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Entry: 2VDK
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HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDK              
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_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 STRAIN: BALB/C;                                                      
SOURCE  24 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  27 ORGANISM_COMMON: MOUSE;                                              
SOURCE  28 ORGANISM_TAXID: 10090;                                               
SOURCE  29 STRAIN: BALB/C;                                                      
SOURCE  30 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, HOST-VIRUS   
KEYWDS   2 INTERACTION, PYRROLIDONE CARBOXYLIC ACID, PHOSPHORYLATION,           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDK    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDK    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDK    0                                                
SPRSDE     02-SEP-08 2VDK      1TY3                                             
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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50725                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2713                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3343                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 198                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10403                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 210                                     
REMARK   3   SOLVENT ATOMS            : 612                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.21000                                              
REMARK   3    B22 (A**2) : 1.21000                                              
REMARK   3    B33 (A**2) : -1.82000                                             
REMARK   3    B12 (A**2) : 0.61000                                              
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): 0.648         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.279         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.187         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.783        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10895 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7298 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14875 ; 0.936 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17733 ; 0.758 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1368 ; 5.264 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   473 ;32.211 ;24.271       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1698 ;11.618 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;13.472 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1675 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12134 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2157 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2003 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7610 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5306 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5668 ; 0.078 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   591 ; 0.124 ; 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):    17 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    61 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.135 ; 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):  6993 ; 1.391 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10878 ; 2.222 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4552 ; 1.293 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3985 ; 2.093 ;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): 133.4040  12.4290  78.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1029 T22:   0.0070                                     
REMARK   3      T33:  -0.0580 T12:   0.0983                                     
REMARK   3      T13:   0.0217 T23:   0.3594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8542 L22:   0.3473                                     
REMARK   3      L33:   6.4696 L12:  -1.7907                                     
REMARK   3      L13:   2.3784 L23:  -0.0729                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.1518 S13:  -0.7180                       
REMARK   3      S21:   0.5668 S22:  -0.2769 S23:  -1.0607                       
REMARK   3      S31:   1.0089 S32:   1.0814 S33:   0.2430                       
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): 129.4040  22.0220  68.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1418 T22:   0.0277                                     
REMARK   3      T33:  -0.0240 T12:   0.0489                                     
REMARK   3      T13:   0.0390 T23:   0.2387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7069 L22:   3.1410                                     
REMARK   3      L33:   1.8400 L12:  -0.2144                                     
REMARK   3      L13:  -0.0018 L23:  -0.3532                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0892 S12:  -0.1503 S13:  -0.1357                       
REMARK   3      S21:  -0.1263 S22:  -0.0455 S23:  -0.4889                       
REMARK   3      S31:   0.1904 S32:   0.3669 S33:   0.1348                       
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): 118.9160  33.7570  64.1670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0928 T22:   0.0068                                     
REMARK   3      T33:   0.0256 T12:  -0.0650                                     
REMARK   3      T13:  -0.0343 T23:   0.1521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9099 L22:   1.4825                                     
REMARK   3      L33:   1.3487 L12:  -0.5198                                     
