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Entry: 2VDN
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HEADER    CELL ADHESION/IMMUNE SYSTEM             10-OCT-07   2VDN              
TITLE     RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO            
TITLE    2 ANTAGONIST EPTIFIBATIDE                                              
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: EPTIFIBATIDE;                                              
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: MPT HRG GLY ASP TRP PRO CYS NH2;                            
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  20 CHAIN: H;                                                            
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  23 CHAIN: L                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 MOL_ID: 4;                                                           
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: 5;                                                           
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, PLATELET     
KEYWDS   2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,       
KEYWDS   3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE  
KEYWDS   4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,   
KEYWDS   5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM      
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,J.ZHU,T.XIAO                                             
REVDAT   3   13-JUL-11 2VDN    1       VERSN                                    
REVDAT   2   24-FEB-09 2VDN    1       VERSN                                    
REVDAT   1   02-SEP-08 2VDN    0                                                
SPRSDE     02-SEP-08 2VDN      1TY6                                             
JRNL        AUTH   T.A.SPRINGER,J.ZHU,T.XIAO                                    
JRNL        TITL   STRUCTURAL BASIS FOR DISTINCTIVE RECOGNITION OF FIBRINOGEN   
JRNL        TITL 2 GAMMAC PEPTIDE BY THE PLATELET INTEGRIN ALPHAIIBBETA3.       
JRNL        REF    J.CELL BIOL.                  V. 182   791 2008              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   18710925                                                     
JRNL        DOI    10.1083/JCB.200801146                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER            
REMARK   1  TITL   STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO   
REMARK   1  TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS                              
REMARK   1  REF    NATURE                        V. 432    59 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15378069                                                     
REMARK   1  DOI    10.1038/NATURE02976                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 46249                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2421                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3085                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10385                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 223                                     
REMARK   3   SOLVENT ATOMS            : 364                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 0.89000                                              
REMARK   3    B33 (A**2) : -1.33000                                             
REMARK   3    B12 (A**2) : 0.44000                                              
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): 1.054         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.311         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.216         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.178        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
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): 10884 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7291 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14848 ; 0.922 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17658 ; 0.759 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1354 ; 5.174 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   466 ;31.968 ;24.356       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1685 ;11.724 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;13.632 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1670 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12089 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2142 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1959 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7414 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5286 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5662 ; 0.078 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   429 ; 0.128 ; 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 ; 0.133 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    51 ; 0.167 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.128 ; 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):  6970 ; 1.302 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10835 ; 2.140 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4568 ; 1.213 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4006 ; 2.062 ;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): 133.9140  12.7020  77.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0741 T22:   0.2919                                     
REMARK   3      T33:   0.1290 T12:   0.1219                                     
REMARK   3      T13:   0.0155 T23:   0.4047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9855 L22:   9.2218                                     
REMARK   3      L33:   1.6837 L12:  -4.8724                                     
REMARK   3      L13:   0.7602 L23:   0.4490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:   0.0961 S13:  -0.5040                       
REMARK   3      S21:   1.2353 S22:  -0.4983 S23:  -0.6348                       
REMARK   3      S31:   0.5142 S32:   0.9656 S33:   0.4504                       
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): 129.9430  22.2810  68.5970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1403 T22:   0.1670                                     
REMARK   3      T33:  -0.0070 T12:   0.0750                                     
REMARK   3      T13:   0.0418 T23:   0.2707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0675 L22:   3.8727                                     
REMARK   3      L33:   1.9525 L12:   1.1833                                     
REMARK   3      L13:   0.3071 L23:  -0.1314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1168 S12:   0.0476 S13:  -0.2906                       
REMARK   3      S21:  -0.1223 S22:  -0.2987 S23:  -0.4112                       
REMARK   3      S31:   0.2466 S32:   0.2622 S33:   0.1819                       
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): 119.3810  34.0160  63.9690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1781 T22:  -0.1011                                     
REMARK   3      T33:  -0.1279 T12:  -0.0454                                     
