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Entry: 3ZDX
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HEADER    CELL ADHESION/IMMUNE SYSTEM             03-DEC-12   3ZDX              
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: INTEGRIN HEADPIECE, RESIDUES 32-488;                       
COMPND   5 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB,     
COMPND   6  CD41, INTEGRIN ALPHA-IIB HEAVY CHAIN;                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: INTEGRIN HEADPIECE, RESIDUES 27-498;                       
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: 10E5 FAB, HEAVY CHAIN;                                     
COMPND  16 CHAIN: H, E;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: 10E5 FAB, LIGHT CHAIN;                                     
COMPND  20 CHAIN: L, F;                                                         
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_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_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PEF1;                                      
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  23 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  24 ORGANISM_TAXID: 10090;                                               
SOURCE  25 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  26 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  30 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  31 ORGANISM_TAXID: 10090;                                               
SOURCE  32 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  33 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 10090                                       
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   2   10-JUL-13 3ZDX    1       JRNL                                     
REVDAT   1   05-JUN-13 3ZDX    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.    2.45 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) : 2.450                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.361                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 145470                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1630                          
REMARK   3   R VALUE            (WORKING SET) : 0.1628                          
REMARK   3   FREE R VALUE                     : 0.1971                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1008                            
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 48.3705 -  4.6855    0.99    21190   159  0.1537 0.1689        
REMARK   3     2  4.6855 -  3.7194    1.00    20713   157  0.1349 0.1630        
REMARK   3     3  3.7194 -  3.2494    1.00    20612   140  0.1598 0.2069        
REMARK   3     4  3.2494 -  2.9523    1.00    20597   121  0.1602 0.1913        
REMARK   3     5  2.9523 -  2.7407    1.00    20491   139  0.1691 0.2203        
REMARK   3     6  2.7407 -  2.5792    1.00    20468   156  0.2055 0.2675        
REMARK   3     7  2.5792 -  2.4500    1.00    20391   136  0.2562 0.3083        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.342                                         
REMARK   3   B_SOL              : 45.758                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.24            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.1149                                               
REMARK   3    B22 (A**2) : 3.6814                                               
REMARK   3    B33 (A**2) : -3.7964                                              
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      :  0.007          21726                                  
REMARK   3   ANGLE     :  0.658          29424                                  
REMARK   3   CHIRALITY :  0.042           3280                                  
REMARK   3   PLANARITY :  0.002           3808                                  
REMARK   3   DIHEDRAL  : 13.782           7878                                  
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):  51.3279  90.3206  54.2853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1716 T22:  -0.0831                                     
REMARK   3      T33:   0.0708 T12:  -0.0005                                     
REMARK   3      T13:   0.0708 T23:   0.0731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3614 L22:   0.6982                                     
REMARK   3      L33:   0.5574 L12:  -0.0954                                     
REMARK   3      L13:  -0.1395 L23:   0.1987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0275 S12:  -0.0322 S13:  -0.0485                       
REMARK   3      S21:   0.0716 S22:  -0.0336 S23:   0.1132                       
REMARK   3      S31:   0.1086 S32:  -0.1275 S33:  -0.0319                       
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):  84.7692  86.4543 118.0825              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1569 T22:   0.2247                                     
REMARK   3      T33:   0.0971 T12:   0.0301                                     
REMARK   3      T13:   0.0793 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8327 L22:   0.3858                                     
REMARK   3      L33:   0.9300 L12:   0.1029                                     
REMARK   3      L13:  -0.3995 L23:  -0.0753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0602 S12:  -0.0258 S13:  -0.0871                       
REMARK   3      S21:  -0.0900 S22:   0.0036 S23:  -0.1134                       
REMARK   3      S31:   0.1620 S32:   0.2839 S33:   0.0174                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 123.6817  88.7128  35.1291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5237 T22:   1.4183                                     
REMARK   3      T33:   0.9871 T12:   0.2779                                     
REMARK   3      T13:   0.0276 T23:  -0.3336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6652 L22:   3.0670                                     
REMARK   3      L33:   1.2655 L12:  -1.8040                                     
REMARK   3      L13:  -0.7789 L23:  -0.8025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3086 S12:  -0.0708 S13:  -0.4549                       
REMARK   3      S21:  -0.1844 S22:  -0.1572 S23:  -0.8987                       
REMARK   3      S31:   0.3139 S32:   0.5334 S33:   0.4342                       
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): 101.4095 107.7070  52.9938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1982 T22:   0.5238                                     
REMARK   3      T33:   0.4644 T12:   0.0764                                     
REMARK   3      T13:  -0.0479 T23:  -0.1739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1892 L22:   2.6178                                     
REMARK   3      L33:   4.5927 L12:  -1.2878                                     
REMARK   3      L13:  -2.6169 L23:   2.1299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:   0.0672 S13:   0.1126                       
REMARK   3      S21:   0.0752 S22:   0.2429 S23:  -0.1634                       
REMARK   3      S31:   0.2757 S32:   0.6344 S33:  -0.1323                       
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):  68.0200 118.5563  63.6902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2118 T22:  -0.0171                                     
REMARK   3      T33:   0.1384 T12:   0.0079                                     
REMARK   3      T13:   0.0672 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6451 L22:   1.6970                                     
REMARK   3      L33:   0.6585 L12:   0.2883                                     
REMARK   3      L13:   0.1419 L23:   0.4342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0301 S12:  -0.0503 S13:   0.1175                       
