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Database: PDB
Entry: 3ZE2
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HEADER    CELL ADHESION/IMMUNE SYSTEM/PEPTIDE     03-DEC-12   3ZE2              
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: RESIDUE 32-488;                                            
COMPND   5 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 27-498;                                           
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 10E5 FAB HEAVY CHAIN;                                      
COMPND  15 CHAIN: H, E;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: 10E5 FAB LIGHT CHAIN;                                      
COMPND  19 CHAIN: L, F;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: RGD PEPTIDE;                                               
COMPND  23 CHAIN: I, J                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PEF1;                                      
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  24 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  26 OTHER_DETAILS: HYBRIDOMA;                                            
SOURCE  27 MOL_ID: 4;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  29 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  30 ORGANISM_TAXID: 10090;                                               
SOURCE  31 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  32 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  34 OTHER_DETAILS: HYBRIDOMA;                                            
SOURCE  35 MOL_ID: 5;                                                           
SOURCE  36 SYNTHETIC: YES;                                                      
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM-PEPTIDE COMPLEX, CELL ADHESIN-IMMUNE      
KEYWDS   2 SYSTEM-PEPTIDE COMPLEX, CELL ADHESION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   2   10-JUL-13 3ZE2    1       JRNL                                     
REVDAT   1   05-JUN-13 3ZE2    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.    2.35 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) : 2.350                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.018                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.96                          
REMARK   3   NUMBER OF REFLECTIONS             : 146559                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1755                          
REMARK   3   R VALUE            (WORKING SET) : 0.1753                          
REMARK   3   FREE R VALUE                     : 0.2037                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1017                            
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 54.0320 -  4.4947    1.00    21443   140  0.1567 0.1813        
REMARK   3     2  4.4947 -  3.5678    1.00    20864   176  0.1476 0.1745        
REMARK   3     3  3.5678 -  3.1168    1.00    20746   137  0.1722 0.1834        
REMARK   3     4  3.1168 -  2.8319    1.00    20686   146  0.1804 0.2380        
REMARK   3     5  2.8319 -  2.6289    1.00    20663   152  0.2027 0.2479        
REMARK   3     6  2.6289 -  2.4739    1.00    20600   132  0.2379 0.3057        
REMARK   3     7  2.4739 -  2.3500    1.00    20540   134  0.2629 0.2697        
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              : 0.333                                         
REMARK   3   B_SOL              : 46.232                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.30             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.12            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.4                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.7988                                               
REMARK   3    B22 (A**2) : -0.6543                                              
REMARK   3    B33 (A**2) : -0.3375                                              
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      :  0.006          21086                                  
REMARK   3   ANGLE     :  0.676          28562                                  
REMARK   3   CHIRALITY :  0.043           3186                                  
REMARK   3   PLANARITY :  0.003           3700                                  
REMARK   3   DIHEDRAL  : 13.902           7674                                  
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):  44.5823  84.4665  53.3158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1817 T22:   0.0810                                     
REMARK   3      T33:   0.1277 T12:  -0.0007                                     
REMARK   3      T13:   0.0012 T23:   0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9445 L22:   0.8007                                     
REMARK   3      L33:   0.7587 L12:  -0.0788                                     
REMARK   3      L13:  -0.3304 L23:   0.3767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:   0.0030 S13:  -0.0049                       
REMARK   3      S21:  -0.0792 S22:  -0.0423 S23:   0.0891                       
REMARK   3      S31:   0.0270 S32:  -0.0378 S33:   0.0268                       
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):  78.9097  82.1180 117.8466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2679 T22:   0.1888                                     
REMARK   3      T33:   0.1273 T12:   0.0449                                     
REMARK   3      T13:   0.0586 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3797 L22:   0.7833                                     
REMARK   3      L33:   1.6570 L12:   0.0142                                     
REMARK   3      L13:  -0.2429 L23:  -0.2802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0774 S12:  -0.0038 S13:  -0.0828                       
REMARK   3      S21:  -0.0627 S22:  -0.0183 S23:  -0.1369                       
REMARK   3      S31:   0.3724 S32:   0.1725 S33:   0.0803                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:56                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 117.3628  83.7845  35.0762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4939 T22:   1.1278                                     
REMARK   3      T33:   0.7299 T12:   0.3152                                     
REMARK   3      T13:  -0.0711 T23:  -0.1019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2159 L22:   0.9767                                     
REMARK   3      L33:   2.4804 L12:  -1.3378                                     
REMARK   3      L13:  -0.0799 L23:   0.5726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2614 S12:   0.0518 S13:  -0.1054                       
REMARK   3      S21:   0.2217 S22:   0.1098 S23:  -0.6032                       
REMARK   3      S31:   0.2866 S32:   0.7165 S33:   0.1648                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 57:108 OR RESID 354:433)            
REMARK   3    ORIGIN FOR THE GROUP (A):  94.9303 102.1685  53.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2626 T22:   0.4293                                     
REMARK   3      T33:   0.4457 T12:   0.0333                                     
REMARK   3      T13:  -0.0550 T23:  -0.0764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5834 L22:   1.2067                                     
REMARK   3      L33:   2.7810 L12:  -0.3256                                     
REMARK   3      L13:  -0.6764 L23:   1.1158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0237 S12:  -0.2778 S13:   0.2733                       
REMARK   3      S21:   0.1184 S22:   0.2052 S23:  -0.2351                       
REMARK   3      S31:   0.1248 S32:   0.5371 S33:  -0.1769                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 109:352 OR RESID 2001:2003)         
REMARK   3    ORIGIN FOR THE GROUP (A):  60.9882 112.2779  63.8442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2205 T22:   0.1241                                     
REMARK   3      T33:   0.1653 T12:  -0.0037                                     
REMARK   3      T13:   0.0299 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4121 L22:   1.9466                                     
REMARK   3      L33:   0.4898 L12:   0.2606                                     
REMARK   3      L13:   0.0082 L23:   0.2384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:  -0.1312 S13:   0.2094                       
REMARK   3      S21:   0.0090 S22:   0.0403 S23:  -0.0272                       
REMARK   3      S31:  -0.1390 S32:   0.0353 S33:  -0.0416                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 434:471                              
REMARK   3    ORIGIN FOR THE GROUP (A): 109.9487  83.6738  19.2078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5623 T22:   0.9402                                     
REMARK   3      T33:   0.5506 T12:   0.2446                                     