REMARK   3      T13:  -0.0172 T23:   0.1362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3431 L22:   2.1599                                     
REMARK   3      L33:   2.0259 L12:  -0.3139                                     
REMARK   3      L13:   0.1043 L23:  -1.3198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0709 S12:  -0.0302 S13:  -0.0328                       
REMARK   3      S21:   0.2200 S22:  -0.1243 S23:  -0.5053                       
REMARK   3      S31:   0.0133 S32:   0.4933 S33:   0.1951                       
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): 107.7010  36.4860  63.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1349 T22:  -0.1423                                     
REMARK   3      T33:  -0.2223 T12:  -0.0952                                     
REMARK   3      T13:  -0.0351 T23:   0.0818                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8617 L22:   2.3473                                     
REMARK   3      L33:   2.6343 L12:  -0.5417                                     
REMARK   3      L13:  -1.5973 L23:   0.0084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0981 S12:   0.1861 S13:  -0.0315                       
REMARK   3      S21:   0.0264 S22:  -0.2348 S23:   0.0456                       
REMARK   3      S31:   0.0357 S32:  -0.0262 S33:   0.1368                       
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): 106.8080  24.7820  63.4510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1385 T22:  -0.1783                                     
REMARK   3      T33:  -0.1466 T12:  -0.0658                                     
REMARK   3      T13:   0.0007 T23:   0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5632 L22:   1.6179                                     
REMARK   3      L33:   2.6445 L12:   0.1690                                     
REMARK   3      L13:  -0.7929 L23:  -1.1041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0140 S12:   0.1007 S13:  -0.2452                       
REMARK   3      S21:   0.0345 S22:  -0.1583 S23:  -0.1005                       
REMARK   3      S31:   0.2552 S32:  -0.1494 S33:   0.1443                       
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): 100.5390  13.2950  71.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0765 T22:  -0.1502                                     
REMARK   3      T33:  -0.0882 T12:  -0.1322                                     
REMARK   3      T13:   0.0536 T23:   0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8695 L22:   2.3561                                     
REMARK   3      L33:   2.4832 L12:  -0.2032                                     
REMARK   3      L13:  -0.1218 L23:   0.3641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0452 S12:   0.0949 S13:  -0.4164                       
REMARK   3      S21:  -0.0916 S22:  -0.0645 S23:  -0.0366                       
REMARK   3      S31:   0.2632 S32:  -0.2458 S33:   0.1097                       
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): 108.5830   7.4270  83.8650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0646 T22:  -0.1805                                     
REMARK   3      T33:   0.0388 T12:  -0.0823                                     
REMARK   3      T13:   0.0922 T23:   0.2006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1542 L22:   6.1962                                     
REMARK   3      L33:   5.6722 L12:  -0.9411                                     
REMARK   3      L13:  -0.5574 L23:   1.8602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1814 S12:  -0.3245 S13:  -0.5544                       
REMARK   3      S21:   0.5130 S22:  -0.0657 S23:   0.0302                       
REMARK   3      S31:   0.7186 S32:  -0.0028 S33:   0.2471                       
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): 111.4080   3.1730  78.2040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2222 T22:  -0.1487                                     
REMARK   3      T33:   0.0335 T12:   0.0237                                     
REMARK   3      T13:   0.0872 T23:   0.2292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9228 L22:   3.7809                                     
REMARK   3      L33:   4.2790 L12:  -0.7369                                     
REMARK   3      L13:  -0.9643 L23:   0.6676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1397 S12:  -0.0458 S13:  -0.4506                       
REMARK   3      S21:  -0.1773 S22:  -0.2443 S23:  -0.0388                       
REMARK   3      S31:   0.7635 S32:  -0.0476 S33:   0.3840                       
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): 125.1880   7.8710  79.6450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1834 T22:   0.0608                                     
REMARK   3      T33:   0.1523 T12:   0.1544                                     
REMARK   3      T13:   0.0393 T23:   0.3154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2717 L22:   1.0976                                     
REMARK   3      L33:   2.7013 L12:   0.2069                                     
REMARK   3      L13:  -0.7363 L23:  -0.2083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1113 S12:  -0.1350 S13:  -0.5132                       
REMARK   3      S21:   0.1389 S22:  -0.2413 S23:  -0.5665                       
REMARK   3      S31:   0.6239 S32:   0.6057 S33:   0.3526                       
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): 107.1150  21.1420 168.6460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0878 T22:   0.1867                                     
REMARK   3      T33:   0.1719 T12:   0.0182                                     
REMARK   3      T13:  -0.1511 T23:  -0.0653                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9026 L22:   2.8105                                     
REMARK   3      L33:   6.8766 L12:  -1.3309                                     
REMARK   3      L13:   1.8520 L23:  -2.1986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2105 S12:  -0.6439 S13:  -0.1235                       
REMARK   3      S21:   1.1271 S22:   0.3333 S23:  -0.0826                       
REMARK   3      S31:  -0.8495 S32:  -0.7197 S33:  -0.1228                       
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): 103.7000  29.7320 149.2830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8512 T22:   0.1488                                     
REMARK   3      T33:  -0.0191 T12:   0.1042                                     
REMARK   3      T13:   0.0239 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.9393 L22:  14.0434                                     
REMARK   3      L33:  43.5833 L12:  -8.3375                                     
REMARK   3      L13:  21.8542 L23: -20.6866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5208 S12:  -0.7923 S13:   0.1458                       
REMARK   3      S21:   1.5793 S22:   0.7725 S23:   0.3230                       
REMARK   3      S31:  -2.5266 S32:  -1.7268 S33:  -0.2517                       
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):  97.9310  38.4100 103.8160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2682 T22:   0.0084                                     
