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Entry: 3ZDZ
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HEADER    CELL ADHESION/IMMUNE SYSTEM/PEPTIDE     03-DEC-12   3ZDZ              
TITLE     INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 32-488;                                           
COMPND   5 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 27-498;                                           
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 10E5 FAB HEAVY CHAIN;                                      
COMPND  15 CHAIN: H, E;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: 10E5 FAB LIGHT CHAIN;                                      
COMPND  19 CHAIN: L, F;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: RGD PEPTIDE;                                               
COMPND  23 CHAIN: I, J                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PEF1;                                      
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  24 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  26 MOL_ID: 4;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  28 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  29 ORGANISM_TAXID: 10090;                                               
SOURCE  30 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  31 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 SYNTHETIC: YES;                                                      
SOURCE  35 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  36 ORGANISM_COMMON: HUMAN;                                              
SOURCE  37 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM-PEPTIDE COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   2   10-JUL-13 3ZDZ    1       JRNL                                     
REVDAT   1   05-JUN-13 3ZDZ    0                                                
JRNL        AUTH   J.ZHU,J.ZHU,T.A.SPRINGER                                     
JRNL        TITL   COMPLETE INTEGRIN HEADPIECE OPENING IN EIGHT STEPS.          
JRNL        REF    J.CELL BIOL.                  V. 201  1053 2013              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   23798730                                                     
JRNL        DOI    10.1083/JCB.201212037                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.750                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.279                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.44                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.81                          
REMARK   3   NUMBER OF REFLECTIONS             : 102822                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1848                          
REMARK   3   R VALUE            (WORKING SET) : 0.1844                          
REMARK   3   FREE R VALUE                     : 0.2211                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1032                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.2863 -  5.2586    0.99    14888   153  0.1826 0.2427        
REMARK   3     2  5.2586 -  4.1747    1.00    14648   142  0.1321 0.1592        
REMARK   3     3  4.1747 -  3.6472    1.00    14552   141  0.1558 0.1694        
REMARK   3     4  3.6472 -  3.3138    1.00    14486   151  0.1846 0.2168        
REMARK   3     5  3.3138 -  3.0763    1.00    14383   155  0.2240 0.2629        
REMARK   3     6  3.0763 -  2.8950    1.00    14432   147  0.2651 0.2988        
REMARK   3     7  2.8950 -  2.7500    1.00    14401   143  0.2965 0.3386        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3   K_SOL              : 0.318                                         
REMARK   3   B_SOL              : 50.516                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.34             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.88            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20834                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 225                                     
REMARK   3   SOLVENT ATOMS            : 540                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.9                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.7084                                              
REMARK   3    B22 (A**2) : 2.8223                                               
REMARK   3    B33 (A**2) : -1.1139                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          21662                                  
REMARK   3   ANGLE     :  0.591          29341                                  
REMARK   3   CHIRALITY :  0.038           3275                                  
REMARK   3   PLANARITY :  0.002           3807                                  
REMARK   3   DIHEDRAL  : 13.273           7864                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 1:454 OR RESID 2004:2007)           
REMARK   3    ORIGIN FOR THE GROUP (A):  51.1004  89.9203  54.1631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3813 T22:  -0.0742                                     
REMARK   3      T33:   0.2208 T12:   0.0356                                     
REMARK   3      T13:   0.1297 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5190 L22:   1.3394                                     
REMARK   3      L33:   0.6940 L12:   0.0508                                     
REMARK   3      L13:  -0.0392 L23:   0.2036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:  -0.0542 S13:  -0.0748                       
REMARK   3      S21:   0.1568 S22:  -0.0986 S23:   0.2451                       
REMARK   3      S31:   0.1809 S32:  -0.1315 S33:  -0.0372                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 1:454 OR RESID 2004:2007)           
REMARK   3    ORIGIN FOR THE GROUP (A):  84.1156  85.9926 117.5764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4272 T22:   0.4585                                     
REMARK   3      T33:   0.1539 T12:   0.1378                                     
REMARK   3      T13:   0.2125 T23:   0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6129 L22:   0.8020                                     
REMARK   3      L33:   1.2436 L12:   0.0014                                     
REMARK   3      L13:  -0.3856 L23:   0.0676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2169 S12:   0.4418 S13:  -0.2184                       
REMARK   3      S21:  -0.3239 S22:  -0.0305 S23:  -0.2560                       
REMARK   3      S31:   0.4259 S32:   0.3139 S33:   0.0188                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 123.2410  86.9017  34.0174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7589 T22:   1.9328                                     
REMARK   3      T33:   1.2191 T12:   0.4717                                     
REMARK   3      T13:   0.0679 T23:  -0.1263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5276 L22:   4.2912                                     
REMARK   3      L33:   0.1263 L12:  -3.8907                                     
REMARK   3      L13:  -0.6676 L23:   0.7364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4052 S12:  -0.2764 S13:  -0.4696                       
REMARK   3      S21:   0.1412 S22:   0.2862 S23:  -1.3635                       
REMARK   3      S31:   0.3760 S32:   1.0490 S33:   0.1728                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 58:107 OR RESID 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A): 101.6129 106.2530  52.1734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2608 T22:   0.8060                                     
REMARK   3      T33:   0.7803 T12:   0.0742                                     
REMARK   3      T13:  -0.0597 T23:   0.0631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4800 L22:   3.5820                                     
REMARK   3      L33:   7.2056 L12:  -1.0065                                     
REMARK   3      L13:  -2.7098 L23:   3.3392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0038 S12:  -0.2222 S13:   0.3083                       
REMARK   3      S21:   0.0084 S22:   0.2218 S23:  -0.2462                       
REMARK   3      S31:   0.1364 S32:   1.2055 S33:  -0.2045                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 109:352 OR RESID                    
REMARK   3             : 2001:2003)                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  68.4779 117.4823  63.4869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3573 T22:  -0.0056                                     
REMARK   3      T33:   0.2288 T12:   0.0071                                     
REMARK   3      T13:   0.0949 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0114 L22:   2.2203                                     
REMARK   3      L33:   0.6796 L12:   0.2790                                     
REMARK   3      L13:  -0.0060 L23:   0.1460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0608 S12:  -0.1102 S13:   0.2048                       
REMARK   3      S21:   0.2643 S22:  -0.0173 S23:  -0.1591                       
REMARK   3      S31:  -0.2259 S32:   0.0567 S33:  -0.0095                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 433:466                              
REMARK   3    ORIGIN FOR THE GROUP (A): 115.6205  87.8736  18.4247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7460 T22:   1.8075                                     
