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Database: PDB
Entry: 5THP
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HEADER    CELL ADHESION                           30-SEP-16   5THP              
TITLE     RHODOCETIN IN COMPLEX WITH THE INTEGRIN ALPHA2-A DOMAIN               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SNACLEC RHODOCETIN SUBUNIT GAMMA;                          
COMPND   3 CHAIN: A, D, G, J, M, P;                                             
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: SNACLEC RHODOCETIN SUBUNIT DELTA;                          
COMPND   6 CHAIN: B, E, H, K, N, Q;                                             
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: INTEGRIN ALPHA-2;                                          
COMPND   9 CHAIN: C, F, I, L, O, R;                                             
COMPND  10 FRAGMENT: UNP RESIDUES 170-366;                                      
COMPND  11 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER B,COLLAGEN RECEPTOR,PLATELET
COMPND  12 MEMBRANE GLYCOPROTEIN IA,GPIA,VLA-2 SUBUNIT ALPHA;                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CALLOSELASMA RHODOSTOMA;                        
SOURCE   3 ORGANISM_COMMON: MALAYAN PIT VIPER;                                  
SOURCE   4 ORGANISM_TAXID: 8717;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: CALLOSELASMA RHODOSTOMA;                        
SOURCE   7 ORGANISM_COMMON: MALAYAN PIT VIPER;                                  
SOURCE   8 ORGANISM_TAXID: 8717;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: ITGA2, CD49B;                                                  
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    C-TYPE LECTIN, INTEGRIN, VENOM, COAGULATION, CELL ADHESION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MCDOUGALL,G.L.ORRISS,J.STETEFELD                                    
REVDAT   1   02-AUG-17 5THP    0                                                
JRNL        AUTH   J.A.EBLE,M.MCDOUGALL,G.L.ORRISS,S.NILAND,B.JOHANNINGMEIER,   
JRNL        AUTH 2 G.POHLENTZ,M.MEIER,S.KARRASCH,M.I.ESTEVAO-COSTA,             
JRNL        AUTH 3 A.MARTINS LIMA,J.STETEFELD                                   
JRNL        TITL   DRAMATIC AND CONCERTED CONFORMATIONAL CHANGES ENABLE         
JRNL        TITL 2 RHODOCETIN TO BLOCK ALPHA 2 BETA 1 INTEGRIN SELECTIVELY.     
JRNL        REF    PLOS BIOL.                    V.  15 01492 2017              
JRNL        REFN                   ESSN 1545-7885                               
JRNL        PMID   28704364                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.2001492                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1-2155_2155: ???)                       
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 82982                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4301                            
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 18.4930 -  7.9572    0.95     3992   209  0.1665 0.2171        
REMARK   3     2  7.9572 -  6.4018    0.95     3963   221  0.2087 0.2800        
REMARK   3     3  6.4018 -  5.6185    0.95     3935   205  0.2128 0.2617        
REMARK   3     4  5.6185 -  5.1167    0.95     3959   198  0.2045 0.2713        
REMARK   3     5  5.1167 -  4.7567    0.95     3929   203  0.1856 0.2252        
REMARK   3     6  4.7567 -  4.4805    0.95     3942   198  0.1784 0.1885        
REMARK   3     7  4.4805 -  4.2589    0.94     3935   238  0.1917 0.2290        
REMARK   3     8  4.2589 -  4.0756    0.94     3905   235  0.2033 0.2532        
REMARK   3     9  4.0756 -  3.9202    0.94     3885   264  0.2215 0.2703        
REMARK   3    10  3.9202 -  3.7862    0.95     3942   188  0.2457 0.2380        
REMARK   3    11  3.7862 -  3.6687    0.95     3905   225  0.2469 0.3085        
REMARK   3    12  3.6687 -  3.5646    0.95     3927   217  0.2526 0.3248        
REMARK   3    13  3.5646 -  3.4714    0.94     3909   239  0.2708 0.3156        
REMARK   3    14  3.4714 -  3.3872    0.95     3945   198  0.2647 0.3523        
REMARK   3    15  3.3872 -  3.3107    0.95     3938   205  0.2797 0.3702        
REMARK   3    16  3.3107 -  3.2406    0.96     3937   174  0.2927 0.3843        
REMARK   3    17  3.2406 -  3.1761    0.95     3923   220  0.3008 0.3127        
REMARK   3    18  3.1761 -  3.1165    0.95     3917   213  0.3022 0.3147        
REMARK   3    19  3.1165 -  3.0610    0.94     3886   229  0.3112 0.3649        
REMARK   3    20  3.0610 -  3.0094    0.93     3887   222  0.3171 0.3732        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.002          21250                                  
REMARK   3   ANGLE     :  0.554          28886                                  
REMARK   3   CHIRALITY :  0.040           3080                                  
REMARK   3   PLANARITY :  0.003           3682                                  
REMARK   3   DIHEDRAL  : 11.542          12396                                  
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 2 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-124.9052 393.5460 -28.2963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8090 T22:   0.9696                                     
REMARK   3      T33:   0.6761 T12:   0.2366                                     
REMARK   3      T13:  -0.2037 T23:  -0.0692                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7146 L22:   3.9970                                     
REMARK   3      L33:   3.9797 L12:  -0.1739                                     
REMARK   3      L13:   0.1427 L23:  -0.2577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2867 S12:   0.6787 S13:  -0.1316                       
REMARK   3      S21:  -0.0329 S22:  -0.1611 S23:   0.0213                       
REMARK   3      S31:   0.6144 S32:   0.6741 S33:  -0.0994                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 122)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-141.7647 415.2724 -31.3897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8209 T22:   0.9848                                     
REMARK   3      T33:   0.8276 T12:   0.3244                                     
REMARK   3      T13:  -0.2170 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6685 L22:   1.1913                                     
REMARK   3      L33:   2.1149 L12:  -0.4267                                     
REMARK   3      L13:   0.4258 L23:  -0.2492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1271 S12:   0.5859 S13:   0.1337                       
REMARK   3      S21:  -0.0199 S22:  -0.3714 S23:   0.3953                       
REMARK   3      S31:  -0.4553 S32:  -0.3953 S33:   0.1967                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 172 THROUGH 363)                  
REMARK   3    ORIGIN FOR THE GROUP (A):-112.1710 422.3575 -18.7188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8859 T22:   0.7681                                     
REMARK   3      T33:   0.4849 T12:   0.1068                                     
REMARK   3      T13:  -0.0423 T23:   0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4041 L22:   2.5208                                     
REMARK   3      L33:   0.3389 L12:   0.7284                                     
REMARK   3      L13:  -1.1137 L23:   0.6444                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2113 S12:   0.5599 S13:  -0.0960                       
REMARK   3      S21:  -0.3012 S22:   0.0311 S23:  -0.1779                       
REMARK   3      S31:  -0.0312 S32:   0.0203 S33:   0.2125                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 2 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -54.8648 461.4876 -14.9339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4783 T22:   0.8120                                     
REMARK   3      T33:   0.5390 T12:   0.1116                                     
REMARK   3      T13:   0.1334 T23:   0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5397 L22:   2.5501                                     
REMARK   3      L33:   2.9025 L12:   0.0540                                     
REMARK   3      L13:   2.6896 L23:   0.3493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1886 S12:   0.2591 S13:  -0.5260                       
REMARK   3      S21:  -0.1419 S22:   0.2315 S23:  -0.1012                       
REMARK   3      S31:   0.0942 S32:   0.6417 S33:   0.0002                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 122)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -81.9635 456.4262 -18.3128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5294 T22:   0.9259                                     
REMARK   3      T33:   1.0170 T12:   0.0114                                     
REMARK   3      T13:   0.1667 T23:   0.2450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3879 L22:   1.0647                                     
REMARK   3      L33:   2.3663 L12:  -0.6856                                     
REMARK   3      L13:   1.0885 L23:   0.5139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0037 S12:   0.1744 S13:  -0.5340                       
REMARK   3      S21:   0.0771 S22:   0.3235 S23:   0.4241                       
REMARK   3      S31:   0.3723 S32:  -0.1270 S33:  -0.3802                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 172 THROUGH 364)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -74.7839 485.7736  -4.5912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8449 T22:   0.8503                                     
REMARK   3      T33:   0.9408 T12:   0.3575                                     
REMARK   3      T13:   0.1602 T23:   0.1826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6197 L22:   0.7670                                     
REMARK   3      L33:   2.0842 L12:   0.2581                                     
REMARK   3      L13:  -0.0618 L23:  -0.1301                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3128 S12:  -0.4203 S13:   0.0208                       
REMARK   3      S21:   0.4490 S22:   0.1338 S23:   0.2269                       
REMARK   3      S31:  -0.0775 S32:  -0.0677 S33:   0.2356                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN 'G' AND RESID 2 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-127.0624 402.7003   6.1720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7957 T22:   0.5273                                     
REMARK   3      T33:   0.5557 T12:   0.1331                                     
REMARK   3      T13:  -0.0741 T23:  -0.0790                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3807 L22:   3.1777                                     
REMARK   3      L33:   2.3760 L12:   0.8416                                     
REMARK   3      L13:  -0.7280 L23:  -1.9302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4130 S12:   0.3867 S13:  -0.0027                       
REMARK   3      S21:   0.5424 S22:  -0.2358 S23:   0.4460                       
REMARK   3      S31:  -0.4252 S32:  -0.0680 S33:  -0.1309                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 122)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-132.0185 376.2282   9.4167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8176 T22:   0.5854                                     
REMARK   3      T33:   1.1100 T12:   0.1604                                     
REMARK   3      T13:  -0.1843 T23:  -0.1118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7566 L22:   1.1555                                     
REMARK   3      L33:   2.0460 L12:  -1.0978                                     
REMARK   3      L13:   0.5661 L23:  -1.4860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3024 S12:   0.0380 S13:  -0.5127                       
REMARK   3      S21:   0.2763 S22:   0.0512 S23:   0.3723                       
REMARK   3      S31:   0.3578 S32:  -0.2112 S33:  -0.3502                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN 'I' AND RESID 173 THROUGH 363)                  
REMARK   3    ORIGIN FOR THE GROUP (A):-103.0612 382.7882  -4.2001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8347 T22:   0.7538                                     
REMARK   3      T33:   0.7196 T12:   0.2990                                     
REMARK   3      T13:  -0.2605 T23:  -0.2224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5955 L22:   2.9806                                     
REMARK   3      L33:   1.8380 L12:   1.1239                                     
REMARK   3      L13:   0.1446 L23:  -1.8732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3261 S12:   0.6930 S13:  -0.4638                       
REMARK   3      S21:   0.2769 S22:  -0.2517 S23:  -0.6685                       
REMARK   3      S31:   0.5068 S32:   0.5027 S33:  -0.0959                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN 'J' AND RESID 3 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -60.2000 456.0934 -43.0410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9110 T22:   1.0548                                     
REMARK   3      T33:   0.5558 T12:  -0.4072                                     
REMARK   3      T13:   0.1616 T23:  -0.1189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8554 L22:   1.9764                                     
REMARK   3      L33:   0.4797 L12:   0.3817                                     
REMARK   3      L13:  -1.3253 L23:  -0.1632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1838 S12:  -0.7921 S13:   0.1783                       
REMARK   3      S21:   0.4514 S22:  -0.1393 S23:   0.2940                       
REMARK   3      S31:  -0.3820 S32:   0.3461 S33:  -0.0755                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN 'K' AND RESID 15 THROUGH 122)                   
REMARK   3    ORIGIN FOR THE GROUP (A): -75.2111 435.4155 -40.7168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8194 T22:   0.9744                                     
REMARK   3      T33:   1.0805 T12:  -0.2922                                     
REMARK   3      T13:   0.2919 T23:  -0.0800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1328 L22:   2.4072                                     
REMARK   3      L33:   4.7485 L12:   0.9564                                     
REMARK   3      L13:  -2.4144 L23:  -2.4643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1586 S12:   0.1766 S13:  -0.1271                       
REMARK   3      S21:   0.1894 S22:   0.3697 S23:   0.6073                       
REMARK   3      S31:   0.2094 S32:  -0.6004 S33:  -0.1380                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN 'L' AND RESID 174 THROUGH 362)                  
REMARK   3    ORIGIN FOR THE GROUP (A): -47.4416 428.0559 -52.5710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5727 T22:   0.7073                                     
REMARK   3      T33:   0.5380 T12:  -0.1507                                     
REMARK   3      T13:   0.0286 T23:   0.0702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0854 L22:   4.1159                                     
REMARK   3      L33:   4.3546 L12:  -1.6081                                     
REMARK   3      L13:  -0.2193 L23:   0.1479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1418 S12:  -0.3055 S13:  -0.1323                       
REMARK   3      S21:  -0.1762 S22:  -0.0295 S23:   0.0842                       
REMARK   3      S31:   0.3533 S32:   0.5985 S33:  -0.1464                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN 'M' AND RESID 2 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-112.4323 470.1544  25.1481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9791 T22:   0.7054                                     
REMARK   3      T33:   1.2802 T12:  -0.0222                                     
REMARK   3      T13:  -0.5216 T23:  -0.1438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3446 L22:   1.7583                                     
REMARK   3      L33:   2.7254 L12:   0.2404                                     
REMARK   3      L13:   0.6013 L23:  -1.7883                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4957 S12:  -0.1340 S13:   1.3099                       
REMARK   3      S21:   0.6669 S22:  -0.4131 S23:  -0.5966                       
REMARK   3      S31:  -0.7158 S32:  -0.3997 S33:   0.7752                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN 'N' AND RESID 1 THROUGH 122)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -99.7026 445.8985  27.4082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7638 T22:   0.4809                                     
REMARK   3      T33:   0.7044 T12:   0.0403                                     