REMARK   3      T33:  -0.1174 T12:  -0.2419                                     
REMARK   3      T13:   0.0310 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2464 L22:   0.5425                                     
REMARK   3      L33:   3.8654 L12:  -0.1432                                     
REMARK   3      L13:  -0.1098 L23:  -1.2601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0364 S12:  -0.2941 S13:  -0.0669                       
REMARK   3      S21:   0.4870 S22:  -0.0583 S23:   0.0108                       
REMARK   3      S31:  -0.5066 S32:   0.0906 S33:   0.0220                       
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): 103.5310  34.6290  95.6250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0561 T22:  -0.0414                                     
REMARK   3      T33:  -0.1383 T12:  -0.1824                                     
REMARK   3      T13:  -0.0178 T23:   0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3934 L22:   1.4175                                     
REMARK   3      L33:   2.2015 L12:  -0.4453                                     
REMARK   3      L13:  -1.3438 L23:  -0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:  -0.3548 S13:   0.0643                       
REMARK   3      S21:   0.3429 S22:  -0.1101 S23:  -0.1166                       
REMARK   3      S31:  -0.1569 S32:   0.2642 S33:   0.0667                       
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): 100.6320  22.6850 130.3420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5076 T22:   0.2072                                     
REMARK   3      T33:   0.1591 T12:  -0.0764                                     
REMARK   3      T13:   0.0518 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1177 L22:   2.2141                                     
REMARK   3      L33:  20.5282 L12:  -1.5173                                     
REMARK   3      L13:   7.9754 L23:  -4.3130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6443 S12:   0.4708 S13:  -0.3131                       
REMARK   3      S21:  -0.1745 S22:   0.0185 S23:  -0.1677                       
REMARK   3      S31:   1.6315 S32:   0.5024 S33:  -0.6628                       
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): 109.8210  28.2090 148.5750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8908 T22:   0.0547                                     
REMARK   3      T33:   0.2229 T12:  -0.1159                                     
REMARK   3      T13:  -0.0965 T23:   0.0507                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2130 L22:   1.2904                                     
REMARK   3      L33:  16.2223 L12:  -0.6957                                     
REMARK   3      L13:   5.5377 L23:  -1.5236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3261 S12:   0.4965 S13:   0.2656                       
REMARK   3      S21:   0.8408 S22:   0.2831 S23:  -0.5380                       
REMARK   3      S31:  -1.6856 S32:   0.9687 S33:   0.0430                       
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): 119.6500  31.2620 182.6750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1005 T22:   1.2511                                     
REMARK   3      T33:   0.9544 T12:  -0.3300                                     
REMARK   3      T13:  -0.5227 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1875 L22:   1.8536                                     
REMARK   3      L33:   8.7346 L12:  -0.6510                                     
REMARK   3      L13:  -4.4473 L23:  -1.1780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1091 S12:  -1.9628 S13:   0.8840                       
REMARK   3      S21:   0.8878 S22:   0.1138 S23:  -1.2250                       
REMARK   3      S31:  -1.3855 S32:   2.8896 S33:   0.9953                       
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):  90.5150  37.1100  32.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1012 T22:  -0.0300                                     
REMARK   3      T33:  -0.0527 T12:  -0.2240                                     
REMARK   3      T13:  -0.0841 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7631 L22:  10.5748                                     
REMARK   3      L33:   9.3400 L12:  -8.7827                                     
REMARK   3      L13:   6.0039 L23:  -6.1561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2710 S12:   0.7987 S13:  -0.9500                       
REMARK   3      S21:  -0.3808 S22:  -0.0209 S23:   0.5736                       
REMARK   3      S31:   0.5936 S32:   0.1377 S33:  -0.2501                       
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):  94.6590  42.4740  40.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2448 T22:  -0.0867                                     
REMARK   3      T33:  -0.1817 T12:  -0.0519                                     
REMARK   3      T13:  -0.0048 T23:   0.0592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7059 L22:   1.3993                                     
REMARK   3      L33:   2.5079 L12:  -0.3533                                     
REMARK   3      L13:   0.6278 L23:  -0.0456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0235 S12:   0.0187 S13:  -0.0786                       
REMARK   3      S21:   0.0602 S22:   0.0609 S23:   0.2229                       
REMARK   3      S31:   0.1624 S32:  -0.2265 S33:  -0.0844                       
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):  94.4940  43.3160  43.0610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2045 T22:  -0.0776                                     
REMARK   3      T33:  -0.1746 T12:  -0.0707                                     
REMARK   3      T13:   0.0298 T23:   0.0591                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2980 L22:   1.0942                                     
REMARK   3      L33:   2.9671 L12:  -0.3585                                     
REMARK   3      L13:   1.3480 L23:  -0.7773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0631 S12:  -0.0347 S13:   0.2173                       
REMARK   3      S21:  -0.0140 S22:  -0.0022 S23:  -0.0036                       
REMARK   3      S31:   0.1608 S32:  -0.2704 S33:   0.0654                       
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):  86.8450  48.0480  12.5840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2198 T22:   0.1293                                     
REMARK   3      T33:  -0.0197 T12:  -0.1000                                     
REMARK   3      T13:  -0.0792 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0449 L22:   2.0594                                     
REMARK   3      L33:   4.6427 L12:  -1.1419                                     
REMARK   3      L13:  -0.3556 L23:   0.2789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1363 S12:   0.4371 S13:  -0.0933                       
REMARK   3      S21:  -0.1712 S22:  -0.2546 S23:   0.0922                       
REMARK   3      S31:  -0.3474 S32:  -0.3744 S33:   0.1183                       
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):  93.0590  45.2150   4.4020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0633 T22:   0.0349                                     