REMARK   3      T33:   0.7230 T12:   0.4680                                     
REMARK   3      T13:   0.1232 T23:   0.1475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9259 L22:   2.0434                                     
REMARK   3      L33:   2.4324 L12:   0.7243                                     
REMARK   3      L13:  -2.4666 L23:  -2.0065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0540 S12:  -0.4284 S13:   0.1421                       
REMARK   3      S21:  -0.3688 S22:   0.0196 S23:  -0.8185                       
REMARK   3      S31:   0.5078 S32:   0.6929 S33:  -0.0776                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9280  71.0125 141.1803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9918 T22:   1.2339                                     
REMARK   3      T33:   1.1909 T12:  -0.5521                                     
REMARK   3      T13:   0.1713 T23:  -0.0973                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2500 L22:   1.9331                                     
REMARK   3      L33:   4.2491 L12:   1.2936                                     
REMARK   3      L13:  -3.9052 L23:  -1.3894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3333 S12:  -0.1026 S13:  -0.9847                       
REMARK   3      S21:   0.0303 S22:  -0.1576 S23:   1.1697                       
REMARK   3      S31:   1.0241 S32:  -1.0496 S33:   0.4555                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 58:107 OR RESID 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1553  87.6757 116.1529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7122 T22:   1.1484                                     
REMARK   3      T33:   0.6052 T12:  -0.4513                                     
REMARK   3      T13:  -0.1263 T23:   0.1224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6345 L22:   0.4046                                     
REMARK   3      L33:   7.0890 L12:  -0.4864                                     
REMARK   3      L13:   0.9580 L23:  -0.1045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3393 S12:   1.0455 S13:   0.1863                       
REMARK   3      S21:  -0.3550 S22:   0.3403 S23:   0.2327                       
REMARK   3      S31:   0.7123 S32:  -0.7904 S33:  -0.0013                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 109:352 OR RESID                    
REMARK   3             : 2001:2003)                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3925 102.3916  99.6952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4929 T22:   1.0962                                     
REMARK   3      T33:   0.3423 T12:  -0.1853                                     
REMARK   3      T13:  -0.0712 T23:   0.2840                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2269 L22:   0.5168                                     
REMARK   3      L33:   1.1485 L12:  -0.4341                                     
REMARK   3      L13:   0.4666 L23:  -0.2875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2143 S12:   1.0413 S13:   0.4134                       
REMARK   3      S21:  -0.3310 S22:   0.1825 S23:   0.1282                       
REMARK   3      S31:  -0.0542 S32:  -0.3675 S33:  -0.1283                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 433:471                              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6739  79.1476 155.0072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6880 T22:   0.6868                                     
REMARK   3      T33:   0.7957 T12:  -0.2764                                     
REMARK   3      T13:   0.1378 T23:  -0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1000 L22:   5.0933                                     
REMARK   3      L33:   7.1488 L12:   2.8084                                     
REMARK   3      L13:   3.0292 L23:   3.5333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0775 S12:  -0.1869 S13:  -1.0583                       
REMARK   3      S21:   0.4952 S22:   0.0258 S23:   0.4729                       
REMARK   3      S31:   1.1759 S32:  -1.2771 S33:  -0.0731                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1984  96.6882  83.0177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4500 T22:   0.6301                                     
REMARK   3      T33:   0.5436 T12:  -0.0444                                     
REMARK   3      T13:   0.2127 T23:  -0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9778 L22:   1.6506                                     
REMARK   3      L33:   2.4496 L12:  -0.1314                                     
REMARK   3      L13:  -1.6904 L23:  -0.9256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0574 S12:  -0.5515 S13:  -0.1230                       
REMARK   3      S21:   0.6783 S22:   0.0219 S23:   0.4002                       
REMARK   3      S31:   0.0355 S32:  -0.4921 S33:   0.0725                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0447  81.5059  93.1804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6517 T22:   0.7701                                     
REMARK   3      T33:   1.8206 T12:   0.0792                                     
REMARK   3      T13:   0.1768 T23:   0.3679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5065 L22:   0.2138                                     
REMARK   3      L33:   6.3187 L12:   0.7517                                     
REMARK   3      L13:   0.4799 L23:   0.9011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0691 S12:  -0.2645 S13:  -1.9428                       
REMARK   3      S21:   0.3386 S22:   0.1141 S23:  -0.0397                       
REMARK   3      S31:   1.1772 S32:  -0.0143 S33:  -0.1158                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8450  96.1192  64.6276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3330 T22:   0.8283                                     
REMARK   3      T33:   0.7372 T12:  -0.0058                                     
REMARK   3      T13:   0.1248 T23:  -0.1986                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3900 L22:   0.3709                                     
REMARK   3      L33:   0.7614 L12:   0.6408                                     
REMARK   3      L13:  -0.5702 L23:  -0.5150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0273 S12:   0.2453 S13:  -0.0935                       
REMARK   3      S21:   0.0315 S22:  -0.1612 S23:   0.8509                       
REMARK   3      S31:   0.1013 S32:  -0.8260 S33:   0.0383                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3530  93.5930  86.5755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3004 T22:   0.7594                                     
REMARK   3      T33:   1.0012 T12:  -0.0646                                     
REMARK   3      T13:   0.1653 T23:   0.1689                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8778 L22:   1.2198                                     
REMARK   3      L33:   2.4105 L12:   0.2428                                     
REMARK   3      L13:  -0.2074 L23:   0.5932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2435 S12:   0.0443 S13:  -0.9773                       
REMARK   3      S21:   0.1920 S22:   0.0127 S23:   0.2261                       
REMARK   3      S31:   0.3111 S32:  -0.2596 S33:   0.2465                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 114.6061  89.6378  85.6520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6936 T22:   1.7283                                     
REMARK   3      T33:   0.6586 T12:   0.1033                                     
REMARK   3      T13:   0.2189 T23:   0.1690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8783 L22:   0.7885                                     
REMARK   3      L33:   3.1613 L12:  -0.4170                                     
REMARK   3      L13:  -2.4111 L23:   0.7487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0104 S12:   1.0164 S13:   0.1247                       
REMARK   3      S21:  -0.3589 S22:   0.0034 S23:  -0.0950                       
REMARK   3      S31:   0.3050 S32:  -0.1039 S33:   0.2496                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 149.8281  81.6242  79.3824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8940 T22:   2.2299                                     
REMARK   3      T33:   0.9844 T12:   0.2578                                     
REMARK   3      T13:   0.2620 T23:   0.0884                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2115 L22:   3.5376                                     
REMARK   3      L33:   0.7416 L12:   0.4754                                     
REMARK   3      L13:  -0.9332 L23:   1.1390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2420 S12:   1.0058 S13:  -0.3493                       
REMARK   3      S21:  -0.9121 S22:   0.0156 S23:  -0.8827                       
REMARK   3      S31:  -0.2361 S32:   0.1763 S33:  -0.1923                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 125.1047  99.5332 101.9005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5154 T22:   1.5200                                     
REMARK   3      T33:   0.8326 T12:   0.0414                                     