REMARK   3      T13:   0.0124 T23:   0.1252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4859 L22:   1.6869                                     
REMARK   3      L33:   4.4313 L12:   0.3221                                     
REMARK   3      L13:   0.0168 L23:  -0.0444                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0138 S12:   0.0963 S13:  -0.1398                       
REMARK   3      S21:   0.0507 S22:   0.3954 S23:  -0.4773                       
REMARK   3      S31:   0.4502 S32:   0.1813 S33:  -0.2196                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 109:352 OR RESID 2001:2003)         
REMARK   3    ORIGIN FOR THE GROUP (A):  54.6832  97.2554  99.6057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2455 T22:   0.4185                                     
REMARK   3      T33:   0.0868 T12:  -0.0475                                     
REMARK   3      T13:   0.0272 T23:   0.0375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0868 L22:   0.7135                                     
REMARK   3      L33:   1.9330 L12:  -0.2137                                     
REMARK   3      L13:   0.5605 L23:  -0.2128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1267 S12:   0.1673 S13:   0.2417                       
REMARK   3      S21:  -0.0746 S22:   0.0525 S23:   0.0701                       
REMARK   3      S31:  -0.0036 S32:  -0.5932 S33:   0.0333                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 57:108 OR RESID 353:433)            
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9148  95.7194 115.8250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7602 T22:   1.2791                                     
REMARK   3      T33:   1.1286 T12:   0.1451                                     
REMARK   3      T13:   0.1861 T23:   0.3192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0509 L22:   0.9505                                     
REMARK   3      L33:   0.3319 L12:   0.1125                                     
REMARK   3      L13:   0.0109 L23:  -0.5572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3051 S12:  -0.1019 S13:  -0.2234                       
REMARK   3      S21:   0.2018 S22:  -0.1310 S23:   0.1736                       
REMARK   3      S31:   0.4157 S32:   0.0548 S33:   0.3445                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN H AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 110.5054  86.7539  87.0947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7396 T22:   1.0917                                     
REMARK   3      T33:   0.6136 T12:   0.3161                                     
REMARK   3      T13:   0.3249 T23:   0.2665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8651 L22:   0.0505                                     
REMARK   3      L33:   1.2199 L12:  -0.0930                                     
REMARK   3      L13:  -0.6644 L23:   0.2202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.4970 S13:  -0.0376                       
REMARK   3      S21:  -0.4988 S22:  -0.3409 S23:  -0.2886                       
REMARK   3      S31:   0.7782 S32:   0.5176 S33:   0.3840                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 146.5635  80.0226  83.3810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4119 T22:   1.0673                                     
REMARK   3      T33:   1.1558 T12:   0.2636                                     
REMARK   3      T13:   0.1487 T23:   0.2074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6396 L22:   1.1726                                     
REMARK   3      L33:   1.1599 L12:  -0.5896                                     
REMARK   3      L13:   0.4661 L23:   0.1951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4002 S12:   0.8650 S13:  -0.1064                       
REMARK   3      S21:  -0.2602 S22:  -0.0664 S23:  -0.7887                       
REMARK   3      S31:  -0.3045 S32:   0.0562 S33:  -0.1398                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 119.7925  97.5928 103.2844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3163 T22:   1.1411                                     
REMARK   3      T33:   0.9598 T12:   0.0078                                     
REMARK   3      T13:   0.0573 T23:   0.3962                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4038 L22:   0.2255                                     
REMARK   3      L33:   0.3329 L12:  -0.1335                                     
REMARK   3      L13:  -0.0884 L23:  -0.1830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0847 S12:   0.0910 S13:   0.5058                       
REMARK   3      S21:   0.0168 S22:  -0.2561 S23:  -0.6528                       
REMARK   3      S31:  -0.0210 S32:   0.8177 S33:  -0.0417                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 150.0809  95.3376  82.6679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1280 T22:   1.4278                                     
REMARK   3      T33:   1.6964 T12:   0.2729                                     
REMARK   3      T13:   0.6509 T23:   0.6103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0968 L22:   0.8049                                     
REMARK   3      L33:   1.3891 L12:   0.1958                                     
REMARK   3      L13:  -0.1806 L23:   0.1231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4573 S12:   0.0979 S13:   0.0678                       
REMARK   3      S21:  -0.8535 S22:  -0.0582 S23:  -0.6220                       
REMARK   3      S31:  -0.5677 S32:   0.2103 S33:  -0.1822                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5213  91.1187  80.7064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1775 T22:   0.2531                                     
REMARK   3      T33:   0.3260 T12:  -0.0149                                     
REMARK   3      T13:   0.0301 T23:  -0.0752                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3409 L22:   0.8334                                     
REMARK   3      L33:   1.1138 L12:   0.5521                                     
REMARK   3      L13:  -0.3135 L23:  -0.1971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1379 S12:  -0.1304 S13:   0.1636                       
REMARK   3      S21:   0.1728 S22:  -0.1908 S23:   0.0605                       
REMARK   3      S31:  -0.0341 S32:  -0.1720 S33:   0.0469                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1378  78.0159  88.4692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3292 T22:   0.4070                                     
REMARK   3      T33:   0.3587 T12:  -0.0964                                     
REMARK   3      T13:  -0.1141 T23:  -0.0929                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5950 L22:   0.9909                                     
REMARK   3      L33:   1.4651 L12:   0.8325                                     
REMARK   3      L13:   0.6431 L23:   0.3623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4510 S12:  -0.6521 S13:  -0.1113                       
REMARK   3      S21:   0.4501 S22:  -0.2937 S23:  -0.1700                       
REMARK   3      S31:   0.3705 S32:  -0.2128 S33:  -0.1085                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5198  90.3747  61.5357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1713 T22:   0.4595                                     
REMARK   3      T33:   0.4263 T12:  -0.0075                                     
REMARK   3      T13:  -0.0386 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2886 L22:   0.0805                                     
REMARK   3      L33:   0.5779 L12:   0.1319                                     
REMARK   3      L13:  -0.0937 L23:   0.0089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0465 S12:   0.3342 S13:   0.2221                       
REMARK   3      S21:  -0.0929 S22:  -0.0408 S23:   0.1575                       
REMARK   3      S31:   0.0252 S32:  -0.3849 S33:  -0.0328                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2430  90.9560  80.8720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2662 T22:   0.3919                                     
REMARK   3      T33:   0.7221 T12:   0.0020                                     
REMARK   3      T13:  -0.0931 T23:  -0.2851                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3133 L22:   1.0709                                     
REMARK   3      L33:   2.6326 L12:  -0.0658                                     
REMARK   3      L13:   0.2211 L23:   0.8404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1465 S12:  -0.2729 S13:   0.9112                       
REMARK   3      S21:   0.0799 S22:  -0.1429 S23:   0.3207                       
REMARK   3      S31:  -0.3563 S32:  -0.2941 S33:   0.2473                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN I                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3904 103.5836  74.0419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3614 T22:   0.3523                                     