REMARK   3      S21:   0.0551 S22:   0.0792 S23:  -0.1138                       
REMARK   3      S31:  -0.0974 S32:   0.0621 S33:  -0.0443                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 433:466                              
REMARK   3    ORIGIN FOR THE GROUP (A): 116.1987  89.0822  19.4413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5744 T22:   1.3909                                     
REMARK   3      T33:   0.6535 T12:   0.2496                                     
REMARK   3      T13:   0.0719 T23:  -0.0763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4889 L22:   6.8851                                     
REMARK   3      L33:   2.9471 L12:   3.6706                                     
REMARK   3      L13:   1.3436 L23:  -2.7089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0417 S12:  -0.1881 S13:  -0.0557                       
REMARK   3      S21:  -0.5347 S22:   0.0968 S23:  -1.0444                       
REMARK   3      S31:   0.1681 S32:   0.7127 S33:  -0.1379                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4230  70.7833 141.1727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6403 T22:   0.9638                                     
REMARK   3      T33:   0.4352 T12:  -0.4450                                     
REMARK   3      T13:   0.1019 T23:  -0.0585                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4435 L22:   3.2441                                     
REMARK   3      L33:   1.6816 L12:   1.2946                                     
REMARK   3      L13:  -1.9091 L23:  -0.9246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2526 S12:  -0.0363 S13:  -0.5601                       
REMARK   3      S21:   0.0548 S22:  -0.0260 S23:   0.4062                       
REMARK   3      S31:   0.4549 S32:  -0.5276 S33:   0.0034                       
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):  31.6173  87.4335 116.1463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2951 T22:   0.5756                                     
REMARK   3      T33:   0.2705 T12:  -0.1768                                     
REMARK   3      T13:  -0.0022 T23:   0.0554                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3261 L22:   1.2910                                     
REMARK   3      L33:   6.9324 L12:   0.3456                                     
REMARK   3      L13:  -1.5270 L23:  -1.3616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2215 S12:   0.3739 S13:  -0.1015                       
REMARK   3      S21:  -0.1089 S22:   0.1650 S23:   0.0683                       
REMARK   3      S31:   0.4994 S32:  -0.7637 S33:   0.0708                       
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):  60.8786 102.3713  99.6384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.1889                                     
REMARK   3      T33:   0.0923 T12:  -0.0519                                     
REMARK   3      T13:   0.0283 T23:   0.0583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9954 L22:   0.6671                                     
REMARK   3      L33:   1.7475 L12:  -0.1984                                     
REMARK   3      L13:   0.2620 L23:  -0.3156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:   0.1393 S13:   0.1709                       
REMARK   3      S21:  -0.0981 S22:   0.0366 S23:   0.0170                       
REMARK   3      S31:  -0.1160 S32:  -0.2035 S33:  -0.0714                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 433:471                              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9410  79.1497 154.9569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3500 T22:   0.3940                                     
REMARK   3      T33:   0.3651 T12:  -0.1241                                     
REMARK   3      T13:   0.1127 T23:  -0.1153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9323 L22:   3.9839                                     
REMARK   3      L33:   4.4530 L12:   3.2512                                     
REMARK   3      L13:  -0.8172 L23:   1.5105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1219 S12:   0.0840 S13:  -0.3102                       
REMARK   3      S21:   0.1620 S22:   0.0273 S23:   0.1291                       
REMARK   3      S31:   0.7466 S32:  -0.6020 S33:   0.0444                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2213  96.9161  82.8803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4090 T22:   0.3799                                     
REMARK   3      T33:   0.2413 T12:  -0.0411                                     
REMARK   3      T13:   0.1396 T23:  -0.0593                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2214 L22:   0.8912                                     
REMARK   3      L33:   2.5442 L12:   0.0988                                     
REMARK   3      L13:  -1.2998 L23:  -0.2349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:  -0.4430 S13:  -0.0174                       
REMARK   3      S21:   0.7144 S22:  -0.0429 S23:   0.2224                       
REMARK   3      S31:   0.2181 S32:  -0.2127 S33:   0.0615                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8385  81.5810  93.3430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5482 T22:   0.5486                                     
REMARK   3      T33:   1.4868 T12:   0.0866                                     
REMARK   3      T13:   0.2307 T23:   0.1252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6904 L22:   0.2507                                     
REMARK   3      L33:   3.7636 L12:   0.0536                                     
REMARK   3      L13:   0.1458 L23:   0.2841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0694 S12:  -0.1365 S13:  -1.5198                       
REMARK   3      S21:   0.2012 S22:  -0.0438 S23:   0.1575                       
REMARK   3      S31:   0.9173 S32:   0.1198 S33:   0.1014                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8339  96.1023  64.5264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2350 T22:   0.5471                                     
REMARK   3      T33:   0.4692 T12:  -0.0226                                     
REMARK   3      T13:   0.0703 T23:  -0.1773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2294 L22:   0.3285                                     
REMARK   3      L33:   0.6301 L12:   0.0973                                     
REMARK   3      L13:  -0.5216 L23:   0.3149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0499 S12:   0.2537 S13:  -0.0492                       
REMARK   3      S21:   0.0204 S22:  -0.3704 S23:   0.5731                       
REMARK   3      S31:   0.1422 S32:  -0.5912 S33:  -0.2425                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1552  93.5959  86.5714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2089 T22:   0.4635                                     
REMARK   3      T33:   0.7166 T12:   0.0005                                     
REMARK   3      T13:   0.1900 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0128 L22:   1.0983                                     
REMARK   3      L33:   2.3317 L12:  -0.1354                                     
REMARK   3      L13:   0.2178 L23:   0.5598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3136 S12:   0.2143 S13:  -0.7937                       
REMARK   3      S21:   0.1287 S22:  -0.0314 S23:   0.2565                       
REMARK   3      S31:   0.2898 S32:  -0.4284 S33:   0.0175                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 115.5575  90.0654  86.4628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7763 T22:   0.7007                                     
