3      T13:   0.1305 T23:   0.1937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1365 L22:   7.1695                                     
REMARK   3      L33:   9.1865 L12:  -0.7694                                     
REMARK   3      L13:  -1.7963 L23:   6.6196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2291 S12:  -0.3808 S13:  -0.3685                       
REMARK   3      S21:   0.3813 S22:  -0.5868 S23:   0.4293                       
REMARK   3      S31:   0.7645 S32:  -0.9096 S33:   0.8159                       
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): 113.6490   3.6330  79.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0745 T22:  -0.2220                                     
REMARK   3      T33:  -0.0559 T12:   0.0157                                     
REMARK   3      T13:   0.0675 T23:   0.2146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0515 L22:   3.2838                                     
REMARK   3      L33:   2.6375 L12:  -0.1103                                     
REMARK   3      L13:  -0.1449 L23:   0.3975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0857 S12:  -0.0342 S13:  -0.3666                       
REMARK   3      S21:  -0.1005 S22:  -0.1327 S23:  -0.2389                       
REMARK   3      S31:   0.5976 S32:   0.2294 S33:   0.2183                       
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): 124.5070   7.6770  80.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0093 T22:  -0.0388                                     
REMARK   3      T33:  -0.0030 T12:   0.1191                                     
REMARK   3      T13:   0.0202 T23:   0.2936                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3363 L22:   2.7976                                     
REMARK   3      L33:   2.4300 L12:   0.1782                                     
REMARK   3      L13:  -0.6420 L23:  -0.1394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1123 S12:  -0.2174 S13:  -0.4054                       
REMARK   3      S21:   0.2705 S22:  -0.2252 S23:  -0.4257                       
REMARK   3      S31:   0.6046 S32:   0.6174 S33:   0.3375                       
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): 113.8000  17.0360 172.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4486 T22:  -0.4309                                     
REMARK   3      T33:  -0.2413 T12:   0.0164                                     
REMARK   3      T13:  -0.3453 T23:  -0.0931                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2350 L22:  14.3805                                     
REMARK   3      L33:   5.1649 L12:  -2.3156                                     
REMARK   3      L13:   3.9937 L23:  -1.2521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1259 S12:  -0.1970 S13:  -0.0384                       
REMARK   3      S21:   1.4073 S22:   0.3054 S23:  -0.6692                       
REMARK   3      S31:  -0.2736 S32:   0.2443 S33:  -0.1795                       
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): 102.3200  23.4350 167.4900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7302 T22:  -0.0102                                     
REMARK   3      T33:  -0.3091 T12:   0.2532                                     
REMARK   3      T13:  -0.0327 T23:  -0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2746 L22:   2.0407                                     
REMARK   3      L33:   2.2909 L12:  -0.8174                                     
REMARK   3      L13:   1.7191 L23:  -0.6076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2260 S12:  -0.8079 S13:  -0.0066                       
REMARK   3      S21:   0.9678 S22:   0.5002 S23:  -0.0709                       
REMARK   3      S31:  -1.2238 S32:  -1.5571 S33:  -0.2742                       
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): 102.3010  29.9010 148.3970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5258 T22:  -0.0713                                     
REMARK   3      T33:  -0.3133 T12:   0.1662                                     
REMARK   3      T13:   0.0410 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2655 L22:   7.6482                                     
REMARK   3      L33:  36.7959 L12:  -2.8276                                     
REMARK   3      L13:  16.7047 L23: -10.2179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0577 S12:  -0.6040 S13:   0.5160                       
REMARK   3      S21:   1.3068 S22:   0.4407 S23:  -0.3001                       
REMARK   3      S31:  -3.3040 S32:  -1.3657 S33:   0.6170                       
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):  93.9350  37.0550 108.0790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2543 T22:  -0.0724                                     
REMARK   3      T33:  -0.1020 T12:  -0.2006                                     
REMARK   3      T13:   0.0686 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1865 L22:   0.6094                                     
REMARK   3      L33:   5.4983 L12:  -0.7332                                     
REMARK   3      L13:   0.7916 L23:  -1.3706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1074 S12:  -0.1572 S13:   0.0511                       
REMARK   3      S21:   0.4877 S22:  -0.0865 S23:   0.0445                       
REMARK   3      S31:  -0.4282 S32:   0.1160 S33:   0.1940                       