REMARK   3      T13:  -0.2435 T23:   0.0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8991 L22:   1.0361                                     
REMARK   3      L33:   3.2494 L12:  -1.1033                                     
REMARK   3      L13:   1.0024 L23:  -0.1786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1574 S12:  -0.0015 S13:  -0.1725                       
REMARK   3      S21:  -0.0449 S22:  -0.1117 S23:  -0.0023                       
REMARK   3      S31:   0.5226 S32:   0.2295 S33:  -0.0311                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN 'O' AND RESID 171 THROUGH 362)                  
REMARK   3    ORIGIN FOR THE GROUP (A):-112.6418 452.5059  -2.7266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5295 T22:   0.6834                                     
REMARK   3      T33:   0.7815 T12:   0.0153                                     
REMARK   3      T13:  -0.0739 T23:   0.1592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4804 L22:   2.6663                                     
REMARK   3      L33:   2.6610 L12:   0.3775                                     
REMARK   3      L13:   0.5626 L23:  -0.2637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0643 S12:   0.5286 S13:   0.5212                       
REMARK   3      S21:   0.0489 S22:  -0.4627 S23:  -0.1708                       
REMARK   3      S31:   0.3721 S32:   0.3580 S33:   0.3498                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN 'P' AND RESID 2 THROUGH 133)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-118.1251 476.0794 -33.7620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6085 T22:   1.0236                                     
REMARK   3      T33:   1.2814 T12:   0.0561                                     
REMARK   3      T13:   0.0360 T23:   0.5320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2087 L22:   3.2095                                     
REMARK   3      L33:   1.3536 L12:   0.0813                                     
REMARK   3      L13:   0.5713 L23:  -1.0188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1083 S12:   0.2992 S13:   0.3343                       
REMARK   3      S21:  -0.4296 S22:  -0.6808 S23:  -1.4727                       
REMARK   3      S31:   0.3875 S32:   0.7096 S33:   0.7252                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN 'Q' AND RESID 1 THROUGH 122)                    
REMARK   3    ORIGIN FOR THE GROUP (A):-142.6650 488.8551 -36.0250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5421 T22:   0.9816                                     
REMARK   3      T33:   0.8723 T12:  -0.2146                                     
REMARK   3      T13:  -0.0933 T23:   0.3687                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1493 L22:   4.0788                                     
REMARK   3      L33:   4.5478 L12:  -1.3621                                     
REMARK   3      L13:  -0.2115 L23:  -2.4239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2646 S12:   0.1882 S13:  -0.1752                       
REMARK   3      S21:  -0.0448 S22:   0.1005 S23:   0.1182                       
REMARK   3      S31:   0.0670 S32:  -0.3465 S33:   0.1520                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN 'R' AND RESID 171 THROUGH 362)                  
REMARK   3    ORIGIN FOR THE GROUP (A):-136.0370 475.9979  -5.9137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5842 T22:   0.5404                                     
REMARK   3      T33:   0.8688 T12:   0.0373                                     
REMARK   3      T13:  -0.2727 T23:  -0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2940 L22:   2.3031                                     
REMARK   3      L33:   4.4238 L12:  -0.7341                                     
REMARK   3      L13:  -0.2448 L23:  -2.9326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3555 S12:  -0.0384 S13:   0.3807                       
REMARK   3      S21:   0.5724 S22:  -0.0772 S23:  -0.5960                       
REMARK   3      S31:  -0.8645 S32:  -0.2159 S33:   0.3485                       
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 5THP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223817.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83038                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.006                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 3GPR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.0, 2.65M AMMONIUM         
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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      125.67550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.83775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      188.51325            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O                               
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R                               
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     ASP A     1                                                      
REMARK 465     ASP A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     ARG A    76                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     CYS A   135                                                      
REMARK 465     SER B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     SER B    43                                                      
REMARK 465     TYR B   123                                                      
REMARK 465     SER B   124                                                      
REMARK 465     MET C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     SER C   152                                                      
REMARK 465     SER C   153                                                      
REMARK 465     HIS C   154                                                      
REMARK 465     HIS C   155                                                      
REMARK 465     HIS C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     HIS C   158                                                      
REMARK 465     HIS C   159                                                      
REMARK 465     SER C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     GLY C   162                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     VAL C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     GLY C   167                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     SER C   169                                                      
REMARK 465     PRO C   170                                                      
REMARK 465     SER C   171                                                      
REMARK 465     TYR C   186                                                      
REMARK 465     PRO C   187                                                      
REMARK 465     ILE C   364                                                      
REMARK 465     GLU C   365                                                      
REMARK 465     GLY C   366                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     LYS D    37                                                      
REMARK 465     ARG D    38                                                      
REMARK 465     GLU D   134                                                      
REMARK 465     CYS D   135                                                      
REMARK 465     TYR E   123                                                      
REMARK 465     SER E   124                                                      
REMARK 465     MET F   150                                                      
REMARK 465     GLY F   151                                                      
REMARK 465     SER F   152                                                      
REMARK 465     SER F   153                                                      
REMARK 465     HIS F   154                                                      
REMARK 465     HIS F   155                                                      
REMARK 465     HIS F   156                                                      
REMARK 465     HIS F   157                                                      
REMARK 465     HIS F   158                                                      
REMARK 465     HIS F   159                                                      
REMARK 465     SER F   160                                                      
REMARK 465     SER F   161                                                      
REMARK 465     GLY F   162                                                      
REMARK 465     LEU F   163                                                      
REMARK 465     VAL F   164                                                      
REMARK 465     PRO F   165                                                      
REMARK 465     ARG F   166                                                      
REMARK 465     GLY F   167                                                      
REMARK 465     GLY F   168                                                      
REMARK 465     SER F   169                                                      
REMARK 465     PRO F   170                                                      
REMARK 465     SER F   171                                                      
REMARK 465     GLU F   365                                                      
REMARK 465     GLY F   366                                                      
REMARK 465     ASP G     1                                                      
REMARK 465     GLU G   134                                                      
REMARK 465     CYS G   135                                                      
REMARK 465     SER H     6                                                      
REMARK 465     SER H     7                                                      
REMARK 465     TYR H   123                                                      
REMARK 465     SER H   124                                                      
REMARK 465     MET I   150                                                      
REMARK 465     GLY I   151                                                      
REMARK 465     SER I   152                                                      
REMARK 465     SER I   153                                                      
REMARK 465     HIS I   154                                                      
REMARK 465     HIS I   155                                                      
REMARK 465     HIS I   156                                                      
REMARK 465     HIS I   157                                                      
REMARK 465     HIS I   158                                                      
REMARK 465     HIS I   159                                                      
REMARK 465     SER I   160                                                      
REMARK 465     SER I   161                                                      
REMARK 465     GLY I   162                                                      
REMARK 465     LEU I   163                                                      
REMARK 465     VAL I   164                                                      
REMARK 465     PRO I   165                                                      
REMARK 465     ARG I   166                                                      
REMARK 465     GLY I   167                                                      
REMARK 465     GLY I   168                                                      
REMARK 465     SER I   169                                                      
REMARK 465     PRO I   170                                                      
REMARK 465     SER I   171                                                      
REMARK 465     LEU I   172                                                      
REMARK 465     ILE I   364                                                      
REMARK 465     GLU I   365                                                      
REMARK 465     GLY I   366                                                      
REMARK 465     ASP J     1                                                      
REMARK 465     PHE J     2                                                      
REMARK 465     GLU J   134                                                      
REMARK 465     CYS J   135                                                      
REMARK 465     CYS K     1                                                      
REMARK 465     PRO K     2                                                      
REMARK 465     LEU K     3                                                      
REMARK 465     HIS K     4                                                      
REMARK 465     TRP K     5                                                      
REMARK 465     SER K     6                                                      
REMARK 465     SER K     7                                                      
REMARK 465     TYR K     8                                                      
REMARK 465     ASN K     9                                                      
REMARK 465     GLY K    10                                                      
REMARK 465     TYR K    11                                                      
REMARK 465     CYS K    12                                                      
REMARK 465     TYR K    13                                                      
REMARK 465     ARG K    14                                                      
REMARK 465     TYR K   123                                                      
REMARK 465     SER K   124                                                      
REMARK 465     MET L   150                                                      
REMARK 465     GLY L   151                                                      
REMARK 465     SER L   152                                                      
REMARK 465     SER L   153                                                      
REMARK 465     HIS L   154                                                      
REMARK 465     HIS L   155                                                      
REMARK 465     HIS L   156                                                      
REMARK 465     HIS L   157                                                      
REMARK 465     HIS L   158                                                      
REMARK 465     HIS L   159                                                      
REMARK 465     SER L   160                                                      
REMARK 465     SER L   161                                                      
REMARK 465     GLY L   162                                                      
REMARK 465     LEU L   163                                                      
REMARK 465     VAL L   164                                                      
REMARK 465     PRO L   165                                                      
REMARK 465     ARG L   166                                                      
REMARK 465     GLY L   167                                                      
REMARK 465     GLY L   168                                                      
REMARK 465     SER L   169                                                      
REMARK 465     PRO L   170                                                      
REMARK 465     SER L   171                                                      
REMARK 465     LEU L   172                                                      
REMARK 465     ILE L   173                                                      
REMARK 465     SER L   363                                                      
REMARK 465     ILE L   364                                                      
REMARK 465     GLU L   365                                                      
REMARK 465     GLY L   366                                                      
REMARK 465     ASP M     1                                                      
REMARK 465     GLU M   134                                                      
REMARK 465     CYS M   135                                                      
REMARK 465     TYR N   123                                                      
REMARK 465     SER N   124                                                      
REMARK 465     MET O   150                                                      
REMARK 465     GLY O   151                                                      
REMARK 465     SER O   152                                                      
REMARK 465     SER O   153                                                      
REMARK 465     HIS O   154                                                      