REMARK   3      T33:   0.4422 T12:  -0.0479                                     
REMARK   3      T13:   0.3030 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1143 L22:   0.5553                                     
REMARK   3      L33:   3.9913 L12:  -0.3431                                     
REMARK   3      L13:  -1.6841 L23:  -0.0936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1494 S12:   0.5147 S13:  -0.2563                       
REMARK   3      S21:  -0.7813 S22:  -0.0675 S23:  -0.2951                       
REMARK   3      S31:   0.8189 S32:   0.1817 S33:   0.4745                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 151.5576  82.9345  80.1343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0440 T22:   1.4472                                     
REMARK   3      T33:   1.0285 T12:   0.6178                                     
REMARK   3      T13:   0.2107 T23:   0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5283 L22:   2.6707                                     
REMARK   3      L33:   1.6593 L12:   0.8894                                     
REMARK   3      L13:  -0.2826 L23:   1.4487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3440 S12:   0.8530 S13:  -0.8050                       
REMARK   3      S21:  -0.2952 S22:   0.0602 S23:  -1.1020                       
REMARK   3      S31:   0.6041 S32:   1.1321 S33:  -0.3634                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 125.7976 100.2442 102.5485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3072 T22:   0.8278                                     
REMARK   3      T33:   0.6642 T12:  -0.0646                                     
REMARK   3      T13:   0.1765 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3204 L22:   0.9384                                     
REMARK   3      L33:   0.6573 L12:  -0.1936                                     
REMARK   3      L13:  -0.3401 L23:  -0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:  -0.1947 S13:   0.3713                       
REMARK   3      S21:  -0.1232 S22:  -0.1288 S23:  -0.7918                       
REMARK   3      S31:   0.0771 S32:   0.6749 S33:  -0.1516                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 154.7635  98.7294  80.6411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7142 T22:   1.3945                                     
REMARK   3      T33:   1.1025 T12:   0.2275                                     
REMARK   3      T13:   0.4018 T23:   0.4210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2853 L22:   2.2741                                     
REMARK   3      L33:   3.2051 L12:   0.9370                                     
REMARK   3      L13:  -0.9361 L23:   0.8530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0832 S12:   0.7643 S13:   0.1452                       
REMARK   3      S21:  -0.8903 S22:   0.1392 S23:  -0.7416                       
REMARK   3      S31:  -0.3342 S32:   0.6751 S33:  -0.3272                       
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 3ZDX 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-54966.                                       
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) : 0.97934                            
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   : 145557                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.45                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.5                                
REMARK 200  R MERGE                    (I) : 0.15                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT      
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      129.85500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.48000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.85500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.48000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 455    CG   CD   CE   NZ                                   
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 B  174   CG   CD   OE1  OE2                                  
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    HIS A   338     O    HOH A  4402              2.12            
REMARK 500   OE1  GLN A   351     O    HOH A  4418              2.19            
REMARK 500   ND2  ASN B   371     C2   NAG B  3371              2.12            
REMARK 500   O    HIS C   338     O    HOH C  4178              2.13            
REMARK 500   OG   SER C   384     O    HOH C  4254              2.17            
REMARK 500   OE1  GLN C   395     O    HOH C  4265              2.11            
REMARK 500   ND2  ASN D   371     C2   NAG D  3371              2.13            
REMARK 500   O    HOH A  4021     O    HOH A  4049              2.14            
REMARK 500   O    HOH A  4036     O    HOH A  4068              2.18            
REMARK 500   O    HOH A  4042     O    HOH A  4069              2.15            
REMARK 500   O    HOH A  4063     O    HOH B  4077              2.16            
REMARK 500   O    HOH A  4064     O    HOH A  4147              2.01            
REMARK 500   O    HOH A  4068     O    HOH A  4069              2.10            
REMARK 500   O    HOH A  4079     O    HOH A  4207              2.16            
REMARK 500   O    HOH A  4085     O    HOH A  4086              2.08            
REMARK 500   O    HOH A  4095     O    HOH A  4098              2.13            
REMARK 500   O    HOH A  4147     O    HOH A  4175              2.08            
REMARK 500   O    HOH A  4171     O    HOH A  4373              1.88            
REMARK 500   O    HOH A  4177     O    HOH A  4415              2.03            
REMARK 500   O    HOH A  4237     O    HOH A  4514              2.15            
REMARK 500   O    HOH A  4352     O    HOH A  4353              2.08            
REMARK 500   O    HOH A  4386     O    HOH A  4395              2.19            
REMARK 500   O    HOH A  4417     O    HOH A  4451              2.15            
REMARK 500   O    HOH A  4458     O    HOH A  4459              2.09            
REMARK 500   O    HOH A  4459     O    HOH A  4490              1.97            
REMARK 500   O    HOH A  4463     O    HOH A  4467              2.11            
REMARK 500   O    HOH A  4467     O    HOH A  4472              2.00            
REMARK 500   O    HOH A  4485     O    HOH A  4486              2.15            
REMARK 500   O    HOH A  4517     O    HOH A  4518              2.17            
REMARK 500   O    HOH B  4018     O    HOH B  4121              2.17            
REMARK 500   O    HOH B  4039     O    HOH B  4040              2.16            
REMARK 500   O    HOH B  4050     O    HOH B  4116              2.11            
REMARK 500   O    HOH B  4071     O    HOH B  4072              2.04            
REMARK 500   O    HOH C  4027     O    HOH C  4028              2.20            
REMARK 500   O    HOH C  4119     O    HOH C  4120              2.15            
REMARK 500   O    HOH C  4165     O    HOH C  4166              2.11            
REMARK 500   O    HOH C  4221     O    HOH C  4223              2.11            
REMARK 500   O    HOH C  4225     O    HOH C  4228              2.16            
REMARK 500   O    HOH C  4260     O    HOH C  4282              1.99            
REMARK 500   O    HOH D  4013     O    HOH D  4070              2.08            
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   NH1  ARG C   386     O    HOH A  4485     1556     2.16            
REMARK 500   O    HOH C  4260     O    HOH A  4459     1556     1.92            
REMARK 500   O    HOH C  4279     O    HOH A  4480     1556     2.09            
REMARK 500   O    HOH C  4282     O    HOH A  4459     1556     1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -131.08     56.92                                   
