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Entry: 2VDL
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HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDL              
TITLE     RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3 HEADPIECE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HEADPIECE, RESIDUES 32-483;                                
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6  INTEGRIN ALPHA-IIB HEAVY CHAIN;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: HEADPIECE, RESIDUES 27-487;                                
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  16 CHAIN: H;                                                            
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  19 CHAIN: L                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  19 ORGANISM_COMMON: MOUSE;                                              
SOURCE  20 ORGANISM_TAXID: 10090;                                               
SOURCE  21 STRAIN: BALB/C;                                                      
SOURCE  22 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: MOUSE;                                              
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 STRAIN: BALB/C;                                                      
SOURCE  28 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, PLATELET     
KEYWDS   2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,       
KEYWDS   3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE  
KEYWDS   4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,   
KEYWDS   5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM      
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDL    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDL    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDL    0                                                
SPRSDE     02-SEP-08 2VDL      1TXV                                             
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.    2.75 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) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 53440                          
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2856                            
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) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3521                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10461                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 210                                     
REMARK   3   SOLVENT ATOMS            : 1129                                    
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) : 36.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.26000                                              
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.89000                                             
REMARK   3    B12 (A**2) : 0.63000                                              
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): 0.562         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.256         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.167         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.066        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10960 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7349 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14972 ; 0.997 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17890 ; 0.767 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1384 ; 5.498 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   476 ;32.846 ;24.286       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1725 ;12.280 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    61 ;14.624 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1686 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12214 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2166 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2133 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7843 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5316 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5753 ; 0.079 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   940 ; 0.135 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    22 ; 0.114 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    87 ; 0.172 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    37 ; 0.109 ; 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):  7018 ; 1.611 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10945 ; 2.584 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4585 ; 1.593 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4008 ; 2.497 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    17                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.4480  12.4440  78.2360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1756 T22:   0.0682                                     
REMARK   3      T33:  -0.0983 T12:   0.1333                                     
REMARK   3      T13:  -0.0017 T23:   0.3306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2770 L22:   3.4378                                     
REMARK   3      L33:   5.5052 L12:  -3.1666                                     
REMARK   3      L13:   0.3709 L23:  -3.0986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:   0.1942 S13:  -0.4221                       
REMARK   3      S21:   0.4774 S22:  -0.4391 S23:  -1.3105                       
REMARK   3      S31:   0.9249 S32:   0.9499 S33:   0.4564                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A    62                          
REMARK   3    ORIGIN FOR THE GROUP (A): 129.4650  22.0450  68.8660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1885 T22:   0.0341                                     
REMARK   3      T33:  -0.0784 T12:   0.0526                                     
REMARK   3      T13:   0.0168 T23:   0.2750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2149 L22:   3.7111                                     
REMARK   3      L33:   2.9137 L12:   0.5069                                     
REMARK   3      L13:  -0.6259 L23:   0.5182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:  -0.1233 S13:  -0.2335                       
REMARK   3      S21:  -0.1148 S22:  -0.1989 S23:  -0.4937                       
REMARK   3      S31:   0.2182 S32:   0.3432 S33:   0.2658                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    63        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 118.9410  33.7800  64.2700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1263 T22:   0.0134                                     