REMARK 465     HIS O   155                                                      
REMARK 465     HIS O   156                                                      
REMARK 465     HIS O   157                                                      
REMARK 465     HIS O   158                                                      
REMARK 465     HIS O   159                                                      
REMARK 465     SER O   160                                                      
REMARK 465     SER O   161                                                      
REMARK 465     GLY O   162                                                      
REMARK 465     LEU O   163                                                      
REMARK 465     VAL O   164                                                      
REMARK 465     PRO O   165                                                      
REMARK 465     ARG O   166                                                      
REMARK 465     GLY O   167                                                      
REMARK 465     GLY O   168                                                      
REMARK 465     SER O   169                                                      
REMARK 465     PRO O   170                                                      
REMARK 465     ALA O   217                                                      
REMARK 465     SER O   363                                                      
REMARK 465     ILE O   364                                                      
REMARK 465     GLU O   365                                                      
REMARK 465     GLY O   366                                                      
REMARK 465     ASP P     1                                                      
REMARK 465     GLU P   134                                                      
REMARK 465     CYS P   135                                                      
REMARK 465     TYR Q   123                                                      
REMARK 465     SER Q   124                                                      
REMARK 465     MET R   150                                                      
REMARK 465     GLY R   151                                                      
REMARK 465     SER R   152                                                      
REMARK 465     SER R   153                                                      
REMARK 465     HIS R   154                                                      
REMARK 465     HIS R   155                                                      
REMARK 465     HIS R   156                                                      
REMARK 465     HIS R   157                                                      
REMARK 465     HIS R   158                                                      
REMARK 465     HIS R   159                                                      
REMARK 465     SER R   160                                                      
REMARK 465     SER R   161                                                      
REMARK 465     GLY R   162                                                      
REMARK 465     LEU R   163                                                      
REMARK 465     VAL R   164                                                      
REMARK 465     PRO R   165                                                      
REMARK 465     ARG R   166                                                      
REMARK 465     GLY R   167                                                      
REMARK 465     GLY R   168                                                      
REMARK 465     SER R   169                                                      
REMARK 465     PRO R   170                                                      
REMARK 465     ASP R   174                                                      
REMARK 465     ILE R   204                                                      
REMARK 465     GLY R   205                                                      
REMARK 465     GLY R   247                                                      
REMARK 465     ASP R   248                                                      
REMARK 465     SER R   363                                                      
REMARK 465     ILE R   364                                                      
REMARK 465     GLU R   365                                                      
REMARK 465     GLY R   366                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  13    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  21    CG   CD   OE1  OE2                                  
REMARK 470     THR A  24    OG1  CG2                                            
REMARK 470     GLN A  35    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     TYR A  67    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     TYR B  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS B  33    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     GLU B  45    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 173    CG1  CG2  CD1                                       
REMARK 470     ILE C 204    CG1  CG2  CD1                                       
REMARK 470     THR C 207    OG1  CG2                                            
REMARK 470     LYS C 230    CG   CD   CE   NZ                                   
REMARK 470     GLN C 241    CG   CD   OE1  NE2                                  
REMARK 470     MET C 291    CG   SD   CE                                        
REMARK 470     LYS C 293    CG   CD   CE   NZ                                   
REMARK 470     ASP C 302    CG   OD1  OD2                                       
REMARK 470     LYS C 323    CG   CD   CE   NZ                                   
REMARK 470     LYS C 330    CG   CD   CE   NZ                                   
REMARK 470     GLU D  21    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  35    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  62    CG   CD   CE   NZ                                   
REMARK 470     LEU D  66    CG   CD1  CD2                                       
REMARK 470     ARG D  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  77    CG   CD   CE   NZ                                   
REMARK 470     ILE D  92    CG1  CG2  CD1                                       
REMARK 470     MET D 103    CG   SD   CE                                        
REMARK 470     LYS D 115    CG   CD   CE   NZ                                   
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     TYR E  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS E  34    CG   CD   CE   NZ                                   
REMARK 470     ARG E  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  72    CG   CD   CE   NZ                                   
REMARK 470     VAL E 119    CG1  CG2                                            
REMARK 470     GLU F 233    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 234    CG   CD   OE1  OE2                                  
REMARK 470     TYR F 264    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG F 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 276    CG   CD   CE   NZ                                   
REMARK 470     LEU F 292    CG   CD1  CD2                                       
REMARK 470     PHE F 307    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU F 320    CG   CD1  CD2                                       
REMARK 470     LYS F 323    CG   CD   CE   NZ                                   
REMARK 470     LYS F 330    CG   CD   CE   NZ                                   
REMARK 470     ILE F 335    CG1  CG2  CD1                                       
REMARK 470     THR F 337    OG1  CG2                                            
REMARK 470     ILE F 364    CG1  CG2  CD1                                       
REMARK 470     GLU G  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  37    CG   CD   CE   NZ                                   
REMARK 470     ARG G  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 124    CD   CE   NZ                                        
REMARK 470     HIS H   4    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR H   8    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR H  13    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG H  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL H  15    CG1  CG2                                            
REMARK 470     PHE H  16    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H  20    CG   CD   CE   NZ                                   
REMARK 470     GLU H  23    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  34    CG   CD   CE   NZ                                   
REMARK 470     ARG H  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE H  49    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU H  58    CG   CD1  CD2                                       
REMARK 470     LYS H  83    CG   CD   CE   NZ                                   
REMARK 470     LYS H 114    CG   CD   CE   NZ                                   
REMARK 470     LYS I 197    CG   CD   CE   NZ                                   
REMARK 470     GLN I 200    CG   CD   OE1  NE2                                  
REMARK 470     LEU I 202    CG   CD1  CD2                                       
REMARK 470     ASP I 203    CG   OD1  OD2                                       
REMARK 470     ILE I 204    CG1  CG2  CD1                                       
REMARK 470     LYS I 208    CG   CD   CE   NZ                                   
REMARK 470     VAL I 211    CG1  CG2                                            
REMARK 470     LYS I 230    CG   CD   CE   NZ                                   
REMARK 470     THR I 231    OG1  CG2                                            
REMARK 470     LYS I 232    CG   CD   CE   NZ                                   
REMARK 470     GLN I 241    CG   CD   OE1  NE2                                  
REMARK 470     ARG I 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 293    CG   CD   CE   NZ                                   
REMARK 470     HIS I 301    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG I 306    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 323    CG   CD   CE   NZ                                   
REMARK 470     LYS I 327    CG   CD   CE   NZ                                   
REMARK 470     ASP I 346    CG   OD1  OD2                                       
REMARK 470     GLU I 352    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 353    CG   CD   CE   NZ                                   
REMARK 470     LEU I 357    CG   CD1  CD2                                       
REMARK 470     GLU I 359    CG   CD   OE1  OE2                                  
REMARK 470     ARG J  30    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J  37    CG   CD   CE   NZ                                   
REMARK 470     ARG J  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 115    CG   CD   CE   NZ                                   
REMARK 470     GLN J 122    CG   CD   OE1  NE2                                  
REMARK 470     ARG K  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU K  38    CG   CD1  CD2                                       
REMARK 470     LEU K  67    CG   CD1  CD2                                       
REMARK 470     LYS K  75    CG   CD   CE   NZ                                   
REMARK 470     ASP K  80    CG   OD1  OD2                                       
REMARK 470     LEU K  84    CG   CD1  CD2                                       
REMARK 470     GLN L 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 208    CG   CD   CE   NZ                                   
REMARK 470     LEU L 226    CG   CD1  CD2                                       
REMARK 470     LYS L 230    CG   CD   CE   NZ                                   
REMARK 470     LYS L 232    CG   CD   CE   NZ                                   
REMARK 470     GLU L 233    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 276    CG   CD   CE   NZ                                   
REMARK 470     GLN L 298    CG   CD   OE1  NE2                                  
REMARK 470     ILE L 335    CG1  CG2  CD1                                       
REMARK 470     GLU L 338    CG   CD   OE1  OE2                                  
REMARK 470     PHE L 342    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN L 343    CG   OD1  ND2                                       
REMARK 470     ASP L 346    CG   OD1  OD2                                       
REMARK 470     LYS L 353    CG   CD   CE   NZ                                   
REMARK 470     GLU L 359    CG   CD   OE1  OE2                                  
REMARK 470     GLN L 360    CG   CD   OE1  NE2                                  
REMARK 470     PHE L 362    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE M  19    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS M  37    CG   CD   CE   NZ                                   
REMARK 470     ARG M  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS M  62    CG   CD   CE   NZ                                   
REMARK 470     ARG M  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU M  65    CG   CD   OE1  OE2                                  
REMARK 470     ARG M  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS M 115    CG   CD   CE   NZ                                   
REMARK 470     LYS O 208    CG   CD   CE   NZ                                   
REMARK 470     LYS O 230    CG   CD   CE   NZ                                   
REMARK 470     GLU O 233    CG   CD   OE1  OE2                                  
REMARK 470     GLN O 257    CG   CD   OE1  NE2                                  
REMARK 470     ARG O 271    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O 293    CG   CD   CE   NZ                                   
REMARK 470     HIS O 301    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS O 323    CG   CD   CE   NZ                                   
REMARK 470     LYS O 330    CE   NZ                                             
REMARK 470     GLU O 338    CG   CD   OE1  OE2                                  
REMARK 470     ARG O 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL O 344    CG1  CG2                                            
REMARK 470     LYS O 353    CG   CD   CE   NZ                                   
REMARK 470     LYS P  37    CG   CD   CE   NZ                                   
REMARK 470     ARG P  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE P  70    CG1  CG2  CD1                                       
REMARK 470     ARG P  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS P 115    CG   CD   CE   NZ                                   
REMARK 470     LEU Q  19    CG   CD1  CD2                                       
REMARK 470     LYS R 197    CG   CD   CE   NZ                                   
REMARK 470     GLN R 200    CG   CD   OE1  NE2                                  
REMARK 470     PRO R 206    CG   CD                                             
REMARK 470     LYS R 230    CG   CD   CE   NZ                                   
REMARK 470     LYS R 261    CG   CD   CE   NZ                                   
REMARK 470     ARG R 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU R 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS R 293    CG   CD   CE   NZ                                   
REMARK 470     ASP R 297    CG   OD1  OD2                                       
REMARK 470     GLN R 298    CG   CD   OE1  NE2                                  
REMARK 470     LYS R 323    CG   CD   CE   NZ                                   
REMARK 470     PHE R 362    CG   CD1  CD2  CE1  CE2  CZ                         
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   OG   SER F   184     OD2  ASP F   283              1.83            
REMARK 500   NH1  ARG K    92     OE2  GLU K   113              1.88            
REMARK 500   O    VAL I   199     N    GLY I   201              1.90            
REMARK 500   OG   SER O   184     OD2  ASP O   283              1.92            
REMARK 500   NH1  ARG G   114     O    HOH G   301              1.97            
REMARK 500   OD1  ASN Q    69     O    HOH Q   301              1.98            
REMARK 500   OG   SER C   184     OD2  ASP C   283              1.99            
REMARK 500   OG1  THR K    21     O    CYS K   112              2.00            
REMARK 500   O    GLN P    17     O    HOH P   301              2.00            
REMARK 500   OD1  ASP H    81     O1   GOL H   204              2.00            
REMARK 500   NZ   LYS O   261     O4   SO4 O   407              2.01            