REMARK   3      T13:   0.1465 T23:   0.2264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0000 L22:   2.5589                                     
REMARK   3      L33:   0.9276 L12:  -0.2706                                     
REMARK   3      L13:  -1.7377 L23:   0.2752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0763 S12:   0.0530 S13:   0.7098                       
REMARK   3      S21:  -0.1437 S22:   0.0619 S23:  -0.8695                       
REMARK   3      S31:   0.0533 S32:   0.7100 S33:  -0.0675                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 154.0354  97.5695  79.8483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9406 T22:   2.1444                                     
REMARK   3      T33:   1.3099 T12:   0.2346                                     
REMARK   3      T13:   0.4279 T23:   0.4093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8304 L22:   2.6726                                     
REMARK   3      L33:   0.6020 L12:   0.3682                                     
REMARK   3      L13:  -0.5779 L23:   0.9281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2104 S12:   0.7487 S13:   0.3757                       
REMARK   3      S21:  -1.1176 S22:  -0.0349 S23:  -0.9175                       
REMARK   3      S31:  -0.3507 S32:   0.6697 S33:  -0.2724                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54970.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE SI CRYSTAL                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102899                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.6                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3T3P                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM             
REMARK 280  SULFATE, 0.1 M TRIS-HCL, PH 8.9                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      129.81000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.23500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.81000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.23500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, I, B                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, E, C, D, J                         
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     ALA A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     GLU B   472                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLU D   472                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     GLY E   220                                                      
REMARK 465     PRO E   221                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 465     PRO J   497                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   61   CD                                                  
REMARK 480     ASP A  159   CG                                                  
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     GLU C   61   CD                                                  
REMARK 480     ARG C   90   CZ                                                  
REMARK 480     GLU D  171   CD                                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
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    LYS B   125     O    HOH B  4012              2.18            
REMARK 500   ND2  ASN B   371     C2   NAG B  3371              2.15            
REMARK 500   OE2  GLU C   243     O    ASP C   247              2.16            
REMARK 500   O    PRO D    68     O    HOH D  4002              2.15            
REMARK 500   O    HIS D   280     O    HOH D  4031              2.17            
REMARK 500   ND2  ASN D   371     C2   NAG D  3371              2.15            
REMARK 500   O    ARG L   155     O    HOH L  4011              2.19            
REMARK 500   O    HOH A  4014     O    HOH A  4026              2.17            
REMARK 500   O    HOH A  4028     O    HOH A  4030              2.17            
REMARK 500   O    HOH A  4054     O    HOH A  4088              2.14            
REMARK 500   O    HOH A  4060     O    HOH B  4103              2.16            
REMARK 500   O    HOH A  4067     O    HOH A  4157              2.05            
REMARK 500   O    HOH A  4070     O    HOH A  4172              2.07            
REMARK 500   O    HOH A  4097     O    HOH A  4251              2.16            
REMARK 500   O    HOH A  4135     O    HOH A  4168              2.11            
REMARK 500   O    HOH A  4168     O    HOH A  4207              2.19            
REMARK 500   O    HOH A  4179     O    HOH A  4180              2.13            
REMARK 500   O    HOH A  4229     O    HOH A  4234              2.10            
REMARK 500   O    HOH A  4232     O    HOH A  4233              1.95            
REMARK 500   O    HOH A  4232     O    HOH A  4234              2.17            
REMARK 500   O    HOH B  4015     O    HOH B  4088              2.01            
REMARK 500   O    HOH C  4028     O    HOH C  4044              2.19            
REMARK 500   O    HOH L  4013     O    HOH L  4014              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  4002     O    HOH A  4236     1556     2.10            
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    PRO A  40        4.59    -67.98                                   
REMARK 500    SER A 101     -132.48     57.92                                   
REMARK 500    LYS A 118     -114.67     61.72                                   
REMARK 500    GLU A 123      128.86    101.46                                   
REMARK 500    LEU A 212      -43.66     75.83                                   
REMARK 500    PRO A 337       91.00    -67.20                                   
REMARK 500    LEU B  33      -78.93    -46.61                                   
REMARK 500    ALA B  61       77.02   -165.69                                   
REMARK 500    ASP B  76      157.67     63.53                                   
REMARK 500    SER B  77       54.27    -91.93                                   
REMARK 500    GLN B 132      -75.49    -43.11                                   
REMARK 500    VAL B 157      -77.30   -128.67                                   
REMARK 500    SER B 213     -146.86   -108.74                                   
REMARK 500    LEU B 258       -5.20     88.79                                   
REMARK 500    HIS B 274       38.90   -141.53                                   
REMARK 500    SER B 334     -159.00   -116.76                                   
REMARK 500    SER B 337     -172.05    163.85                                   
REMARK 500    ASN B 339      125.64    166.16                                   
REMARK 500    LEU B 341        6.34    129.13                                   
REMARK 500    LEU B 343      -43.81    -19.13                                   
REMARK 500    LEU B 375      -85.65     52.21                                   
REMARK 500    ALA B 439       40.96    -86.19                                   
REMARK 500    GLN B 440       47.75   -177.45                                   
REMARK 500    ASN B 449       27.34     49.64                                   
REMARK 500    SER C 101     -136.84     55.71                                   
REMARK 500    LYS C 118     -109.39     65.65                                   
REMARK 500    GLU C 123      132.59     99.41                                   
REMARK 500    ALA C 198      136.76   -174.19                                   
REMARK 500    LEU C 212      -40.17     71.28                                   
REMARK 500    TRP C 235      108.97    -54.56                                   
REMARK 500    TRP C 262       71.43     54.68                                   
REMARK 500    THR C 263       29.43     49.13                                   
REMARK 500    THR D   7       30.30    -92.99                                   
REMARK 500    SER D  20      148.83   -171.61                                   
REMARK 500    ASP D  47       35.31    -95.29                                   
REMARK 500    PHE D  56       76.60   -151.56                                   
REMARK 500    LEU D  64      -78.23   -100.68                                   
REMARK 500    ASP D  66       67.85   -151.03                                   
REMARK 500    PRO D 111      153.03    -48.28                                   
REMARK 500    LEU D 120       40.84   -105.67                                   
REMARK 500    VAL D 157      -79.89   -132.82                                   
REMARK 500    CYS D 177       46.03    -99.05                                   
REMARK 500    LYS D 181       42.78    -93.88                                   
REMARK 500    VAL D 193      -72.35    -96.00                                   
REMARK 500    LYS D 209       31.81    -98.29                                   
REMARK 500    SER D 213     -158.81   -114.89                                   
REMARK 500    ARG D 216      -62.18    -99.70                                   
REMARK 500    CYS D 232       76.67   -101.29                                   
REMARK 500    LYS D 253      170.29    -57.02                                   
REMARK 500    LEU D 258       -8.48     83.03                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      77 RAMACHANDRAN OUTLIERS.                        