REMARK   3      T33:   0.1725 T12:  -0.0463                                     
REMARK   3      T13:  -0.0002 T23:   0.0624                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8167 L22:   1.3652                                     
REMARK   3      L33:   6.0801 L12:  -2.0311                                     
REMARK   3      L13:  -0.6067 L23:  -0.7400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4060 S12:  -0.5273 S13:  -0.2410                       
REMARK   3      S21:   0.3738 S22:   0.0214 S23:   0.1399                       
REMARK   3      S31:   0.0839 S32:  -0.2747 S33:  -0.1531                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN J                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  71.0147  90.5198  91.4768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5698 T22:   0.4156                                     
REMARK   3      T33:   0.2324 T12:  -0.0228                                     
REMARK   3      T13:   0.0188 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5950 L22:   0.3928                                     
REMARK   3      L33:   2.5984 L12:  -0.4193                                     
REMARK   3      L13:   1.8002 L23:  -0.9739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2787 S12:   0.2197 S13:  -0.4949                       
REMARK   3      S21:  -0.2563 S22:  -0.0551 S23:  -0.1592                       
REMARK   3      S31:   0.5715 S32:   0.4495 S33:  -0.1278                       
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 3ZE2 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-54974.                                       
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                       : 23ID                               
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   : 146644                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
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      116.60500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      116.60500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       71.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, I                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, J, L                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
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     ASN D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     CYS D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     ARG D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     VAL D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     CYS D    13                                                      
REMARK 465     GLN D    14                                                      
REMARK 465     GLN D    15                                                      
REMARK 465     CYS D    16                                                      
REMARK 465     LEU D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     VAL D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     MET D    22                                                      
REMARK 465     CYS D    23                                                      
REMARK 465     ALA D    24                                                      
REMARK 465     TRP D    25                                                      
REMARK 465     CYS D    26                                                      
REMARK 465     SER D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     GLU D    29                                                      
REMARK 465     ALA D    30                                                      
REMARK 465     LEU D    31                                                      
REMARK 465     PRO D    32                                                      
REMARK 465     LEU D    33                                                      
REMARK 465     GLY D    34                                                      
REMARK 465     SER D    35                                                      
REMARK 465     PRO D    36                                                      
REMARK 465     ARG D    37                                                      
REMARK 465     CYS D    38                                                      
REMARK 465     ASP D    39                                                      
REMARK 465     LEU D    40                                                      
REMARK 465     LYS D    41                                                      
REMARK 465     GLU D    42                                                      
REMARK 465     ASN D    43                                                      
REMARK 465     LEU D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     LYS D    46                                                      
REMARK 465     ASP D    47                                                      
REMARK 465     ASN D    48                                                      
REMARK 465     CYS D    49                                                      
REMARK 465     ALA D    50                                                      
REMARK 465     PRO D    51                                                      
REMARK 465     GLU D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     ILE D    54                                                      
REMARK 465     GLU D    55                                                      
REMARK 465     PHE D    56                                                      
REMARK 465     PRO D    57                                                      
REMARK 465     VAL D    58                                                      
REMARK 465     LYS D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     SER D    74                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     SER D    77                                                      
REMARK 465     SER D    78                                                      
REMARK 465     GLN D    79                                                      
REMARK 465     ASP D   434                                                      
REMARK 465     CYS D   435                                                      
REMARK 465     ALA D   436                                                      
REMARK 465     CYS D   437                                                      
REMARK 465     GLN D   438                                                      
REMARK 465     ALA D   439                                                      
REMARK 465     GLN D   440                                                      
REMARK 465     ALA D   441                                                      
REMARK 465     GLU D   442                                                      
REMARK 465     PRO D   443                                                      
REMARK 465     ASN D   444                                                      
REMARK 465     SER D   445                                                      
REMARK 465     HIS D   446                                                      
REMARK 465     ARG D   447                                                      
REMARK 465     CYS D   448                                                      
REMARK 465     ASN D   449                                                      
REMARK 465     ASN D   450                                                      
REMARK 465     GLY D   451                                                      
REMARK 465     ASN D   452                                                      
REMARK 465     GLY D   453                                                      
REMARK 465     THR D   454                                                      
REMARK 465     PHE D   455                                                      
REMARK 465     GLU D   456                                                      
REMARK 465     CYS D   457                                                      
REMARK 465     GLY D   458                                                      
REMARK 465     VAL D   459                                                      
REMARK 465     CYS D   460                                                      
REMARK 465     ARG D   461                                                      
REMARK 465     CYS D   462                                                      
REMARK 465     GLY D   463                                                      
REMARK 465     PRO D   464                                                      
REMARK 465     GLY D   465                                                      
REMARK 465     TRP D   466                                                      
REMARK 465     LEU D   467                                                      