REMARK   3      T33:  -0.0020 T12:  -0.0584                                     
REMARK   3      T13:  -0.0334 T23:   0.1512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6496 L22:   1.4775                                     
REMARK   3      L33:   1.5406 L12:  -0.4853                                     
REMARK   3      L13:  -0.5024 L23:  -0.4728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0197 S12:  -0.1339 S13:  -0.0201                       
REMARK   3      S21:   0.1673 S22:  -0.1461 S23:  -0.3157                       
REMARK   3      S31:  -0.0122 S32:   0.4246 S33:   0.1658                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   116        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.3550  36.2950  63.5570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1032 T22:  -0.0462                                     
REMARK   3      T33:  -0.1024 T12:  -0.0794                                     
REMARK   3      T13:  -0.0429 T23:   0.0956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8324 L22:   1.7169                                     
REMARK   3      L33:   2.8825 L12:  -0.2806                                     
REMARK   3      L13:  -1.7908 L23:  -0.0730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0556 S12:  -0.0854 S13:  -0.2132                       
REMARK   3      S21:  -0.0749 S22:  -0.2028 S23:   0.2063                       
REMARK   3      S31:  -0.0167 S32:  -0.0226 S33:   0.1472                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   168        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.3390  24.6580  63.8120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0658 T22:  -0.0549                                     
REMARK   3      T33:  -0.0443 T12:  -0.0636                                     
REMARK   3      T13:  -0.0055 T23:   0.0767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2883 L22:   1.4837                                     
REMARK   3      L33:   1.3090 L12:  -0.0540                                     
REMARK   3      L13:  -0.7534 L23:  -0.5347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:   0.1658 S13:  -0.0821                       
REMARK   3      S21:   0.0048 S22:  -0.0978 S23:  -0.0382                       
REMARK   3      S31:   0.2894 S32:  -0.1506 S33:   0.0873                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   290                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.0560  13.2450  72.1500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0254 T22:  -0.1757                                     
REMARK   3      T33:  -0.0391 T12:  -0.1106                                     
REMARK   3      T13:   0.0759 T23:   0.0736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2491 L22:   2.6851                                     
REMARK   3      L33:   3.5651 L12:  -0.1755                                     
REMARK   3      L13:  -0.3379 L23:   0.5707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0595 S12:   0.1045 S13:  -0.2600                       
REMARK   3      S21:  -0.0256 S22:  -0.1517 S23:   0.1196                       
REMARK   3      S31:   0.2357 S32:  -0.2381 S33:   0.2111                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   291        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A): 108.1080   7.2930  84.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0276 T22:  -0.3071                                     
REMARK   3      T33:  -0.0622 T12:  -0.0640                                     
REMARK   3      T13:   0.0861 T23:   0.2221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8946 L22:   6.2146                                     
REMARK   3      L33:   7.3394 L12:  -0.2963                                     
REMARK   3      L13:  -0.9735 L23:   3.4506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1523 S12:  -0.2746 S13:  -0.4420                       
REMARK   3      S21:   0.4741 S22:   0.0389 S23:   0.1051                       
REMARK   3      S31:   0.7217 S32:   0.1704 S33:   0.1134                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   327        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A): 110.6780   2.9350  78.3060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1013 T22:  -0.2549                                     
REMARK   3      T33:  -0.1025 T12:   0.0026                                     
REMARK   3      T13:   0.0765 T23:   0.1982                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8336 L22:   3.8076                                     
REMARK   3      L33:   3.8208 L12:  -0.4342                                     
REMARK   3      L13:  -0.8807 L23:   1.9030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1510 S12:   0.1308 S13:  -0.2462                       
REMARK   3      S21:  -0.0649 S22:  -0.2816 S23:  -0.0141                       
REMARK   3      S31:   0.7446 S32:   0.1146 S33:   0.4326                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   373        A   452                          
REMARK   3    ORIGIN FOR THE GROUP (A): 124.6960   7.6970  79.9100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0191 T22:  -0.1026                                     
REMARK   3      T33:  -0.0076 T12:   0.1149                                     
REMARK   3      T13:   0.0303 T23:   0.2968                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5948 L22:   2.5703                                     
REMARK   3      L33:   2.7992 L12:   0.1463                                     
REMARK   3      L13:  -0.3990 L23:  -0.0499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0165 S12:  -0.1946 S13:  -0.4404                       
REMARK   3      S21:   0.2131 S22:  -0.3230 S23:  -0.4663                       
REMARK   3      S31:   0.5102 S32:   0.6137 S33:   0.3395                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    72                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.8630  21.1360 169.0610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4710 T22:  -0.4175                                     
REMARK   3      T33:  -0.3736 T12:   0.0598                                     
REMARK   3      T13:  -0.1659 T23:  -0.0937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0997 L22:   3.3231                                     
REMARK   3      L33:   7.8111 L12:  -2.1837                                     