REMARK   3      L13:  -0.6678 L23:  -0.4323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0027 S12:  -0.1389 S13:  -0.0252                       
REMARK   3      S21:   0.1927 S22:  -0.1496 S23:  -0.3490                       
REMARK   3      S31:   0.0171 S32:   0.3760 S33:   0.1523                       
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): 107.3330  36.3070  63.4490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0715 T22:  -0.0351                                     
REMARK   3      T33:  -0.0909 T12:  -0.0901                                     
REMARK   3      T13:  -0.0449 T23:   0.0855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9776 L22:   1.9144                                     
REMARK   3      L33:   2.2869 L12:  -0.5619                                     
REMARK   3      L13:  -1.4956 L23:  -0.2828                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0639 S12:  -0.0628 S13:  -0.1976                       
REMARK   3      S21:   0.0128 S22:  -0.2206 S23:   0.1439                       
REMARK   3      S31:  -0.0167 S32:   0.0516 S33:   0.1567                       
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): 106.2780  24.6340  63.7060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0285 T22:  -0.0524                                     
REMARK   3      T33:  -0.0262 T12:  -0.0715                                     
REMARK   3      T13:  -0.0026 T23:   0.0657                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8671 L22:   1.5963                                     
REMARK   3      L33:   1.7222 L12:  -0.0029                                     
REMARK   3      L13:  -0.6024 L23:  -0.8380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0649 S12:   0.1272 S13:  -0.0975                       
REMARK   3      S21:  -0.0069 S22:  -0.1357 S23:  -0.0522                       
REMARK   3      S31:   0.2522 S32:  -0.0776 S33:   0.0708                       
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): 100.0270  13.1980  72.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0021 T22:  -0.1328                                     
REMARK   3      T33:  -0.0048 T12:  -0.1155                                     
REMARK   3      T13:   0.0785 T23:   0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6649 L22:   2.9109                                     
REMARK   3      L33:   3.6359 L12:  -0.5156                                     
REMARK   3      L13:  -0.1259 L23:   0.2742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0958 S12:   0.0898 S13:  -0.3031                       
REMARK   3      S21:  -0.0647 S22:  -0.1289 S23:   0.1013                       
REMARK   3      S31:   0.2493 S32:  -0.1506 S33:   0.2247                       
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): 108.0460   7.3110  84.0410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0424 T22:  -0.2635                                     
REMARK   3      T33:  -0.0313 T12:  -0.0558                                     
REMARK   3      T13:   0.0679 T23:   0.2231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7126 L22:   6.3929                                     
REMARK   3      L33:   5.1977 L12:   0.0138                                     
REMARK   3      L13:  -0.3475 L23:   2.1607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0280 S12:  -0.2419 S13:  -0.4280                       
REMARK   3      S21:   0.3674 S22:   0.0743 S23:   0.0389                       
REMARK   3      S31:   0.5735 S32:   0.0404 S33:  -0.0463                       
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): 110.8020   2.9720  78.3640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1381 T22:  -0.2607                                     
REMARK   3      T33:  -0.0731 T12:   0.0115                                     
REMARK   3      T13:   0.0688 T23:   0.2061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8436 L22:   3.5664                                     
REMARK   3      L33:   3.9820 L12:   0.3144                                     
REMARK   3      L13:  -0.3963 L23:   1.3151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1009 S12:   0.0651 S13:  -0.3432                       
REMARK   3      S21:  -0.1734 S22:  -0.2519 S23:  -0.0339                       
REMARK   3      S31:   0.6679 S32:  -0.0301 S33:   0.3528                       
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): 124.5510   7.7620  79.8450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0238 T22:  -0.1271                                     
REMARK   3      T33:   0.0063 T12:   0.1047                                     
REMARK   3      T13:   0.0371 T23:   0.2581                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7391 L22:   1.7804                                     
REMARK   3      L33:   2.4070 L12:   0.0386                                     
REMARK   3      L13:  -0.3656 L23:  -0.5098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.1973 S13:  -0.3718                       
REMARK   3      S21:   0.2330 S22:  -0.2935 S23:  -0.4886                       
REMARK   3      S31:   0.5747 S32:   0.5560 S33:   0.3124                       
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): 106.8580  21.1190 168.7730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4843 T22:  -0.3760                                     
REMARK   3      T33:  -0.3563 T12:   0.0725                                     
REMARK   3      T13:  -0.1775 T23:  -0.1157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4435 L22:   3.4148                                     
REMARK   3      L33:   7.2168 L12:  -2.3896                                     
REMARK   3      L13:   2.7182 L23:  -3.0205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2317 S12:  -0.7806 S13:  -0.0312                       
REMARK   3      S21:   1.1365 S22:   0.3983 S23:  -0.2074                       