REMARK   3      T33:   0.0645 T12:   0.0880                                     
REMARK   3      T13:  -0.0303 T23:   0.0522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8200 L22:   0.8814                                     
REMARK   3      L33:  11.3175 L12:  -0.7058                                     
REMARK   3      L13:  -4.0960 L23:   2.8343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2447 S12:   0.4373 S13:  -0.4141                       
REMARK   3      S21:  -0.2231 S22:  -0.1889 S23:  -0.0897                       
REMARK   3      S31:   0.7652 S32:  -0.0498 S33:  -0.0558                       
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):  95.0420  47.9990   8.9230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0007 T22:  -0.0215                                     
REMARK   3      T33:  -0.1159 T12:   0.0905                                     
REMARK   3      T13:  -0.0442 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5528 L22:   1.9816                                     
REMARK   3      L33:  15.9061 L12:   1.6792                                     
REMARK   3      L13:  -3.9915 L23:  -0.6047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3456 S12:  -0.5333 S13:   0.2213                       
REMARK   3      S21:  -0.4204 S22:  -0.2084 S23:   0.0643                       
REMARK   3      S31:   0.4549 S32:   0.3780 S33:  -0.1372                       
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):  94.4800  41.0480  -4.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8198 T22:   0.2833                                     
REMARK   3      T33:   0.1518 T12:   0.2477                                     
REMARK   3      T13:   0.0072 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9617 L22:   3.4247                                     
REMARK   3      L33:   1.7704 L12:  -1.3183                                     
REMARK   3      L13:   1.2938 L23:   1.7552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2750 S12:   0.3984 S13:  -1.2056                       
REMARK   3      S21:  -0.3446 S22:  -0.6613 S23:  -0.0136                       
REMARK   3      S31:   0.8145 S32:   0.5732 S33:   0.3863                       
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):  86.6030  44.2030  -2.2430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1401 T22:   0.3192                                     
REMARK   3      T33:   0.1443 T12:   0.0455                                     
REMARK   3      T13:  -0.2251 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4750 L22:   6.4648                                     
REMARK   3      L33:  23.1076 L12:   6.2846                                     
REMARK   3      L13: -10.3215 L23:  -2.8090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2018 S12:   0.5481 S13:  -0.5947                       
REMARK   3      S21:  -1.0733 S22:   0.1217 S23:   0.6778                       
REMARK   3      S31:   1.3684 S32:  -1.0390 S33:   0.0800                       
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): 114.8860  50.6330  34.8420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2433 T22:  -0.0627                                     
REMARK   3      T33:  -0.0695 T12:   0.0312                                     
REMARK   3      T13:   0.0206 T23:   0.1525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9107 L22:   2.3350                                     
REMARK   3      L33:   6.3748 L12:   0.0216                                     
REMARK   3      L13:  -2.1006 L23:   1.8397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0884 S12:   0.1963 S13:   0.1455                       
REMARK   3      S21:  -0.1132 S22:  -0.0406 S23:  -0.0389                       
REMARK   3      S31:  -0.1329 S32:   0.3619 S33:  -0.0478                       
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): 114.2270  39.6750  35.8120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2451 T22:  -0.1093                                     
REMARK   3      T33:  -0.1654 T12:   0.0717                                     
REMARK   3      T13:  -0.0167 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4978 L22:   3.1030                                     
REMARK   3      L33:   2.4328 L12:   1.1665                                     
REMARK   3      L13:  -0.9176 L23:  -2.6462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:   0.3906 S13:  -0.3091                       
REMARK   3      S21:  -0.1364 S22:  -0.0271 S23:  -0.0959                       
REMARK   3      S31:   0.5094 S32:   0.0894 S33:  -0.1080                       
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): 112.9810  46.2130  35.2670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2454 T22:  -0.1343                                     
REMARK   3      T33:  -0.1267 T12:  -0.0050                                     
REMARK   3      T13:  -0.0466 T23:   0.0999                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1778 L22:   1.3949                                     
REMARK   3      L33:   3.1205 L12:  -0.5453                                     
REMARK   3      L13:  -2.0312 L23:  -0.4520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:   0.3796 S13:  -0.0023                       
REMARK   3      S21:  -0.0853 S22:  -0.0458 S23:   0.0195                       
REMARK   3      S31:   0.3116 S32:  -0.1002 S33:   0.0614                       
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): 100.9480  53.6840   7.8740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1510 T22:   0.2026                                     
REMARK   3      T33:  -0.0835 T12:   0.0293                                     
REMARK   3      T13:   0.0314 T23:   0.1054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1735 L22:   2.4344                                     
REMARK   3      L33:   5.7867 L12:  -1.4497                                     
REMARK   3      L13:   2.4174 L23:  -2.2656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4944 S12:   0.3350 S13:  -0.3131                       
REMARK   3      S21:  -0.2805 S22:  -0.2248 S23:   0.2381                       
REMARK   3      S31:   0.6417 S32:   0.2813 S33:  -0.2695                       
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): 102.1040  60.2780   8.5740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2120 T22:   0.2860                                     
REMARK   3      T33:  -0.1393 T12:   0.0109                                     
REMARK   3      T13:   0.0212 T23:   0.1055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8060 L22:   8.4501                                     
REMARK   3      L33:   3.3075 L12:  -5.3615                                     
REMARK   3      L13:   4.4004 L23:  -2.0685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0895 S12:  -0.3425 S13:   0.6247                       
REMARK   3      S21:   0.0447 S22:  -0.1484 S23:  -0.5572                       
REMARK   3      S31:   0.1363 S32:   0.2823 S33:   0.2379                       
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):  95.6180  60.6510   2.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2016 T22:   0.1759                                     