REMARK   3      L13:   2.6257 L23:  -2.9229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2156 S12:  -0.7802 S13:  -0.0129                       
REMARK   3      S21:   1.0421 S22:   0.4400 S23:  -0.2005                       
REMARK   3      S31:  -0.9491 S32:  -0.7747 S33:  -0.2244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    78        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.1230  30.1390 148.9770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7139 T22:  -0.1714                                     
REMARK   3      T33:  -0.2518 T12:   0.2049                                     
REMARK   3      T13:  -0.0194 T23:  -0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8554 L22:   7.2095                                     
REMARK   3      L33:  38.2042 L12:  -4.4166                                     
REMARK   3      L13:  16.5641 L23: -14.7858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8453 S12:  -0.6184 S13:   0.6063                       
REMARK   3      S21:   1.1989 S22:   0.3624 S23:  -0.5616                       
REMARK   3      S31:  -2.9152 S32:  -1.5318 S33:   0.4828                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    99        B   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  97.6850  38.2560 104.2300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1644 T22:  -0.0596                                     
REMARK   3      T33:  -0.1239 T12:  -0.1686                                     
REMARK   3      T13:   0.0413 T23:   0.0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5255 L22:   0.5307                                     
REMARK   3      L33:   2.8991 L12:  -0.0459                                     
REMARK   3      L13:  -0.4335 L23:  -1.1191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0017 S12:  -0.1184 S13:   0.0116                       
REMARK   3      S21:   0.3632 S22:  -0.0205 S23:   0.0084                       
REMARK   3      S31:  -0.4546 S32:   0.0937 S33:   0.0188                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   173        B   338                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.2000  34.3920  95.9580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0055 T22:  -0.0804                                     
REMARK   3      T33:  -0.1513 T12:  -0.1414                                     
REMARK   3      T13:  -0.0070 T23:   0.0843                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7190 L22:   1.4292                                     
REMARK   3      L33:   1.9033 L12:  -0.2640                                     
REMARK   3      L13:  -0.9250 L23:   0.0035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0167 S12:  -0.2567 S13:  -0.0075                       
REMARK   3      S21:   0.3687 S22:  -0.0968 S23:  -0.1372                       
REMARK   3      S31:  -0.0556 S32:   0.1618 S33:   0.0801                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   339        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.3770  22.6130 130.7940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1440 T22:  -0.1938                                     
REMARK   3      T33:  -0.1672 T12:  -0.0449                                     
REMARK   3      T13:   0.0628 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8352 L22:   3.2159                                     
REMARK   3      L33:  21.5841 L12:  -2.0142                                     
REMARK   3      L13:   7.8112 L23:  -5.2121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6442 S12:   0.4442 S13:  -0.4782                       
REMARK   3      S21:  -0.2629 S22:   0.1397 S23:  -0.0388                       
REMARK   3      S31:   1.5513 S32:   0.4544 S33:  -0.7839                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   394        B   437                          
REMARK   3    ORIGIN FOR THE GROUP (A): 109.5360  28.1050 148.9570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3224 T22:  -0.4391                                     
REMARK   3      T33:  -0.2543 T12:  -0.1263                                     
REMARK   3      T13:  -0.0445 T23:   0.0600                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6347 L22:   2.3749                                     
REMARK   3      L33:  21.3191 L12:  -1.6700                                     
REMARK   3      L13:   7.3714 L23:  -1.4969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2175 S12:   0.6241 S13:   0.2653                       
REMARK   3      S21:   0.8418 S22:   0.3000 S23:  -0.5600                       
REMARK   3      S31:  -1.6418 S32:   1.3732 S33:  -0.0825                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   438        B   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): 119.4190  31.2240 182.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8950 T22:   1.2423                                     
REMARK   3      T33:   1.0367 T12:  -0.0741                                     
REMARK   3      T13:  -0.7764 T23:  -0.2894                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3997 L22:   1.9223                                     
REMARK   3      L33:   7.1076 L12:   0.8765                                     
REMARK   3      L13:  -1.6854 L23:  -3.6963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0493 S12:  -2.5590 S13:   1.5405                       
REMARK   3      S21:  -0.0851 S22:  -0.2903 S23:  -0.5016                       
REMARK   3      S31:  -1.6858 S32:   3.4624 S33:   0.2410                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H    13                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.0950  36.8750  33.2610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0455 T22:  -0.0111                                     
REMARK   3      T33:  -0.0442 T12:  -0.2050                                     
REMARK   3      T13:  -0.0025 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3653 L22:   7.9854                                     
REMARK   3      L33:  10.6333 L12:  -6.4844                                     
REMARK   3      L13:   7.7869 L23:  -6.5637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4278 S12:   0.2920 S13:  -0.8284                       
REMARK   3      S21:  -0.9524 S22:   0.0172 S23:   0.3480                       
REMARK   3      S31:   0.9204 S32:  -0.0049 S33:  -0.4450                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    14        H    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  94.2650  42.2440  41.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1646 T22:  -0.0201                                     