REMARK   3      S31:  -1.0758 S32:  -0.7251 S33:  -0.1666                       
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    79        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.1110  30.0870 148.7500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5630 T22:  -0.1505                                     
REMARK   3      T33:  -0.1705 T12:   0.1780                                     
REMARK   3      T13:  -0.0396 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1334 L22:  11.8711                                     
REMARK   3      L33:  39.6766 L12:  -5.9665                                     
REMARK   3      L13:  18.4456 L23: -16.4466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2000 S12:  -0.9643 S13:   0.5065                       
REMARK   3      S21:   1.4911 S22:   0.6796 S23:  -0.6431                       
REMARK   3      S31:  -3.3078 S32:  -2.0432 S33:   0.5204                       
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):  97.6000  38.2160 104.0550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1784 T22:  -0.0696                                     
REMARK   3      T33:  -0.0946 T12:  -0.1777                                     
REMARK   3      T13:   0.0296 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5361 L22:   0.4293                                     
REMARK   3      L33:   3.0679 L12:  -0.1732                                     
REMARK   3      L13:  -0.1769 L23:  -1.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0258 S12:  -0.1035 S13:  -0.0277                       
REMARK   3      S21:   0.3452 S22:  -0.0588 S23:  -0.0048                       
REMARK   3      S31:  -0.4315 S32:   0.0171 S33:   0.0846                       
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): 103.1110  34.3330  95.8090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0409 T22:  -0.0734                                     
REMARK   3      T33:  -0.1158 T12:  -0.1402                                     
REMARK   3      T13:  -0.0124 T23:   0.0631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7751 L22:   1.1894                                     
REMARK   3      L33:   2.0008 L12:  -0.3811                                     
REMARK   3      L13:  -0.9842 L23:  -0.0941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:  -0.2674 S13:   0.0283                       
REMARK   3      S21:   0.3356 S22:  -0.0664 S23:  -0.1425                       
REMARK   3      S31:  -0.0514 S32:   0.1559 S33:   0.0601                       
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): 100.2610  22.5570 130.5970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0767 T22:  -0.1905                                     
REMARK   3      T33:  -0.1888 T12:  -0.0218                                     
REMARK   3      T13:   0.0455 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3791 L22:   3.1517                                     
REMARK   3      L33:  23.7094 L12:  -1.6520                                     
REMARK   3      L13:   8.9365 L23:  -4.7903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7051 S12:   0.4028 S13:  -0.5122                       
REMARK   3      S21:  -0.1137 S22:   0.1055 S23:  -0.0459                       
REMARK   3      S31:   1.4974 S32:   0.4634 S33:  -0.8106                       
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): 109.4840  28.0840 148.6830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3225 T22:  -0.3978                                     
REMARK   3      T33:  -0.2316 T12:  -0.1077                                     
REMARK   3      T13:  -0.0805 T23:   0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5806 L22:   2.1046                                     
REMARK   3      L33:  19.7418 L12:  -1.1262                                     
REMARK   3      L13:   7.3788 L23:  -1.3520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2947 S12:   0.7425 S13:   0.0897                       
REMARK   3      S21:   0.7300 S22:   0.4744 S23:  -0.7443                       
REMARK   3      S31:  -1.8493 S32:   1.2909 S33:  -0.1797                       
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): 119.4680  31.1090 182.6540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8135 T22:   0.5504                                     
REMARK   3      T33:   0.4830 T12:  -0.2024                                     
REMARK   3      T13:  -0.8420 T23:  -0.2340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9676 L22:  13.5549                                     
REMARK   3      L33:   9.1428 L12:   3.6215                                     
REMARK   3      L13:  -2.9743 L23: -11.1324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6064 S12:  -2.1629 S13:   0.8326                       
REMARK   3      S21:   1.6236 S22:  -0.1915 S23:  -1.1158                       
REMARK   3      S31:  -3.0834 S32:   3.1376 S33:   0.7979                       
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):  90.0490  36.8710  33.2470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0643 T22:   0.0136                                     
REMARK   3      T33:   0.0524 T12:  -0.2048                                     
REMARK   3      T13:  -0.0610 T23:   0.0391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2173 L22:   4.8143                                     
REMARK   3      L33:  10.8333 L12:  -5.1507                                     
REMARK   3      L13:   5.8943 L23:  -5.2659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3702 S12:   0.5788 S13:  -0.7370                       
REMARK   3      S21:  -0.6322 S22:  -0.1115 S23:   0.2980                       
REMARK   3      S31:   0.8421 S32:   0.1383 S33:  -0.2587                       
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):  94.2600  42.2240  41.1920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1649 T22:  -0.0173                                     