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): 101.2600  43.1150  94.8760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1063 T22:  -0.1225                                     
REMARK   3      T33:  -0.1318 T12:  -0.1774                                     
REMARK   3      T13:   0.0201 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2960 L22:   0.9821                                     
REMARK   3      L33:   4.6923 L12:   0.0436                                     
REMARK   3      L13:  -1.5197 L23:  -0.5624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1561 S12:  -0.1548 S13:   0.1829                       
REMARK   3      S21:   0.4261 S22:  -0.0306 S23:  -0.0659                       
REMARK   3      S31:  -0.5996 S32:   0.2147 S33:  -0.1255                       
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): 102.4620  31.5100  97.1020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0491 T22:  -0.0650                                     
REMARK   3      T33:  -0.1562 T12:  -0.1644                                     
REMARK   3      T13:  -0.0101 T23:   0.0660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5493 L22:   1.8464                                     
REMARK   3      L33:   2.0068 L12:  -0.5912                                     
REMARK   3      L13:  -0.8140 L23:   0.1812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0193 S12:  -0.3055 S13:   0.0652                       
REMARK   3      S21:   0.4279 S22:  -0.0598 S23:  -0.0981                       
REMARK   3      S31:   0.0238 S32:   0.2493 S33:   0.0791                       
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): 101.5280  21.6940 133.0120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2288 T22:  -0.1804                                     
REMARK   3      T33:  -0.2087 T12:  -0.0399                                     
REMARK   3      T13:   0.0243 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8048 L22:   2.5615                                     
REMARK   3      L33:  19.7061 L12:  -1.6337                                     
REMARK   3      L13:   6.6871 L23:  -4.2707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7710 S12:   0.5888 S13:  -0.4580                       
REMARK   3      S21:  -0.3756 S22:   0.0546 S23:  -0.1430                       
REMARK   3      S31:   1.5450 S32:   0.9774 S33:  -0.8256                       
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): 108.4880  28.4820 149.8610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4416 T22:  -0.3811                                     
REMARK   3      T33:  -0.2293 T12:  -0.0648                                     
REMARK   3      T13:  -0.0475 T23:   0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3091 L22:   1.7811                                     
REMARK   3      L33:  16.7006 L12:  -0.6451                                     
REMARK   3      L13:   5.0743 L23:  -0.9941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2339 S12:   0.4819 S13:   0.1202                       
REMARK   3      S21:   0.6757 S22:   0.3232 S23:  -0.3835                       
REMARK   3      S31:  -1.7264 S32:   0.9200 S33:  -0.0893                       
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): 119.6940  30.8980 184.5140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7696 T22:   1.0824                                     
REMARK   3      T33:   0.6805 T12:  -0.3199                                     
REMARK   3      T13:  -0.6514 T23:  -0.0787                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4814 L22:  12.9537                                     
REMARK   3      L33:   5.8462 L12:  -8.7206                                     
REMARK   3      L13:   5.7023 L23:  -8.6783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4790 S12:  -0.3372 S13:   0.7357                       
REMARK   3      S21:   2.5891 S22:  -0.9301 S23:  -2.9384                       
REMARK   3      S31:  -0.4542 S32:   3.0396 S33:   1.4091                       
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):  89.7040  36.1840  37.9770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1584 T22:  -0.0427                                     
REMARK   3      T33:  -0.0594 T12:  -0.1632                                     
REMARK   3      T13:  -0.0325 T23:   0.0509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2129 L22:   6.5952                                     
REMARK   3      L33:   6.4030 L12:  -3.7054                                     
REMARK   3      L13:   3.2611 L23:  -3.7758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1135 S12:   0.2041 S13:  -0.4749                       
REMARK   3      S21:  -0.1797 S22:   0.0011 S23:   0.2137                       
REMARK   3      S31:   0.6590 S32:  -0.1045 S33:  -0.1146                       
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):  93.5980  43.8570  41.0650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1500 T22:  -0.0201                                     
REMARK   3      T33:  -0.0549 T12:  -0.0551                                     
REMARK   3      T13:  -0.0069 T23:   0.0745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5888 L22:   0.5146                                     
REMARK   3      L33:   2.9964 L12:  -0.2564                                     
REMARK   3      L13:   0.8972 L23:  -0.7348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0770 S12:   0.0424 S13:   0.0811                       