REMARK   3      T33:  -0.1957 T12:  -0.0230                                     
REMARK   3      T13:   0.0497 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3678 L22:   4.9817                                     
REMARK   3      L33:   3.6254 L12:  -4.6469                                     
REMARK   3      L13:   3.5673 L23:  -1.0830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0239 S12:   0.3217 S13:  -0.0162                       
REMARK   3      S21:  -0.3210 S22:  -0.1381 S23:  -0.0136                       
REMARK   3      S31:  -0.0503 S32:   0.3352 S33:   0.1621                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   198        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.4940  63.0850  -2.2930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0608 T22:   0.2465                                     
REMARK   3      T33:  -0.1685 T12:   0.1398                                     
REMARK   3      T13:   0.1358 T23:   0.1423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7744 L22:   7.2184                                     
REMARK   3      L33:   6.1378 L12:  -5.9583                                     
REMARK   3      L13:   1.4024 L23:  -4.6122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4725 S12:   1.6877 S13:  -0.3658                       
REMARK   3      S21:  -0.8299 S22:  -0.6015 S23:  -0.3561                       
REMARK   3      S31:  -0.1131 S32:   1.0988 S33:   0.1290                       
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 1TY6. 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 2VDN 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-34085.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A-1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9760                             
REMARK 200  MONOCHROMATOR                  : RH-COATED SI                       
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7                                  
REMARK 200  R MERGE                    (I) : 0.15                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1TXV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM            
REMARK 280  ACETATE, 0.1 M IMIDAZOLE, PH 6.5, VAPOR DIFFUSION, HANGING          
REMARK 280  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      117.12200            
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       58.56100            
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       58.56100            
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      117.12200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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  4043     O    HOH A  4101              1.88            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -119.60     52.38                                   
REMARK 500    LYS A 118     -127.86     52.43                                   
REMARK 500    GLU A 123      133.66     95.61                                   
REMARK 500    LEU A 212      -49.05     72.36                                   
REMARK 500    SER A 261       72.78     45.60                                   
REMARK 500    TYR A 353       17.68     59.36                                   
REMARK 500    THR B   7       42.63   -101.12                                   
REMARK 500    ARG B   8       68.57   -151.29                                   
REMARK 500    VAL B  10       77.26     37.18                                   
REMARK 500    PHE B  56       81.39   -158.61                                   
REMARK 500    ASP B  66       47.07   -142.34                                   
REMARK 500    ASP B  71     -168.73   -127.95                                   
REMARK 500    VAL B  80      108.09     70.77                                   
REMARK 500    ASN B 148       31.75    -96.85                                   
REMARK 500    VAL B 157      -84.50   -122.78                                   
REMARK 500    LEU B 196      109.93    -48.03                                   
REMARK 500    SER B 213     -151.33   -112.66                                   
REMARK 500    LEU B 258       -5.77     82.60                                   
REMARK 500    VAL B 275      -80.12   -105.97                                   
REMARK 500    LYS B 410      -32.04     74.84                                   
REMARK 500    GLU B 442       73.81     55.83                                   
REMARK 500    HIS B 446      -60.66     73.41                                   
REMARK 500    THR B 454      154.29     67.68                                   
REMARK 500    SER L  30       56.23     33.90                                   
REMARK 500    SER L  31        7.31     59.73                                   
REMARK 500    SER L  77       88.22     64.03                                   
REMARK 500    ASN L 212       76.54     52.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C   4   OD2                                                    
REMARK 620 2 HOH B4035   O   104.0                                              
REMARK 620 3 SER B 121   OG   87.0 169.0                                        
REMARK 620 4 SER B 123   OG   91.2  90.0  90.8                                  
REMARK 620 5 GLU B 220   OE1  91.6  94.2  84.3 174.3                            
REMARK 620 6 HOH B4005   O   166.8  88.4  80.8  84.0  92.2                      
REMARK 620 N                    1     2     3     4     5                       
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  49.1                                              
REMARK 620 3 ASP A 245   OD2 112.1  64.8                                        
REMARK 620 4 ASP A 247   O    87.2  77.3  92.7                                  
REMARK 620 5 THR A 250   C   102.6 149.0 145.3  90.4                            
REMARK 620 6 THR A 250   O    82.0 127.7 165.4  83.8  21.4                      
REMARK 620 7 THR A 250   OG1 157.0 141.4  86.8  78.7  59.9  78.6                
REMARK 620 8 GLU A 252   OE1  81.3  80.9  74.5 157.9 110.5 112.9 117.7          
REMARK 620 9 GLU A 252   OE2 125.5 126.1  80.2 146.9  78.5  95.0  68.7  49.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 299   OD1  86.7                                              
REMARK 620 3 ASP A 301   OD1  77.5  75.1                                        
REMARK 620 4 HOH A4124   O   153.7  90.1  76.4                                  
REMARK 620 5 ARG A 303   O    82.2 168.3  98.6  98.1                            
REMARK 620 6 ASP A 305   OD1 139.8  94.9 141.6  66.5  96.0                      
REMARK 620 7 ASP A 305   OD2  94.3  73.5 147.9 109.8 111.2  48.8                
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  70.8                                              
REMARK 620 3 TYR A 371   O    64.7  84.2                                        
REMARK 620 4 ASP A 367   OD1  83.7  87.9 148.3                                  
REMARK 620 5 ASP A 373   OD1  91.0 156.4 102.0  74.8                            
REMARK 620 6 ASP A 373   OD2 128.6 153.0  88.7 110.8  50.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 432   O                                                      