REMARK   3      T33:  -0.0565 T12:  -0.0440                                     
REMARK   3      T13:  -0.0016 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4314 L22:   2.5418                                     
REMARK   3      L33:   3.0549 L12:  -0.4056                                     
REMARK   3      L13:   1.1968 L23:  -0.8031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0082 S12:  -0.1078 S13:  -0.1308                       
REMARK   3      S21:   0.0984 S22:  -0.0588 S23:   0.0604                       
REMARK   3      S31:   0.2327 S32:  -0.1015 S33:   0.0670                       
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):  94.0800  43.0920  43.4110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1406 T22:  -0.0459                                     
REMARK   3      T33:  -0.0318 T12:  -0.0726                                     
REMARK   3      T13:   0.0036 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5601 L22:   1.3828                                     
REMARK   3      L33:   3.4154 L12:  -0.7327                                     
REMARK   3      L13:   1.4730 L23:  -1.3824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0680 S12:  -0.1130 S13:   0.1271                       
REMARK   3      S21:   0.0080 S22:   0.0136 S23:   0.0622                       
REMARK   3      S31:   0.1607 S32:  -0.1866 S33:   0.0545                       
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):  86.4710  47.7740  12.7570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2089 T22:   0.1014                                     
REMARK   3      T33:   0.0325 T12:  -0.0759                                     
REMARK   3      T13:  -0.0732 T23:   0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3523 L22:   1.3247                                     
REMARK   3      L33:   3.5701 L12:  -0.9360                                     
REMARK   3      L13:  -0.4568 L23:   1.2659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0522 S12:   0.2290 S13:  -0.0788                       
REMARK   3      S21:  -0.1586 S22:  -0.0962 S23:   0.0927                       
REMARK   3      S31:  -0.1893 S32:  -0.5180 S33:   0.0440                       
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):  92.5870  44.8460   4.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1608 T22:  -0.0882                                     
REMARK   3      T33:  -0.1118 T12:   0.0553                                     
REMARK   3      T13:  -0.0825 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5062 L22:   1.2383                                     
REMARK   3      L33:  12.9400 L12:  -0.3213                                     
REMARK   3      L13:  -4.1538 L23:   1.2934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1654 S12:   0.3948 S13:  -0.4307                       
REMARK   3      S21:  -0.1370 S22:   0.0601 S23:  -0.2344                       
REMARK   3      S31:   1.2814 S32:  -0.1713 S33:  -0.2254                       
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):  94.5950  47.6160   9.2290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1571 T22:  -0.1775                                     
REMARK   3      T33:  -0.1560 T12:   0.1001                                     
REMARK   3      T13:  -0.0247 T23:   0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3813 L22:   3.4021                                     
REMARK   3      L33:  13.2127 L12:   0.2307                                     
REMARK   3      L13:  -1.4830 L23:   0.5180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2216 S12:  -0.0428 S13:   0.0009                       
REMARK   3      S21:  -0.2578 S22:  -0.1102 S23:   0.3331                       
REMARK   3      S31:   0.5495 S32:   0.1618 S33:  -0.1114                       
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):  93.9740  40.6180  -3.6560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6228 T22:   0.0237                                     
REMARK   3      T33:  -0.0444 T12:   0.2667                                     
REMARK   3      T13:  -0.0145 T23:  -0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6159 L22:   2.2700                                     
REMARK   3      L33:   8.2544 L12:  -2.1416                                     
REMARK   3      L13:  -3.2842 L23:   4.3077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4565 S12:   0.4901 S13:  -1.5845                       
REMARK   3      S21:  -0.1981 S22:  -1.0473 S23:  -0.2150                       
REMARK   3      S31:   0.0962 S32:   0.4463 S33:   0.5908                       
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):  86.2090  44.2280  -2.4190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1162 T22:   0.1289                                     
REMARK   3      T33:  -0.2363 T12:   0.0370                                     
REMARK   3      T13:  -0.2522 T23:  -0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1279 L22:   9.6128                                     
REMARK   3      L33:  24.7977 L12:   8.3666                                     
REMARK   3      L13: -13.6939 L23:  -6.4038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3114 S12:   0.9509 S13:  -0.4901                       
REMARK   3      S21:  -1.1936 S22:   0.3881 S23:   0.8933                       
REMARK   3      S31:   1.5849 S32:  -1.4770 S33:  -0.0768                       
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): 114.3650  50.3300  35.0740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1189 T22:   0.0431                                     
REMARK   3      T33:   0.0581 T12:   0.0232                                     
REMARK   3      T13:   0.0028 T23:   0.1284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0139 L22:   0.6984                                     