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                              MN B2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 220   OE2                                                    
REMARK 620 2 ASP I 495   OD1  96.4                                              
REMARK 620 3 HOH B4010   O    82.0  97.0                                        
REMARK 620 4 SER B 123   OG  172.4  84.0  90.4                                  
REMARK 620 5 HOH B4009   O   101.5 162.1  85.8  78.3                            
REMARK 620 6 SER B 121   OG   92.1  97.8 164.5  95.4  81.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 251   OD2                                                    
REMARK 620 2 HOH B4015   O   109.0                                              
REMARK 620 3 SER B 123   O    77.1 165.2                                        
REMARK 620 4 ASP B 126   OD1 146.8  99.2  71.5                                  
REMARK 620 5 ASP B 127   OD2  97.8  74.6  91.4  72.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1  99.5                                              
REMARK 620 3 ASP B 217   OD1  97.7  86.9                                        
REMARK 620 4 PRO B 219   O    82.0 171.3 101.5                                  
REMARK 620 5 GLU B 220   OE1  89.9  87.5 171.3  83.8                            
REMARK 620 6 ASP B 217   O   165.2  90.4  71.6  90.0 101.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D4022   O                                                      
REMARK 620 2 SER D 121   OG  151.8                                              
REMARK 620 3 HOH D4010   O    64.6  89.3                                        
REMARK 620 4 GLU D 220   OE2  85.2 108.5  94.3                                  
REMARK 620 5 ASP J 495   OD1 113.6  82.6 148.2 117.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 127   OD1                                                    
REMARK 620 2 MET D 335   O    87.7                                              
REMARK 620 3 ASP D 126   OD1  63.1  99.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 220   OE1                                                    
REMARK 620 2 ASP D 217   O   106.5                                              
REMARK 620 3 PRO D 219   O    82.8  94.6                                        
REMARK 620 4 ASP D 158   OD2  87.7 164.6  81.2                                  
REMARK 620 5 ASN D 215   OD1  96.0  84.1 177.9 100.5                            
REMARK 620 6 ASP D 217   OD1 173.1  77.3 102.8  89.1  78.6                      
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 THR A 250   O                                                      
REMARK 620 2 GLU A 243   OE1  70.8                                              
REMARK 620 3 GLU A 243   OE2 124.7  54.1                                        
REMARK 620 4 ASP A 245   OD1 169.0 113.5  59.6                                  
REMARK 620 5 ASP A 247   O    90.7  77.5  74.0  80.7                            
REMARK 620 6 GLU A 252   OE1 105.1  84.5  76.7  85.6 150.7                      
REMARK 620 7 ASP A 245   OD2 132.1 156.9 102.8  43.4  96.7  90.7                
REMARK 620 8 THR A 250   OG1  82.7 141.8 138.9  88.5  75.7 129.8  54.2          
REMARK 620 9 GLU A 252   OE2  85.8 125.7 129.0  98.8 153.1  54.6  67.1  77.3    
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 ARG A 303   O                                                      
REMARK 620 2 ASP A 297   OD1  79.5                                              
REMARK 620 3 ASN A 299   OD1 153.3  74.6                                        
REMARK 620 4 ASP A 301   OD1  90.8  74.9  76.1                                  
REMARK 620 5 ASP A 305   OD1  90.5 132.9 112.0 151.8                            
REMARK 620 6 ASP A 305   OD2  93.4  82.3  89.9 155.7  52.2                      
REMARK 620 7 HOH A4176   O   107.7 152.9  92.7  78.8  73.9 122.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD1                                                    
REMARK 620 2 ASP A 367   OD1  80.8                                              
REMARK 620 3 ASP A 369   OD1  77.1  80.4                                        
REMARK 620 4 TYR A 371   O    68.8 149.3  89.3                                  
REMARK 620 5 ASP A 373   OD1 136.8 113.6 143.3  91.9                            
REMARK 620 6 ASP A 373   OD2  88.1  91.3 163.9  91.1  52.8                      
REMARK 620 7 HOH A4211   O   150.2  98.0  73.4 106.6  71.2 121.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 430   OD1                                                    
REMARK 620 2 ASP A 428   OD1  85.3                                              
REMARK 620 3 ASP A 426   OD1  89.0  70.0                                        
REMARK 620 4 TYR A 432   O    86.2 150.6  81.7                                  
REMARK 620 5 ASP A 434   OD2 172.0  92.6  83.0  91.9                            
REMARK 620 6 HOH A4245   O    78.8  77.8 146.4 127.8 108.3                      
REMARK 620 7 ASP A 434   OD1 133.4 118.7 135.3  87.1  54.2  69.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 252   OE1                                                    
REMARK 620 2 ASP C 245   OD1  66.3                                              
REMARK 620 3 ASP C 247   O   138.6  81.7                                        
REMARK 620 4 THR C 250   OG1 126.3  85.1  73.0                                  
REMARK 620 5 GLU C 243   OE2  87.2  64.1  54.3 120.8                            
REMARK 620 6 THR C 250   O   126.1 167.4  88.1  84.8 115.2                      
REMARK 620 7 GLU C 252   OE2  55.0  79.5 145.2  76.5 136.3 105.5                
REMARK 620 8 GLU C 243   OE1  84.9 113.5  84.6 148.7  55.5  72.5 129.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASN C 299   OD1  74.9                                              
REMARK 620 3 ASP C 301   OD1  72.1  72.3                                        
REMARK 620 4 ARG C 303   O    91.5 165.2  98.1                                  
REMARK 620 5 ASP C 305   OD1 144.7 101.3 141.2  93.2                            
REMARK 620 6 ASP C 305   OD2  93.2  86.6 156.7 100.3  51.6                      
REMARK 620 7 HOH C4050   O   147.9  77.4  84.4 113.6  57.2 101.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 373   OD1                                                    
REMARK 620 2 HOH C4068   O    74.2                                              
REMARK 620 3 ASP C 365   OD1 137.4 141.5                                        
REMARK 620 4 ASP C 367   OD1 125.7  92.5  83.5                                  
REMARK 620 5 ASP C 369   OD1 145.9  75.6  66.8  70.8                            
REMARK 620 6 TYR C 371   O    80.0 103.6  70.4 153.0  92.2                      
REMARK 620 7 ASP C 373   OD2  54.0 114.4 103.8  88.7 157.9 103.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 426   OD1                                                    
REMARK 620 2 ASN C 430   OD1  83.8                                              
REMARK 620 3 TYR C 432   O    81.6  86.7                                        
REMARK 620 4 ASP C 428   OD1  65.3  79.5 145.1                                  
REMARK 620 5 ASP C 434   OD1 140.5 135.3  93.4 118.8                            
REMARK 620 6 ASP C 434   OD2  88.1 165.1 104.6  85.7  55.1                      
REMARK 620 7 HOH C4089   O   148.8  74.4 118.4  88.6  66.4 107.6                
REMARK 620 N                    1     2     3     4     5     6                 
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  MN B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1456                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L1215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1454                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B3099  BOUND TO ASN B  99                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B3320  THROUGH MAN B3324  BOUND TO ASN B 320           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B3371  THROUGH NAG B3372  BOUND TO ASN B 371           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG D3099  BOUND TO ASN D  99                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG D3320  THROUGH MAN D3323  BOUND TO ASN D 320           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG D3371  THROUGH NAG D3372  BOUND TO ASN D 371           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZDX   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZDY   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZE0   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZE1   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZE2   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
DBREF  3ZDZ A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDZ B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDZ C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDZ D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDZ E    1   221  PDB    3ZDZ     3ZDZ             1    221             