REMARK   3      S21:  -0.0244 S22:   0.0011 S23:   0.0408                       
REMARK   3      S31:   0.1133 S32:  -0.1712 S33:   0.0759                       
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):  91.7810  46.9000   5.7420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1853 T22:  -0.1288                                     
REMARK   3      T33:  -0.1833 T12:   0.0971                                     
REMARK   3      T13:  -0.0786 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6097 L22:   2.1076                                     
REMARK   3      L33:  10.5564 L12:  -0.0641                                     
REMARK   3      L13:  -1.3610 L23:  -0.1894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2233 S12:   0.0699 S13:  -0.2752                       
REMARK   3      S21:  -0.2555 S22:  -0.0670 S23:   0.0416                       
REMARK   3      S31:   0.7554 S32:  -0.1287 S33:  -0.1563                       
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):  90.7430  42.4610  -2.8470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1559 T22:  -0.0254                                     
REMARK   3      T33:  -0.1917 T12:   0.1211                                     
REMARK   3      T13:  -0.1144 T23:  -0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3754 L22:   2.3729                                     
REMARK   3      L33:   9.1575 L12:  -0.2426                                     
REMARK   3      L13:  -3.2760 L23:   1.4832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0017 S12:   0.4591 S13:  -0.8232                       
REMARK   3      S21:  -0.9248 S22:  -0.2149 S23:   0.1839                       
REMARK   3      S31:   1.3992 S32:   0.0136 S33:   0.2166                       
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): 112.9200  45.4330  35.3160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1527 T22:  -0.0198                                     
REMARK   3      T33:  -0.0507 T12:   0.0129                                     
REMARK   3      T13:  -0.0032 T23:   0.1030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8916 L22:   0.8321                                     
REMARK   3      L33:   3.1132 L12:   0.4356                                     
REMARK   3      L13:  -0.6627 L23:  -0.2977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0485 S12:   0.3396 S13:   0.0734                       
REMARK   3      S21:  -0.1143 S22:   0.0269 S23:  -0.0932                       
REMARK   3      S31:   0.1940 S32:  -0.0075 S33:  -0.0753                       
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):  99.5950  57.8730   5.3460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2398 T22:   0.1780                                     
REMARK   3      T33:  -0.2300 T12:   0.0632                                     
REMARK   3      T13:   0.0286 T23:   0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8024 L22:   4.6700                                     
REMARK   3      L33:   4.5960 L12:  -3.8360                                     
REMARK   3      L13:   3.5112 L23:  -3.0959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1552 S12:   0.1478 S13:   0.3314                       
REMARK   3      S21:  -0.1327 S22:  -0.2888 S23:  -0.2126                       
REMARK   3      S31:   0.2817 S32:   0.4145 S33:   0.1335                       
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):  95.9170  57.1970   5.4750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2553 T22:   0.0716                                     
REMARK   3      T33:  -0.2129 T12:   0.0159                                     
REMARK   3      T13:  -0.0046 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1771 L22:   4.3622                                     
REMARK   3      L33:   4.8740 L12:  -4.0231                                     
REMARK   3      L13:   3.0620 L23:  -2.4983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0387 S12:   0.0186 S13:  -0.2004                       
REMARK   3      S21:  -0.1131 S22:   0.0112 S23:   0.1335                       
REMARK   3      S31:   0.0200 S32:   0.1143 S33:  -0.0499                       
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): 102.6440  62.6170  -1.3920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1754 T22:   0.2033                                     
REMARK   3      T33:  -0.1359 T12:   0.1658                                     
REMARK   3      T13:   0.0558 T23:   0.1594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4686 L22:   4.4340                                     
REMARK   3      L33:   9.1253 L12:  -5.5279                                     
REMARK   3      L13:   7.4256 L23:  -5.0830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4608 S12:   1.3891 S13:  -0.0285                       
REMARK   3      S21:  -0.4251 S22:  -0.6294 S23:  -0.4311                       
REMARK   3      S31:  -0.0613 S32:   1.0102 S33:   0.1686                       
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 2VDQ 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-34087.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07223                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM (SBC2 3K)                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 416764                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6                                  
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM            