REMARK   3      L33:   0.5101 L12:   0.6109                                     
REMARK   3      L13:  -0.3612 L23:  -0.5726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0496 S12:   0.1401 S13:   0.0766                       
REMARK   3      S21:  -0.1047 S22:  -0.0864 S23:  -0.0197                       
REMARK   3      S31:  -0.0230 S32:   0.1315 S33:   0.0369                       
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): 113.7050  39.4180  36.1360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0513 T22:   0.0310                                     
REMARK   3      T33:   0.0104 T12:   0.0151                                     
REMARK   3      T13:  -0.0065 T23:   0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8357 L22:   1.4014                                     
REMARK   3      L33:   2.2041 L12:  -0.0739                                     
REMARK   3      L13:  -0.2406 L23:  -1.7459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1034 S12:   0.4733 S13:  -0.2887                       
REMARK   3      S21:  -0.1626 S22:   0.0390 S23:  -0.0393                       
REMARK   3      S31:   0.6029 S32:   0.2706 S33:  -0.1424                       
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): 112.4640  45.9050  35.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1338 T22:  -0.0267                                     
REMARK   3      T33:  -0.0288 T12:   0.0048                                     
REMARK   3      T13:  -0.0446 T23:   0.0868                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6879 L22:   0.6861                                     
REMARK   3      L33:   4.2853 L12:   0.1199                                     
REMARK   3      L13:  -2.2718 L23:  -0.4841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0925 S12:   0.2550 S13:  -0.1202                       
REMARK   3      S21:  -0.0392 S22:  -0.0480 S23:   0.0748                       
REMARK   3      S31:   0.2667 S32:   0.0928 S33:   0.1406                       
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): 100.4580  53.2970   8.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1323 T22:   0.1424                                     
REMARK   3      T33:  -0.0170 T12:   0.0601                                     
REMARK   3      T13:   0.0212 T23:   0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6319 L22:   2.1707                                     
REMARK   3      L33:   7.5284 L12:  -1.6304                                     
REMARK   3      L13:   3.2544 L23:  -2.5014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5145 S12:   0.2071 S13:  -0.2084                       
REMARK   3      S21:  -0.3897 S22:  -0.3058 S23:   0.1412                       
REMARK   3      S31:   0.7217 S32:   0.2342 S33:  -0.2087                       
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): 101.6260  59.8920   8.8210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2183 T22:   0.2243                                     
REMARK   3      T33:  -0.1287 T12:   0.0129                                     
REMARK   3      T13:  -0.0081 T23:   0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4667 L22:   7.7987                                     
REMARK   3      L33:   2.5708 L12:  -5.4148                                     
REMARK   3      L13:   3.2560 L23:  -1.9850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1138 S12:  -0.1298 S13:   0.5189                       
REMARK   3      S21:   0.1965 S22:  -0.0814 S23:  -0.3896                       
REMARK   3      S31:  -0.0436 S32:   0.4265 S33:   0.1953                       
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):  95.1450  60.2460   2.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2195 T22:   0.0943                                     
REMARK   3      T33:  -0.1534 T12:   0.0339                                     
REMARK   3      T13:   0.0068 T23:   0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5391 L22:   3.8034                                     
REMARK   3      L33:   3.8771 L12:  -3.3657                                     
REMARK   3      L13:   2.8744 L23:  -1.4300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0818 S12:   0.3458 S13:   0.0266                       
REMARK   3      S21:  -0.2967 S22:  -0.0848 S23:  -0.0051                       
REMARK   3      S31:   0.0326 S32:   0.0873 S33:   0.1666                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   198        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.9720  62.6710  -2.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2154 T22:   0.2462                                     
REMARK   3      T33:  -0.1136 T12:   0.1244                                     
REMARK   3      T13:   0.0726 T23:   0.1676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2961 L22:   6.0706                                     
REMARK   3      L33:   4.4701 L12:  -1.4101                                     
REMARK   3      L13:  -1.7455 L23:  -2.9727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0966 S12:   1.5287 S13:   0.2088                       
REMARK   3      S21:  -0.3934 S22:  -0.5259 S23:  -0.2768                       
REMARK   3      S31:  -0.3359 S32:   1.2219 S33:   0.6225                       
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 1TY3. 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 ALSO          
REMARK   3  CORRECTED.                                                          
REMARK   4                                                                      
REMARK   4 2VDK 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-34076.                                       
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   : 55875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
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                : 7.5                                