REMARK 465     GLY D   468                                                      
REMARK 465     SER D   469                                                      
REMARK 465     GLN D   470                                                      
REMARK 465     CYS D   471                                                      
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 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     ARG A   90   CZ                                                  
REMARK 480     GLN A  177   CD                                                  
REMARK 480     GLU C   48   CD                                                  
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   OE1  GLN A   351     O    HOH A  3394              2.19            
REMARK 500   OG   SER A   384     O    HOH A  3430              2.06            
REMARK 500   OD1  ASP B   126     O    HOH B  3039              2.13            
REMARK 500   HG A SER B   130     HG A SER B   337              1.32            
REMARK 500   OG B SER B   130     OD2  ASP B   336              2.14            
REMARK 500   OD1  ASN B   148     O    HOH B  3048              2.10            
REMARK 500   OE1B GLN B   319     O    HOH B  3169              2.13            
REMARK 500   O    MET B   335     O    HOH B  3040              2.10            
REMARK 500   ND2  ASN B   371     C1   NAG B  3371              1.44            
REMARK 500   ND2  ASN B   371     C2   NAG B  3371              2.12            
REMARK 500   OD1B ASN C     2     O    HOH C  3001              2.12            
REMARK 500   OE1  GLN C   351     O    HOH C  3221              2.13            
REMARK 500   OG   SER C   384     O    HOH C  3243              2.05            
REMARK 500   N  B GLY I   492     O    HOH A  3238              2.03            
REMARK 500   NH2A ARG I   493     O    HOH A  3222              2.17            
REMARK 500   OG   SER L     9     O    HOH L  3004              2.19            
REMARK 500   O3   SO4 A  1457     O    HOH A  3482              2.09            
REMARK 500   O    HOH A  3052     O    HOH A  3126              2.18            
REMARK 500   O    HOH A  3052     O    HOH B  3055              1.98            
REMARK 500   O    HOH A  3058     O    HOH A  3096              2.08            
REMARK 500   O    HOH A  3077     O    HOH A  3210              2.05            
REMARK 500   O    HOH A  3077     O    HOH A  3220              2.06            
REMARK 500   O    HOH A  3111     O    HOH A  3270              2.20            
REMARK 500   O    HOH A  3137     O    HOH A  3138              2.19            
REMARK 500   O    HOH A  3137     O    HOH A  3320              1.95            
REMARK 500   O    HOH A  3138     O    HOH A  3319              2.03            
REMARK 500   O    HOH A  3140     O    HOH A  3323              1.85            
REMARK 500   O    HOH A  3195     O    HOH A  3445              1.80            
REMARK 500   O    HOH A  3195     O    HOH A  3449              1.77            
REMARK 500   O    HOH A  3195     O    HOH A  3446              1.90            
REMARK 500   O    HOH A  3199     O    HOH A  3255              2.11            
REMARK 500   O    HOH A  3200     O    HOH A  3255              2.18            
REMARK 500   O    HOH A  3216     O    HOH A  3476              2.15            
REMARK 500   O    HOH A  3216     O    HOH A  3217              2.15            
REMARK 500   O    HOH A  3217     O    HOH A  3476              2.03            
REMARK 500   O    HOH A  3220     O    HOH A  3223              2.09            
REMARK 500   O    HOH A  3237     O    HOH A  3238              2.16            
REMARK 500   O    HOH A  3314     O    HOH A  3319              2.14            
REMARK 500   O    HOH A  3316     O    HOH A  3381              2.07            
REMARK 500   O    HOH A  3322     O    HOH A  3323              2.07            
REMARK 500   O    HOH A  3323     O    HOH A  3324              2.19            
REMARK 500   O    HOH A  3343     O    HOH A  3360              2.05            
REMARK 500   O    HOH A  3358     O    HOH A  3359              2.17            
REMARK 500   O    HOH A  3360     O    HOH A  3425              2.02            
REMARK 500   O    HOH A  3381     O    HOH A  3382              2.09            
REMARK 500   O    HOH A  3445     O    HOH A  3449              1.81            
REMARK 500   O    HOH A  3446     O    HOH A  3449              2.03            
REMARK 500   O    HOH B  3031     O    HOH B  3164              2.15            
REMARK 500   O    HOH B  3040     O    HOH B  3041              2.11            
REMARK 500   O    HOH C  3018     O    HOH C  3036              2.08            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  3252     O    HOH A  3480     1556     2.18            
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    GLN A  47       -2.95     79.21                                   
REMARK 500    SER A 101     -127.40     57.07                                   
REMARK 500    LYS A 118     -116.99     60.04                                   
REMARK 500    GLU A 123      133.98     98.52                                   
REMARK 500    PHE A 191       12.67     83.63                                   
REMARK 500    LEU A 212      -43.97     74.79                                   
REMARK 500    TRP A 235      108.22    -57.36                                   
REMARK 500    THR A 296      145.68   -171.36                                   
REMARK 500    ARG B   8      -45.25   -141.42                                   
REMARK 500    PHE B  56       77.30   -161.97                                   
REMARK 500    ASP B  66       48.35   -152.83                                   
REMARK 500    ILE B 131       30.27    -87.80                                   
REMARK 500    VAL B 157      -85.27   -124.50                                   
REMARK 500    PRO B 169     -178.56    -69.40                                   
REMARK 500    LYS B 181       56.85    -92.75                                   
REMARK 500    SER B 213     -151.70   -110.00                                   
REMARK 500    ASP B 241       70.82   -107.68                                   
REMARK 500    LEU B 258      -10.04     86.05                                   
REMARK 500    SER B 334       82.81    -63.83                                   
REMARK 500    MET B 335      -60.72     74.61                                   
REMARK 500    CYS B 374      -82.84    -97.84                                   
REMARK 500    SER C 101     -133.05     50.20                                   
REMARK 500    LYS C 118     -118.91     64.65                                   
REMARK 500    GLU C 123      138.81     96.22                                   
REMARK 500    PHE C 191       14.16     80.14                                   
REMARK 500    LEU C 212      -49.19     75.74                                   
REMARK 500    THR C 296      143.89   -173.87                                   
REMARK 500    VAL C 325      -31.11   -132.87                                   
REMARK 500    PRO C 337       90.92    -66.66                                   
REMARK 500    VAL D 107      -58.21   -133.11                                   
REMARK 500    MET D 142      -40.64   -173.54                                   
REMARK 500    ASN D 148       65.99   -104.58                                   
REMARK 500    VAL D 157      -83.51   -127.72                                   
REMARK 500    SER D 213     -147.01   -103.82                                   
REMARK 500    ARG D 214      135.65   -170.79                                   
REMARK 500    LEU D 258       -6.38     85.82                                   
REMARK 500    SER D 334     -169.73   -163.56                                   
REMARK 500    LYS D 410      -13.89     74.21                                   
REMARK 500    LEU E 100      -67.27    -90.89                                   
REMARK 500    VAL E 133      -73.28    -64.63                                   
REMARK 500    SER E 162       29.69     41.68                                   
REMARK 500    SER E 178       67.31     37.65                                   
REMARK 500    ASP E 179      -13.81     78.23                                   
REMARK 500    SER F  77       83.93     64.45                                   
REMARK 500    ASN F 190      -68.23   -121.07                                   
REMARK 500    ASN F 212      -66.76     67.92                                   
REMARK 500    SER H  85       58.03     38.64                                   
REMARK 500    ALA H  92     -179.14   -172.46                                   
REMARK 500    TYR H 101      -58.11   -124.02                                   
REMARK 500    THR H 122       97.13    -67.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 495   OD1                                                    