REMARK 500    LYS A 118     -115.90     61.62                                   
REMARK 500    GLU A 123      135.15     98.76                                   
REMARK 500    LEU A 212      -49.53     76.02                                   
REMARK 500    THR A 296      139.73   -172.22                                   
REMARK 500    ASP A 319       38.13     72.79                                   
REMARK 500    PRO A 337       91.31    -64.94                                   
REMARK 500    PRO B  32      172.82    -51.38                                   
REMARK 500    LEU B  33      -81.06    -48.55                                   
REMARK 500    ALA B  61       89.90   -154.42                                   
REMARK 500    ASP B  66       45.69   -142.20                                   
REMARK 500    ASP B  76      158.49     61.94                                   
REMARK 500    SER B  78       54.43     87.51                                   
REMARK 500    VAL B 157      -81.15   -124.51                                   
REMARK 500    LYS B 181       48.31   -109.39                                   
REMARK 500    SER B 213     -165.07   -126.10                                   
REMARK 500    LEU B 258      -11.95     87.86                                   
REMARK 500    LEU B 375      -82.08     56.63                                   
REMARK 500    SER C 101     -125.03     59.16                                   
REMARK 500    LYS C 118     -112.37     66.10                                   
REMARK 500    GLU C 123      136.88     96.64                                   
REMARK 500    LEU C 212      -44.15     71.21                                   
REMARK 500    ASP C 247      109.78    -57.54                                   
REMARK 500    THR D   7       37.60    -94.36                                   
REMARK 500    ASP D  47       30.50    -93.34                                   
REMARK 500    PHE D  56       80.28   -152.04                                   
REMARK 500    LEU D  64      -61.95   -100.80                                   
REMARK 500    ASP D  66       49.27   -150.76                                   
REMARK 500    SER D  74     -177.40    -69.55                                   
REMARK 500    VAL D 157      -79.89   -130.49                                   
REMARK 500    SER D 213     -154.67   -120.06                                   
REMARK 500    ASP D 241       79.98   -107.33                                   
REMARK 500    LYS D 253      174.30    -59.27                                   
REMARK 500    LEU D 258       -9.00     91.87                                   
REMARK 500    CYS D 374     -117.54    -97.27                                   
REMARK 500    ASN D 376     -156.17     54.20                                   
REMARK 500    ASN D 377       42.74   -100.12                                   
REMARK 500    SER E  85       74.89     50.74                                   
REMARK 500    VAL E 133      -84.72    -63.72                                   
REMARK 500    SER E 178       72.95     39.84                                   
REMARK 500    ASP E 179      -16.16     77.04                                   
REMARK 500    SER F  31        7.37     58.99                                   
REMARK 500    SER F  77       75.55     54.47                                   
REMARK 500    ALA F  84     -169.16   -161.60                                   
REMARK 500    ASN F 138       70.98     42.07                                   
REMARK 500    ASN F 190      -74.01   -116.09                                   
REMARK 500    ASN F 212      -63.12     69.31                                   
REMARK 500    ALA H  92     -179.85   -170.16                                   
REMARK 500    SER H 166      -65.06   -108.33                                   
REMARK 500    SER H 178       79.77     39.50                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 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                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 250   O                                                      
REMARK 620 2 GLU A 243   OE1  71.4                                              
REMARK 620 3 GLU A 243   OE2 125.9  54.9                                        
REMARK 620 4 ASP A 247   O    86.0  76.0  76.1                                  
REMARK 620 5 ASP A 245   OD1 165.4 121.4  66.5  90.5                            
REMARK 620 6 THR A 250   OG1  77.3 141.3 144.4  79.7  88.1                      
REMARK 620 7 GLU A 252   OE1 102.9  85.1  80.2 155.4  86.1 124.4                
REMARK 620 8 GLU A 252   OE2  86.8 127.2 129.3 151.5  89.6  71.8  53.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 303   O                                                      
REMARK 620 2 ASP A 297   OD1  78.7                                              
REMARK 620 3 ASN A 299   OD1 157.5  79.2                                        
REMARK 620 4 ASP A 301   OD1  88.2  75.9  82.8                                  
REMARK 620 5 ASP A 305   OD1  83.5 130.6 114.2 149.3                            
REMARK 620 6 ASP A 305   OD2  97.8  84.4  83.7 157.8  52.9                      
REMARK 620 7 HOH A4377   O   109.9 154.9  89.0  80.8  74.4 116.5                
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  84.6                                              
REMARK 620 3 ASP A 369   OD1  77.5  87.6                                        
REMARK 620 4 TYR A 371   O    72.0 156.6  88.3                                  
REMARK 620 5 ASP A 373   OD1 129.9 114.5 144.1  81.2                            
REMARK 620 6 ASP A 373   OD2  87.4  84.8 163.7  92.9  52.0                      
REMARK 620 7 HOH A4437   O   153.8 100.0  77.0 101.6  71.7 118.6                
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  86.5                                              
REMARK 620 3 ASP A 426   OD1  86.4  75.4                                        
REMARK 620 4 ASP A 434   OD2 171.4  87.9  85.8                                  
REMARK 620 5 ASP A 434   OD1 134.8 118.9 133.6  53.8                            
REMARK 620 6 HOH A4504   O    76.2  74.9 146.3 108.7  75.9                      
REMARK 620 7 TYR A 432   O    88.5 153.9  78.7  93.6  81.9 128.4                
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 243   OE2                                                    
REMARK 620 2 ASP C 245   OD1  66.6                                              
REMARK 620 3 ASP C 247   O    71.0  84.9                                        
REMARK 620 4 THR C 250   OG1 138.1  83.1  78.4                                  
REMARK 620 5 GLU C 243   OE1  54.1 120.3  83.1 148.7                            
REMARK 620 6 THR C 250   O   125.0 165.7  91.4  82.6  72.7                      
REMARK 620 7 GLU C 252   OE1  81.5  83.2 152.4 124.4  81.7 105.8                
REMARK 620 8 GLU C 252   OE2 126.7  80.5 147.9  71.7 128.9  95.8  53.0          
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 305   OD1                                                    
REMARK 620 2 ASP C 297   OD1 134.0                                              
REMARK 620 3 ASN C 299   OD1 109.1  75.6                                        
REMARK 620 4 ASP C 301   OD1 153.2  71.6  82.1                                  
REMARK 620 5 ARG C 303   O    88.4  80.3 155.9  89.5                            
REMARK 620 6 ASP C 305   OD2  53.0  83.3  84.2 153.8  94.1                      
REMARK 620 7 HOH C4201   O    71.2 153.9  90.5  84.8 111.3 117.7                
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 HOH C4245   O                                                      
REMARK 620 2 ASP C 369   OD1  73.6                                              