REMARK 280  ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.71133            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.85567            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.85567            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.71133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.3 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     HIS C   400                                                      
REMARK 465     HIS C   401                                                      
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  4142     O    HOH A  4314              2.18            
REMARK 500   O    HOH B  4165     O    HOH A  4278              1.88            
REMARK 500   O    HOH L  4014     O    HOH H  4078              2.11            
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     -125.76     49.72                                   
REMARK 500    LYS A 118     -123.27     51.84                                   
REMARK 500    GLU A 123      135.55     99.31                                   
REMARK 500    LEU A 212      -46.13     72.93                                   
REMARK 500    THR A 296      140.06   -170.58                                   
REMARK 500    PRO A 337       44.63    -83.60                                   
REMARK 500    THR B   7       35.71    -97.31                                   
REMARK 500    PHE B  56       81.80   -156.64                                   
REMARK 500    ASP B  71     -159.68   -122.94                                   
REMARK 500    VAL B  80      104.38     68.02                                   
REMARK 500    VAL B 157      -83.91   -124.12                                   
REMARK 500    SER B 213     -154.40   -110.90                                   
REMARK 500    LEU B 258      -15.36     88.12                                   
REMARK 500    VAL B 275      -86.25    -88.22                                   
REMARK 500    LYS B 410      -27.77     71.05                                   
REMARK 500    HIS B 446      -60.00     70.22                                   
REMARK 500    THR B 454      154.18     68.38                                   
REMARK 500    VAL H 133     -156.65    -76.82                                   
REMARK 500    ASP H 179      -12.92     77.12                                   
REMARK 500    SER L  30       57.58     28.03                                   
REMARK 500    SER L  77       79.43     67.13                                   
REMARK 500    ASN L 212       80.57     50.95                                   
REMARK 500    GLU L 213       90.84   -164.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  51.3                                              
REMARK 620 3 ASP A 245   OD2 121.5  70.9                                        
REMARK 620 4 ASP A 247   O    76.2  78.1  84.5                                  
REMARK 620 5 THR A 250   C    92.6 143.1 141.0  86.3                            
REMARK 620 6 THR A 250   O    72.0 122.5 156.5  80.4  20.7                      
REMARK 620 7 THR A 250   OG1 137.9 137.4  79.1  69.4  62.2  78.8                
REMARK 620 8 GLU A 252   OE1  89.9  79.0  87.4 157.1 112.9 113.0 129.9          
REMARK 620 9 GLU A 252   OE2 132.9 129.3  88.8 147.4  79.1  94.3  78.0  53.4    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  78.5                                              
REMARK 620 3 ASP A 297   OD1  82.3  78.4                                        
REMARK 620 4 ARG A 303   O   160.1  89.5  79.8                                  
REMARK 620 5 ASP A 305   OD1 117.3 148.0 128.8  81.0                            
REMARK 620 6 ASP A 305   OD2  90.9 161.5  85.2  96.1  50.5                      
REMARK 620 7 HOH A4359   O    94.5  83.1 161.5  99.8  68.8 113.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 369   OD1  79.3                                              
REMARK 620 3 TYR A 371   O    73.2  81.7                                        
REMARK 620 4 ASP A 367   OD1  90.9  92.5 163.8                                  
REMARK 620 5 HOH A4391   O   145.5  69.4  88.0 104.2                            
REMARK 620 6 ASP A 373   OD1  94.7 173.9  97.5  86.5 116.6                      
REMARK 620 7 ASP A 373   OD2 130.8 135.8  79.1 114.7  70.4  49.5                
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  89.7                                              
REMARK 620 3 ASP A 426   OD1  80.3  89.2                                        
REMARK 620 4 ASP A 428   OD1 158.0  92.4  77.9                                  
REMARK 620 5 ASP A 434   OD1  98.3 170.9  87.9  78.6                            
REMARK 620 6 ASP A 434   OD2  82.3 136.7 130.5 110.4  49.6                      
REMARK 620 7 HOH A4436   O   130.8  86.2 148.5  71.2  91.7  68.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1462   C2                                                     
REMARK 620 2 GOL B1462   O2   27.9                                              
REMARK 620 3 HOH C4013   O   101.0  79.5                                        
REMARK 620 4 ASP B 251   OD2 105.4 127.2 101.0                                  
REMARK 620 5 GOL B1462   O1   48.9  58.2  75.0  70.8                            
REMARK 620 6 SER B 123   O   177.6 150.0  78.2  77.0 132.6                      
REMARK 620 7 ASP B 126   OD1 106.5  86.6  83.5 146.2 141.2  71.2                