REMARK 620 2 SER B 121   OG   92.8                                              
REMARK 620 3 SER B 123   OG   86.3  91.5                                        
REMARK 620 4 GLU B 220   OE2  92.4  88.8 178.7                                  
REMARK 620 5 HOH B3035   O   162.7  79.0  78.8 102.6                            
REMARK 620 6 HOH B3038   O    96.3 169.3  94.6  85.3  93.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 251   OD2                                                    
REMARK 620 2 HOH B3117   O    90.7                                              
REMARK 620 3 SER B 123   O    80.4 105.3                                        
REMARK 620 4 HOH B3041   O    97.8 146.6 107.9                                  
REMARK 620 N                    1     2     3                                   
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 217   OD1                                                    
REMARK 620 2 ASP B 217   O    76.2                                              
REMARK 620 3 ASP B 158   OD2 100.3 169.4                                        
REMARK 620 4 ASN B 215   OD1  87.5  90.5  99.5                                  
REMARK 620 5 PRO B 219   O   105.1  87.8  83.4 166.5                            
REMARK 620 6 GLU B 220   OE1 166.6  93.2  91.6  84.5  82.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D3011   O                                                      
REMARK 620 2 SER D 121   OG  172.2                                              
REMARK 620 3 SER D 123   OG   96.4  90.2                                        
REMARK 620 4 GLU D 220   OE2  86.0  87.9 173.0                                  
REMARK 620 5 ASP J 495   OD1  93.6  91.2  84.1  89.2                            
REMARK 620 6 HOH D3009   O   102.2  74.9  79.4 106.5 158.2                      
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 HOH D3014   O                                                      
REMARK 620 2 ASP D 127   OD2  78.1                                              
REMARK 620 3 ASP D 251   OD2 102.6  90.0                                        
REMARK 620 4 HOH D3010   O    90.3 167.5  87.9                                  
REMARK 620 5 SER D 123   O   171.9  94.2  80.0  97.5                            
REMARK 620 6 ASP D 126   OD1  96.7  82.0 157.1 104.3  79.3                      
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 PRO D 219   O                                                      
REMARK 620 2 ASP D 158   OD2  78.5                                              
REMARK 620 3 GLU D 220   OE1  86.8  97.0                                        
REMARK 620 4 ASP D 217   O    93.5 166.1  93.8                                  
REMARK 620 5 ASN D 215   OD1 174.4  97.0  90.5  91.6                            
REMARK 620 6 ASP D 217   OD1  96.8  93.5 169.3  76.0  86.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 GLU A 243   OE2  54.6                                              
REMARK 620 3 ASP A 245   OD1 122.1  67.4                                        
REMARK 620 4 ASP A 247   O    79.8  79.1  91.3                                  
REMARK 620 5 THR A 250   O    70.7 125.0 166.5  86.7                            
REMARK 620 6 THR A 250   OG1 139.6 145.3  90.1  75.2  76.5                      
REMARK 620 7 GLU A 252   OE1  85.0  80.3  84.5 159.0 102.0 125.2                
REMARK 620 8 GLU A 252   OE2 124.7 131.0  91.3 147.8  83.4  72.7  53.1          
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 ASP A 301   OD1                                                    
REMARK 620 2 ASP A 297   OD1  77.7                                              
REMARK 620 3 ASN A 299   OD1  82.4  77.6                                        
REMARK 620 4 ARG A 303   O    90.5  82.7 160.1                                  
REMARK 620 5 ASP A 305   OD1 148.9 130.6 113.1  82.2                            
REMARK 620 6 ASP A 305   OD2 157.8  81.8  84.9  95.4  53.3                      
REMARK 620 7 HOH A3348   O    81.4 156.5  89.1 108.2  72.4 116.6                
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 TYR A 371   O    75.8                                              
REMARK 620 3 ASP A 373   OD2  88.7  93.3                                        
REMARK 620 4 ASP A 369   OD1  75.2  89.0 162.7                                  
REMARK 620 5 ASP A 367   OD1  81.5 157.2  84.6  86.6                            
REMARK 620 6 ASP A 373   OD1 134.4  82.4  52.9 144.3 113.5                      
REMARK 620 7 HOH A3413   O   149.5 100.1 121.8  74.5 100.2  73.1                
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 ASP A 426   OD1                                                    
REMARK 620 2 ASN A 430   OD1  85.0                                              
REMARK 620 3 TYR A 432   O    79.2  87.4                                        
REMARK 620 4 ASP A 428   OD1  77.0  86.0 155.7                                  
REMARK 620 5 ASP A 434   OD1 134.4 134.4  81.0 119.7                            
REMARK 620 6 ASP A 434   OD2  87.5 171.0  96.1  87.4  54.5                      
REMARK 620 7 HOH A3470   O   147.7  79.5 127.8  73.8  73.7 104.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 243   OE2                                                    
REMARK 620 2 ASP C 245   OD1  59.9                                              
REMARK 620 3 GLU C 252   OE1  81.1  87.6                                        
REMARK 620 4 GLU C 252   OE2 128.1  90.5  54.1                                  
REMARK 620 5 ASP C 247   O    68.4  82.4 148.9 154.6                            
REMARK 620 6 THR C 250   O   127.3 167.2 103.6  91.1  90.7                      
REMARK 620 7 THR C 250   OG1 138.8  90.7 129.2  75.2  80.5  77.5                
REMARK 620 8 GLU C 243   OE1  54.9 114.8  84.1 130.8  73.7  73.1 140.2          
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 ASN C 299   OD1                                                    
REMARK 620 2 ASP C 305   OD1 116.2                                              
REMARK 620 3 HOH C3201   O    98.1  76.3                                        
REMARK 620 4 ASP C 297   OD1  74.9 130.5 153.0                                  
REMARK 620 5 ASP C 301   OD1  80.1 153.3  80.7  72.4                            
REMARK 620 6 ARG C 303   O   154.7  81.1 104.1  79.9  91.7                      
REMARK 620 7 ASP C 305   OD2  83.3  53.6 122.8  82.9 153.0  94.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 369   OD1                                                    
REMARK 620 2 ASP C 373   OD1 144.6                                              
REMARK 620 3 ASP C 367   OD1  81.4 114.5                                        
REMARK 620 4 ASP C 373   OD2 162.6  52.9  88.8                                  
REMARK 620 5 HOH C3236   O    72.5  73.9  98.0 123.4                            
REMARK 620 6 TYR C 371   O    92.2  81.9 159.4  92.0  98.7                      
REMARK 620 7 ASP C 365   OD1  74.7 136.2  82.3  89.8 146.8  77.1                
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 434   OD1                                                    
REMARK 620 2 HOH C3274   O    73.1                                              
REMARK 620 3 ASP C 426   OD1 136.3 147.4                                        
REMARK 620 4 ASN C 430   OD1 134.7  79.3  83.0                                  
REMARK 620 5 TYR C 432   O    86.1 129.2  75.3  84.3                            
REMARK 620 6 ASP C 428   OD1 115.7  76.4  76.7  91.0 152.0                      
REMARK 620 7 ASP C 434   OD2  54.1 104.9  89.6 171.2  98.4  82.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1454                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1456                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E1220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1456                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J1498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1457                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1457                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B3320  THROUGH MAN B3325  BOUND TO ASN B 320           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG C2015  BOUND TO ASN C  15                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
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: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-SACCHARIDE                     
REMARK 800  NAG B3371  AND NAG B3372                                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZDX   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 3ZDY   RELATED DB: PDB                                   
REMARK 900  INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE                   
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 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                                                             