REMARK 500   OG   SER C   286     OE2  GLU C   328              2.01            
REMARK 500   OD2  ASP G    47     O    HOH G   302              2.01            
REMARK 500   O    THR J    33     O1   GOL J   205              2.03            
REMARK 500   O    VAL A    68     O    HOH A   301              2.03            
REMARK 500   NZ   LYS L   261     O    HOH L   501              2.03            
REMARK 500   O    ASP K    85     O    HOH K   201              2.03            
REMARK 500   O    ILE F   304     NH1  ARG F   306              2.05            
REMARK 500   O    GLU R   352     O    HOH R   501              2.05            
REMARK 500   N    CYS P   129     O    HOH P   301              2.05            
REMARK 500   OG   SER O   334     O    HOH O   501              2.05            
REMARK 500   OG   SER L   182     O    HOH L   502              2.06            
REMARK 500   O    HOH A   303     O    HOH A   313              2.06            
REMARK 500   N    ARG G   114     O    HOH G   303              2.06            
REMARK 500   O    PHE C   362     O    HOH C   501              2.07            
REMARK 500   O    LEU F   325     O    HOH F   501              2.07            
REMARK 500   OG1  THR B    21     O    HOH B   301              2.07            
REMARK 500   O    LEU O   226     O    HOH O   502              2.08            
REMARK 500   OE1  GLN F   215     O    HOH F   502              2.08            
REMARK 500   OG   SER O   286     OE2  GLU O   328              2.08            
REMARK 500   O    LYS Q    59     O    HOH Q   302              2.09            
REMARK 500   O    PHE J   113     O3   GOL J   204              2.10            
REMARK 500   O    SER K    79     O    HOH K   202              2.10            
REMARK 500   O    LEU O   357     O    HOH O   503              2.10            
REMARK 500   NH1  ARG D   114     O    HOH D   301              2.10            
REMARK 500   O    ILE Q    41     O    HOH Q   303              2.10            
REMARK 500   O    GLN G   105     O    HOH G   304              2.11            
REMARK 500   N    LEU K    65     O    HOH K   203              2.11            
REMARK 500   O    TRP G     8     O    HOH G   305              2.11            
REMARK 500   O    ARG I   271     O    HOH I   501              2.11            
REMARK 500   OG1  THR Q    21     O    CYS Q   112              2.11            
REMARK 500   O    ALA K    96     O    HOH K   203              2.12            
REMARK 500   OD2  ASP A    47     NZ   LYS G   115              2.12            
REMARK 500   OE1  GLN D   102     NH1  ARG E    91              2.12            
REMARK 500   NZ   LYS C   232     O    HOH C   502              2.12            
REMARK 500   N    TRP D    85     O    ALA D    89              2.13            
REMARK 500   O    GLU O   352     O    HOH O   504              2.13            
REMARK 500   O4   SO4 L   406     O    HOH L   502              2.13            
REMARK 500   OG   SER C   184     O    HOH C   503              2.14            
REMARK 500   N    GLY I   254     O    HOH I   502              2.14            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 CLOSE CONTACTS                                
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    ASP A  12     -128.59     56.11                                   
REMARK 500    ASN A  20       81.81     69.57                                   
REMARK 500    GLU A  21       72.36     67.34                                   
REMARK 500    TRP A  25      -66.97    -99.56                                   
REMARK 500    ALA A  36      163.08    178.80                                   
REMARK 500    GLU A  65     -136.15     59.36                                   
REMARK 500    LEU A  66     -134.75     44.85                                   
REMARK 500    MET A  87      -80.76   -119.16                                   
REMARK 500    SER A  88      -69.58   -136.04                                   
REMARK 500    ALA A  89     -140.54     50.29                                   
REMARK 500    SER A  90     -177.57   -172.50                                   
REMARK 500    ILE A  92      -66.58   -131.49                                   
REMARK 500    PRO A 126      178.69    -59.93                                   
REMARK 500    LEU B   3     -136.21     55.38                                   
REMARK 500    ALA B  31     -114.74     59.22                                   
REMARK 500    THR B  57     -138.31     59.28                                   
REMARK 500    LEU B  58     -149.51     52.59                                   
REMARK 500    LYS B  59     -134.92     68.01                                   
REMARK 500    ASN B  69       71.96     43.56                                   
REMARK 500    ASP B  85      -64.58   -128.23                                   
REMARK 500    ILE C 204       72.23     58.63                                   
REMARK 500    THR C 209       70.67     43.47                                   
REMARK 500    ALA C 217      -74.37   -128.97                                   
REMARK 500    TYR C 262      -61.61   -121.39                                   
REMARK 500    ARG C 272      -57.42   -129.14                                   
REMARK 500    THR C 275       71.67     68.03                                   
REMARK 500    PHE C 341       72.57     60.61                                   
REMARK 500    VAL C 344       71.72     63.07                                   
REMARK 500    ASN D   3      -70.06    -90.62                                   
REMARK 500    TYR D  11      -76.12   -110.36                                   
REMARK 500    GLU D  65     -151.94     53.62                                   
REMARK 500    LEU D  66      -67.62   -141.05                                   
REMARK 500    ARG D  76      157.87    179.00                                   
REMARK 500    SER D  83      -72.16    -88.83                                   
REMARK 500    SER D  88       -5.21     90.60                                   
REMARK 500    SER D  90      -79.86   -119.43                                   
REMARK 500    ASN D  95      -60.33   -103.46                                   
REMARK 500    TRP D  96     -139.56     60.39                                   
REMARK 500    ASN D  97     -169.75   -164.82                                   
REMARK 500    GLU D 100      -19.35     76.56                                   
REMARK 500    GLN D 102       67.58     66.15                                   
REMARK 500    ARG D 114      -63.45    -93.26                                   
REMARK 500    ALA D 123     -141.40     58.71                                   
REMARK 500    LEU E   3     -125.71     46.88                                   
REMARK 500    TYR E  30     -168.27    -73.84                                   
REMARK 500    GLN E  32      -68.14   -127.98                                   
REMARK 500    SER E  36      -73.08    -96.70                                   
REMARK 500    LYS E  59     -133.82     67.61                                   
REMARK 500    ASN E  69       72.44     49.48                                   
REMARK 500    ASP E 103      -62.54   -129.07                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     180 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A   19     ASN A   20                   31.48                    
REMARK 500 LEU E   58     LYS E   59                   34.71                    
REMARK 500 PRO F  206     THR F  207                  144.05                    
REMARK 500 THR F  207     LYS F  208                  137.17                    
REMARK 500 LEU I  202     ASP I  203                  149.70                    
REMARK 500 LEU K   53     ALA K   54                  126.13                    
REMARK 500 SER K   55     GLN K   56                  -32.57                    
REMARK 500 ASN M    3     CYS M    4                 -146.48                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 514        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH C 515        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH J 310        DISTANCE =  5.94 ANGSTROMS                       
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                              NA A 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  27   OE2                                                    
REMARK 620 2 HOH A 316   O   132.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  18   OE1                                                    
REMARK 620 2 GLU B  18   OE2  50.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 180   OD1                                                    
REMARK 620 2 ASP C 180   OD2  50.6                                              
REMARK 620 3 SER C 182   OG   69.9 118.3                                        
REMARK 620 4 SER C 184   OG  119.2 155.7  65.2                                  
REMARK 620 5 THR C 250   OG1 101.2  72.6 109.3 130.8                            
REMARK 620 6 ASP C 283   OD1  91.3  67.2 135.4  93.2 114.0                      
REMARK 620 7 ASP C 283   OD2  90.4 108.9  83.4  46.7 165.1  55.8                
REMARK 620 8 HOH C 503   O   174.3 129.8 111.0  57.8  83.9  84.2  84.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 285   OE2                                                    
REMARK 620 2 ASP C 321   O   139.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 411  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASP O 297   OD1  94.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO D  22   O                                                      
REMARK 620 2 GLU D  27   OE1 161.6                                              
REMARK 620 3 HOH D 309   O   107.4  84.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  27   OE1                                                    
REMARK 620 2 GLU D  27   OE2  52.8                                              
REMARK 620 3 GLU J  34   OE1 149.0 113.8                                        
REMARK 620 4 GLU J  34   OE2 131.7  79.5  52.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 209  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D  43   OG                                                     
REMARK 620 2 SER E  79   OG  133.3                                              
REMARK 620 3 ASP E  80   OD1  73.0 132.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU E   3   O                                                      
REMARK 620 2 HOH E 309   O   133.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 182   OG                                                     
REMARK 620 2 SER F 184   OG   90.0                                              
REMARK 620 3 ASP F 283   OD1 114.5 102.3                                        
REMARK 620 4 ASP F 283   OD2 122.5  48.7  56.8                                  
REMARK 620 5 SO4 F 401   O1   87.0 101.8 147.4 132.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 189   OD1                                                    
REMARK 620 2 ASP F 189   OD2  50.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA G 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  47   OD1                                                    
REMARK 620 2 HOH G 315   O    89.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 180   OD2                                                    
REMARK 620 2 SER I 182   OG  104.4                                              
REMARK 620 3 SER I 184   OG  132.4  62.4                                        
REMARK 620 4 THR I 250   OG1  75.5 114.1 152.0                                  
REMARK 620 5 ASP I 283   OD1  71.1 109.8  71.9 129.8                            
REMARK 620 6 SO4 I 407   O1  144.0 111.0  72.8  84.1 101.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 248   OD1                                                    
REMARK 620 2 ASP I 248   OD2  53.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY I 284   O                                                      
REMARK 620 2 SER I 286   OG  139.3                                              
REMARK 620 3 GLU I 328   OE1 142.0  68.4                                        
REMARK 620 4 HOH I 503   O    81.8  91.3 130.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA L 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER L 286   O                                                      
REMARK 620 2 SER L 286   OG   69.8                                              
REMARK 620 3 GLU L 328   OE2 118.4  59.5                                        
REMARK 620 4 HOH L 510   O   127.9 118.6  62.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA N 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER N  43   OG                                                     
REMARK 620 2 GLU N  45   OE1 109.6                                              
REMARK 620 3 GLU N  45   OE2  68.6  50.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA O 404  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP O 189   OD1                                                    
REMARK 620 2 HOH O 519   O    86.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA O 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP O 248   O                                                      
REMARK 620 2 SO4 O 402   O2  117.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA O 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP O 248   OD1                                                    
REMARK 620 2 ASP O 248   OD2  53.4                                              
REMARK 620 3 HOH O 520   O   123.4 173.4                                        
REMARK 620 4 HOH O 518   O    97.2  76.7 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA P 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU P  65   OE1                                                    
REMARK 620 2 GLU P  65   OE2  50.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA Q 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR Q  60   OH                                                     
REMARK 620 2 THR R 322   OG1  74.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG R 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER R 182   OG                                                     
REMARK 620 2 SER R 184   OG   59.2                                              
REMARK 620 3 SO4 R 404   O4   77.0  99.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 411                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA I 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA I 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA J 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA J 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL J 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL J 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL J 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA L 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA L 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL L 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA M 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA N 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA O 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 O 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA O 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA O 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG O 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 O 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA P 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL P 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA Q 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA Q 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA R 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG R 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 R 404                 
DBREF  5THP A    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP B    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP C  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  5THP D    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP E    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP F  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  5THP G    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP H    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP I  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  5THP J    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP K    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP L  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  5THP M    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP N    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP O  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  5THP P    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  5THP Q    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  5THP R  170   366  UNP    P17301   ITA2_HUMAN     170    366             