REMARK 620 2 ASN A 430   OD1  94.6                                              
REMARK 620 3 HOH A4138   O   133.5  85.1                                        
REMARK 620 4 ASP A 426   OD1  77.2  84.8 148.4                                  
REMARK 620 5 ASP A 428   OD1 151.0  87.4  75.5  74.1                            
REMARK 620 6 ASP A 434   OD1 106.6 158.6  82.5  96.8  72.7                      
REMARK 620 7 ASP A 434   OD2  85.0 139.1  67.0 134.1 112.0  48.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B1462   O1                                                     
REMARK 620 2 HOH B4040   O    70.0                                              
REMARK 620 3 ASP B 127   OD1 106.7 161.5                                        
REMARK 620 4 ASP B 251   OD2 107.3  76.9  87.1                                  
REMARK 620 5 SER B 123   O   155.1  85.3  97.8  68.9                            
REMARK 620 6 ASP B 126   OD1 124.3 117.7  79.6 128.4  64.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 162.4                                              
REMARK 620 3 ASN B 215   OD1  90.6 101.4                                        
REMARK 620 4 ASP B 217   OD1  73.5  93.7  88.7                                  
REMARK 620 5 PRO B 219   O    89.2  78.8 179.8  91.2                            
REMARK 620 6 GLU B 220   OE2  87.9 105.7  85.8 160.6  94.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPT C   1                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1462                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MK7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A                         
REMARK 900  CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,                            
REMARK 900  HHLGGAKQRGDV                                                        
REMARK 900 RELATED ID: 1M8O   RELATED DB: PDB                                   
REMARK 900  PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC                         
REMARK 900  DOMAIN                                                              
REMARK 900 RELATED ID: 1S4X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC                        
REMARK 900   DOMAIN IN DPCMICELLES                                              
REMARK 900 RELATED ID: 1UV9   RELATED DB: PDB                                   
REMARK 900  HOMOLOGY MODELING OF GPIIB                                          
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS                         
REMARK 900  AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO                        
REMARK 900  THE PLATELET RECEPTOR FORFIBRINOGEN                                 
REMARK 900 RELATED ID: 1S4W   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF                          
REMARK 900  INTEGRIN AIIB INDPC MICELLES                                        
REMARK 900 RELATED ID: 1MK9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1M1X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHA VBETA3 BOUND TO MN2+                              
REMARK 900 RELATED ID: 1RN0   RELATED DB: PDB                                   
REMARK 900  A REFINED THREE-DIMENSIONAL MODEL OF                                
REMARK 900  INTEGRIN AIIBB3                                                     
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-                            
REMARK 900  GLY-ASP LIGAND                                                      
REMARK 900 RELATED ID: 2VDM   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST TIROFIBAN                             
REMARK 900 RELATED ID: 1DPQ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CONSTITUTIVELY                            
REMARK 900  ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB                             
REMARK 900  CYTOPLASMIC DOMAIN.                                                 
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV                        
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV                           
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT                      
REMARK 900   OF INTEGRINALPHAVBETA3                                             
REMARK 900 RELATED ID: 1DPK   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN                        
REMARK 900  OF THE INTEGRIN ALPHA-IIB SUBUNIT                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO                           
REMARK 900  FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,                             
REMARK 900  LGGAKQRGDV                                                          
REMARK 900 RELATED ID: 2VDK   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1KUP   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 1KUZ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL                         
REMARK 900  REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS                            
REMARK 900 RELATED ID: 2VDL   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE                                                           
REMARK 900 RELATED ID: 1MIZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN                        
REMARK 900   CHIMERA                                                            
REMARK 900 RELATED ID: 1U8C   RELATED DB: PDB                                   
REMARK 900  A NOVEL ADAPTATION OF THE INTEGRIN PSI                              
REMARK 900  DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE                           
REMARK 900 RELATED ID: 1JX5   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE BETA-PROPELLER                             
REMARK 900  DOMAIN OF INTEGRINALPHAIIB                                          
REMARK 900 RELATED ID: 2VC2   RELATED DB: PDB                                   
REMARK 900  RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3                             
REMARK 900  HEADPIECE BOUND TO ANTAGONIST L-739758                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS             
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED             
REMARK 999 IN PLACE OF P08514.                                                  
DBREF  2VDN A    1   452  UNP    P08514   ITA2B_HUMAN     32    483             
DBREF  2VDN B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  2VDN C    2     7  PDB    2VDN     2VDN             2      7             
DBREF  2VDN H    1   221  PDB    2VDN     2VDN             1    221             
DBREF  2VDN L    1   214  PDB    2VDN     2VDN             1    214             
SEQADV 2VDN GLY A  282  UNP  P08514    ALA   313 CONFLICT SEE REMARK 999        
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 C    7  HRG GLY ASP TRP PRO CYS NH2                                  
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                                      
MODRES 2VDN HRG C    2  ARG  L-HOMOARGININE                                     
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3249      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    MAN  B3374      11                                                       