DBREF  3ZE2 A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZE2 B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZE2 C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZE2 D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZE2 E    1   221  PDB    3ZE2     3ZE2             1    221             
DBREF  3ZE2 F    1   214  PDB    3ZE2     3ZE2             1    214             
DBREF  3ZE2 H    1   221  PDB    3ZE2     3ZE2             1    221             
DBREF  3ZE2 I  492   497  PDB    3ZE2     3ZE2           492    497             
DBREF  3ZE2 J  492   497  PDB    3ZE2     3ZE2           492    497             
DBREF  3ZE2 L    1   214  PDB    3ZE2     3ZE2             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 I    6  GLY ARG GLY ASP SER PRO                                      
SEQRES   1 J    6  GLY ARG GLY ASP SER PRO                                      
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     MN  B2001       1                                                       
HET     MN  B2002       1                                                       
HET     MN  B2003       1                                                       
HET    NAG  B3320      26                                                       
HET    NAG  B3321      26                                                       
HET    BMA  B3322      19                                                       
HET    MAN  B3323      21                                                       
HET    MAN  B3324      20                                                       
HET    MAN  B3325      21                                                       
HET    NAG  B3371      26                                                       
HET    NAG  B3372      27                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    NAG  C2015      27                                                       
HET     MN  D2001       1                                                       
HET     MN  D2002       1                                                       
HET     MN  D2003       1                                                       
HET    NAG  D3320      26                                                       
HET    NAG  D3321      26                                                       
HET    BMA  D3322      20                                                       
HET    MAN  D3323      21                                                       
HET    GOL  A1455      14                                                       
HET    GOL  C1454      14                                                       
HET    GOL  F1215      14                                                       
HET    GOL  A1456      14                                                       
HET    GOL  C1455      14                                                       
HET    GOL  E1220      14                                                       
HET    GOL  F1216      14                                                       
HET    GOL  C1456      14                                                       
HET    GOL  J1498      14                                                       
HET    GOL  C1457      14                                                       
HET    SO4  A1457       5                                                       
HET    SO4  A1458       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  11   MN    6(MN 2+)                                                     
FORMUL  12  SO4    2(O4 S 2-)                                                   
FORMUL  13  GOL    10(C3 H8 O3)                                                 
FORMUL  14   CA    8(CA 2+)                                                     
FORMUL  15  BMA    2(C6 H12 O6)                                                 
FORMUL  16  MAN    4(C6 H12 O6)                                                 
FORMUL  17  NAG    7(C8 H15 N O6)                                               
FORMUL  18  HOH   *1318(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  SER B   20  1                                   9    
HELIX    8   8 LEU B   40  ASP B   47  1                                   8    
HELIX    9   9 ALA B   50  GLU B   52  5                                   3    
HELIX   10  10 ASP B   76  VAL B   80  5                                   5    
HELIX   11  11 SER B  121  LYS B  125  5                                   5    
HELIX   12  12 ASP B  126  GLN B  132  5                                   7    
HELIX   13  13 ASN B  133  ARG B  143  1                                  11    
HELIX   14  14 PRO B  169  ASN B  175  1                                   7    
HELIX   15  15 GLN B  199  LYS B  209  1                                  11    
HELIX   16  16 GLY B  221  CYS B  232  1                                  12    
HELIX   17  17 CYS B  232  GLY B  237  1                                   6    
HELIX   18  18 LEU B  258  GLY B  264  5                                   7    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  ILE B  325  1                                  12    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  441  5                                   7    
HELIX   23  23 CYS B  448  GLY B  451  5                                   4    
HELIX   24  24 LEU C  151  ASN C  158  1                                   8    
HELIX   25  25 GLY C  187  LEU C  192  1                                   6    
HELIX   26  26 VAL C  200  TYR C  207  1                                   8    
HELIX   27  27 ASN C  227  PHE C  231  5                                   5    
HELIX   28  28 THR C  259  LEU C  264  1                                   6    
HELIX   29  29 TYR C  440  ALA C  442  5                                   3    
HELIX   30  30 SER D  121  ASP D  126  5                                   6    
HELIX   31  31 ASP D  127  LYS D  144  1                                  18    
HELIX   32  32 PRO D  169  ASN D  175  1                                   7    
HELIX   33  33 CYS D  177  LYS D  181  5                                   5    
HELIX   34  34 GLN D  199  LYS D  209  1                                  11    
HELIX   35  35 GLY D  221  CYS D  232  1                                  12    
HELIX   36  36 CYS D  232  GLY D  237  1                                   6    
HELIX   37  37 LEU D  258  GLY D  264  5                                   7    
HELIX   38  38 SER D  291  LYS D  302  1                                  12    
HELIX   39  39 VAL D  314  LEU D  324  1                                  11    
HELIX   40  40 SER D  337  ARG D  352  1                                  16    
HELIX   41  41 ASN E   28  THR E   32  5                                   5    
HELIX   42  42 PRO E   62  PHE E   64  5                                   3    
HELIX   43  43 THR E   74  SER E   76  5                                   3    
HELIX   44  44 THR E   87  THR E   91  5                                   5    
HELIX   45  45 SER E  162  SER E  164  5                                   3    
HELIX   46  46 PRO E  206  SER E  209  5                                   4    
HELIX   47  47 ASP F   79  PHE F   83  5                                   5    
HELIX   48  48 SER F  121  SER F  127  1                                   7    
HELIX   49  49 LYS F  183  GLU F  187  1                                   5    
HELIX   50  50 ASN H   28  THR H   32  5                                   5    
HELIX   51  51 PRO H   62  PHE H   64  5                                   3    
HELIX   52  52 SER H  162  SER H  164  5                                   3    
HELIX   53  53 SER L  121  SER L  127  1                                   7    
HELIX   54  54 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 4 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 4 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    4  AB 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AD 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AD 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AD 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AE 4 SER A 172  VAL A 175  0                                        
SHEET    2  AE 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AE 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AE 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AF 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AF 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AF 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AF 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AG 4 VAL A 293  THR A 296  0                                        
SHEET    2  AG 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AG 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AG 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AH 2 MET A 314  ARG A 317  0                                        