SEQADV 5THP MET C  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY C  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER C  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER C  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS C  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER C  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER C  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY C  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU C  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL C  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO C  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG C  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY C  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY C  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER C  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP MET F  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY F  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER F  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER F  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS F  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER F  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER F  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY F  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU F  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL F  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO F  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG F  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY F  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY F  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER F  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP MET I  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY I  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER I  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER I  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS I  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER I  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER I  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY I  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU I  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL I  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO I  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG I  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY I  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY I  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER I  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP MET L  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY L  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER L  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER L  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS L  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER L  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER L  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY L  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU L  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL L  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO L  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG L  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY L  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY L  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER L  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP MET O  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY O  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER O  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER O  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS O  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER O  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER O  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY O  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU O  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL O  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO O  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG O  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY O  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY O  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER O  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP MET R  150  UNP  P17301              INITIATING METHIONINE          
SEQADV 5THP GLY R  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER R  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER R  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP HIS R  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER R  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER R  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY R  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP LEU R  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP VAL R  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP PRO R  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP ARG R  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY R  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP GLY R  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 5THP SER R  169  UNP  P17301              EXPRESSION TAG                 
SEQRES   1 A  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 A  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 A  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 A  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 A  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 A  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 A  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 A  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 A  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 A  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 A  135  PHE PRO SER GLU CYS                                          
SEQRES   1 B  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 B  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 B  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 B  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 B  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 B  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 B  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 B  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 B  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 B  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 C  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 C  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 C  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 C  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 C  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 C  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 C  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 C  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 C  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 C  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 C  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 C  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 C  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 C  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 C  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 C  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 D  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 D  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 D  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 D  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 D  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 D  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 D  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 D  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 D  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 D  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 D  135  PHE PRO SER GLU CYS                                          
SEQRES   1 E  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 E  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 E  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 E  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 E  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 E  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 E  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 E  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 E  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 E  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 F  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 F  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 F  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 F  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 F  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 F  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 F  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 F  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 F  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 F  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 F  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 F  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 F  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 F  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 F  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 F  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 G  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 G  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 G  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 G  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 G  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 G  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 G  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 G  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 G  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 G  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 G  135  PHE PRO SER GLU CYS                                          
SEQRES   1 H  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 H  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 H  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 H  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 H  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 H  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 H  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 H  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 H  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 H  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 I  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 I  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 I  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 I  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 I  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 I  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 I  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 I  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 I  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 I  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 I  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 I  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 I  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 I  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 I  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 I  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 I  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 J  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 J  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 J  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 J  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 J  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 J  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 J  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 J  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 J  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 J  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 J  135  PHE PRO SER GLU CYS                                          
SEQRES   1 K  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 K  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 K  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 K  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 K  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 K  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 K  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 K  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 K  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 K  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 L  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 L  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 L  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 L  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 L  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 L  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 L  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 L  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 L  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 L  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 L  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 L  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 L  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 L  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 L  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 L  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 L  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 M  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 M  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 M  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 M  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 M  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 M  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 M  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 M  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 M  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 M  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 M  135  PHE PRO SER GLU CYS                                          
SEQRES   1 N  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 N  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 N  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 N  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 N  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 N  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 N  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 N  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 N  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 N  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 O  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 O  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 O  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 O  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 O  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 O  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 O  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 O  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 O  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 O  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 O  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 O  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 O  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 O  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 O  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 O  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 O  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 P  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 P  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 P  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 P  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 P  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 P  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 P  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 P  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 P  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 P  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 P  135  PHE PRO SER GLU CYS                                          