REMARK   3      T33:  -0.0857 T12:  -0.0586                                     
REMARK   3      T13:  -0.0100 T23:   0.0547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0779 L22:   1.6746                                     
REMARK   3      L33:   2.7407 L12:  -0.5306                                     
REMARK   3      L13:   1.5035 L23:  -0.1858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:  -0.1711 S13:  -0.0180                       
REMARK   3      S21:   0.0974 S22:  -0.0130 S23:   0.1166                       
REMARK   3      S31:   0.2336 S32:  -0.1644 S33:   0.0140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    55        H   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):  94.0930  43.1090  43.4950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1560 T22:  -0.0532                                     
REMARK   3      T33:  -0.0198 T12:  -0.0542                                     
REMARK   3      T13:  -0.0028 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0131 L22:   0.4930                                     
REMARK   3      L33:   3.4497 L12:  -0.1166                                     
REMARK   3      L13:   1.0781 L23:  -1.1469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0849 S12:  -0.1109 S13:   0.1063                       
REMARK   3      S21:  -0.0234 S22:   0.0512 S23:   0.0495                       
REMARK   3      S31:   0.1767 S32:  -0.2434 S33:   0.0336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   111        H   134                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.4970  47.8270  12.7870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1988 T22:  -0.0003                                     
REMARK   3      T33:  -0.0634 T12:  -0.0961                                     
REMARK   3      T13:  -0.0877 T23:   0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3774 L22:   0.6648                                     
REMARK   3      L33:   5.0433 L12:  -0.7257                                     
REMARK   3      L13:  -1.0720 L23:   0.7615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1390 S12:   0.3391 S13:  -0.1471                       
REMARK   3      S21:  -0.1606 S22:  -0.0248 S23:   0.1003                       
REMARK   3      S31:  -0.3052 S32:  -0.7344 S33:  -0.1142                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   137        H   164                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.5960  44.8960   4.7390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1549 T22:  -0.1581                                     
REMARK   3      T33:  -0.1652 T12:   0.0344                                     
REMARK   3      T13:  -0.0791 T23:  -0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1228 L22:   1.1577                                     
REMARK   3      L33:  12.1449 L12:  -1.4310                                     
REMARK   3      L13:  -4.5295 L23:   1.9535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1123 S12:   0.2144 S13:  -0.4454                       
REMARK   3      S21:  -0.2062 S22:  -0.0823 S23:  -0.0984                       
REMARK   3      S31:   1.2922 S32:  -0.0178 S33:  -0.0300                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   165        H   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  94.6030  47.6800   9.2620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2097 T22:  -0.1947                                     
REMARK   3      T33:  -0.2593 T12:   0.0968                                     
REMARK   3      T13:  -0.0594 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9767 L22:   2.0551                                     
REMARK   3      L33:  11.7254 L12:   1.3117                                     
REMARK   3      L13:  -1.7022 L23:  -1.8286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4007 S12:  -0.0964 S13:   0.3780                       
REMARK   3      S21:  -0.5129 S22:  -0.0404 S23:   0.0403                       
REMARK   3      S31:   0.5116 S32:   0.2411 S33:  -0.3603                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   190        H   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9970  40.6350  -3.6340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4133 T22:  -0.0060                                     
REMARK   3      T33:  -0.1111 T12:   0.1906                                     
REMARK   3      T13:  -0.0220 T23:  -0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8896 L22:   3.3784                                     
REMARK   3      L33:   5.7450 L12:  -1.2913                                     
REMARK   3      L13:  -0.3663 L23:   2.5541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2515 S12:   0.0875 S13:  -1.3867                       
REMARK   3      S21:  -0.9505 S22:  -0.8000 S23:  -0.1055                       
REMARK   3      S31:   0.4070 S32:   0.6858 S33:   0.5485                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   207        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.2460  44.2590  -2.4320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0256 T22:   0.1195                                     
REMARK   3      T33:  -0.1362 T12:  -0.0089                                     
REMARK   3      T13:  -0.2839 T23:  -0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.9065 L22:   5.8130                                     
REMARK   3      L33:  17.3841 L12:   6.1813                                     
REMARK   3      L13: -11.5919 L23:  -0.2873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3615 S12:   0.8343 S13:  -0.1730                       
REMARK   3      S21:  -1.3596 S22:   0.5363 S23:   0.8244                       
REMARK   3      S31:   1.7555 S32:  -1.3424 S33:  -0.1748                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L    38                          
REMARK   3    ORIGIN FOR THE GROUP (A): 114.3960  50.3810  35.1590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1629 T22:   0.0070                                     
REMARK   3      T33:   0.0032 T12:   0.0347                                     
REMARK   3      T13:   0.0211 T23:   0.1498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8566 L22:   1.6429                                     
REMARK   3      L33:   2.2684 L12:   0.2974                                     