REMARK 620 3 TYR C 371   O    98.4  89.7                                        
REMARK 620 4 ASP C 373   OD1  74.5 144.9  80.9                                  
REMARK 620 5 ASP C 365   OD1 149.2  75.7  78.7 133.9                            
REMARK 620 6 ASP C 367   OD1 101.4  81.2 154.9 119.2  76.3                      
REMARK 620 7 ASP C 373   OD2 120.4 162.3  98.1  52.5  90.2  85.1                
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  84.2                                              
REMARK 620 3 TYR C 432   O    78.0  85.4                                        
REMARK 620 4 ASP C 428   OD1  73.7  89.3 151.6                                  
REMARK 620 5 ASP C 434   OD1 134.9 136.9  86.7 115.4                            
REMARK 620 6 ASP C 434   OD2  87.4 169.0  99.8  81.6  53.6                      
REMARK 620 7 HOH C4295   O   146.0  79.4 129.4  76.5  73.5 104.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 HOH B4038   O   166.6                                              
REMARK 620 3 HOH B4039   O    88.5  79.6                                        
REMARK 620 4 HOH B4126   O    87.7  86.0  89.4                                  
REMARK 620 5 SER B 121   OG   96.0  92.1  99.6 170.4                            
REMARK 620 6 HOH B4036   O   108.2  84.2 163.0  94.6  75.8                      
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 SER B 123   O                                                      
REMARK 620 2 ASP B 126   OD1  85.5                                              
REMARK 620 3 ASP B 127   OD1  94.5  83.5                                        
REMARK 620 4 MET B 335   O   162.9 111.3  84.5                                  
REMARK 620 5 HOH B4043   O    87.3 167.3  86.6  75.6                            
REMARK 620 6 HOH B4044   O    85.1  93.6 177.2  96.7  96.2                      
REMARK 620 N                    1     2     3     4     5                       
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 100.8                                              
REMARK 620 3 ASP B 217   OD1  93.6  90.5                                        
REMARK 620 4 PRO B 219   O    84.9 165.7 102.4                                  
REMARK 620 5 GLU B 220   OE1  94.6  85.5 171.4  80.9                            
REMARK 620 6 ASP B 217   O   166.3  88.2  75.8  88.8  96.4                      
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 SER D 121   OG                                                     
REMARK 620 2 GLU D 220   OE2  92.9                                              
REMARK 620 3 HOH D4033   O    74.9 101.8                                        
REMARK 620 4 HOH D4034   O    85.8 173.1  84.4                                  
REMARK 620 5 HOH D4082   O   169.4  85.8  95.0  96.7                            
REMARK 620 6 SO4 D1473   O3   95.8  85.2 168.5  88.2  94.6                      
REMARK 620 N                    1     2     3     4     5                       
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    83.8                                              
REMARK 620 3 HOH D4038   O    90.0  80.9                                        
REMARK 620 4 SER D 123   O    94.2 164.8  84.0                                  
REMARK 620 5 ASP D 126   OD1  80.7 108.7 165.6  85.7                            
REMARK 620 6 HOH D4039   O   174.5  92.9  93.9  90.1  96.2                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP D 217   O                                                      
REMARK 620 2 PRO D 219   O    89.3                                              
REMARK 620 3 ASP D 158   OD2 163.4  82.2                                        
REMARK 620 4 ASN D 215   OD1  88.9 168.1 102.3                                  
REMARK 620 5 ASP D 217   OD1  75.5  99.0  91.7  92.0                            
REMARK 620 6 GLU D 220   OE1  94.0  80.0  98.5  88.4 169.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1468                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1454                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1456                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1457                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L1215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
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: DC6                                                 
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: DC7                                                 
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: DC8                                                 
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: DC9                                                 
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: EC1                                                 
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: 3ZDY   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZDZ   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  3ZDX A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDX B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDX C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDX D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDX H    1   221  PDB    3ZDX     3ZDX             1    221             
DBREF  3ZDX E    1   221  PDB    3ZDX     3ZDX             1    221             
DBREF  3ZDX L    1   214  PDB    3ZDX     3ZDX             1    214             
DBREF  3ZDX F    1   214  PDB    3ZDX     3ZDX             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 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 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 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 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 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 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
MODRES 3ZDX ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDX ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDX ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDX ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDX ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDX ASN D  371  ASN  GLYCOSYLATION SITE                                 
HET    GOL  A1458      14                                                       
HET    GOL  A1459      14                                                       
HET    GOL  A1460      14                                                       
HET    SO4  A1461       5                                                       
HET    SO4  A1462       5                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    GOL  B1467      14                                                       
HET     CL  B1468       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    GOL  C1454      14                                                       
HET    GOL  C1455      14                                                       
HET    SO4  C1456       5                                                       
HET    SO4  C1457       5                                                       
HET    SO4  C1458       5                                                       
HET    SO4  C1459       5                                                       
HET    SO4  C1460       5                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    SO4  D1472       5                                                       
HET    SO4  D1473       5                                                       
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  L1215       5                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  GOL    6(C3 H8 O3)                                                  
FORMUL  10  SO4    10(O4 S 2-)                                                  