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1TXV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 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      117.42467            
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       58.71233            
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       58.71233            
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      117.42467            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  4024     O    HOH B  4109              1.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   2       46.65   -141.69                                   
REMARK 500    SER A 101     -120.66     48.01                                   
REMARK 500    LYS A 118     -127.49     50.98                                   
REMARK 500    GLU A 123      134.62    105.31                                   
REMARK 500    SER A 144       72.46   -150.75                                   
REMARK 500    LEU A 212      -45.97     74.62                                   
REMARK 500    THR B   7       50.25    -95.32                                   
REMARK 500    ARG B   8       66.06   -154.57                                   
REMARK 500    VAL B  10       73.84     40.72                                   
REMARK 500    ASP B  47       30.22    -99.46                                   
REMARK 500    PHE B  56       79.48   -151.35                                   
REMARK 500    ASP B  66       58.11   -146.54                                   
REMARK 500    VAL B  80       96.62     64.05                                   
REMARK 500    ASN B 148       37.22    -94.27                                   
REMARK 500    VAL B 157      -83.55   -126.48                                   
REMARK 500    SER B 213     -154.20   -117.05                                   
REMARK 500    LYS B 253      172.18    -57.91                                   
REMARK 500    LEU B 258       -8.38     86.48                                   
REMARK 500    LYS B 410      -28.71     76.14                                   
REMARK 500    GLU B 442       71.57     57.74                                   
REMARK 500    HIS B 446      -65.03     68.36                                   
REMARK 500    THR B 454      120.18     66.08                                   
REMARK 500    TYR H 101      -59.04   -122.06                                   
REMARK 500    SER L  30       65.63     24.50                                   
REMARK 500    SER L  77       73.98     56.10                                   
REMARK 500    LYS L 169      -64.61    -95.34                                   
REMARK 500    ASN L 212       70.80     49.56                                   
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  110.9                                              
REMARK 620 3 CAC B1462   O2  110.3 106.7                                        
REMARK 620 4 CAC B1462   C1  108.9 110.5 109.5                                  
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  48.4                                              
REMARK 620 3 ASP A 245   OD2 120.7  72.4                                        
REMARK 620 4 ASP A 247   O    74.5  71.8  92.1                                  
REMARK 620 5 THR A 250   C    91.8 139.1 146.9  90.8                            
REMARK 620 6 THR A 250   O    71.2 118.3 165.2  82.5  20.8                      
REMARK 620 7 THR A 250   OG1 142.2 145.2  87.9  80.7  60.1  77.7                
REMARK 620 8 GLU A 252   OE1  81.2  79.1  85.4 150.2 107.2 106.0 128.8          
REMARK 620 9 GLU A 252   OE2 123.7 125.6  85.2 159.9  80.9  95.1  79.3  49.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 301   OD1  77.7                                              
REMARK 620 3 ARG A 303   O   167.0  98.3                                        
REMARK 620 4 ASP A 297   OD1  84.8  77.2  82.3                                  
REMARK 620 5 ASP A 305   OD1 101.7 150.6  87.8 132.2                            
REMARK 620 6 ASP A 305   OD2  78.2 152.6 102.3  87.9  48.8                      
REMARK 620 7 HOH A4180   O    89.1  77.2 102.1 154.4  73.4 115.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD2                                                    
REMARK 620 2 ASP A 369   OD1  80.5                                              
REMARK 620 3 TYR A 371   O    74.3  87.4                                        
REMARK 620 4 ASP A 367   OD1  87.8  98.5 160.1                                  
REMARK 620 5 HOH A4206   O   149.3  69.5  97.5 102.4                            
REMARK 620 6 ASP A 373   OD1  95.9 171.8  98.7  73.9 114.7                      
REMARK 620 7 ASP A 373   OD2 131.3 139.4  80.3 106.1  74.0  47.8                
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  91.6                                              
REMARK 620 3 ASP A 426   OD1  73.4  86.1                                        
REMARK 620 4 ASP A 428   OD1 150.1  87.0  76.7                                  
REMARK 620 5 ASP A 434   OD1 102.4 163.3  89.1  76.3                            
REMARK 620 6 ASP A 434   OD2  89.2 142.1 130.0 109.9  48.6                      
REMARK 620 7 HOH A4217   O   141.6  84.6 143.8  67.9  89.9  71.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1463   O2                                                     
REMARK 620 2 HOH B4125   O    94.7                                              
REMARK 620 3 ASP B 127   OD1  85.5 178.3                                        
REMARK 620 4 ASP B 251   OD2 121.7  89.9  88.6                                  
REMARK 620 5 GOL B1463   O1   62.2  67.8 110.9  66.4                            
REMARK 620 6 SER B 123   O   158.4  85.5  94.9  79.9 136.0                      
REMARK 620 7 ASP B 126   OD1  83.6 101.8  79.9 151.5 142.1  75.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 158.2                                              