HET    MAN  B3375      11                                                       
HET    MAN  B3376      11                                                       
HET    MAN  B3377      11                                                       
HET    MPT  C   1       5                                                       
HET    HRG  C   2      12                                                       
HET    NH2  C   8       1                                                       
HET    GOL  A1453       6                                                       
HET    GOL  B1462       6                                                       
HETNAM     HRG L-HOMOARGININE                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MPT BETA-MERCAPTOPROPIONIC ACID                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   6  HRG    C7 H16 N4 O2 1+                                              
FORMUL   7   MG    MG 2+                                                        
FORMUL   8  NAG    7(C8 H15 N O6)                                               
FORMUL   9  MPT    C3 H6 O2 S                                                   
FORMUL  10  GOL    2(C3 H8 O3)                                                  
FORMUL  11  MAN    8(C6 H12 O6)                                                 
FORMUL  12  NH2    H2 N                                                         
FORMUL  13   CA    6(CA 2+)                                                     
FORMUL  14  HOH   *364(H2 O)                                                    
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LYS B   41  ASP B   47  1                                   7    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
HELIX   10  10 SER B  121  ASP B  126  5                                   6    
HELIX   11  11 ASP B  127  THR B  146  1                                  20    
HELIX   12  12 PRO B  169  GLU B  174  5                                   6    
HELIX   13  13 CYS B  177  LYS B  181  5                                   5    
HELIX   14  14 GLN B  199  GLN B  210  1                                  12    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 CYS B  232  GLY B  237  1                                   6    
HELIX   17  17 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   74  SER H   76  5                                   3    
HELIX   25  25 THR H   87  THR H   91  5                                   5    
HELIX   26  26 SER H  162  SER H  164  5                                   3    
HELIX   27  27 PRO H  206  SER H  209  5                                   4    
HELIX   28  28 ASP L   79  PHE L   83  5                                   5    
HELIX   29  29 SER L  121  GLY L  128  1                                   8    
HELIX   30  30 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 5 GLY A  63  GLN A  64  0                                        
SHEET    2  AA 5 THR A   9  ALA A  12  1  O  PHE A  10   N  GLY A  63           
SHEET    3  AA 5 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    4  AA 5 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    5  AA 5 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 3 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 3 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 3 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AD 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AD 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AD 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AE 4 SER A 172  VAL A 175  0                                        
SHEET    2  AE 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AE 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AE 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AF 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AF 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AF 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AF 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AG 4 VAL A 293  THR A 296  0                                        
SHEET    2  AG 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AG 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AG 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AH 2 MET A 314  ARG A 317  0                                        
SHEET    2  AH 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AI 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AI 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AI 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AI 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AJ 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AJ 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  LEU B  40  0                                        
SHEET    2  BA 3 CYS B  23  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BA 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BB 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 SER B 353  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  LEU B 389 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HB 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HB 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HC 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HD 4 SER H 126  LEU H 130  0                                        
SHEET    2  HD 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HD 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HD 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177 -1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 3 THR H 157  TRP H 160  0                                        
SHEET    2  HF 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HF 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 6 SER L  10  VAL L  13  0                                        
SHEET    2  LB 6 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 6 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 6 ILE L  33  GLN L  38 -1  O  GLY L  34   N  VAL L  89           
SHEET    5  LB 6 PHE L  44  TYR L  49 -1  O  MET L  45   N  GLN L  37           
SHEET    6  LB 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LC 4 SER L  10  VAL L  13  0                                        
SHEET    2  LC 4 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LC 4 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LC 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  LD 4 THR L 114  PHE L 118  0                                        
SHEET    2  LD 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LD 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LD 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LE 4 SER L 153  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  2.04  
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  2.04  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  15 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  16 CYS H  146    CYS H  201                          1555   1555  2.02  
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  1.45  
LINK         ND2 ASN A 249                 C1  NAG A3249     1555   1555  1.44  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.46  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.77  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  2.34  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.33  