DBREF  3ZDZ F    1   214  PDB    3ZDZ     3ZDZ             1    214             
DBREF  3ZDZ H    1   221  PDB    3ZDZ     3ZDZ             1    221             
DBREF  3ZDZ I  492   497  PDB    3ZDZ     3ZDZ           492    497             
DBREF  3ZDZ J  492   497  PDB    3ZDZ     3ZDZ           492    497             
DBREF  3ZDZ L    1   214  PDB    3ZDZ     3ZDZ             1    214             
SEQRES   1 A  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  457  ALA SER                                                      
SEQRES   1 C  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  457  ALA SER                                                      
SEQRES   1 B  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  472  SER GLN CYS GLU                                              
SEQRES   1 D  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  472  SER GLN CYS GLU                                              
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 E  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  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                                      
SEQRES   1 F  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 F  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 F  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 F  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 F  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 F  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 F  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 F  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 F  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 F  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 F  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 F  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 F  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 F  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 F  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 F  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 F  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 I    6  GLY ARG GLY ASP SER PRO                                      
SEQRES   1 J    6  GLY ARG GLY ASP SER PRO                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     MN  B2001       1                                                       
HET     MN  B2002       1                                                       
HET     MN  B2003       1                                                       
HET    NAG  B3099      27                                                       
HET    NAG  B3320      26                                                       
HET    NAG  B3321      26                                                       
HET    BMA  B3322      19                                                       
HET    MAN  B3323      21                                                       
HET    MAN  B3324      21                                                       
HET    NAG  B3371      26                                                       
HET    NAG  B3372      27                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET     MN  D2001       1                                                       
HET     MN  D2002       1                                                       
HET     MN  D2003       1                                                       
HET    NAG  D3099      27                                                       
HET    NAG  D3320      26                                                       
HET    NAG  D3321      26                                                       
HET    BMA  D3322      20                                                       
HET    MAN  D3323      21                                                       
HET    NAG  D3371      26                                                       
HET    NAG  D3372      27                                                       
HET    SO4  A1456       5                                                       
HET    SO4  L1215       5                                                       
HET    SO4  C1454       5                                                       
HET     CL  C1455       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5   MN    6(MN 2+)                                                     
FORMUL   6  SO4    3(O4 S 2-)                                                   
FORMUL   7   CL    CL 1-                                                        
FORMUL   8   CA    8(CA 2+)                                                     
FORMUL   9  MAN    3(C6 H12 O6)                                                 
FORMUL  10  BMA    2(C6 H12 O6)                                                 
FORMUL  11  NAG    10(C8 H15 N O6)                                              
FORMUL  12  HOH   *540(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 ASN B    3  ARG B    8  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LEU B   40  LYS B   46  1                                   7    
HELIX   10  10 ALA B   50  GLU B   52  5                                   3    
HELIX   11  11 SER B  121  GLN B  132  5                                  12    
HELIX   12  12 ASN B  133  GLN B  141  1                                   9    
HELIX   13  13 PRO B  169  ASN B  175  1                                   7    
HELIX   14  14 GLN B  199  LYS B  208  1                                  10    
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 GLN B  342  ARG B  352  1                                  11    
HELIX   21  21 CYS B  435  ALA B  441  5                                   7    
HELIX   22  22 LEU C  151  ASN C  158  1                                   8    
HELIX   23  23 GLY C  187  LEU C  192  1                                   6    
HELIX   24  24 VAL C  200  TYR C  207  1                                   8    
HELIX   25  25 ASN C  227  PHE C  231  5                                   5    
HELIX   26  26 THR C  259  LEU C  264  1                                   6    
HELIX   27  27 TYR C  440  ALA C  442  5                                   3    
HELIX   28  28 CYS D    5  GLY D    9  5                                   5    
HELIX   29  29 SER D   12  ALA D   18  1                                   7    
HELIX   30  30 LEU D   40  ASP D   47  1                                   8    
HELIX   31  31 ALA D   50  GLU D   52  5                                   3    
HELIX   32  32 TYR D  122  LYS D  125  5                                   4    
HELIX   33  33 ASP D  126  ILE D  131  1                                   6    
HELIX   34  34 ASN D  133  ARG D  143  1                                  11    
HELIX   35  35 PRO D  169  ASN D  175  1                                   7    
HELIX   36  36 GLN D  199  LYS D  208  1                                  10    
HELIX   37  37 GLY D  221  CYS D  232  1                                  12    
HELIX   38  38 CYS D  232  GLY D  237  1                                   6    
HELIX   39  39 LEU D  258  GLY D  264  5                                   7    
HELIX   40  40 SER D  282  THR D  286  5                                   5    
HELIX   41  41 SER D  291  LYS D  302  1                                  12    
HELIX   42  42 GLU D  312  GLU D  323  1                                  12    
HELIX   43  43 ASN D  339  ARG D  352  1                                  14    
HELIX   44  44 CYS D  435  ALA D  441  5                                   7    
HELIX   45  45 ASN E   28  THR E   32  5                                   5    
HELIX   46  46 SER E  162  SER E  164  5                                   3    
HELIX   47  47 ASP F   79  PHE F   83  5                                   5    
HELIX   48  48 SER F  121  THR F  126  1                                   6    
HELIX   49  49 LYS F  183  GLU F  187  1                                   5    
HELIX   50  50 ASN H   28  THR H   32  5                                   5    
HELIX   51  51 THR H   87  THR H   91  5                                   5    
HELIX   52  52 ASP L   79  PHE L   83  5                                   5    
HELIX   53  53 SER L  121  GLY L  128  1                                   8    
HELIX   54  54 LYS L  183  ARG L  188  1                                   6    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 4 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4  AB 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1  AC 4 GLU A  75  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 GLU A  75  VAL A  79  0                                        
SHEET    2  AD 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AD 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AD 4 THR A 125  PRO A 126 -1  O  THR A 125   N  TRP A 113           