FORMUL  11   CA    8(CA 2+)                                                     
FORMUL  12   CL    CL 1-                                                        
FORMUL  13   MN    6(MN 2+)                                                     
FORMUL  14  NAG    10(C8 H15 N O6)                                              
FORMUL  15  BMA    2(C6 H12 O6)                                                 
FORMUL  16  MAN    3(C6 H12 O6)                                                 
FORMUL  17  HOH   *1324(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  ALA B   18  1                                   7    
HELIX    8   8 LEU B   40  LYS B   46  1                                   7    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
HELIX   10  10 SER B  121  SER B  123  5                                   3    
HELIX   11  11 MET B  124  ILE B  131  1                                   8    
HELIX   12  12 ASN B  133  ARG B  143  1                                  11    
HELIX   13  13 PRO B  169  ASN B  175  1                                   7    
HELIX   14  14 VAL B  200  LYS B  208  1                                   9    
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 ASN B  339  ARG B  352  1                                  14    
HELIX   21  21 CYS B  435  ALA B  441  5                                   7    
HELIX   22  22 CYS B  448  GLY B  451  5                                   4    
HELIX   23  23 LEU C  151  ASN C  158  1                                   8    
HELIX   24  24 GLY C  187  LEU C  192  1                                   6    
HELIX   25  25 VAL C  200  TYR C  207  1                                   8    
HELIX   26  26 ASN C  227  PHE C  231  5                                   5    
HELIX   27  27 THR C  259  LEU C  264  1                                   6    
HELIX   28  28 CYS D    5  GLY D    9  5                                   5    
HELIX   29  29 SER D   12  SER D   20  1                                   9    
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 ASP D   76  VAL D   80  5                                   5    
HELIX   33  33 SER D  121  SER D  123  5                                   3    
HELIX   34  34 MET D  124  ILE D  131  1                                   8    
HELIX   35  35 ASN D  133  ARG D  143  1                                  11    
HELIX   36  36 PRO D  169  ASN D  175  1                                   7    
HELIX   37  37 GLN D  199  LYS D  209  1                                  11    
HELIX   38  38 GLY D  221  CYS D  232  1                                  12    
HELIX   39  39 CYS D  232  GLY D  237  1                                   6    
HELIX   40  40 LEU D  258  GLY D  264  5                                   7    
HELIX   41  41 SER D  291  ASN D  303  1                                  13    
HELIX   42  42 VAL D  314  GLU D  323  1                                  10    
HELIX   43  43 ASN D  339  ARG D  352  1                                  14    
HELIX   44  44 CYS D  435  ALA D  439  5                                   5    
HELIX   45  45 ASN E   28  THR E   32  5                                   5    
HELIX   46  46 PRO E   62  GLN E   65  5                                   4    
HELIX   47  47 THR E   87  THR E   91  5                                   5    
HELIX   48  48 SER E  162  SER E  164  5                                   3    
HELIX   49  49 ASP F   79  PHE F   83  5                                   5    
HELIX   50  50 SER F  121  THR F  126  1                                   6    
HELIX   51  51 LYS F  183  GLU F  187  1                                   5    
HELIX   52  52 ASN H   28  THR H   32  5                                   5    
HELIX   53  53 PRO H   62  PHE H   64  5                                   3    
HELIX   54  54 THR H   74  SER H   76  5                                   3    
HELIX   55  55 THR H   87  THR H   91  5                                   5    
HELIX   56  56 ASP L   79  PHE L   83  5                                   5    
HELIX   57  57 SER L  121  THR L  126  1                                   6    
HELIX   58  58 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 5 GLY A  63  GLN A  64  0                                        
SHEET    2  AA 5 THR A   9  ALA A  12  1  O  PHE A  10   N  GLY A  63           
SHEET    3  AA 5 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    4  AA 5 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    5  AA 5 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 4 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4  AB 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 GLU A 120  GLU A 121  1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 THR A  76  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  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AF 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
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  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  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 LEU C 421  VAL C 425 -1  O  ARG C 422   N  ILE C 436           
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 VAL C  97  TRP C 100  0                                        
SHEET    2  CD 4 VAL C 103  ALA C 108 -1  O  VAL C 103   N  TRP C 100           
SHEET    3  CD 4 SER C 129  GLN C 134 -1  O  SER C 129   N  ALA C 108           
SHEET    4  CD 4 ARG C 139  TYR C 143 -1  O  ARG C 139   N  GLN C 134           
SHEET    1  CE 4 SER C 173  VAL C 175  0                                        
SHEET    2  CE 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3  CE 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4  CE 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1  CF 4 VAL C 239  GLY C 242  0                                        
SHEET    2  CF 4 GLU C 252  ALA C 257 -1  O  GLU C 252   N  GLY C 242           
SHEET    3  CF 4 ALA C 266  LEU C 270 -1  O  ALA C 266   N  ALA C 257           
SHEET    4  CF 4 ARG C 276  ARG C 281 -1  N  LEU C 277   O  ILE C 269           
SHEET    1  CG 4 VAL C 293  THR C 296  0                                        
SHEET    2  CG 4 ASP C 305  ALA C 310 -1  O  ASP C 305   N  THR C 296           
SHEET    3  CG 4 ARG C 327  PHE C 331 -1  O  ARG C 327   N  ALA C 310           
SHEET    4  CG 4 LEU C 345  THR C 348 -1  O  LEU C 345   N  LEU C 330           
SHEET    1  CH 2 MET C 314  ARG C 317  0                                        
SHEET    2  CH 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1  CI 4 ILE C 360  GLY C 364  0                                        
SHEET    2  CI 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  LEU C 363           
SHEET    3  CI 4 GLN C 388  PHE C 392 -1  O  GLN C 388   N  ALA C 378           
SHEET    4  CI 4 GLN C 405  ASP C 408 -1  O  GLN C 405   N  VAL C 391           
SHEET    1  CJ 2 GLY C 394  GLN C 395  0                                        
SHEET    2  CJ 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 GLU D  60  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 VAL D 355  ARG D 360 -1  O  GLU D 358   N  LYS D 417           
SHEET    6  DB 6 SER D 385  CYS D 386 -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 LEU D 366  THR D 373 -1  O  SER D 367   N  LYS D 402           
SHEET    5  DC 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  DD 6 TYR D 190  THR D 197  0                                        
SHEET    2  DD 6 LEU D 149  PHE D 156 -1  O  ILE D 151   N  THR D 197           
SHEET    3  DD 6 VAL D 112  ASP D 119  1  O  VAL D 112   N  ARG D 150           
SHEET    4  DD 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  DD 6 ASN D 305  THR D 311  1  O  ASN D 305   N  LEU D 246           