LINK        CA    CA A2004                 C   THR A 250     1555   1555  3.13  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.46  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.52  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.56  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.63  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.34  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.24  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.41  
LINK        CA    CA A2005                 O   HOH A4124     1555   1555  2.30  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.27  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.54  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.75  
LINK        CA    CA A2006                 OD2 ASP A 365     1555   1555  2.79  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.43  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.38  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.70  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.40  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.32  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.39  
LINK        CA    CA A2007                 O   HOH A4138     1555   1555  2.22  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.60  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.46  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.26  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.71  
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                 OD2 ASP C   4     1555   1555  2.08  
LINK        MG    MG B2001                 O   HOH B4035     1555   1555  2.15  
LINK        MG    MG B2001                 O   HOH B4005     1555   1555  1.96  
LINK        MG    MG B2001                 OE1 GLU B 220     1555   1555  1.93  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.40  
LINK        MG    MG B2001                 OG  SER B 123     1555   1555  2.10  
LINK        CA    CA B2002                 O1  GOL B1462     1555   1555  3.05  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.30  
LINK        CA    CA B2002                 OD2 ASP B 251     1555   1555  2.54  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.69  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.70  
LINK        CA    CA B2002                 O   HOH B4040     1555   1555  2.25  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.27  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.34  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.16  
LINK        CA    CA B2003                 OE2 GLU B 220     1555   1555  2.36  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.51  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.37  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.45  
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  
LINK         SG  MPT C   1                 SG  CYS C   7     1555   1555  2.05  
LINK         C   MPT C   1                 N   HRG C   2     1555   1555  1.33  
LINK         C   HRG C   2                 N   GLY C   3     1555   1555  1.33  
LINK         C   CYS C   7                 N   NH2 C   8     1555   1555  1.33  
CISPEP   1 SER B   84    PRO B   85          0        -3.11                     
CISPEP   2 SER B  162    PRO B  163          0         6.20                     
CISPEP   3 SER B  168    PRO B  169          0       -11.09                     
CISPEP   4 PHE H  152    PRO H  153          0        -2.17                     
CISPEP   5 GLU H  154    PRO H  155          0         1.49                     
CISPEP   6 TRP H  194    PRO H  195          0         2.69                     
CISPEP   7 SER L    7    PRO L    8          0       -10.34                     
CISPEP   8 LEU L   94    PRO L   95          0        -0.51                     
CISPEP   9 TYR L  140    PRO L  141          0         1.17                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A4124                                          
SITE     1 AC3  5 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  5 ASP A 373                                                     
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4138                                          
SITE     1 AC5  3 ASN A  15  HOH A4002  HOH A4142                               
SITE     1 AC6  1 ASN A 249                                                     
SITE     1 AC7  6 SER B 121  SER B 123  GLU B 220  HOH B4005                    
SITE     2 AC7  6 HOH B4035  ASP C   4                                          
SITE     1 AC8  6 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC8  6 GOL B1462  HOH B4040                                          
SITE     1 AC9  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC9  5 GLU B 220                                                     
SITE     1 BC1  3 ASN B  99  HOH B4072  HOH B4073                               
SITE     1 BC2  5 LEU B 317  ASN B 320  NAG B3321  HOH B4074                    
SITE     2 BC2  5 HOH B4075                                                     
SITE     1 BC3  4 ARG A 281  NAG B3320  MAN B3322  HOH B4076                    
SITE     1 BC4  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC5  2 ARG A 281  MAN B3322                                          
SITE     1 BC6  1 MAN B3322                                                     
SITE     1 BC7  5 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC7  5 NAG B3372                                                     
SITE     1 BC8  5 NAG B3371  MAN B3373  MAN B3375  MAN B3376                    
SITE     2 BC8  5 HOH B4077                                                     
SITE     1 BC9  6 LEU A 332  SER A 344  NAG B3372  MAN B3374                    
SITE     2 BC9  6 MAN B3375  HOH B4077                                          
SITE     1 CC1  5 ASN A 299  LEU A 332  SER A 396  GLU A 397                    
SITE     2 CC1  5 MAN B3373                                                     
SITE     1 CC2  6 ALA A 342  PRO A 343  NAG B3372  MAN B3373                    
SITE     2 CC2  6 MAN B3376  MAN B3377                                          
SITE     1 CC3  6 PRO A 343  SER A 344  LEU A 345  LEU A 346                    
SITE     2 CC3  6 NAG B3372  MAN B3375                                          
SITE     1 CC4  1 MAN B3375                                                     
SITE     1 CC5  4 HRG C   2  GLY C   3  TRP C   5  CYS C   7                    
SITE     1 CC6  6 PHE A  87  ARG A  90  HIS A 112  LYS A 124                    
SITE     2 CC6  6 HOH A4043  HOH A4141                                          
SITE     1 CC7  7 ASP B 127  GLU B 312  ASN B 313   CA B2002                    
SITE     2 CC7  7 HOH B4061  HOH B4071  PRO H  14                               
CRYST1  149.593  149.593  175.683  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      0.006685  0.003859  0.000000        0.00000                         
SCALE2      0.000000  0.007719  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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