SHEET    2  AH 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AI 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AI 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AI 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AI 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AJ 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AJ 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  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 VAL B 355  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  THR B 373 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  VAL B 310  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1  BE 2 GLY B 453  GLU B 456  0                                        
SHEET    2  BE 2 VAL B 459  CYS B 462 -1  O  VAL B 459   N  GLU B 456           
SHEET    1  CA 4 THR C   9  ALA C  12  0                                        
SHEET    2  CA 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3  CA 4 ASP C 434  ALA C 439 -1  O  LEU C 435   N  TYR C 448           
SHEET    4  CA 4 SER C 420  VAL C 425 -1  O  SER C 420   N  GLY C 438           
SHEET    1  CB 3 LEU C  23  LYS C  27  0                                        
SHEET    2  CB 3 VAL C  33  ALA C  39 -1  O  ALA C  34   N  HIS C  26           
SHEET    3  CB 3 GLY C  52  PRO C  57 -1  O  GLY C  52   N  ALA C  39           
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  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4  CD 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1  CE 4 SER C 172  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 6 GLU D  60  GLU D  65  0                                        
SHEET    2  DA 6 ARG D  87  LEU D  92 -1  O  ARG D  87   N  LEU D  64           
SHEET    3  DA 6 LEU D 425  PHE D 431  1  O  ILE D 426   N  ILE D  88           
SHEET    4  DA 6 GLU D 411  PRO D 418 -1  O  LYS D 412   N  VAL D 429           
SHEET    5  DA 6 VAL D 355  ARG D 360 -1  O  GLU D 358   N  LYS D 417           
SHEET    6  DA 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  DB 5 VAL D  83  SER D  84  0                                        
SHEET    2  DB 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  DB 5 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    4  DB 5 LEU D 366  THR D 373 -1  O  SER D 367   N  LYS D 402           
SHEET    5  DB 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  DC 6 TYR D 190  THR D 197  0                                        
SHEET    2  DC 6 LEU D 149  PHE D 156 -1  O  ILE D 151   N  THR D 197           
SHEET    3  DC 6 VAL D 112  ASP D 119  1  O  VAL D 112   N  ARG D 150           
SHEET    4  DC 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  DC 6 ILE D 304  VAL D 310  1  O  ASN D 305   N  LEU D 246           
SHEET    6  DC 6 THR D 329  VAL D 332  1  O  THR D 329   N  PHE D 308           
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  TYR E 151           
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  TYR E 151           
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  HIS E 205 -1  O  ASN E 202   N  THR E 159           
SHEET    3  EH 3 THR E 210  LYS E 215 -1  O  THR E 210   N  HIS E 205           
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  GLY H 150           
SHEET    4  HE 4 VAL H 175  GLN H 177  1  N  VAL H 175   O  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  GLY H 150           
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 ASN L 145  ILE L 150 -1  O  TRP L 148   N  ARG L 155           
SHEET    3  LF 4 SER L 191  THR L 197 -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  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  15 CYS C   56    CYS C   65                          1555   1555  2.04  
SSBOND  16 CYS C  107    CYS C  130                          1555   1555  2.03  
SSBOND  17 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  18 CYS D  177    CYS D  184                          1555   1555  2.04  
SSBOND  19 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  20 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  21 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  22 CYS E   22    CYS E   96                          1555   1555  2.04  
SSBOND  23 CYS E  134    CYS F  214                          1555   1555  2.03  
SSBOND  24 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  25 CYS F   23    CYS F   88                          1555   1555  2.04  
SSBOND  26 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  27 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  28 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  29 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  30 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND  31 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.38  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.40  
LINK        CA    CA A2004                 OD1 ASP A 245     1555   1555  2.28  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.35  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.30  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.43  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.42  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.47  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.47  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.38  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.29  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.31  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.47  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.39  
LINK        CA    CA A2005                 O   HOH A3348     1555   1555  2.41  
LINK        CA    CA A2006                 OD1 ASP A 365     1555   1555  2.51  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.26  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.44  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.42  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.33  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.48  
LINK        CA    CA A2006                 O   HOH A3413     1555   1555  2.39  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.36  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.38  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.33  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.32  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.38  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.41  
LINK        CA    CA A2007                 O   HOH A3470     1555   1555  2.37  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK        MN    MN B2001                 OD1 ASP I 495     1555   1555  2.14  
LINK        MN    MN B2001                 OG  SER B 121     1555   1555  2.22  
LINK        MN    MN B2001                 OG  SER B 123     1555   1555  2.27  
LINK        MN    MN B2001                 OE2 GLU B 220     1555   1555  2.23  
LINK        MN    MN B2001                 O   HOH B3035     1555   1555  2.10  
LINK        MN    MN B2001                 O   HOH B3038     1555   1555  2.19  
LINK        MN    MN B2002                 OD2 ASP B 251     1555   1555  2.36  
LINK        MN    MN B2002                 O   HOH B3117     1555   1555  2.75  
LINK        MN    MN B2002                 O   SER B 123     1555   1555  2.29  
LINK        MN    MN B2002                 O   HOH B3041     1555   1555  2.44  
LINK        MN    MN B2003                 OD1 ASP B 217     1555   1555  2.25  
LINK        MN    MN B2003                 O   ASP B 217     1555   1555  2.32  
LINK        MN    MN B2003                 OD2 ASP B 158     1555   1555  2.27  
LINK        MN    MN B2003                 OD1 ASN B 215     1555   1555  2.28  
LINK        MN    MN B2003                 O   PRO B 219     1555   1555  2.20  
LINK        MN    MN B2003                 OE1 GLU B 220     1555   1555  2.30  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         C1  BMA B3322                 O4  NAG B3321     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         O3  MAN B3324                 C1  MAN B3325     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         ND2 ASN C  15                 C1  NAG C2015     1555   1555  1.44  
LINK        CA    CA C2004                 OE2 GLU C 243     1555   1555  2.39  
LINK        CA    CA C2004                 O   THR C 250     1555   1555  2.36  
LINK        CA    CA C2004                 OD1 ASP C 245     1555   1555  2.29  
LINK        CA    CA C2004                 OE1 GLU C 252     1555   1555  2.40  
LINK        CA    CA C2004                 OE2 GLU C 252     1555   1555  2.43  
LINK        CA    CA C2004                 OE1 GLU C 243     1555   1555  2.37  
LINK        CA    CA C2004                 OG1 THR C 250     1555   1555  2.40  
LINK        CA    CA C2004                 O   ASP C 247     1555   1555  2.35  
LINK        CA    CA C2005                 OD1 ASN C 299     1555   1555  2.29  
LINK        CA    CA C2005                 OD1 ASP C 305     1555   1555  2.42  