REMARK   3      L13:  -0.7531 L23:   0.7780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1303 S12:   0.2128 S13:   0.1628                       
REMARK   3      S21:  -0.0587 S22:  -0.0941 S23:  -0.0148                       
REMARK   3      S31:  -0.1025 S32:   0.1427 S33:  -0.0362                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    39        L    69                          
REMARK   3    ORIGIN FOR THE GROUP (A): 113.7230  39.4260  36.2060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1263 T22:  -0.0284                                     
REMARK   3      T33:  -0.0685 T12:   0.0353                                     
REMARK   3      T13:   0.0130 T23:   0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6703 L22:   2.5915                                     
REMARK   3      L33:   2.5238 L12:   0.2058                                     
REMARK   3      L13:  -0.0946 L23:  -1.5106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0693 S12:   0.2481 S13:  -0.4668                       
REMARK   3      S21:  -0.1593 S22:   0.1211 S23:  -0.1745                       
REMARK   3      S31:   0.6021 S32:   0.1664 S33:  -0.1904                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    70        L    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): 112.4860  45.9480  35.6140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1421 T22:  -0.0470                                     
REMARK   3      T33:  -0.0483 T12:  -0.0060                                     
REMARK   3      T13:  -0.0345 T23:   0.0766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4393 L22:   0.8187                                     
REMARK   3      L33:   4.2633 L12:  -0.1322                                     
REMARK   3      L13:  -1.9572 L23:  -0.2816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1780 S12:   0.2907 S13:  -0.1592                       
REMARK   3      S21:  -0.0159 S22:  -0.0523 S23:   0.0379                       
REMARK   3      S31:   0.3042 S32:   0.1331 S33:   0.2303                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    98        L   135                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.4950  53.3550   8.2120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1326 T22:   0.1439                                     
REMARK   3      T33:  -0.0458 T12:   0.0555                                     
REMARK   3      T13:   0.0173 T23:   0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0533 L22:   2.0924                                     
REMARK   3      L33:   6.8677 L12:  -1.6156                                     
REMARK   3      L13:   3.7309 L23:  -2.6660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4332 S12:   0.1455 S13:  -0.3293                       
REMARK   3      S21:  -0.3148 S22:  -0.1380 S23:   0.2364                       
REMARK   3      S31:   0.5271 S32:   0.0949 S33:  -0.2952                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   136        L   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.6350  59.9270   8.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2093 T22:   0.1630                                     
REMARK   3      T33:  -0.1733 T12:   0.0093                                     
REMARK   3      T13:  -0.0147 T23:   0.0464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7331 L22:   6.0580                                     
REMARK   3      L33:   2.1273 L12:  -4.6104                                     
REMARK   3      L13:   2.8185 L23:  -1.5305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1925 S12:  -0.1843 S13:   0.5345                       
REMARK   3      S21:   0.1639 S22:  -0.1165 S23:  -0.2984                       
REMARK   3      S31:  -0.0524 S32:   0.2574 S33:   0.3090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   168        L   197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  95.1990  60.2780   2.9690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2584 T22:   0.0834                                     
REMARK   3      T33:  -0.1815 T12:   0.0245                                     
REMARK   3      T13:   0.0061 T23:   0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9623 L22:   4.9284                                     
REMARK   3      L33:   5.2017 L12:  -4.1842                                     
REMARK   3      L13:   4.0956 L23:  -3.0694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:   0.3875 S13:   0.0694                       
REMARK   3      S21:  -0.3655 S22:  -0.1511 S23:  -0.0314                       
REMARK   3      S31:   0.0575 S32:   0.1447 S33:   0.1078                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   198        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.0350  62.6820  -2.0170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2287 T22:   0.1106                                     
REMARK   3      T33:  -0.2355 T12:   0.1473                                     
REMARK   3      T13:   0.1259 T23:   0.1392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1710 L22:   5.7268                                     
REMARK   3      L33:   6.0140 L12:  -2.2754                                     
REMARK   3      L13:   1.1443 L23:  -3.5125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2111 S12:   1.2002 S13:   0.0786                       
REMARK   3      S21:  -0.3692 S22:  -0.4667 S23:  -0.3222                       
REMARK   3      S31:  -0.1882 S32:   1.0733 S33:   0.2556                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. THESE ARE RE-REFINED COORDINATES OF THE           
REMARK   3  PREVIOUS WWPDB SUBMISSION 1TXV. THE STARTING MODEL WAS A 2.4        
REMARK   3  ANGSTROM STRUCTURE WITH A DIFFERENT BOUND LIGAND. THE MODEL IS      
REMARK   3  REFINED TO LOWER RFREE. ONE SEQUENCE MISTAKE IN THE AIIB            
REMARK   3  SUBUNIT IS CORRECTED. MORE OF BETA SUBUNIT DOMAIN I-EGF1 IS         
REMARK   3  BUILT. MISTAKES IN CARBOHYDRATE ANOMERIC LINKAGES ARE               
REMARK   3  CORRECTED.                                                          
REMARK   4                                                                      
REMARK   4 2VDL 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-34077.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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) : 0.9793                             
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   : 62512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.1                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1JV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.7                      