SHEET    1  AE 2 GLU A 120  GLU A 121  0                                        
SHEET    2  AE 2 HIS A 112  GLU A 117  1  O  GLU A 117   N  GLU A 120           
SHEET    1  AF 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AF 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AF 4 SER A 129  GLN A 134 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AF 4 ARG A 139  TYR A 143 -1  O  ARG A 139   N  GLN A 134           
SHEET    1  AG 4 SER A 172  VAL A 175  0                                        
SHEET    2  AG 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AG 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AG 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AH 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AH 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AH 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AH 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AI 4 VAL A 293  THR A 296  0                                        
SHEET    2  AI 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AI 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AI 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AJ 2 MET A 314  ARG A 317  0                                        
SHEET    2  AJ 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AK 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AK 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AK 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AK 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AL 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AL 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  ASP B  39  0                                        
SHEET    2  BA 3 ALA B  24  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 LYS B 354  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  MET B 387 -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  CYS B 374 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 GLU B 378  PRO B 381 -1  O  GLU B 378   N  CYS B 374           
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 ILE B 304  VAL B 310  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1  BE 2 GLY B 453  GLU B 456  0                                        
SHEET    2  BE 2 VAL B 459  CYS B 462 -1  O  VAL B 459   N  GLU B 456           
SHEET    1  CA 4 THR C   9  ALA C  12  0                                        
SHEET    2  CA 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3  CA 4 ASP C 434  ALA C 439 -1  O  LEU C 435   N  TYR C 448           
SHEET    4  CA 4 SER C 420  VAL C 425 -1  O  SER C 420   N  GLY C 438           
SHEET    1  CB 4 LEU C  23  LYS C  27  0                                        
SHEET    2  CB 4 VAL C  33  GLY C  38 -1  O  ALA C  34   N  HIS C  26           
SHEET    3  CB 4 VAL C  53  PRO C  57 -1  O  PHE C  54   N  VAL C  37           
SHEET    4  CB 4 SER C  67  LEU C  68 -1  O  LEU C  68   N  VAL C  53           
SHEET    1  CC 4 THR C  76  VAL C  79  0                                        
SHEET    2  CC 4 GLN C  82  PHE C  87 -1  O  GLN C  82   N  VAL C  79           
SHEET    3  CC 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4  CC 4 GLU C 120  GLU C 121  1  O  GLU C 120   N  GLU C 117           
SHEET    1  CD 4 THR C  76  VAL C  79  0                                        
SHEET    2  CD 4 GLN C  82  PHE C  87 -1  O  GLN C  82   N  VAL C  79           
SHEET    3  CD 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4  CD 4 THR C 125  PRO C 126 -1  O  THR C 125   N  TRP C 113           
SHEET    1  CE 2 GLU C 120  GLU C 121  0                                        
SHEET    2  CE 2 HIS C 112  GLU C 117  1  O  GLU C 117   N  GLU C 120           
SHEET    1  CF 4 VAL C  97  TRP C 100  0                                        
SHEET    2  CF 4 VAL C 103  ALA C 108 -1  O  VAL C 103   N  TRP C 100           
SHEET    3  CF 4 SER C 129  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4  CF 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1  CG 4 SER C 172  VAL C 175  0                                        
SHEET    2  CG 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3  CG 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4  CG 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1  CH 4 VAL C 239  GLY C 242  0                                        
SHEET    2  CH 4 GLU C 252  ALA C 257 -1  O  GLU C 252   N  GLY C 242           
SHEET    3  CH 4 ALA C 266  LEU C 270 -1  O  ALA C 266   N  ALA C 257           
SHEET    4  CH 4 ARG C 276  ARG C 281 -1  N  LEU C 277   O  ILE C 269           
SHEET    1  CI 4 VAL C 293  THR C 296  0                                        
SHEET    2  CI 4 ASP C 305  ALA C 310 -1  O  ASP C 305   N  THR C 296           
SHEET    3  CI 4 ARG C 327  PHE C 331 -1  O  ARG C 327   N  ALA C 310           
SHEET    4  CI 4 LEU C 345  THR C 348 -1  O  LEU C 345   N  LEU C 330           
SHEET    1  CJ 2 MET C 314  ARG C 317  0                                        
SHEET    2  CJ 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1  CK 4 ILE C 360  GLY C 364  0                                        
SHEET    2  CK 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  LEU C 363           
SHEET    3  CK 4 GLN C 388  PHE C 392 -1  O  GLN C 388   N  ALA C 378           
SHEET    4  CK 4 GLN C 405  ASP C 408 -1  O  GLN C 405   N  VAL C 391           
SHEET    1  CL 2 GLY C 394  GLN C 395  0                                        
SHEET    2  CL 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1  DA 3 CYS D  38  ASP D  39  0                                        
SHEET    2  DA 3 ALA D  24  CYS D  26 -1  O  ALA D  24   N  ASP D  39           
SHEET    3  DA 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  DB 6 ALA D  61  GLU D  65  0                                        
SHEET    2  DB 6 ARG D  87  LEU D  92 -1  O  ARG D  87   N  LEU D  64           
SHEET    3  DB 6 LEU D 425  PHE D 431  1  O  ILE D 426   N  ILE D  88           
SHEET    4  DB 6 GLU D 411  PRO D 418 -1  O  LYS D 412   N  VAL D 429           
SHEET    5  DB 6 LYS D 354  ARG D 360 -1  O  GLU D 358   N  LYS D 417           
SHEET    6  DB 6 SER D 385  MET D 387 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  DC 5 VAL D  83  SER D  84  0                                        
SHEET    2  DC 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  DC 5 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    4  DC 5 PHE D 370  THR D 373 -1  O  ASN D 371   N  SER D 398           
SHEET    5  DC 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  DD 4 VAL D  83  SER D  84  0                                        
SHEET    2  DD 4 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  DD 4 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    4  DD 4 LEU D 366  SER D 367  1  O  SER D 367   N  LYS D 402           
SHEET    1  DE 6 TYR D 190  THR D 197  0                                        
SHEET    2  DE 6 LEU D 149  PHE D 156 -1  O  ILE D 151   N  THR D 197           
SHEET    3  DE 6 VAL D 112  ASP D 119  1  O  VAL D 112   N  ARG D 150           
SHEET    4  DE 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  DE 6 ASN D 305  THR D 311  1  O  ASN D 305   N  LEU D 246           
SHEET    6  DE 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  DF 2 GLY D 453  GLU D 456  0                                        
SHEET    2  DF 2 VAL D 459  CYS D 462 -1  O  VAL D 459   N  GLU D 456           
SHEET    1  EA 4 GLN E   3  GLN E   6  0                                        
SHEET    2  EA 4 VAL E  18  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3  EA 4 THR E  78  LEU E  83 -1  O  ALA E  79   N  CYS E  22           
SHEET    4  EA 4 ALA E  68  ASP E  73 -1  O  THR E  69   N  GLN E  82           
SHEET    1  EB 4 GLU E  10  VAL E  12  0                                        
SHEET    2  EB 4 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  EB 4 ALA E  92  ARG E  98 -1  O  ALA E  92   N  VAL E 115           
SHEET    4  EB 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1  EC 6 GLU E  10  VAL E  12  0                                        
SHEET    2  EC 6 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  EC 6 ALA E  92  ARG E  98 -1  O  ALA E  92   N  VAL E 115           
SHEET    4  EC 6 VAL E  34  ARG E  40 -1  O  HIS E  35   N  VAL E  97           
SHEET    5  EC 6 GLY E  44  ILE E  51 -1  O  GLY E  44   N  ARG E  40           
SHEET    6  EC 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1  ED 2 TYR E 108  TRP E 109  0                                        
SHEET    2  ED 2 ALA E  92  ARG E  98 -1  O  ARG E  98   N  TYR E 108           
SHEET    1  EE 4 SER E 126  LEU E 130  0                                        
SHEET    2  EE 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  EE 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  GLY E 150           