REMARK 620 8 ASP B 127   OD1  82.1  99.8 168.8  88.4 114.3  98.3  85.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1  98.2                                              
REMARK 620 3 ASP B 217   O   165.7  92.4                                        
REMARK 620 4 ASP B 217   OD1  92.5  96.1  76.7                                  
REMARK 620 5 PRO B 219   O    83.9 166.3  88.2  97.3                            
REMARK 620 6 GLU B 220   OE2 101.9  79.7  89.4 165.4  86.6                      
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 B4148   O                                                      
REMARK 620 2 SER B 123   OG   94.7                                              
REMARK 620 3 GLU B 220   OE1  88.2 175.4                                        
REMARK 620 4 HOH B4057   O    94.3  83.2 100.2                                  
REMARK 620 5 ASP C 410   OD1  95.1  86.1  90.1 166.3                            
REMARK 620 6 SER B 121   OG  172.4  90.6  86.8  81.0  90.6                      
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: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514. 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  2VDQ A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDQ B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDQ H    1   221  PDB    2VDQ     2VDQ             1    221             
DBREF  2VDQ L    1   214  PDB    2VDQ     2VDQ             1    214             
DBREF  2VDQ C  400   411  UNP    Q53Y18   Q53Y18_HUMAN   426    437             
SEQADV 2VDQ GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQADV 2VDQ ARG C  408  UNP  Q53Y18    ALA   434 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   12  HIS HIS 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   *1332(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  439  5                                   5    
HELIX   21  21 ASN H   28  THR H   32  5                                   5    
HELIX   22  22 PRO H   62  PHE H   64  5                                   3    
HELIX   23  23 THR H   87  THR H   91  5                                   5    
HELIX   24  24 SER H  162  SER H  164  5                                   3    
HELIX   25  25 PRO H  206  SER H  209  5                                   4    
HELIX   26  26 ASP L   79  PHE L   83  5                                   5    
HELIX   27  27 SER L  121  GLY L  128  1                                   8    
HELIX   28  28 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 3 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 3 VAL A  33  GLY A  38 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 3 VAL A  53  PRO A  57 -1  O  PHE A  54   N  VAL A  37           
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  VAL B 310  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 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  ARG L 155  0                                        
SHEET    2  LE 4 ASN L 145  ILE L 150 -1  O  TRP L 148   N  ARG L 155           
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  2.03  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.08  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.05  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.05  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.09  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.07  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.05  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.04  
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  2.04  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.04  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.11  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.45  
LINK         ND2 ASN A 249                 C1  NAG A3249     1555   1555  1.45  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.32  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.47  
LINK        CA    CA A2004                 C   THR A 250     1555   1555  3.14  
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  2.40  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.48  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.46  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.61  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.27  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.40  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.56  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.58  
LINK        CA    CA A2005                 O   HOH A4359     1555   1555  2.22  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.47  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.26  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.36  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.26  
LINK        CA    CA A2006                 O   HOH A4391     1555   1555  2.29  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.62  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.62  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.49  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.58  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.27  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.67  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.54  
LINK        CA    CA A2007                 O   HOH A4436     1555   1555  2.22  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.27  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.17  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.43  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.43  