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      117.59867            
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       58.79933            
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       58.79933            
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      117.59867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 10480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  4058     O    HOH A  4242              2.18            
REMARK 500   O    HOH A  4062     O    HOH A  4064              2.20            
REMARK 500   O    HOH B  4016     O    HOH B  4100              2.18            
REMARK 500   O    HOH L  4038     O    HOH L  4055              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -124.71     50.76                                   
REMARK 500    LYS A 118     -123.59     56.15                                   
REMARK 500    GLU A 123      135.73     98.51                                   
REMARK 500    LEU A 212      -48.01     71.97                                   
REMARK 500    SER A 222     -169.82    -73.60                                   
REMARK 500    SER A 261       71.48     51.07                                   
REMARK 500    THR B   7       48.18    -91.37                                   
REMARK 500    ARG B   8       73.28   -153.66                                   
REMARK 500    VAL B  10       71.36     38.19                                   
REMARK 500    VAL B  80       92.76     62.02                                   
REMARK 500    ASN B 148       33.71    -98.01                                   
REMARK 500    VAL B 157      -82.70   -125.03                                   
REMARK 500    SER B 213     -152.86   -114.62                                   
REMARK 500    LYS B 253      171.22    -54.33                                   
REMARK 500    LEU B 258       -7.91     86.50                                   
REMARK 500    LYS B 410      -20.04     76.49                                   
REMARK 500    GLU B 442       71.85     57.72                                   
REMARK 500    HIS B 446      -63.01     70.27                                   
REMARK 500    THR B 454      145.51     66.75                                   
REMARK 500    ASP H 179       -8.63     67.77                                   
REMARK 500    SER L  30       60.17     30.28                                   
REMARK 500    SER L  43     -159.88    -88.02                                   
REMARK 500    SER L  77       74.13     62.70                                   
REMARK 500    LYS L 169      -65.00    -92.61                                   
REMARK 500    ASN L 212       81.76     54.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CACODYLATE ION (CAC): CACODYLATE IS FOUND IN THE LIGAND              
REMARK 600 BINDING SITE. BASED ON  IMPURITIES IN CACODYLATE AND                 
REMARK 600 HYDROGEN BOND DONORS NEAR THE CACODYLATE, IT IS POSSIBLE             
REMARK 600 THAT ONE OR TWO METHYL GROUPS HAVE BEEN LOST.                        
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                             CAC B1462  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC B1462   C2                                                     
REMARK 620 2 CAC B1462   O1  110.4                                              
REMARK 620 3 CAC B1462   O2  112.1 105.9                                        
REMARK 620 4 CAC B1462   C1  106.7 109.5 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  50.0                                              
REMARK 620 3 ASP A 245   OD2 120.0  70.9                                        
REMARK 620 4 ASP A 247   O    79.5  73.0  93.7                                  
REMARK 620 5 THR A 250   O    69.3 117.3 169.8  83.4                            
REMARK 620 6 THR A 250   OG1 142.5 147.0  92.5  80.2  77.3                      
REMARK 620 7 GLU A 252   OE1  77.1  77.6  82.1 150.1 105.2 129.5                
REMARK 620 8 GLU A 252   OE2 119.3 125.7  85.0 158.8  94.1  78.8  50.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  79.6                                              
REMARK 620 3 ARG A 303   O   164.7  98.9                                        
REMARK 620 4 ASP A 297   OD1  83.2  80.6  81.5                                  
REMARK 620 5 ASP A 305   OD1 104.6 151.7  84.0 127.5                            
REMARK 620 6 ASP A 305   OD2  78.8 154.7  98.5  84.0  48.8                      
REMARK 620 7 HOH A4332   O    96.5  82.0  98.4 162.3  69.8 113.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 367   OD1  93.4                                              
REMARK 620 3 ASP A 369   OD1  81.7  98.1                                        
REMARK 620 4 TYR A 371   O    76.3 169.8  80.5                                  
REMARK 620 5 HOH A4362   O   144.6 106.9  67.2  82.0                            
REMARK 620 6 ASP A 373   OD1  99.8  84.3 177.1  97.5 110.6                      
REMARK 620 7 ASP A 373   OD2 132.4 113.9 128.0  74.2  64.9  49.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 432   O                                                      
REMARK 620 2 ASN A 430   OD1  87.9                                              
REMARK 620 3 ASP A 426   OD1  75.9  88.1                                        
REMARK 620 4 ASP A 428   OD1 153.0  90.5  77.0                                  
REMARK 620 5 ASP A 434   OD1 103.3 168.0  90.4  77.5                            
REMARK 620 6 ASP A 434   OD2  88.1 136.8 132.2 110.9  49.5                      
REMARK 620 7 HOH A4402   O   136.6  86.6 146.7  70.1  88.2  67.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1463   C2                                                     
REMARK 620 2 GOL B1463   O2   26.6                                              
REMARK 620 3 HOH B4231   O    98.3  87.7                                        
REMARK 620 4 ASP B 251   OD2  98.9 124.8  99.2                                  
REMARK 620 5 GOL B1463   O1   46.7  63.3  70.3  67.9                            
REMARK 620 6 SER B 123   O   178.0 154.0  83.7  80.9 134.6                      
REMARK 620 7 ASP B 126   OD1 103.2  79.1  90.8 154.1 137.8  76.6                
REMARK 620 8 ASP B 127   OD1  79.2  85.4 168.9  91.9 113.8  98.8  79.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 159.0                                              
REMARK 620 3 ASN B 215   OD1  98.2  96.8                                        