SHEET    4  EE 4 VAL E 175  GLN E 177  1  O  VAL E 175   N  THR E 182           
SHEET    1  EF 4 SER E 126  LEU E 130  0                                        
SHEET    2  EF 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  EF 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  GLY E 150           
SHEET    4  EF 4 VAL E 169  THR E 171 -1  O  HIS E 170   N  SER E 186           
SHEET    1  EG 2 VAL E 175  GLN E 177  0                                        
SHEET    2  EG 2 LEU E 180  THR E 190  1  O  LEU E 180   N  GLN E 177           
SHEET    1  EH 3 THR E 157  TRP E 160  0                                        
SHEET    2  EH 3 THR E 200  ALA E 204 -1  O  ASN E 202   N  THR E 159           
SHEET    3  EH 3 LYS E 211  LYS E 215 -1  O  VAL E 212   N  VAL E 203           
SHEET    1  FA 4 MET F   4  SER F   7  0                                        
SHEET    2  FA 4 VAL F  19  ALA F  25 -1  O  THR F  22   N  SER F   7           
SHEET    3  FA 4 ASP F  70  ILE F  75 -1  O  TYR F  71   N  CYS F  23           
SHEET    4  FA 4 PHE F  62  SER F  67 -1  O  SER F  63   N  THR F  74           
SHEET    1  FB 4 SER F  10  VAL F  13  0                                        
SHEET    2  FB 4 THR F 102  ILE F 106  1  O  LYS F 103   N  MET F  11           
SHEET    3  FB 4 ASP F  85  GLN F  90 -1  O  TYR F  86   N  THR F 102           
SHEET    4  FB 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1  FC 6 SER F  10  VAL F  13  0                                        
SHEET    2  FC 6 THR F 102  ILE F 106  1  O  LYS F 103   N  MET F  11           
SHEET    3  FC 6 ASP F  85  GLN F  90 -1  O  TYR F  86   N  THR F 102           
SHEET    4  FC 6 ILE F  33  GLN F  38 -1  O  GLY F  34   N  VAL F  89           
SHEET    5  FC 6 PHE F  44  TYR F  49 -1  O  MET F  45   N  GLN F  37           
SHEET    6  FC 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1  FD 2 THR F  97  PHE F  98  0                                        
SHEET    2  FD 2 ASP F  85  GLN F  90 -1  O  GLN F  90   N  THR F  97           
SHEET    1  FE 4 THR F 114  PHE F 118  0                                        
SHEET    2  FE 4 GLY F 129  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3  FE 4 TYR F 173  THR F 182 -1  O  TYR F 173   N  PHE F 139           
SHEET    4  FE 4 VAL F 159  TRP F 163 -1  O  LEU F 160   N  THR F 178           
SHEET    1  FF 4 SER F 153  ARG F 155  0                                        
SHEET    2  FF 4 ASN F 145  ILE F 150 -1  O  TRP F 148   N  ARG F 155           
SHEET    3  FF 4 SER F 191  THR F 197 -1  O  THR F 193   N  LYS F 149           
SHEET    4  FF 4 ILE F 205  ASN F 210 -1  O  ILE F 205   N  ALA F 196           
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 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HC 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HC 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HC 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HD 2 TYR H 108  TRP H 109  0                                        
SHEET    2  HD 2 ALA H  92  ARG H  98 -1  O  ARG H  98   N  TYR H 108           
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 TYR H 181  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  LEU H 176  1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 4 SER H 126  LEU H 130  0                                        
SHEET    2  HF 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HF 4 TYR H 181  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HF 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HG 2 VAL H 175  LEU H 176  0                                        
SHEET    2  HG 2 TYR H 181  THR H 190  1  O  THR H 182   N  VAL H 175           
SHEET    1  HH 3 THR H 157  TRP H 160  0                                        
SHEET    2  HH 3 THR H 200  ALA H 204 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HH 3 ASP H 213  LYS H 215 -1  O  LYS H 214   N  CYS H 201           
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 4 SER L  10  VAL L  13  0                                        
SHEET    2  LB 4 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 4 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  LC 6 SER L  10  VAL L  13  0                                        
SHEET    2  LC 6 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LC 6 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LC 6 ILE L  33  GLN L  38 -1  O  GLY L  34   N  VAL L  89           
SHEET    5  LC 6 PHE L  44  TYR L  49 -1  O  MET L  45   N  GLN L  37           
SHEET    6  LC 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LD 2 THR L  97  PHE L  98  0                                        
SHEET    2  LD 2 ASP L  85  GLN L  90 -1  O  GLN L  90   N  THR L  97           
SHEET    1  LE 4 THR L 114  PHE L 118  0                                        
SHEET    2  LE 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LE 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LE 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LF 4 SER L 153  ARG L 155  0                                        
SHEET    2  LF 4 ILE L 144  ILE L 150 -1  O  TRP L 148   N  ARG L 155           
SHEET    3  LF 4 SER L 191  HIS L 198 -1  O  THR L 193   N  LYS L 149           
SHEET    4  LF 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  2.04  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.04  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.03  
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  2.03  
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  2.03  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.03  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.03  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.03  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.03  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.03  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.03  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.03  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.03  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.29  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.43  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.40  
LINK        CA    CA A2004                 OD1 ASP A 245     1555   1555  2.27  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.36  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.37  
LINK        CA    CA A2004                 OD2 ASP A 245     1555   1555  3.19  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.30  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.40  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.27  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.40  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.31  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.42  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.54  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.45  
LINK        CA    CA A2005                 O   HOH A4176     1555   1555  2.32  
LINK        CA    CA A2006                 OD1 ASP A 365     1555   1555  2.37  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.36  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.39  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.29  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.44  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.48  
LINK        CA    CA A2006                 O   HOH A4211     1555   1555  2.37  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.31  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.31  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.27  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.42  
LINK        CA    CA A2007                 O   HOH A4245     1555   1555  2.38  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.40  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
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        MN    MN B2001                 O   HOH B4010     1555   1555  2.20  
LINK        MN    MN B2001                 OG  SER B 123     1555   1555  2.17  
LINK        MN    MN B2001                 O   HOH B4009     1555   1555  2.19  
LINK        MN    MN B2001                 OG  SER B 121     1555   1555  2.18  
LINK        MN    MN B2001                 OE2 GLU B 220     1555   1555  2.16  
LINK        MN    MN B2001                 OD1 ASP I 495     1555   1555  2.12  
LINK        MN    MN B2002                 O   SER B 123     1555   1555  2.37  
LINK        MN    MN B2002                 OD1 ASP B 126     1555   1555  2.45  
LINK        MN    MN B2002                 OD2 ASP B 127     1555   1555  2.34  
LINK        MN    MN B2002                 OD2 ASP B 251     1555   1555  2.36  
LINK        MN    MN B2002                 O   HOH B4015     1555   1555  2.58  
LINK        MN    MN B2003                 OD1 ASP B 217     1555   1555  2.26  
LINK        MN    MN B2003                 O   PRO B 219     1555   1555  2.06  