LINK        MG    MG B2001                 O   HOH B4057     1555   1555  2.27  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.06  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.27  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.18  
LINK        MG    MG B2001                 OD1 ASP C 410     1555   1555  2.12  
LINK        MG    MG B2001                 O   HOH B4148     1555   1555  2.27  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.24  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.32  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.46  
LINK        CA    CA B2002                 O1  GOL B1462     1555   1555  2.71  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.26  
LINK        CA    CA B2002                 O   HOH C4013     1555   1555  2.28  
LINK        CA    CA B2002                 O2  GOL B1462     1555   1555  2.83  
LINK        CA    CA B2002                 C2  GOL B1462     1555   1555  2.98  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.32  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.29  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.22  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.38  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.25  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.32  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.43  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.45  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
LINK         O3  MAN B3373                 C1  MAN B3374     1555   1555  1.44  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.44  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0        -2.76                     
CISPEP   2 SER B  162    PRO B  163          0         6.28                     
CISPEP   3 SER B  168    PRO B  169          0        -8.97                     
CISPEP   4 PHE H  152    PRO H  153          0        -4.67                     
CISPEP   5 GLU H  154    PRO H  155          0         1.78                     
CISPEP   6 TRP H  194    PRO H  195          0         3.81                     
CISPEP   7 SER L    7    PRO L    8          0        -7.18                     
CISPEP   8 LEU L   94    PRO L   95          0        -3.91                     
CISPEP   9 TYR L  140    PRO L  141          0         3.22                     
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 A4359                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4391                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4436                                          
SITE     1 AC5  2 ASN A  15  HOH A4454                                          
SITE     1 AC6  2 ASN A 249  HOH A4455                                          
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  HOH B4057                    
SITE     2 AC7  6 HOH B4148  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 C4013                                          
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  7 ASN B  99  SER B 398  NAG B3371  HOH B4309                    
SITE     2 BC1  7 HOH B4310  HOH B4311  HOH B4322                               
SITE     1 BC2  9 MET A 285  LEU B 317  ASN B 320  NAG B3321                    
SITE     2 BC2  9 HOH B4312  HOH B4313  HOH B4314  HOH B4315                    
SITE     3 BC2  9 HOH B4316                                                     
SITE     1 BC3  7 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     2 BC3  7 HOH B4316  HOH B4317  HOH B4318                               
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  4 ARG A 281  MAN B3322  HOH B4319  HOH B4320                    
SITE     1 BC6  3 NAG B3321  MAN B3322  HOH B4321                               
SITE     1 BC7  7 ASN B 371  SER B 398  GLU B 400  NAG B3099                    
SITE     2 BC7  7 NAG B3372  HOH B4322  HOH B4323                               
SITE     1 BC8  5 NAG B3371  MAN B3373  MAN B3376  HOH B4323                    
SITE     2 BC8  5 HOH B4325                                                     
SITE     1 BC9  7 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  7 MAN B3375  HOH B4326  HOH B4328                               
SITE     1 CC1  6 ASN A 299  LEU A 332  SER A 396  GLU A 397                    
SITE     2 CC1  6 MAN B3373  HOH B4329                                          
SITE     1 CC2  6 ALA A 342  PRO A 343  MAN B3373  MAN B3376                    
SITE     2 CC2  6 MAN B3377  HOH B4330                                          
SITE     1 CC3  7 PRO A 343  SER A 344  LEU A 346  NAG B3372                    
SITE     2 CC3  7 MAN B3375  HOH B4334  HOH B4335                               
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  5 ARG A  90  HOH A4126  HOH A4172  HOH A4452                    
SITE     2 CC5  5 HOH A4453                                                     
SITE     1 CC6  9 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 CC6  9  CA B2002  HOH B4306  HOH B4307  HOH C4013                    
SITE     3 CC6  9 HOH H4028                                                     
CRYST1  148.331  148.331  176.567  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006742  0.003892  0.000000        0.00000                         
SCALE2      0.000000  0.007785  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005664        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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