SEQRES   1 Q  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 Q  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 Q  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 Q  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 Q  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 Q  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 Q  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 Q  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 Q  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 Q  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 R  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 R  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 R  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 R  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 R  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 R  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 R  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 R  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 R  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 R  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 R  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 R  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 R  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 R  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 R  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 R  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 R  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
HET     NA  A 201       1                                                       
HET     CL  A 202       1                                                       
HET    GOL  A 203       6                                                       
HET     NA  B 201       1                                                       
HET     NA  C 401       1                                                       
HET     NA  C 402       1                                                       
HET     NA  C 403       1                                                       
HET     MG  C 404       1                                                       
HET     CL  C 405       1                                                       
HET     CL  C 406       1                                                       
HET     CL  C 407       1                                                       
HET     CL  C 408       1                                                       
HET    SO4  C 409       5                                                       
HET    GOL  C 410       6                                                       
HET     NA  C 411       1                                                       
HET     NA  D 201       1                                                       
HET     NA  D 202       1                                                       
HET     CL  D 203       1                                                       
HET     CL  D 204       1                                                       
HET     CL  D 205       1                                                       
HET     CL  D 206       1                                                       
HET     CL  D 207       1                                                       
HET    SO4  D 208       5                                                       
HET     NA  D 209       1                                                       
HET     NA  E 201       1                                                       
HET     NA  E 202       1                                                       
HET     NA  E 203       1                                                       
HET     CL  E 204       1                                                       
HET     CL  E 205       1                                                       
HET     CL  E 206       1                                                       
HET    SO4  E 207       5                                                       
HET    SO4  F 401       5                                                       
HET     NA  F 402       1                                                       
HET     NA  F 403       1                                                       
HET     MG  F 404       1                                                       
HET     CL  F 405       1                                                       
HET    SO4  F 406       5                                                       
HET     NA  G 201       1                                                       
HET     CL  G 202       1                                                       
HET     CL  G 203       1                                                       
HET    GOL  G 204       6                                                       
HET    GOL  G 205      14                                                       
HET     NA  H 201       1                                                       
HET     CL  H 202       1                                                       
HET     CL  H 203       1                                                       
HET    GOL  H 204       6                                                       
HET     NA  I 401       1                                                       
HET     NA  I 402       1                                                       
HET     MG  I 403       1                                                       
HET     CL  I 404       1                                                       
HET     CL  I 405       1                                                       
HET     CL  I 406       1                                                       
HET    SO4  I 407       5                                                       
HET     NA  J 201       1                                                       
HET     NA  J 202       1                                                       
HET     CL  J 203       1                                                       
HET    GOL  J 204       6                                                       
HET    GOL  J 205       6                                                       
HET     NA  L 401       1                                                       
HET     NA  L 402       1                                                       
HET     MG  L 403       1                                                       
HET     CL  L 404       1                                                       
HET     CL  L 405       1                                                       
HET    SO4  L 406       5                                                       
HET     NA  M 201       1                                                       
HET     CL  M 202       1                                                       
HET     CL  M 203       1                                                       
HET     NA  N 201       1                                                       
HET     CL  N 202       1                                                       
HET     CL  N 203       1                                                       
HET     CL  N 204       1                                                       
HET     NA  O 401       1                                                       
HET    SO4  O 402       5                                                       
HET     NA  O 403       1                                                       
HET     NA  O 404       1                                                       
HET     MG  O 405       1                                                       
HET     CL  O 406       1                                                       
HET    SO4  O 407       5                                                       
HET     NA  P 201       1                                                       
HET     CL  P 202       1                                                       
HET     CL  P 203       1                                                       
HET    GOL  P 204       6                                                       
HET     NA  Q 201       1                                                       
HET     NA  Q 202       1                                                       
HET     CL  Q 203       1                                                       
HET     CL  Q 204       1                                                       
HET     NA  R 401       1                                                       
HET     MG  R 402       1                                                       
HET     CL  R 403       1                                                       
HET    SO4  R 404       5                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  19   NA    31(NA 1+)                                                    
FORMUL  20   CL    35(CL 1-)                                                    
FORMUL  21  GOL    8(C3 H8 O3)                                                  
FORMUL  26   MG    6(MG 2+)                                                     
FORMUL  31  SO4    10(O4 S 2-)                                                  
FORMUL  09  HOH   *218(H2 O)                                                    
HELIX    1 AA1 TRP A   25  THR A   33  1                                   9    
HELIX    2 AA2 SER A   46  ILE A   61  1                                  16    
HELIX    3 AA3 THR B   21  CYS B   29  1                                   9    
HELIX    4 AA4 GLU B   45  GLN B   56  1                                  12    
HELIX    5 AA5 ASP C  189  GLN C  200  1                                  12    
HELIX    6 AA6 THR C  231  THR C  242  1                                  12    
HELIX    7 AA7 ASN C  251  TYR C  262  1                                  12    
HELIX    8 AA8 SER C  265  GLY C  269  5                                   5    
HELIX    9 AA9 MET C  291  HIS C  301  1                                  11    
HELIX   10 AB1 LEU C  312  ASN C  318  1                                   7    
HELIX   11 AB2 THR C  322  ALA C  333  1                                  12    
HELIX   12 AB3 PRO C  336  TYR C  340  5                                   5    
HELIX   13 AB4 ASP C  346  ALA C  348  5                                   3    
HELIX   14 AB5 ALA C  349  GLN C  360  1                                  12    
HELIX   15 AB6 THR D   24  THR D   33  1                                  10    
HELIX   16 AB7 SER D   46  ILE D   61  1                                  16    
HELIX   17 AB8 ARG D  109  GLY D  112  5                                   4    
HELIX   18 AB9 THR E   21  CYS E   29  1                                   9    
HELIX   19 AC1 SER E   43  LEU E   58  1                                  16    
HELIX   20 AC2 PRO F  187  LEU F  202  1                                  16    
HELIX   21 AC3 THR F  231  THR F  242  1                                  12    
HELIX   22 AC4 ASN F  251  TYR F  262  1                                  12    
HELIX   23 AC5 SER F  265  GLY F  269  5                                   5    
HELIX   24 AC6 MET F  291  ASP F  302  1                                  12    
HELIX   25 AC7 LEU F  312  ASN F  318  1                                   7    
HELIX   26 AC8 THR F  322  ALA F  333  1                                  12    
HELIX   27 AC9 ALA F  349  GLY F  358  1                                  10    
HELIX   28 AD1 GLU F  359  ILE F  361  5                                   3    
HELIX   29 AD2 THR G   24  GLU G   34  1                                  11    
HELIX   30 AD3 SER G   46  ILE G   61  1                                  16    
HELIX   31 AD4 TRP H   22  CYS H   29  1                                   8    
HELIX   32 AD5 SER H   43  THR H   57  1                                  15    
HELIX   33 AD6 PRO I  187  VAL I  199  1                                  13    
HELIX   34 AD7 THR I  231  THR I  242  1                                  12    
HELIX   35 AD8 ASN I  251  TYR I  262  1                                  12    
HELIX   36 AD9 SER I  265  GLY I  269  5                                   5    
HELIX   37 AE1 MET I  291  HIS I  301  1                                  11    
HELIX   38 AE2 LEU I  312  ASN I  318  1                                   7    
HELIX   39 AE3 THR I  322  ALA I  333  1                                  12    
HELIX   40 AE4 GLU I  347  ALA I  349  5                                   3    
HELIX   41 AE5 LEU I  350  GLN I  360  1                                  11    
HELIX   42 AE6 THR J   24  GLU J   34  1                                  11    
HELIX   43 AE7 SER J   46  ILE J   61  1                                  16    
HELIX   44 AE8 THR K   21  GLU K   26  1                                   6    
HELIX   45 AE9 SER K   43  LEU K   53  1                                  11    
HELIX   46 AF1 PRO L  187  GLN L  200  1                                  14    
HELIX   47 AF2 THR L  231  THR L  242  1                                  12    
HELIX   48 AF3 ASN L  251  TYR L  262  1                                  12    
HELIX   49 AF4 SER L  265  GLY L  269  5                                   5    
HELIX   50 AF5 MET L  291  ASP L  302  1                                  12    
HELIX   51 AF6 LEU L  312  ASN L  318  1                                   7    
HELIX   52 AF7 THR L  322  ALA L  333  1                                  12    
HELIX   53 AF8 ASP L  346  ALA L  348  5                                   3    
HELIX   54 AF9 ALA L  349  GLY L  358  1                                  10    
HELIX   55 AG1 THR M   24  THR M   33  1                                  10    
HELIX   56 AG2 SER M   46  THR M   58  1                                  13    
HELIX   57 AG3 TRP M  110  GLY M  112  5                                   3    
HELIX   58 AG4 THR N   21  CYS N   29  1                                   9    
HELIX   59 AG5 SER N   43  GLN N   56  1                                  14    
HELIX   60 AG6 PRO N   70  CYS N   74  5                                   5    
HELIX   61 AG7 PRO O  187  LEU O  202  1                                  16    
HELIX   62 AG8 THR O  231  THR O  242  1                                  12    
HELIX   63 AG9 ASN O  251  TYR O  262  1                                  12    
HELIX   64 AH1 MET O  291  ASP O  302  1                                  12    
HELIX   65 AH2 LEU O  312  ASN O  318  1                                   7    
HELIX   66 AH3 THR O  322  ALA O  333  1                                  12    
HELIX   67 AH4 PRO O  336  ARG O  339  5                                   4    
HELIX   68 AH5 ASP O  346  ALA O  348  5                                   3    
HELIX   69 AH6 ALA O  349  ILE O  361  1                                  13    
HELIX   70 AH7 THR P   24  THR P   33  1                                  10    
HELIX   71 AH8 SER P   46  ASN P   60  1                                  15    
HELIX   72 AH9 THR Q   21  CYS Q   29  1                                   9    
HELIX   73 AI1 SER Q   43  SER Q   55  1                                  13    
HELIX   74 AI2 PRO R  187  GLN R  200  1                                  14    
HELIX   75 AI3 THR R  231  GLN R  241  1                                  11    
HELIX   76 AI4 ASN R  251  TYR R  262  1                                  12    
HELIX   77 AI5 SER R  265  GLY R  269  5                                   5    
HELIX   78 AI6 MET R  291  ASP R  302  1                                  12    
HELIX   79 AI7 LEU R  312  ASN R  318  1                                   7    
HELIX   80 AI8 THR R  322  ALA R  333  1                                  12    
HELIX   81 AI9 ALA R  349  GLN R  360  1                                  12    
SHEET    1 AA1 4 SER A   9  TYR A  11  0                                        
SHEET    2 AA1 4 HIS A  14  PHE A  19 -1  O  HIS A  14   N  TYR A  11           
SHEET    3 AA1 4 PHE A 127  PHE A 131 -1  O  PHE A 127   N  PHE A  19           
SHEET    4 AA1 4 HIS A  40  LEU A  41 -1  N  HIS A  40   O  LYS A 130           
SHEET    1 AA2 3 VAL A  68  TRP A  69  0                                        
SHEET    2 AA2 3 CYS A 104  LEU A 107 -1  O  LEU A 107   N  VAL A  68           
SHEET    3 AA2 3 TRP A 116  SER A 119 -1  O  SER A 119   N  CYS A 104           
SHEET    1 AA3 2 TYR B  13  LYS B  20  0                                        
SHEET    2 AA3 2 VAL B 116  LYS B 121 -1  O  PHE B 118   N  PHE B  16           
SHEET    1 AA4 3 MET B  63  ASN B  68  0                                        