SHEET    6  DD 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  DE 2 GLY D 453  GLU D 456  0                                        
SHEET    2  DE 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 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177  1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 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 LEU H 180  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  GLN H 177  0                                        
SHEET    2  HG 2 LEU H 180  THR H 190  1  O  LEU H 180   N  GLN H 177           
SHEET    1  HH 3 THR H 157  TRP H 160  0                                        
SHEET    2  HH 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HH 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 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  2.05  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.05  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.04  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.04  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.04  
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  2.04  
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  2.04  
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  2.04  
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  2.37  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.39  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.37  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.33  
LINK        CA    CA A2004                 OD1 ASP A 245     1555   1555  2.27  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.38  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.48  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.43  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.33  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.39  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.28  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.50  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.46  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.46  
LINK        CA    CA A2005                 O   HOH A4377     1555   1555  2.38  
LINK        CA    CA A2006                 OD1 ASP A 365     1555   1555  2.40  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.32  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.46  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.24  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.48  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.51  
LINK        CA    CA A2006                 O   HOH A4437     1555   1555  2.39  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.40  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.32  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.30  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.45  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.40  
LINK        CA    CA A2007                 O   HOH A4504     1555   1555  2.39  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.30  
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                 OE2 GLU B 220     1555   1555  2.20  
LINK        MN    MN B2001                 O   HOH B4038     1555   1555  2.10  
LINK        MN    MN B2001                 O   HOH B4039     1555   1555  2.30  
LINK        MN    MN B2001                 O   HOH B4126     1555   1555  2.27  
LINK        MN    MN B2001                 OG  SER B 121     1555   1555  2.30  
LINK        MN    MN B2001                 O   HOH B4036     1555   1555  2.18  
LINK        MN    MN B2002                 O   SER B 123     1555   1555  2.36  
LINK        MN    MN B2002                 O   HOH B4044     1555   1555  2.35  
LINK        MN    MN B2002                 O   HOH B4043     1555   1555  2.35  
LINK        MN    MN B2002                 O   MET B 335     1555   1555  2.51  
LINK        MN    MN B2002                 OD1 ASP B 127     1555   1555  2.31  
LINK        MN    MN B2002                 OD1 ASP B 126     1555   1555  2.33  
LINK        MN    MN B2003                 O   ASP B 217     1555   1555  2.33  
LINK        MN    MN B2003                 OE1 GLU B 220     1555   1555  2.27  
LINK        MN    MN B2003                 O   PRO B 219     1555   1555  2.28  
LINK        MN    MN B2003                 OD1 ASP B 217     1555   1555  2.24  
LINK        MN    MN B2003                 OD1 ASN B 215     1555   1555  2.30  
LINK        MN    MN B2003                 OD2 ASP B 158     1555   1555  2.31  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  BMA B3322     1555   1555  1.44  
LINK         O3  BMA B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         O6  BMA B3322                 C1  MAN B3324     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK        CA    CA C2004                 OE2 GLU C 243     1555   1555  2.40  
LINK        CA    CA C2004                 OD1 ASP C 245     1555   1555  2.31  
LINK        CA    CA C2004                 OE1 GLU C 252     1555   1555  2.49  
LINK        CA    CA C2004                 O   ASP C 247     1555   1555  2.34  
LINK        CA    CA C2004                 OG1 THR C 250     1555   1555  2.41  
LINK        CA    CA C2004                 OE1 GLU C 243     1555   1555  2.42  
LINK        CA    CA C2004                 O   THR C 250     1555   1555  2.34  
LINK        CA    CA C2004                 OE2 GLU C 252     1555   1555  2.42  
LINK        CA    CA C2005                 OD1 ASP C 305     1555   1555  2.47  
LINK        CA    CA C2005                 O   HOH C4201     1555   1555  2.40  
LINK        CA    CA C2005                 OD2 ASP C 305     1555   1555  2.44  
LINK        CA    CA C2005                 O   ARG C 303     1555   1555  2.30  
LINK        CA    CA C2005                 OD1 ASP C 301     1555   1555  2.46  
LINK        CA    CA C2005                 OD1 ASN C 299     1555   1555  2.27  
LINK        CA    CA C2005                 OD1 ASP C 297     1555   1555  2.40  
LINK        CA    CA C2006                 OD2 ASP C 373     1555   1555  2.48  
LINK        CA    CA C2006                 OD1 ASP C 367     1555   1555  2.34  
LINK        CA    CA C2006                 OD1 ASP C 365     1555   1555  2.45  
LINK        CA    CA C2006                 OD1 ASP C 373     1555   1555  2.47  
LINK        CA    CA C2006                 O   TYR C 371     1555   1555  2.22  
LINK        CA    CA C2006                 OD1 ASP C 369     1555   1555  2.41  
LINK        CA    CA C2006                 O   HOH C4245     1555   1555  2.39  
LINK        CA    CA C2007                 O   HOH C4295     1555   1555  2.37  
LINK        CA    CA C2007                 OD2 ASP C 434     1555   1555  2.45  
LINK        CA    CA C2007                 OD1 ASP C 434     1555   1555  2.42  
LINK        CA    CA C2007                 OD1 ASP C 428     1555   1555  2.32  
LINK        CA    CA C2007                 O   TYR C 432     1555   1555  2.27  
LINK        CA    CA C2007                 OD1 ASN C 430     1555   1555  2.37  
LINK        CA    CA C2007                 OD1 ASP C 426     1555   1555  2.37  
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         O3  SO4 D1473                MN    MN D2001     1555   1555  2.36  
LINK        MN    MN D2001                 O   HOH D4082     1555   1555  2.27  
LINK        MN    MN D2001                 O   HOH D4034     1555   1555  2.31  
LINK        MN    MN D2001                 O   HOH D4033     1555   1555  2.08  
LINK        MN    MN D2001                 OE2 GLU D 220     1555   1555  2.16  
LINK        MN    MN D2001                 OG  SER D 121     1555   1555  2.32  
LINK        MN    MN D2002                 O   HOH D4039     1555   1555  2.23  
LINK        MN    MN D2002                 OD1 ASP D 126     1555   1555  2.33  
LINK        MN    MN D2002                 O   SER D 123     1555   1555  2.36  