REMARK 620 4 ASP B 217   OD1  74.3  90.8  91.5                                  
REMARK 620 5 PRO B 219   O    86.7  80.3 171.6  96.4                            
REMARK 620 6 GLU B 220   OE2  93.4 102.8  83.7 166.0  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 220   OE1                                                    
REMARK 620 2 HOH B4101   O    84.0                                              
REMARK 620 3 SER B 123   OG  177.4  93.4                                        
REMARK 620 4 HOH B4033   O    95.7  91.4  84.4                                  
REMARK 620 5 CAC B1462   O1   93.7 100.8  86.7 165.3                            
REMARK 620 6 SER B 121   OG   84.6 165.8  97.9  81.2  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  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 CAC B1462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1463                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514.                                                  
DBREF  2VDL A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDL B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDL H    1   221  PDB    2VDL     2VDL             1    221             
DBREF  2VDL L    1   214  PDB    2VDL     2VDL             1    214             
SEQADV 2VDL GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HET    CAC  B1462       5                                                       
HET    GOL  A1453       6                                                       
HET    GOL  B1463       6                                                       
HETNAM     CAC CACODYLATE ION                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  CAC    C2 H6 AS O2 1-                                               
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   *1129(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
HELIX   10  10 SER B  121  ASP B  126  5                                   6    
HELIX   11  11 ASP B  127  THR B  146  1                                  20    
HELIX   12  12 PRO B  169  LEU B  173  5                                   5    
HELIX   13  13 CYS B  177  LYS B  181  5                                   5    
HELIX   14  14 GLN B  199  GLN B  210  1                                  12    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 CYS B  232  GLY B  237  1                                   6    
HELIX   17  17 ASP B  259  GLY B  264  5                                   6    
HELIX   18  18 SER B  291  ASN B  303  1                                  13    
HELIX   19  19 VAL B  314  ILE B  325  1                                  12    
HELIX   20  20 SER B  337  LYS B  350  1                                  14    
HELIX   21  21 CYS B  435  ALA B  439  5                                   5    
HELIX   22  22 ASN H   28  THR H   32  5                                   5    
HELIX   23  23 PRO H   62  PHE H   64  5                                   3    
HELIX   24  24 THR H   87  THR H   91  5                                   5    
HELIX   25  25 SER H  162  SER H  164  5                                   3    
HELIX   26  26 PRO H  206  SER H  209  5                                   4    
HELIX   27  27 ASP L   79  PHE L   83  5                                   5    
HELIX   28  28 SER L  121  GLY L  128  1                                   8    
HELIX   29  29 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 4 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4  AB 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AD 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AD 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AD 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AE 4 SER A 172  VAL A 175  0                                        
SHEET    2  AE 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AE 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AE 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AF 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AF 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AF 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AF 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AG 4 VAL A 293  THR A 296  0                                        
SHEET    2  AG 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AG 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AG 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AH 2 MET A 314  ARG A 317  0                                        
SHEET    2  AH 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AI 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AI 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AI 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AI 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AJ 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AJ 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  LEU B  40  0                                        
SHEET    2  BA 3 CYS B  23  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BA 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BB 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 SER B 353  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  LEU B 389 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  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  2.07  
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  2.04  
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  2.08  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.06  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.05  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.04  
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  2.09  
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  2.23  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.30  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.62  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.51  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.56  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.56  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.48  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.70  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.38  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.34  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.45  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.80  
LINK        CA    CA A2005                 O   HOH A4332     1555   1555  2.34  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.37  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.13  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.74  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.38  