SHEET    2 AA4 3 TYR B  94  VAL B 100 -1  O  ALA B  96   N  LEU B  67           
SHEET    3 AA4 3 ILE B 105  GLY B 111 -1  O  PHE B 106   N  VAL B  99           
SHEET    1 AA5 5 PRO C 220  PHE C 224  0                                        
SHEET    2 AA5 5 VAL C 211  TYR C 216 -1  N  LEU C 213   O  PHE C 224           
SHEET    3 AA5 5 ASP C 174  ASP C 180  1  N  VAL C 177   O  ILE C 214           
SHEET    4 AA5 5 LYS C 276  VAL C 280  1  O  VAL C 277   N  ASP C 174           
SHEET    5 AA5 5 ILE C 304  PHE C 307  1  O  PHE C 307   N  VAL C 280           
SHEET    1 AA6 4 SER D   9  ALA D  10  0                                        
SHEET    2 AA6 4 HIS D  14  LYS D  23 -1  O  TYR D  16   N  SER D   9           
SHEET    3 AA6 4 ASN D 125  PRO D 132 -1  O  PHE D 131   N  CYS D  15           
SHEET    4 AA6 4 HIS D  40  LEU D  41 -1  N  HIS D  40   O  LYS D 130           
SHEET    1 AA7 3 VAL D  68  TRP D  69  0                                        
SHEET    2 AA7 3 CYS D 104  LEU D 107 -1  O  LEU D 107   N  VAL D  68           
SHEET    3 AA7 3 TRP D 116  SER D 119 -1  O  ASP D 117   N  GLY D 106           
SHEET    1 AA8 2 LEU D  72  ARG D  73  0                                        
SHEET    2 AA8 2 GLU E  77  TRP E  78 -1  O  GLU E  77   N  ARG D  73           
SHEET    1 AA9 3 SER E   6  TYR E   8  0                                        
SHEET    2 AA9 3 TYR E  11  LYS E  20 -1  O  TYR E  11   N  TYR E   8           
SHEET    3 AA9 3 VAL E 116  CYS E 120 -1  O  PHE E 118   N  PHE E  16           
SHEET    1 AB1 3 SER E  62  ASN E  68  0                                        
SHEET    2 AB1 3 TYR E  94  VAL E 100 -1  O  MET E  98   N  MET E  63           
SHEET    3 AB1 3 ILE E 105  GLY E 111 -1  O  PHE E 106   N  VAL E  99           
SHEET    1 AB2 5 PRO F 220  PHE F 224  0                                        
SHEET    2 AB2 5 GLN F 210  TYR F 216 -1  N  LEU F 213   O  PHE F 224           
SHEET    3 AB2 5 ASP F 174  ASP F 180  1  N  VAL F 177   O  ILE F 214           
SHEET    4 AB2 5 LYS F 276  THR F 282  1  O  VAL F 279   N  VAL F 178           
SHEET    5 AB2 5 LEU F 305  ALA F 310  1  O  LEU F 305   N  MET F 278           
SHEET    1 AB3 4 SER G   9  TYR G  11  0                                        
SHEET    2 AB3 4 HIS G  14  LYS G  23 -1  O  HIS G  14   N  TYR G  11           
SHEET    3 AB3 4 ASN G 125  PRO G 132 -1  O  PHE G 131   N  CYS G  15           
SHEET    4 AB3 4 HIS G  40  LEU G  41 -1  N  HIS G  40   O  LYS G 130           
SHEET    1 AB4 4 TRP G 116  SER G 119  0                                        
SHEET    2 AB4 4 CYS G 104  ALA G 108 -1  N  CYS G 104   O  SER G 119           
SHEET    3 AB4 4 TYR G  67  ARG G  73 -1  N  VAL G  68   O  LEU G 107           
SHEET    4 AB4 4 GLU H  77  TRP H  78 -1  O  GLU H  77   N  ARG G  73           
SHEET    1 AB5 2 TYR H  13  ARG H  14  0                                        
SHEET    2 AB5 2 CYS H 120  LYS H 121 -1  O  CYS H 120   N  ARG H  14           
SHEET    1 AB6 5 LYS H  20  THR H  21  0                                        
SHEET    2 AB6 5 THR H 115  PHE H 118 -1  O  VAL H 116   N  LYS H  20           
SHEET    3 AB6 5 SER H  62  ASN H  68  1  N  TRP H  64   O  SER H 117           
SHEET    4 AB6 5 TYR H  94  VAL H 100 -1  O  MET H  98   N  MET H  63           
SHEET    5 AB6 5 ILE H 105  GLY H 111 -1  O  PHE H 106   N  VAL H  99           
SHEET    1 AB7 4 PRO I 220  PHE I 224  0                                        
SHEET    2 AB7 4 GLN I 210  TYR I 216 -1  N  LEU I 213   O  PHE I 224           
SHEET    3 AB7 4 ASP I 174  ASP I 180  1  N  VAL I 177   O  ILE I 214           
SHEET    4 AB7 4 LYS I 276  VAL I 281  1  O  VAL I 277   N  ASP I 174           
SHEET    1 AB8 2 ILE I 309  VAL I 311  0                                        
SHEET    2 AB8 2 PHE I 342  VAL I 344  1  O  PHE I 342   N  ALA I 310           
SHEET    1 AB9 4 SER J   9  TYR J  11  0                                        
SHEET    2 AB9 4 HIS J  14  PHE J  19 -1  O  HIS J  14   N  TYR J  11           
SHEET    3 AB9 4 PHE J 127  PHE J 131 -1  O  PHE J 131   N  CYS J  15           
SHEET    4 AB9 4 HIS J  40  LEU J  41 -1  N  HIS J  40   O  LYS J 130           
SHEET    1 AC1 4 TRP J 116  SER J 119  0                                        
SHEET    2 AC1 4 CYS J 104  ALA J 108 -1  N  CYS J 104   O  SER J 119           
SHEET    3 AC1 4 TYR J  67  ASP J  74 -1  N  VAL J  68   O  LEU J 107           
SHEET    4 AC1 4 TRP K  76  GLU K  77 -1  O  GLU K  77   N  ARG J  73           
SHEET    1 AC2 2 PHE K  16  LYS K  20  0                                        
SHEET    2 AC2 2 VAL K 116  PHE K 118 -1  O  VAL K 116   N  LYS K  20           
SHEET    1 AC3 3 MET K  63  ASN K  68  0                                        
SHEET    2 AC3 3 TYR K  94  LYS K 101 -1  O  MET K  98   N  MET K  63           
SHEET    3 AC3 3 ARG K 104  GLY K 111 -1  O  PHE K 106   N  VAL K  99           
SHEET    1 AC4 5 PRO L 220  PHE L 224  0                                        
SHEET    2 AC4 5 VAL L 211  TYR L 216 -1  N  LEU L 213   O  PHE L 224           
SHEET    3 AC4 5 VAL L 175  ASP L 180  1  N  VAL L 177   O  ILE L 214           
SHEET    4 AC4 5 VAL L 277  VAL L 281  1  O  VAL L 281   N  VAL L 178           
SHEET    5 AC4 5 LEU L 305  PHE L 307  1  O  PHE L 307   N  VAL L 280           
SHEET    1 AC5 4 SER M   9  ALA M  10  0                                        
SHEET    2 AC5 4 CYS M  15  TYR M  16 -1  O  TYR M  16   N  SER M   9           
SHEET    3 AC5 4 CYS M 129  PHE M 131 -1  O  PHE M 131   N  CYS M  15           
SHEET    4 AC5 4 HIS M  40  LEU M  41 -1  N  HIS M  40   O  LYS M 130           
SHEET    1 AC6 2 PHE M  19  LYS M  23  0                                        
SHEET    2 AC6 2 ASN M 125  PHE M 127 -1  O  PHE M 127   N  PHE M  19           
SHEET    1 AC7 3 TYR M  67  TRP M  69  0                                        
SHEET    2 AC7 3 CYS M 104  ALA M 108 -1  O  LEU M 107   N  VAL M  68           
SHEET    3 AC7 3 TRP M 116  SER M 119 -1  O  SER M 119   N  CYS M 104           
SHEET    1 AC8 2 ARG M  73  ASP M  74  0                                        
SHEET    2 AC8 2 TRP N  76  GLU N  77 -1  O  GLU N  77   N  ARG M  73           
SHEET    1 AC9 3 SER N   6  TYR N   8  0                                        
SHEET    2 AC9 3 TYR N  11  LYS N  20 -1  O  TYR N  13   N  SER N   6           
SHEET    3 AC9 3 VAL N 116  CYS N 120 -1  O  PHE N 118   N  PHE N  16           
SHEET    1 AD1 3 MET N  63  ASN N  68  0                                        
SHEET    2 AD1 3 TYR N  94  VAL N 100 -1  O  ALA N  96   N  LEU N  67           
SHEET    3 AD1 3 ILE N 105  GLY N 111 -1  O  PHE N 106   N  VAL N  99           
SHEET    1 AD2 6 ARG O 221  PHE O 224  0                                        
SHEET    2 AD2 6 GLN O 210  TYR O 216 -1  N  LEU O 213   O  PHE O 224           
SHEET    3 AD2 6 ASP O 174  ASP O 180  1  N  VAL O 175   O  GLY O 212           
SHEET    4 AD2 6 LYS O 276  VAL O 281  1  O  VAL O 279   N  VAL O 178           
SHEET    5 AD2 6 ILE O 304  VAL O 311  1  O  LEU O 305   N  MET O 278           
SHEET    6 AD2 6 PHE O 341  VAL O 344  1  O  VAL O 344   N  ALA O 310           
SHEET    1 AD3 3 SER P   9  TYR P  11  0                                        
SHEET    2 AD3 3 HIS P  14  LYS P  23 -1  O  TYR P  16   N  SER P   9           
SHEET    3 AD3 3 ASN P 125  PRO P 132 -1  O  PHE P 131   N  CYS P  15           
SHEET    1 AD4 3 TYR P  67  TRP P  69  0                                        
SHEET    2 AD4 3 CYS P 104  ALA P 108 -1  O  LEU P 107   N  VAL P  68           
SHEET    3 AD4 3 TRP P 116  SER P 119 -1  O  SER P 119   N  CYS P 104           
SHEET    1 AD5 3 SER Q   6  TYR Q   8  0                                        
SHEET    2 AD5 3 TYR Q  11  LYS Q  20 -1  O  TYR Q  11   N  TYR Q   8           
SHEET    3 AD5 3 VAL Q 116  LYS Q 121 -1  O  PHE Q 118   N  PHE Q  16           
SHEET    1 AD6 3 SER Q  62  ASN Q  68  0                                        
SHEET    2 AD6 3 TYR Q  94  VAL Q 100 -1  O  MET Q  98   N  MET Q  63           
SHEET    3 AD6 3 ILE Q 105  GLY Q 111 -1  O  ARG Q 110   N  CYS Q  95           
SHEET    1 AD7 6 PRO R 220  PHE R 224  0                                        
SHEET    2 AD7 6 GLY R 212  TYR R 216 -1  N  LEU R 213   O  PHE R 224           
SHEET    3 AD7 6 VAL R 176  ASP R 180  1  N  VAL R 177   O  ILE R 214           
SHEET    4 AD7 6 LYS R 276  THR R 282  1  O  VAL R 279   N  VAL R 176           
SHEET    5 AD7 6 ILE R 304  VAL R 311  1  O  LEU R 305   N  MET R 278           
SHEET    6 AD7 6 PHE R 342  VAL R 344  1  O  PHE R 342   N  ALA R 310           
SSBOND   1 CYS A    4    CYS A   15                          1555   1555  2.03  
SSBOND   2 CYS A   32    CYS A  129                          1555   1555  2.03  
SSBOND   3 CYS A   81    CYS B   74                          1555   1555  2.03  
SSBOND   4 CYS A  104    CYS A  121                          1555   1555  2.03  
SSBOND   5 CYS B    1    CYS B   12                          1555   1555  2.03  
SSBOND   6 CYS B   29    CYS B  120                          1555   1555  2.03  
SSBOND   7 CYS B   95    CYS B  112                          1555   1555  2.03  
SSBOND   8 CYS D    4    CYS D   15                          1555   1555  2.03  
SSBOND   9 CYS D   32    CYS D  129                          1555   1555  2.03  
SSBOND  10 CYS D   81    CYS E   74                          1555   1555  2.03  
SSBOND  11 CYS D  104    CYS D  121                          1555   1555  2.03  
SSBOND  12 CYS E    1    CYS E   12                          1555   1555  2.03  
SSBOND  13 CYS E   29    CYS E  120                          1555   1555  2.03  
SSBOND  14 CYS E   95    CYS E  112                          1555   1555  2.03  
SSBOND  15 CYS G    4    CYS G   15                          1555   1555  2.03  
SSBOND  16 CYS G   32    CYS G  129                          1555   1555  2.03  
SSBOND  17 CYS G   81    CYS H   74                          1555   1555  2.03  
SSBOND  18 CYS G  104    CYS G  121                          1555   1555  2.03  
SSBOND  19 CYS H    1    CYS H   12                          1555   1555  2.03  
SSBOND  20 CYS H   29    CYS H  120                          1555   1555  2.03  
SSBOND  21 CYS H   95    CYS H  112                          1555   1555  2.03  
SSBOND  22 CYS J    4    CYS J   15                          1555   1555  2.03  
SSBOND  23 CYS J   32    CYS J  129                          1555   1555  2.03  
SSBOND  24 CYS J   81    CYS K   74                          1555   1555  2.03  
SSBOND  25 CYS J  104    CYS J  121                          1555   1555  2.03  
SSBOND  26 CYS K   95    CYS K  112                          1555   1555  2.03  
SSBOND  27 CYS M    4    CYS M   15                          1555   1555  2.03  
SSBOND  28 CYS M   32    CYS M  129                          1555   1555  2.03  
SSBOND  29 CYS M   81    CYS N   74                          1555   1555  2.03  
SSBOND  30 CYS M  104    CYS M  121                          1555   1555  2.03  
SSBOND  31 CYS N    1    CYS N   12                          1555   1555  2.03  
SSBOND  32 CYS N   29    CYS N  120                          1555   1555  2.03  
SSBOND  33 CYS N   95    CYS N  112                          1555   1555  2.03  
SSBOND  34 CYS P    4    CYS P   15                          1555   1555  2.03  
SSBOND  35 CYS P   32    CYS P  129                          1555   1555  2.03  
SSBOND  36 CYS P   81    CYS Q   74                          1555   1555  2.03  
SSBOND  37 CYS P  104    CYS P  121                          1555   1555  2.03  
SSBOND  38 CYS Q    1    CYS Q   12                          1555   1555  2.03  
SSBOND  39 CYS Q   29    CYS Q  120                          1555   1555  2.03  
SSBOND  40 CYS Q   95    CYS Q  112                          1555   1555  2.03  
LINK         OE2 GLU A  27                NA    NA A 201     1555   1555  2.48  
LINK         OE1 GLU B  18                NA    NA B 201     1555   1555  2.65  
LINK         OE2 GLU B  18                NA    NA B 201     1555   1555  2.50  
LINK         OD1 ASP C 180                MG    MG C 404     1555   1555  2.57  
LINK         OD2 ASP C 180                MG    MG C 404     1555   1555  2.57  
LINK         OG  SER C 182                MG    MG C 404     1555   1555  1.88  
LINK         OG  SER C 184                MG    MG C 404     1555   1555  2.39  
LINK         OG1 THR C 250                MG    MG C 404     1555   1555  2.36  
LINK         OD1 ASP C 283                MG    MG C 404     1555   1555  1.89  
LINK         OD2 ASP C 283                MG    MG C 404     1555   1555  2.61  
LINK         OE2 GLU C 285                NA    NA C 402     1555   1555  2.43  
LINK         OD1 ASP C 297                NA    NA C 411     1555   1555  2.34  
LINK         OD1 ASN C 303                NA    NA C 401     1555   1555  2.56  
LINK         O   ASP C 321                NA    NA C 402     1555   1555  2.41  
LINK         O   PRO D  22                NA    NA D 202     1555   1555  2.57  
LINK         OE1 GLU D  27                NA    NA D 201     1555   1555  2.46  
LINK         OE1 GLU D  27                NA    NA D 202     1555   1555  2.89  
LINK         OE2 GLU D  27                NA    NA D 201     1555   1555  2.48  
LINK         OG  SER D  43                NA    NA D 209     1555   1555  2.43  
LINK         O   LEU E   3                NA    NA E 201     1555   1555  2.40  
LINK         OG  SER E  79                NA    NA D 209     1555   1555  2.78  
LINK         OD1 ASP E  80                NA    NA D 209     1555   1555  2.35  
LINK         OG  SER F 182                MG    MG F 404     1555   1555  2.41  
LINK         OG  SER F 184                MG    MG F 404     1555   1555  2.05  
LINK         OD1 ASP F 189                NA    NA F 403     1555   1555  2.67  
LINK         OD2 ASP F 189                NA    NA F 403     1555   1555  2.50  
LINK         OD1 ASP F 283                MG    MG F 404     1555   1555  2.27  
LINK         OD2 ASP F 283                MG    MG F 404     1555   1555  2.34  
LINK         OD1 ASN F 318                NA    NA F 402     1555   1555  2.74  
LINK         OD1 ASP G  47                NA    NA G 201     1555   1555  2.54  
LINK         OD2 ASP I 180                MG    MG I 403     1555   1555  2.57  
LINK         OG  SER I 182                MG    MG I 403     1555   1555  1.92  
LINK         OG  SER I 184                MG    MG I 403     1555   1555  2.64  
LINK         OD1 ASP I 248                NA    NA I 401     1555   1555  2.52  
LINK         OD2 ASP I 248                NA    NA I 401     1555   1555  2.32  
LINK         OG1 THR I 250                MG    MG I 403     1555   1555  2.57  
LINK         OD1 ASP I 283                MG    MG I 403     1555   1555  2.35  
LINK         O   GLY I 284                NA    NA I 402     1555   1555  2.54  
LINK         OG  SER I 286                NA    NA I 402     1555   1555  3.05  
LINK         OE1 GLU I 328                NA    NA I 402     1555   1555  2.43  
LINK         OD2 ASP J  12                NA    NA J 201     1555   1555  2.42  
LINK         OE1 GLU J  34                NA    NA D 201     1555   1555  2.45  
LINK         OE2 GLU J  34                NA    NA D 201     1555   1555  2.54  
LINK         OD2 ASP J  47                NA    NA J 202     1555   1555  2.54  
LINK         OG  SER L 184                MG    MG L 403     1555   1555  2.87  
LINK         O   SER L 286                NA    NA L 402     1555   1555  2.40  
LINK         OG  SER L 286                NA    NA L 402     1555   1555  2.76  
LINK         OE2 GLU L 328                NA    NA L 402     1555   1555  2.32  
LINK         OE1 GLU M  27                NA    NA M 201     1555   1555  2.52  
LINK         OG  SER N  43                NA    NA N 201     1555   1555  2.50  
LINK         OE1 GLU N  45                NA    NA N 201     1555   1555  2.64  
LINK         OE2 GLU N  45                NA    NA N 201     1555   1555  2.51  
LINK         OG  SER O 182                MG    MG O 405     1555   1555  2.14  
LINK         OD1 ASP O 189                NA    NA O 404     1555   1555  2.45  
LINK         O   ASP O 248                NA    NA O 401     1555   1555  2.62  
LINK         OD1 ASP O 248                NA    NA O 403     1555   1555  2.35  
LINK         OD2 ASP O 248                NA    NA O 403     1555   1555  2.53  
LINK         OD1 ASP O 297                NA    NA C 411     1555   1555  2.42  
LINK         OE1 GLU P  65                NA    NA P 201     1555   1555  2.45  
LINK         OE2 GLU P  65                NA    NA P 201     1555   1555  2.64  
LINK         OE1 GLU Q  46                NA    NA Q 202     1555   1555  2.48  
LINK         OH  TYR Q  60                NA    NA Q 201     1555   1555  2.57  