LINK        CA    CA C2005                 OD1 ASP C 301     1555   1555  2.44  
LINK        CA    CA C2005                 O   ARG C 303     1555   1555  2.34  
LINK        CA    CA C2005                 OD2 ASP C 305     1555   1555  2.44  
LINK        CA    CA C2005                 O   HOH C3201     1555   1555  2.37  
LINK        CA    CA C2005                 OD1 ASP C 297     1555   1555  2.35  
LINK        CA    CA C2006                 OD1 ASP C 373     1555   1555  2.46  
LINK        CA    CA C2006                 OD1 ASP C 367     1555   1555  2.31  
LINK        CA    CA C2006                 OD2 ASP C 373     1555   1555  2.45  
LINK        CA    CA C2006                 O   TYR C 371     1555   1555  2.26  
LINK        CA    CA C2006                 OD1 ASP C 365     1555   1555  2.46  
LINK        CA    CA C2006                 OD1 ASP C 369     1555   1555  2.39  
LINK        CA    CA C2006                 O   HOH C3236     1555   1555  2.40  
LINK        CA    CA C2007                 OD1 ASP C 434     1555   1555  2.41  
LINK        CA    CA C2007                 O   HOH C3274     1555   1555  2.39  
LINK        CA    CA C2007                 OD1 ASP C 426     1555   1555  2.33  
LINK        CA    CA C2007                 OD1 ASN C 430     1555   1555  2.40  
LINK        CA    CA C2007                 O   TYR C 432     1555   1555  2.34  
LINK        CA    CA C2007                 OD1 ASP C 428     1555   1555  2.29  
LINK        CA    CA C2007                 OD2 ASP C 434     1555   1555  2.41  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK        MN    MN D2001                 O   HOH D3009     1555   1555  2.09  
LINK        MN    MN D2001                 OD1 ASP J 495     1555   1555  2.19  
LINK        MN    MN D2001                 OE2 GLU D 220     1555   1555  2.09  
LINK        MN    MN D2001                 OG  SER D 123     1555   1555  2.18  
LINK        MN    MN D2001                 OG  SER D 121     1555   1555  2.27  
LINK        MN    MN D2001                 O   HOH D3011     1555   1555  2.25  
LINK        MN    MN D2002                 OD1 ASP D 126     1555   1555  2.19  
LINK        MN    MN D2002                 O   SER D 123     1555   1555  2.22  
LINK        MN    MN D2002                 O   HOH D3010     1555   1555  2.21  
LINK        MN    MN D2002                 OD2 ASP D 251     1555   1555  2.20  
LINK        MN    MN D2002                 OD2 ASP D 127     1555   1555  2.03  
LINK        MN    MN D2002                 O   HOH D3014     1555   1555  2.28  
LINK        MN    MN D2003                 OD1 ASP D 217     1555   1555  2.25  
LINK        MN    MN D2003                 OD1 ASN D 215     1555   1555  2.27  
LINK        MN    MN D2003                 O   ASP D 217     1555   1555  2.32  
LINK        MN    MN D2003                 OE1 GLU D 220     1555   1555  2.27  
LINK        MN    MN D2003                 OD2 ASP D 158     1555   1555  2.29  
LINK        MN    MN D2003                 O   PRO D 219     1555   1555  2.35  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O3  BMA D3322                 C1  MAN D3323     1555   1555  1.44  
LINK         C1  BMA D3322                 O4  NAG D3321     1555   1555  1.44  
CISPEP   1 SER B   84    PRO B   85          0        -0.78                     
CISPEP   2 SER B  162    PRO B  163          0         6.70                     
CISPEP   3 SER B  168    PRO B  169          0        -7.90                     
CISPEP   4 LEU C    1    ASN C    2          0         1.70                     
CISPEP   5 SER D   84    PRO D   85          0         1.26                     
CISPEP   6 SER D  162    PRO D  163          0         5.20                     
CISPEP   7 SER D  168    PRO D  169          0        -7.21                     
CISPEP   8 PHE E  152    PRO E  153          0        -3.03                     
CISPEP   9 GLU E  154    PRO E  155          0        -1.09                     
CISPEP  10 TRP E  194    PRO E  195          0         4.65                     
CISPEP  11 SER F    7    PRO F    8          0        -5.79                     
CISPEP  12 LEU F   94    PRO F   95          0        -1.15                     
CISPEP  13 TYR F  140    PRO F  141          0         2.78                     
CISPEP  14 PHE H  152    PRO H  153          0        -2.97                     
CISPEP  15 GLU H  154    PRO H  155          0        -4.92                     
CISPEP  16 TRP H  194    PRO H  195          0         0.87                     
CISPEP  17 SER L    7    PRO L    8          0        -1.54                     
CISPEP  18 LEU L   94    PRO L   95          0        -1.12                     
CISPEP  19 TYR L  140    PRO L  141          0         2.22                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A3348                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A3413                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A3470                                          
SITE     1 AC5  6 SER B 121  SER B 123  GLU B 220  HOH B3035                    
SITE     2 AC5  6 HOH B3038  ASP I 495                                          
SITE     1 AC6  7 SER B 123  ASP B 126  ASP B 251  HOH B3039                    
SITE     2 AC6  7 HOH B3041  HOH B3117  HOH B3200                               
SITE     1 AC7  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC7  5 GLU B 220                                                     
SITE     1 AC8  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AC8  5 GLU C 252                                                     
SITE     1 AC9  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AC9  6 ASP C 305  HOH C3201                                          
SITE     1 BC1  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 BC1  6 ASP C 373  HOH C3236                                          
SITE     1 BC2  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 BC2  6 ASP C 434  HOH C3274                                          
SITE     1 BC3  6 SER D 121  SER D 123  GLU D 220  HOH D3009                    
SITE     2 BC3  6 HOH D3011  ASP J 495                                          
SITE     1 BC4  6 SER D 123  ASP D 126  ASP D 127  ASP D 251                    
SITE     2 BC4  6 HOH D3010  HOH D3014                                          
SITE     1 BC5  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 BC5  5 GLU D 220                                                     
SITE     1 BC6  5 HIS A 112  LYS A 124  HOH A3067  HOH A3125                    
SITE     2 BC6  5 ILE B 167                                                     
SITE     1 BC7  4 ALA C  89  HIS C 112  HOH C3071  HOH C3281                    
SITE     1 BC8  4 GLN F  37  PRO F  59  PHE F  62  HOH F3018                    
SITE     1 BC9  7 GLN A  18  ARG A  41  ARG A  90  GLY A  92                    
SITE     2 BC9  7 TRP A 110  HOH A3127  GLY B 264                               
SITE     1 CC1  3 ARG C 279  ARG C 281  HOH C3178                               
SITE     1 CC2  5 LYS E  38  ARG E  40  GLU E  46  PHE E  64                    
SITE     2 CC2  5 GLU E  89                                                     
SITE     1 CC3  7 ARG A 208  LEU F  54  VAL F  55  ASP F  56                    
SITE     2 CC3  7 GLY F  57  VAL F  58  HOH F3068                               
SITE     1 CC4  4 PRO A 383  PRO C 410  GLN C 444  HOH C3282                    
SITE     1 CC5  6 PHE C 160  TYR C 190  GLY J 492  ARG J 493                    
SITE     2 CC5  6 GLY J 494  SER J 496                                          
SITE     1 CC6  4 ARG C  90  HOH C3283  SER D 162  ALA D 263                    
SITE     1 CC7  6 ARG A 386  PRO A 412  THR A 413  HOH A3482                    
SITE     2 CC7  6 HOH A3483  ARG C 386                                          
SITE     1 CC8  4 ASN A 227  ARG A 276  ARG A 279  HOH A3277                    
SITE     1 CC9 15 ARG A 281  MET A 285  HOH A3302  HOH A3325                    
SITE     2 CC9 15 ASN B 320  HOH B3170  HOH B3173  HOH B3201                    
SITE     3 CC9 15 HOH B3202  HOH B3203  HOH B3205  HOH B3206                    
SITE     4 CC9 15 HOH B3207  HOH B3209  PRO J 497                               
SITE     1 DC1  1 ASN C  15                                                     
SITE     1 DC2  9 ARG C 281  MET C 285  HOH C3172  ASN D 320                    
SITE     2 DC2  9 HOH D3089  HOH D3104  HOH D3105  HOH D3106                    
SITE     3 DC2  9 HOH D3107                                                     
SITE     1 DC3  3 ASN B 371  SER B 398  HOH B3211                               
CRYST1  233.210  143.560  104.730  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      0.004288  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006966  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009548        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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