LINK        CA    CA A2006                 O   HOH A4362     1555   1555  2.29  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.59  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.69  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.42  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.35  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.35  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.40  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.73  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.51  
LINK        CA    CA A2007                 O   HOH A4402     1555   1555  2.20  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.30  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.13  
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 B4033     1555   1555  2.26  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.01  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.28  
LINK        MG    MG B2001                 O   HOH B4101     1555   1555  2.23  
LINK        MG    MG B2001                 O1  CAC B1462     1555   1555  1.94  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.09  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.14  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.42  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.36  
LINK        CA    CA B2002                 O1  GOL B1463     1555   1555  2.84  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.30  
LINK        CA    CA B2002                 O   HOH B4231     1555   1555  2.50  
LINK        CA    CA B2002                 O2  GOL B1463     1555   1555  2.69  
LINK        CA    CA B2002                 C2  GOL B1463     1555   1555  3.14  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.38  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.26  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.28  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.25  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.34  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.31  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.43  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.44  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.44  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
LINK         O3  MAN B3373                 C1  MAN B3374     1555   1555  1.45  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.44  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0        -0.05                     
CISPEP   2 SER B  162    PRO B  163          0         7.61                     
CISPEP   3 SER B  168    PRO B  169          0        -9.08                     
CISPEP   4 PHE H  152    PRO H  153          0        -1.09                     
CISPEP   5 GLU H  154    PRO H  155          0         0.90                     
CISPEP   6 TRP H  194    PRO H  195          0         5.51                     
CISPEP   7 SER L    7    PRO L    8          0        -5.69                     
CISPEP   8 LEU L   94    PRO L   95          0        -2.71                     
CISPEP   9 TYR L  140    PRO L  141          0         3.95                     
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 A4332                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4362                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4402                                          
SITE     1 AC5  2 ASN A  15  HOH A4010                                          
SITE     1 AC6  2 ASN A 249  HOH A4268                                          
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  CAC B1462                    
SITE     2 AC7  6 HOH B4033  HOH B4101                                          
SITE     1 AC8  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC8  6 GOL B1463  HOH B4231                                          
SITE     1 AC9  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC9  5 GLU B 220                                                     
SITE     1 BC1  5 ASN B  99  SER B 398  HOH B4020  HOH B4232                    
SITE     2 BC1  5 HOH B4233                                                     
SITE     1 BC2  7 LEU B 317  ASN B 320  NAG B3321  HOH B4234                    
SITE     2 BC2  7 HOH B4235  HOH B4236  HOH B4239                               
SITE     1 BC3  5 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     2 BC3  5 HOH B4240                                                     
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  4 ARG A 281  MAN B3322  HOH B4241  HOH B4242                    
SITE     1 BC6  3 NAG B3321  MAN B3322  HOH B4243                               
SITE     1 BC7  6 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC7  6 NAG B3372  HOH B4244                                          
SITE     1 BC8  5 NAG B3371  MAN B3373  MAN B3376  HOH B4245                    
SITE     2 BC8  5 HOH B4247                                                     
SITE     1 BC9  6 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  6 MAN B3375  HOH B4246                                          
SITE     1 CC1  5 ASN A 299  LEU A 332  SER A 396  GLU A 397                    
SITE     2 CC1  5 MAN B3373                                                     
SITE     1 CC2  7 ALA A 342  PRO A 343  MAN B3373  MAN B3376                    
SITE     2 CC2  7 MAN B3377  HOH B4247  HOH B4248                               
SITE     1 CC3  7 PRO A 343  SER A 344  LEU A 346  NAG B3372                    
SITE     2 CC3  7 MAN B3375  HOH B4249  HOH B4250                               
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  9 SER B 121  TYR B 122  SER B 123  ARG B 214                    
SITE     2 CC5  9 ASN B 215  ASP B 217  GLU B 220   MG B2001                    
SITE     3 CC5  9 HOH B4099                                                     
SITE     1 CC6  4 ALA A  89  ARG A  90  HOH A4110  HOH A4146                    
SITE     1 CC7  6 ASP B 126  ASP B 127  ASP B 251   CA B2002                    
SITE     2 CC7  6 HOH B4112  HOH B4231                                          
CRYST1  148.927  148.927  176.398  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      0.006715  0.003877  0.000000        0.00000                         
SCALE2      0.000000  0.007753  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005669        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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