LINK        MN    MN B2003                 OE1 GLU B 220     1555   1555  2.29  
LINK        MN    MN B2003                 O   ASP B 217     1555   1555  2.27  
LINK        MN    MN B2003                 OD1 ASN B 215     1555   1555  2.27  
LINK        MN    MN B2003                 OD2 ASP B 158     1555   1555  2.25  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         C1  BMA B3322                 O4  NAG B3321     1555   1555  1.44  
LINK         C1  MAN B3323                 O3  BMA B3322     1555   1555  1.44  
LINK         C1  MAN B3324                 O6  BMA B3322     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK        CA    CA C2004                 OG1 THR C 250     1555   1555  2.35  
LINK        CA    CA C2004                 OE2 GLU C 243     1555   1555  2.35  
LINK        CA    CA C2004                 O   ASP C 247     1555   1555  2.38  
LINK        CA    CA C2004                 O   THR C 250     1555   1555  2.38  
LINK        CA    CA C2004                 OE2 GLU C 252     1555   1555  2.37  
LINK        CA    CA C2004                 OE1 GLU C 252     1555   1555  2.38  
LINK        CA    CA C2004                 OD1 ASP C 245     1555   1555  2.31  
LINK        CA    CA C2004                 OE1 GLU C 243     1555   1555  2.37  
LINK        CA    CA C2005                 OD1 ASN C 299     1555   1555  2.32  
LINK        CA    CA C2005                 OD1 ASP C 301     1555   1555  2.34  
LINK        CA    CA C2005                 O   ARG C 303     1555   1555  2.12  
LINK        CA    CA C2005                 OD1 ASP C 305     1555   1555  2.63  
LINK        CA    CA C2005                 OD2 ASP C 305     1555   1555  2.38  
LINK        CA    CA C2005                 OD1 ASP C 297     1555   1555  2.32  
LINK        CA    CA C2005                 O   HOH C4050     1555   1555  2.41  
LINK        CA    CA C2006                 OD1 ASP C 369     1555   1555  2.39  
LINK        CA    CA C2006                 O   TYR C 371     1555   1555  2.27  
LINK        CA    CA C2006                 OD2 ASP C 373     1555   1555  2.44  
LINK        CA    CA C2006                 O   HOH C4068     1555   1555  2.36  
LINK        CA    CA C2006                 OD1 ASP C 365     1555   1555  2.37  
LINK        CA    CA C2006                 OD1 ASP C 373     1555   1555  2.39  
LINK        CA    CA C2006                 OD1 ASP C 367     1555   1555  2.31  
LINK        CA    CA C2007                 OD1 ASP C 426     1555   1555  2.36  
LINK        CA    CA C2007                 OD2 ASP C 434     1555   1555  2.39  
LINK        CA    CA C2007                 O   HOH C4089     1555   1555  2.40  
LINK        CA    CA C2007                 OD1 ASP C 428     1555   1555  2.25  
LINK        CA    CA C2007                 O   TYR C 432     1555   1555  2.28  
LINK        CA    CA C2007                 OD1 ASN C 430     1555   1555  2.32  
LINK        CA    CA C2007                 OD1 ASP C 434     1555   1555  2.35  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK        MN    MN D2001                 OD1 ASP J 495     1555   1555  2.19  
LINK        MN    MN D2001                 OE2 GLU D 220     1555   1555  2.15  
LINK        MN    MN D2001                 O   HOH D4010     1555   1555  2.20  
LINK        MN    MN D2001                 OG  SER D 121     1555   1555  2.17  
LINK        MN    MN D2001                 O   HOH D4022     1555   1555  2.19  
LINK        MN    MN D2002                 OD1 ASP D 126     1555   1555  2.61  
LINK        MN    MN D2002                 O   MET D 335     1555   1555  2.57  
LINK        MN    MN D2002                 OD1 ASP D 127     1555   1555  2.52  
LINK        MN    MN D2003                 OD1 ASP D 217     1555   1555  2.20  
LINK        MN    MN D2003                 OD1 ASN D 215     1555   1555  2.28  
LINK        MN    MN D2003                 OD2 ASP D 158     1555   1555  2.26  
LINK        MN    MN D2003                 O   PRO D 219     1555   1555  2.18  
LINK        MN    MN D2003                 O   ASP D 217     1555   1555  2.29  
LINK        MN    MN D2003                 OE1 GLU D 220     1555   1555  2.26  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         C1  BMA D3322                 O4  NAG D3321     1555   1555  1.44  
LINK         C1  MAN D3323                 O3  BMA D3322     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
CISPEP   1 SER B   84    PRO B   85          0        -3.63                     
CISPEP   2 SER B  162    PRO B  163          0         5.54                     
CISPEP   3 SER B  168    PRO B  169          0        -2.75                     
CISPEP   4 SER D   84    PRO D   85          0        -0.67                     
CISPEP   5 SER D  162    PRO D  163          0         4.79                     
CISPEP   6 SER D  168    PRO D  169          0        -2.58                     
CISPEP   7 PHE E  152    PRO E  153          0        -2.24                     
CISPEP   8 GLU E  154    PRO E  155          0        -3.71                     
CISPEP   9 TRP E  194    PRO E  195          0        -0.38                     
CISPEP  10 SER F    7    PRO F    8          0        -2.46                     
CISPEP  11 LEU F   94    PRO F   95          0        -0.99                     
CISPEP  12 TYR F  140    PRO F  141          0         2.50                     
CISPEP  13 PHE H  152    PRO H  153          0        -3.57                     
CISPEP  14 GLU H  154    PRO H  155          0        -3.48                     
CISPEP  15 TRP H  194    PRO H  195          0         1.39                     
CISPEP  16 SER L    7    PRO L    8          0        -1.02                     
CISPEP  17 LEU L   94    PRO L   95          0         0.79                     
CISPEP  18 TYR L  140    PRO L  141          0         2.21                     
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 A4176                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A4211                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A4245                                          
SITE     1 AC5  6 SER B 121  SER B 123  GLU B 220  HOH B4009                    
SITE     2 AC5  6 HOH B4010  ASP I 495                                          
SITE     1 AC6  5 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC6  5 HOH B4015                                                     
SITE     1 AC7  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC7  5 GLU B 220                                                     
SITE     1 AC8  6 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AC8  6 THR C 251  GLU C 252                                          
SITE     1 AC9  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AC9  6 ASP C 305  HOH C4050                                          
SITE     1 BC1  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 BC1  6 ASP C 373  HOH C4068                                          
SITE     1 BC2  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 BC2  6 ASP C 434  HOH C4089                                          
SITE     1 BC3  6 SER D 121  SER D 123  GLU D 220  HOH D4010                    
SITE     2 BC3  6 HOH D4022  ASP J 495                                          
SITE     1 BC4  5 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 BC4  5 HOH D4026                                                     
SITE     1 BC5  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 BC5  5 GLU D 220                                                     
SITE     1 BC6  7 ARG A 386  PRO A 412  THR A 413  HOH A4225                    
SITE     2 BC6  7 ARG C 386  PRO C 412  THR C 413                               
SITE     1 BC7  4 SER L  30  SER L  67  GLY L  68  HOH L4005                    
SITE     1 BC8  4 ALA C  89  HIS C 112  LYS C 124  HOH C4026                    
SITE     1 BC9  2 LYS B  98  ASN B  99                                          
SITE     1 CC1  6 MET A 285  HOH A4146  HOH A4154  ASN B 320                    
SITE     2 CC1  6 HOH B4090  HOH B4102                                          
SITE     1 CC2  6 SER B 369  ASN B 371  PRO B 381  SER B 398                    
SITE     2 CC2  6 ILE B 399  GLU B 400                                          
SITE     1 CC3  4 ASN D  99  PHE D 100  SER D 101  NAG D3372                    
SITE     1 CC4  5 ARG C 281  ASN D 316  LEU D 317  ASN D 320                    
SITE     2 CC4  5 HOH D4045                                                     
SITE     1 CC5  4 ASN D 371  SER D 398  GLU D 400  NAG D3099                    
CRYST1  259.620  144.470  104.750  90.00  90.00  90.00 P 21 21 2     2          
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      0.003852  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006922  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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