REMARK 620 3 ASN B 215   OD1  96.1 100.5                                        
REMARK 620 4 ASP B 217   OD1  73.3  92.3  90.8                                  
REMARK 620 5 PRO B 219   O    84.2  80.4 175.2  93.8                            
REMARK 620 6 GLU B 220   OE2  94.4 101.2  83.9 166.1  91.3                      
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 B4060   O    84.0                                              
REMARK 620 3 SER B 121   OG   86.2 169.0                                        
REMARK 620 4 SER B 123   OG  172.5  95.5  94.9                                  
REMARK 620 5 HOH B4014   O   101.2  94.2  82.9  86.4                            
REMARK 620 6 CAC B1462   O1   92.6 100.3  85.1  80.1 161.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B1462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1463                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF                        
REMARK 800  SUGAR BOUND TO ASN B 320 RESIDUES 3320 TO 3324                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF                        
REMARK 800  SUGAR BOUND TO ASN B 371 RESIDUES 3371 TO 3377                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 2VDN   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE                          
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514.                                                  
DBREF  2VDK A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDK B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDK H    1   221  PDB    2VDK     2VDK             1    221             
DBREF  2VDK L    1   214  PDB    2VDK     2VDK             1    214             
SEQADV 2VDK GLY A  282  UNP  P08514    ALA   313 SEE REMARK 999                 
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET    GOL  A1453       6                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET    CAC  B1462       5                                                       
HET    GOL  B1463       6                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HETNAM     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   *612(H2 O)                                                    
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
HELIX   10  10 SER B  121  LYS B  125  5                                   5    
HELIX   11  11 ASP B  127  THR B  146  1                                  20    
HELIX   12  12 PRO B  169  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 LEU B  258  GLY B  264  5                                   7    
HELIX   18  18 SER B  291  LYS B  302  1                                  12    
HELIX   19  19 VAL B  314  GLU B  323  1                                  10    
HELIX   20  20 SER B  337  LYS B  350  1                                  14    
HELIX   21  21 CYS B  435  ALA B  439  5                                   5    
HELIX   22  22 ASN H   28  THR H   32  5                                   5    
HELIX   23  23 PRO H   62  PHE H   64  5                                   3    
HELIX   24  24 THR H   87  THR H   91  5                                   5    
HELIX   25  25 SER H  162  SER H  164  5                                   3    
HELIX   26  26 ASP L   79  PHE L   83  5                                   5    
HELIX   27  27 SER L  121  GLY L  128  1                                   8    
HELIX   28  28 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 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  LYS B 402 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 SER B 367  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 6 SER L  10  VAL L  13  0                                        
SHEET    2  LB 6 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 6 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 6 ILE L  33  GLN L  38 -1  O  GLY L  34   N  VAL L  89           
SHEET    5  LB 6 PHE L  44  TYR L  49 -1  O  MET L  45   N  GLN L  37           
SHEET    6  LB 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LC 4 SER L  10  VAL L  13  0                                        
SHEET    2  LC 4 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LC 4 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LC 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  LD 4 THR L 114  PHE L 118  0                                        
SHEET    2  LD 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LD 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LD 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LE 4 SER L 153  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  2.05  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.05  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.05  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.44  
LINK         ND2 ASN A 249                 C1  NAG A3249     1555   1555  1.45  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.31  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.35  
LINK        CA    CA A2004                 C   THR A 250     1555   1555  3.14  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.43  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.59  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.56  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.67  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.60  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.74  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.29  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.30  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.41  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.82  
LINK        CA    CA A2005                 O   HOH A4180     1555   1555  2.21  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.42  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.18  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.32  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.48  