LINK         OG  SER R 182                MG    MG R 402     1555   1555  2.97  
LINK         OG  SER R 184                MG    MG R 402     1555   1555  1.99  
LINK         OE2 GLU R 196                NA    NA R 401     1555   1555  2.27  
LINK         OG1 THR R 322                NA    NA Q 201     1555   1555  2.56  
LINK        NA    NA A 201                 O   HOH A 316     1555   1555  2.50  
LINK        MG    MG C 404                 O   HOH C 503     1555   1555  1.97  
LINK        NA    NA D 202                 O   HOH D 309     1555   1555  2.40  
LINK        NA    NA E 201                 O   HOH E 309     1555   1555  2.43  
LINK        NA    NA E 202                 O3  SO4 E 207     1555   1555  2.47  
LINK         O1  SO4 F 401                MG    MG F 404     1555   1555  2.38  
LINK        NA    NA G 201                 O   HOH G 315     1555   1555  2.62  
LINK        NA    NA H 201                 O   HOH H 307     1555   1555  2.50  
LINK        NA    NA I 402                 O   HOH I 503     1555   1555  2.33  
LINK        MG    MG I 403                 O1  SO4 I 407     1555   1555  2.53  
LINK        NA    NA L 402                 O   HOH L 510     1555   1555  2.46  
LINK        NA    NA O 401                 O2  SO4 O 402     1555   1555  2.80  
LINK        NA    NA O 403                 O   HOH O 520     1555   1555  2.51  
LINK        NA    NA O 403                 O   HOH O 518     1555   1555  2.38  
LINK        NA    NA O 404                 O   HOH O 519     1555   1555  2.33  
LINK        MG    MG R 402                 O4  SO4 R 404     1555   1555  2.33  
CISPEP   1 PHE A    2    ASN A    3          0        -0.36                     
CISPEP   2 THR A   24    TRP A   25          0         8.67                     
CISPEP   3 GLU A   34    GLN A   35          0         0.26                     
CISPEP   4 SER A  101    GLN A  102          0         4.47                     
CISPEP   5 CYS B   29    TYR B   30          0         8.37                     
CISPEP   6 GLY B   35    SER B   36          0        -8.10                     
CISPEP   7 LEU B   58    LYS B   59          0       -27.81                     
CISPEP   8 GLN C  200    GLY C  201          0        15.18                     
CISPEP   9 ARG C  271    ARG C  272          0        -1.66                     
CISPEP  10 ARG C  272    SER C  273          0        21.70                     
CISPEP  11 SER C  273    ALA C  274          0        18.61                     
CISPEP  12 HIS C  301    ASP C  302          0        -5.20                     
CISPEP  13 ILE C  335    PRO C  336          0        -2.65                     
CISPEP  14 ASN C  343    VAL C  344          0         8.23                     
CISPEP  15 ILE C  361    PHE C  362          0         2.79                     
CISPEP  16 PHE D    2    ASN D    3          0         0.43                     
CISPEP  17 GLU D   34    GLN D   35          0         0.77                     
CISPEP  18 PRO D   64    GLU D   65          0         6.72                     
CISPEP  19 SER D  101    GLN D  102          0         2.93                     
CISPEP  20 CYS E   29    TYR E   30          0        12.34                     
CISPEP  21 GLY E   35    SER E   36          0         4.21                     
CISPEP  22 TYR F  186    PRO F  187          0        -5.03                     
CISPEP  23 GLN F  200    GLY F  201          0        20.41                     
CISPEP  24 ILE F  335    PRO F  336          0        -1.57                     
CISPEP  25 PHE F  362    SER F  363          0       -12.85                     
CISPEP  26 SER F  363    ILE F  364          0         0.01                     
CISPEP  27 PHE G    2    ASN G    3          0        -2.14                     
CISPEP  28 GLU G   34    GLN G   35          0        13.46                     
CISPEP  29 SER G  101    GLN G  102          0         6.63                     
CISPEP  30 PHE H   16    SER H   17          0       -18.01                     
CISPEP  31 CYS H   29    TYR H   30          0        14.29                     
CISPEP  32 LEU H   58    LYS H   59          0       -11.23                     
CISPEP  33 TYR I  186    PRO I  187          0        -5.97                     
CISPEP  34 THR I  207    LYS I  208          0        24.83                     
CISPEP  35 ARG I  271    ARG I  272          0        -5.75                     
CISPEP  36 ARG I  272    SER I  273          0       -10.82                     
CISPEP  37 ASN I  303    ILE I  304          0        29.84                     
CISPEP  38 ILE I  335    PRO I  336          0        -0.19                     
CISPEP  39 TYR I  340    PHE I  341          0        -0.70                     
CISPEP  40 ILE I  361    PHE I  362          0         2.56                     
CISPEP  41 PRO J   64    GLU J   65          0         1.37                     
CISPEP  42 SER J  101    GLN J  102          0         5.99                     
CISPEP  43 CYS K   29    TYR K   30          0         9.50                     
CISPEP  44 TYR K   30    ALA K   31          0        23.19                     
CISPEP  45 GLY K   35    SER K   36          0        -5.52                     
CISPEP  46 TYR L  186    PRO L  187          0        -3.00                     
CISPEP  47 GLN L  200    GLY L  201          0         0.28                     
CISPEP  48 GLY L  201    LEU L  202          0         4.00                     
CISPEP  49 THR L  207    LYS L  208          0        23.36                     
CISPEP  50 ARG L  271    ARG L  272          0        -1.18                     
CISPEP  51 ARG L  272    SER L  273          0        25.48                     
CISPEP  52 ILE L  335    PRO L  336          0       -12.70                     
CISPEP  53 ILE L  361    PHE L  362          0        -0.08                     
CISPEP  54 PHE M    2    ASN M    3          0        -8.54                     
CISPEP  55 GLU M   34    GLN M   35          0         1.85                     
CISPEP  56 PRO M   64    GLU M   65          0       -10.17                     
CISPEP  57 SER M  101    GLN M  102          0         9.69                     
CISPEP  58 ALA M  123    LYS M  124          0        -2.67                     
CISPEP  59 CYS N   29    TYR N   30          0         1.63                     
CISPEP  60 TYR N   30    ALA N   31          0         7.19                     
CISPEP  61 GLY N   35    SER N   36          0         8.58                     
CISPEP  62 TYR O  186    PRO O  187          0       -11.13                     
CISPEP  63 GLN O  200    GLY O  201          0        28.52                     
CISPEP  64 ASP O  203    ILE O  204          0        -6.75                     
CISPEP  65 ARG O  271    ARG O  272          0        -2.37                     
CISPEP  66 ARG O  272    SER O  273          0        23.19                     
CISPEP  67 SER O  273    ALA O  274          0        16.21                     
CISPEP  68 ILE O  335    PRO O  336          0        -0.10                     
CISPEP  69 ILE O  361    PHE O  362          0         1.21                     
CISPEP  70 GLU P   34    GLN P   35          0         3.21                     
CISPEP  71 GLN P   35    ALA P   36          0        -4.36                     
CISPEP  72 PRO P   64    GLU P   65          0         4.23                     
CISPEP  73 SER P  101    GLN P  102          0         6.61                     
CISPEP  74 CYS Q   29    TYR Q   30          0       -12.97                     
CISPEP  75 GLY Q   35    SER Q   36          0         2.22                     
CISPEP  76 LEU Q   58    LYS Q   59          0        22.35                     
CISPEP  77 TYR R  186    PRO R  187          0        -5.96                     
CISPEP  78 GLN R  200    GLY R  201          0        -7.60                     
CISPEP  79 GLY R  201    LEU R  202          0        -9.62                     
CISPEP  80 THR R  207    LYS R  208          0         4.43                     
CISPEP  81 ARG R  271    ARG R  272          0         2.39                     
CISPEP  82 ARG R  272    SER R  273          0        -5.08                     
CISPEP  83 ILE R  335    PRO R  336          0        -4.34                     
CISPEP  84 ILE R  361    PHE R  362          0         0.25                     
SITE     1 AC1  2 GLU A  27  HOH A 316                                          
SITE     1 AC2  4 GLN A  55  HOH A 310  TYR I 258  HOH I 514                    
SITE     1 AC3  4 TYR A  11  SER A  46  HOH A 312  HIS I 287                    
SITE     1 AC4  1 GLU B  18                                                     
SITE     1 AC5  2 ASN C 303  THR O 337                                          
SITE     1 AC6  2 GLU C 285  ASP C 321                                          
SITE     1 AC7  1 HIS C 287                                                     
SITE     1 AC8  6 ASP C 180  SER C 182  SER C 184  THR C 250                    
SITE     2 AC8  6 ASP C 283  HOH C 503                                          
SITE     1 AC9  2 SER C 334  ILE C 335                                          
SITE     1 AD1  2 TRP C 188  ASP C 189                                          
SITE     1 AD2  2 ARG C 339  PHE O 362                                          
SITE     1 AD3  1 SER C 184                                                     
SITE     1 AD4  5 ARG B 110  LYS B 114  SER C 184  TYR C 314                    
SITE     2 AD4  5 HOH C 503                                                     
SITE     1 AD5  4 ASP C 297  ASN C 300  ASP O 297  ASN O 300                    
SITE     1 AD6  2 GLU D  27  GLU J  34                                          
SITE     1 AD7  4 PRO D  22  LYS D  23  GLU D  27  HOH D 309                    
SITE     1 AD8  3 ASN D   3  GLN D  13  HOH D 316                               
SITE     1 AD9  1 LYS D  23                                                     
SITE     1 AE1  1 LYS D  23                                                     
SITE     1 AE2  1 GLN D 122                                                     
SITE     1 AE3  2 ASP D  51  ARG D 114                                          
SITE     1 AE4  3 ASN D  20  GLU D  21  HOH D 304                               
SITE     1 AE5  5 SER D  43  GLY D  71  TRP E  78  SER E  79                    
SITE     2 AE5  5 ASP E  80                                                     
SITE     1 AE6  3 LEU E   3  HIS E   4  HOH E 309                               
SITE     1 AE7  1 SO4 E 207                                                     
SITE     1 AE8  1 ILE E 105                                                     
SITE     1 AE9  3 CYS E   1  TRP E   5  HOH E 308                               
SITE     1 AF1  3 TYR D 118  ASN E  69  ARG E  91                               
SITE     1 AF2  3 ASN E  68  LYS E  72   NA E 202                               
SITE     1 AF3  6 ARG E 110  LYS E 114  SER F 182  SER F 184                    
SITE     2 AF3  6 THR F 250   MG F 404                                          
SITE     1 AF4  1 ASN F 318                                                     
SITE     1 AF5  1 ASP F 189                                                     
SITE     1 AF6  4 SER F 182  SER F 184  ASP F 283  SO4 F 401                    
SITE     1 AF7  1 HOH F 510                                                     
SITE     1 AF8  1 ASN F 343                                                     
SITE     1 AF9  2 ASP G  47  HOH G 315                                          
SITE     1 AG1  1 ASN G 125                                                     
SITE     1 AG2  5 ARG C 221  VAL C 222  TYR C 258  GLN G  55                    
SITE     2 AG2  5 ASN G  59                                                     
SITE     1 AG3  1 TYR G  67                                                     
SITE     1 AG4  2 TYR H  86  HOH H 307                                          
SITE     1 AG5  1 LYS H  75                                                     
SITE     1 AG6  1 LYS H  59                                                     
SITE     1 AG7  5 TRP G  25  GLU H  77  TRP H  78  SER H  79                    
SITE     2 AG7  5 ASP H  81                                                     
SITE     1 AG8  3 LEU H  90  ASN I 218  ASP I 248                               
SITE     1 AG9  5 GLY I 284  GLU I 285  SER I 286  GLU I 328                    
SITE     2 AG9  5 HOH I 503                                                     
SITE     1 AH1  6 ASP I 180  SER I 182  SER I 184  THR I 250                    
SITE     2 AH1  6 ASP I 283  SO4 I 407                                          
SITE     1 AH2  2 LEU I 305  ILE I 335                                          
SITE     1 AH3  1 GLU I 347                                                     
SITE     1 AH4  1 GLN I 244                                                     
SITE     1 AH5  5 SER I 182  SER I 184  THR I 250  TYR I 314                    
SITE     2 AH5  5  MG I 403                                                     
SITE     1 AH6  2 ASP J  12  HIS J  14                                          
SITE     1 AH7  1 ASP J  47                                                     
SITE     1 AH8  1 ARG J 114                                                     
SITE     1 AH9  9 ILE J  44  ALA J  50  VAL J  53  ALA J  54                    
SITE     2 AH9  9 LEU J 107  PHE J 113  ARG J 114  TRP J 116                    
SITE     3 AH9  9 TYR K  86                                                     
SITE     1 AI1  3 THR J  33  GLU J  34  ALA J  36                               
SITE     1 AI2  1 HIS L 287                                                     
SITE     1 AI3  3 SER L 286  GLU L 328  HOH L 510                               
SITE     1 AI4  4 SER L 184  ASP L 283  GLY L 284  SO4 L 406                    
SITE     1 AI5  1 ASN L 318                                                     
SITE     1 AI6  6 ARG K  92  SER L 182  ASP L 248  THR L 250                    
SITE     2 AI6  6  MG L 403  HOH L 502                                          
SITE     1 AI7  1 GLU M  27                                                     
SITE     1 AI8  2 GLN M  17  ALA M  18                                          
SITE     1 AI9  1 PHE M   2                                                     
SITE     1 AJ1  2 SER N  43  GLU N  45                                          
SITE     1 AJ2  1 ARG N  44                                                     
SITE     1 AJ3  6 ARG N  92  GLU N 113  LYS N 114  LEU O 249                    
SITE     2 AJ3  6 HIS O 287   NA O 401                                          
SITE     1 AJ4  4 ARG N  92   CL N 203  ASP O 248  SO4 O 402                    
SITE     1 AJ5  5 ARG N 110  LYS N 114  TYR O 314   NA O 401                    
SITE     2 AJ5  5  MG O 405                                                     
SITE     1 AJ6  4 LEU N  90  ASP O 248  HOH O 518  HOH O 520                    
SITE     1 AJ7  4 PRO O 187  TRP O 188  ASP O 189  HOH O 519                    
SITE     1 AJ8  4 ASP O 180  SER O 182  SER O 184  SO4 O 402                    
SITE     1 AJ9  3 ARG O 221  VAL O 222  ASN R 227                               
SITE     1 AK1  2 ARG O 260  LYS O 261                                          
SITE     1 AK2  2 PRO P  22  GLU P  65                                          
SITE     1 AK3  1 ASN P  59                                                     
SITE     1 AK4  2 ASN P  95  TRP P  96                                          
SITE     1 AK5  3 GLU P 100  GLN P 102  HOH P 305                               
SITE     1 AK6  2 TYR Q  60  THR R 322                                          
SITE     1 AK7  1 GLU Q  46                                                     
SITE     1 AK8  1 ARG Q  44                                                     
SITE     1 AK9  1 LYS Q  75                                                     
SITE     1 AL1  1 GLU R 196                                                     
SITE     1 AL2  7 ASP R 180  SER R 182  SER R 184  THR R 250                    
SITE     2 AL2  7 ASP R 283  GLY R 284  SO4 R 404                               
SITE     1 AL3  2 LYS R 192  THR R 242                                          
SITE     1 AL4  7 SER R 182  SER R 184  LEU R 249  THR R 250                    
SITE     2 AL4  7  MG R 402  HOH R 506  HOH R 507                               
CRYST1  130.763  130.763  251.351  90.00  90.00  90.00 P 41         24          
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      0.007647  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003979        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system