LINK        MN    MN D2002                 O   HOH D4038     1555   1555  2.36  
LINK        MN    MN D2002                 O   MET D 335     1555   1555  2.41  
LINK        MN    MN D2002                 OD1 ASP D 127     1555   1555  2.27  
LINK        MN    MN D2003                 OE1 GLU D 220     1555   1555  2.26  
LINK        MN    MN D2003                 OD1 ASP D 217     1555   1555  2.24  
LINK        MN    MN D2003                 OD1 ASN D 215     1555   1555  2.30  
LINK        MN    MN D2003                 OD2 ASP D 158     1555   1555  2.30  
LINK        MN    MN D2003                 O   PRO D 219     1555   1555  2.25  
LINK        MN    MN D2003                 O   ASP D 217     1555   1555  2.33  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O4  NAG D3321                 C1  BMA D3322     1555   1555  1.44  
LINK         O3  BMA D3322                 C1  MAN D3323     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
CISPEP   1 SER B   84    PRO B   85          0        -2.67                     
CISPEP   2 SER B  162    PRO B  163          0         3.45                     
CISPEP   3 SER B  168    PRO B  169          0        -5.11                     
CISPEP   4 SER D   84    PRO D   85          0        -3.43                     
CISPEP   5 SER D  162    PRO D  163          0         8.22                     
CISPEP   6 SER D  168    PRO D  169          0        -3.23                     
CISPEP   7 PHE E  152    PRO E  153          0        -3.53                     
CISPEP   8 GLU E  154    PRO E  155          0        -3.39                     
CISPEP   9 TRP E  194    PRO E  195          0         0.44                     
CISPEP  10 SER F    7    PRO F    8          0        -4.35                     
CISPEP  11 LEU F   94    PRO F   95          0         0.63                     
CISPEP  12 TYR F  140    PRO F  141          0         3.76                     
CISPEP  13 PHE H  152    PRO H  153          0        -2.44                     
CISPEP  14 GLU H  154    PRO H  155          0        -2.46                     
CISPEP  15 TRP H  194    PRO H  195          0         1.16                     
CISPEP  16 SER L    7    PRO L    8          0        -4.87                     
CISPEP  17 LEU L   94    PRO L   95          0        -0.02                     
CISPEP  18 TYR L  140    PRO L  141          0         3.39                     
SITE     1 AC1  6 PHE A 160  TYR A 190  GOL A1459  HOH A4244                    
SITE     2 AC1  6 HOH A4524  HOH A4525                                          
SITE     1 AC2  7 PHE A 231  GOL A1458  HOH A4260  HOH A4297                    
SITE     2 AC2  7 HOH A4314  HOH A4315  HOH A4525                               
SITE     1 AC3  7 SER A 225  ASN A 227  TYR A 230  ARG A 276                    
SITE     2 AC3  7 ARG A 279  HOH A4298  HOH A4526                               
SITE     1 AC4  4 PHE A  10  GLN A 444  HOH A4527  PRO C 383                    
SITE     1 AC5  3 TYR A 155  ASN A 158  SER A 161                               
SITE     1 AC6  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC6  5 GLU A 252                                                     
SITE     1 AC7  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC7  6 ASP A 305  HOH A4377                                          
SITE     1 AC8  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC8  6 ASP A 373  HOH A4437                                          
SITE     1 AC9  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC9  6 ASP A 434  HOH A4504                                          
SITE     1 BC1  8 GLN B  82  GLN B 106  SER B 243  ARG B 352                    
SITE     2 BC1  8 GLY B 420  PHE B 421  HOH B4019  HOH B4183                    
SITE     1 BC2  6 SER B 121  TYR B 122  ASN B 215  HOH B4039                    
SITE     2 BC2  6 HOH B4040  HOH B4124                                          
SITE     1 BC3  6 SER B 121  GLU B 220  HOH B4036  HOH B4038                    
SITE     2 BC3  6 HOH B4039  HOH B4126                                          
SITE     1 BC4  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 BC4  6 HOH B4043  HOH B4044                                          
SITE     1 BC5  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC5  5 GLU B 220                                                     
SITE     1 BC6  5 PHE C  87  ALA C  89  HIS C 112  HOH C4073                    
SITE     2 BC6  5 ILE D 167                                                     
SITE     1 BC7  3 PHE C 160  TYR C 190  HOH C4118                               
SITE     1 BC8  4 PHE C  10  PRO C 410  GLN C 444  HOH C4300                    
SITE     1 BC9  4 ASN C 227  TYR C 230  ARG C 276  ARG C 279                    
SITE     1 CC1  5 THR C 296  ASP C 297  HIS C 304  ASN C 372                    
SITE     2 CC1  5 HOH C4306                                                     
SITE     1 CC2  5 GLN C 395  ARG C 400  SER C 401  HOH C4269                    
SITE     2 CC2  5 HOH C4307                                                     
SITE     1 CC3  3 ARG C 281  GLU C 283  PRO C 343                               
SITE     1 CC4  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 CC4  5 GLU C 252                                                     
SITE     1 CC5  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 CC5  6 ASP C 305  HOH C4201                                          
SITE     1 CC6  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 CC6  6 ASP C 373  HOH C4245                                          
SITE     1 CC7  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 CC7  6 ASP C 434  HOH C4295                                          
SITE     1 CC8  8 GLN D  82  GLN D 106  TYR D 110  SER D 243                    
SITE     2 CC8  8 ARG D 352  GLY D 420  HOH D4018  HOH D4022                    
SITE     1 CC9 12 SER D 121  TYR D 122  SER D 123  ARG D 214                    
SITE     2 CC9 12 ASN D 215  GLU D 220   MN D2001  HOH D4034                    
SITE     3 CC9 12 HOH D4059  HOH D4080  HOH D4081  HOH D4173                    
SITE     1 DC1  6 SER D 121  GLU D 220  SO4 D1473  HOH D4033                    
SITE     2 DC1  6 HOH D4034  HOH D4082                                          
SITE     1 DC2  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 DC2  6 HOH D4038  HOH D4039                                          
SITE     1 DC3  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 DC3  5 GLU D 220                                                     
SITE     1 DC4  4 SER L  30  SER L  67  GLY L  68  HOH L4009                    
SITE     1 DC5  2 ASN B  99  PHE B 100                                          
SITE     1 DC6  9 ARG A 281  MET A 285  HOH A4334  HOH A4355                    
SITE     2 DC6  9 LEU B 317  ASN B 320  HOH B4218  HOH B4219                    
SITE     3 DC6  9 HOH B4220                                                     
SITE     1 DC7  5 SER B 369  ASN B 371  PRO B 381  SER B 398                    
SITE     2 DC7  5 GLU B 400                                                     
SITE     1 DC8  3 ASN D  99  SER D 101  NAG D3372                               
SITE     1 DC9  7 ARG C 281  MET C 285  HOH C4174  ASN D 320                    
SITE     2 DC9  7 HOH D4174  HOH D4176  HOH D4177                               
SITE     1 EC1  4 ASN D 371  SER D 398  GLU D 400  NAG D3099                    
CRYST1  259.710  144.960  104.770  90.00  90.00  90.00 P 21 21 2     8          
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      0.003850  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009545        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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