LINK        CA    CA A2006                 O   HOH A4206     1555   1555  2.34  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.81  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.59  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.46  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.57  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.37  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.48  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.79  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.50  
LINK        CA    CA A2007                 O   HOH A4217     1555   1555  2.34  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.35  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.20  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.45  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.11  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.27  
LINK        MG    MG B2001                 O   HOH B4060     1555   1555  2.19  
LINK        MG    MG B2001                 O1  CAC B1462     1555   1555  2.05  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  2.07  
LINK        MG    MG B2001                 O   HOH B4014     1555   1555  1.99  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.44  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.32  
LINK        CA    CA B2002                 O1  GOL B1463     1555   1555  3.04  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.32  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.20  
LINK        CA    CA B2002                 O   HOH B4125     1555   1555  2.37  
LINK        CA    CA B2002                 O2  GOL B1463     1555   1555  2.44  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.36  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.32  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.31  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.25  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.33  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.40  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.44  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.45  
LINK         O6  MAN B3373                 C1  MAN B3375     1555   1555  1.44  
LINK         O3  MAN B3373                 C1  MAN B3374     1555   1555  1.44  
LINK         O6  MAN B3375                 C1  MAN B3377     1555   1555  1.44  
LINK         O3  MAN B3375                 C1  MAN B3376     1555   1555  1.43  
CISPEP   1 SER B   84    PRO B   85          0        -0.75                     
CISPEP   2 SER B  162    PRO B  163          0         3.39                     
CISPEP   3 SER B  168    PRO B  169          0       -10.54                     
CISPEP   4 PHE H  152    PRO H  153          0        -2.00                     
CISPEP   5 GLU H  154    PRO H  155          0        -0.69                     
CISPEP   6 TRP H  194    PRO H  195          0         6.50                     
CISPEP   7 SER L    7    PRO L    8          0        -3.74                     
CISPEP   8 LEU L   94    PRO L   95          0        -2.89                     
CISPEP   9 TYR L  140    PRO L  141          0         5.39                     
SITE     1 AC1  5 ALA A  89  ARG A  90  HIS A 112  HOH A4056                    
SITE     2 AC1  5 HOH A4080                                                     
SITE     1 AC2  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC2  5 GLU A 252                                                     
SITE     1 AC3  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC3  6 ASP A 305  HOH A4180                                          
SITE     1 AC4  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC4  6 ASP A 373  HOH A4206                                          
SITE     1 AC5  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC5  6 ASP A 434  HOH A4217                                          
SITE     1 AC6  2 ASN A  15  HOH A4223                                          
SITE     1 AC7  1 ASN A 249                                                     
SITE     1 AC8  8 SER B 121  TYR B 122  SER B 123  ARG B 214                    
SITE     2 AC8  8 ASN B 215  ASP B 217  GLU B 220   MG B2001                    
SITE     1 AC9  8 ASP B 126  ASP B 127  ASP B 251  ASN B 313                    
SITE     2 AC9  8  CA B2002  HOH B4018  HOH B4124  HOH B4125                    
SITE     1 BC1  6 SER B 121  SER B 123  GLU B 220  CAC B1462                    
SITE     2 BC1  6 HOH B4014  HOH B4060                                          
SITE     1 BC2  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 BC2  6 GOL B1463  HOH B4125                                          
SITE     1 BC3  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC3  5 GLU B 220                                                     
SITE     1 BC4  2 ASN B  99  HOH B4008                                          
SITE     1 BC5  9 ARG A 281  LEU B 317  ASN B 320  HOH B4126                    
SITE     2 BC5  9 HOH B4128  HOH B4129  HOH B4130  HOH B4131                    
SITE     3 BC5  9 HOH B4132                                                     
SITE     1 BC6 14 ASN A 299  LEU A 332  ALA A 342  PRO A 343                    
SITE     2 BC6 14 SER A 344  LEU A 346  SER A 396  GLU A 397                    
SITE     3 BC6 14 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     4 BC6 14 HOH B4133  HOH B4136                                          
CRYST1  148.869  148.869  176.137  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      0.006717  0.003878  0.000000        0.00000                         
SCALE2      0.000000  0.007756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005677        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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