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Database: PDB
Entry: 5IRV
LinkDB: 5IRV
Original site: 5IRV 
HEADER    OXIDOREDUCTASE, LYASE/INHIBITOR         14-MAR-16   5IRV              
TITLE     HUMAN CYTOCHROME P450 17A1 BOUND TO INHIBITOR VT-464                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 24-508;                                       
COMPND   5 SYNONYM: 17-ALPHA-HYDROXYPROGESTERONE ALDOLASE, CYPXVII, CYTOCHROME  
COMPND   6 P450 17A1, CYTOCHROME P450-C17, CYTOCHROME P450C17, STEROID 17-ALPHA-
COMPND   7 MONOOXYGENASE;                                                       
COMPND   8 EC: 1.14.14.19, 4.1.2.30;                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP17A1, CYP17, S17AH;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, INHIBITOR COMPLEX, LYASE-INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.E.SCOTT,E.M.PETRUNAK                                                
REVDAT   5   25-DEC-19 5IRV    1       REMARK                                   
REVDAT   4   13-SEP-17 5IRV    1       REMARK                                   
REVDAT   3   17-MAY-17 5IRV    1       JRNL                                     
REVDAT   2   19-APR-17 5IRV    1       JRNL                                     
REVDAT   1   15-MAR-17 5IRV    0                                                
JRNL        AUTH   E.M.PETRUNAK,S.A.ROGERS,J.AUBE,E.E.SCOTT                     
JRNL        TITL   STRUCTURAL AND FUNCTIONAL EVALUATION OF CLINICALLY RELEVANT  
JRNL        TITL 2 INHIBITORS OF STEROIDOGENIC CYTOCHROME P450 17A1.            
JRNL        REF    DRUG METAB. DISPOS.           V.  45   635 2017              
JRNL        REFN                   ESSN 1521-009X                               
JRNL        PMID   28373265                                                     
JRNL        DOI    10.1124/DMD.117.075317                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 42930                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2160                            
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 39.4441 -  7.6219    0.97     2864   147  0.1564 0.1823        
REMARK   3     2  7.6219 -  6.0568    0.99     2811   131  0.1834 0.2011        
REMARK   3     3  6.0568 -  5.2933    0.99     2762   153  0.1803 0.2320        
REMARK   3     4  5.2933 -  4.8102    0.98     2728   135  0.1527 0.2318        
REMARK   3     5  4.8102 -  4.4659    0.99     2755   155  0.1547 0.2200        
REMARK   3     6  4.4659 -  4.2030    1.00     2756   152  0.1810 0.2455        
REMARK   3     7  4.2030 -  3.9927    0.98     2702   133  0.1800 0.2613        
REMARK   3     8  3.9927 -  3.8190    0.98     2681   150  0.1958 0.2498        
REMARK   3     9  3.8190 -  3.6721    0.99     2717   162  0.2148 0.2764        
REMARK   3    10  3.6721 -  3.5455    0.99     2731   133  0.2404 0.3076        
REMARK   3    11  3.5455 -  3.4347    0.99     2728   130  0.2505 0.3361        
REMARK   3    12  3.4347 -  3.3366    0.99     2719   147  0.2533 0.2758        
REMARK   3    13  3.3366 -  3.2488    0.98     2644   128  0.2615 0.3115        
REMARK   3    14  3.2488 -  3.1695    0.98     2686   157  0.2899 0.3285        
REMARK   3    15  3.1695 -  3.0975    0.92     2486   147  0.3281 0.3887        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.31                          
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      :  0.004          15674                                  
REMARK   3   ANGLE     :  0.810          21290                                  
REMARK   3   CHIRALITY :  0.048           2368                                  
REMARK   3   PLANARITY :  0.006           2695                                  
REMARK   3   DIHEDRAL  : 14.671           9366                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND ((RESID 36 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD1)  
REMARK   3                          ) OR (RESID 38 AND (NAME N OR NAME CA OR    
REMARK   3                          NAME C )) OR (RESID 39 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME CB OR NAME OG )) OR         
REMARK   3                          (RESID 40 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          CB OR NAME CG OR NAME CD1 OR NAME CD2))     
REMARK   3                          OR (RESID 41 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME CB OR NAME CG OR NAME CD )) OR         
REMARK   3                          RESSEQ 47:155 OR RESSEQ 157:210 OR RESSEQ   
REMARK   3                          213:214 OR (RESID 217 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME CD2)) OR (RESID 219 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD )  
REMARK   3                          ) OR (RESID 221 AND (NAME N OR NAME CA OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD1 OR NAME      
REMARK   3                          CD2)) OR (RESID 222 AND (NAME N OR NAME     
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD OR      
REMARK   3                          NAME CE OR NAME NZ )) OR RESSEQ 227:228     
REMARK   3                          OR RESSEQ 231:247 OR RESSEQ 249:254 OR      
REMARK   3                          RESSEQ 256:270 OR RESSEQ 272:273 OR         
REMARK   3                          (RESID 274 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME OD2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 275 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME ND2 OR NAME C OR NAME   
REMARK   3                          O )) OR (RESID 281 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME CB OR NAME CG OR NAME OD1 OR NAME   
REMARK   3                          OD2 OR NAME C OR NAME O )) OR (RESID 282    
REMARK   3                          AND (NAME N OR NAME CA OR NAME CB OR NAME   
REMARK   3                          CG OR NAME CD OR NAME OE1 OR NAME NE2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 283 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME OD2 OR NAME C OR NAME   
REMARK   3                          O )) OR RESSEQ 284:337 OR (RESID 338 AND    
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME CD2 OR NAME C OR NAME O OR NAME H   
REMARK   3                          OR NAME HA OR NAME HB2 OR NAME HB3 OR       
REMARK   3                          NAME HD2 OR NAME HE2 OR NAME HZ )) OR       
REMARK   3                          RESSEQ 339:365 OR RESSEQ 367:383 OR         
REMARK   3                          (RESID 384 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 385:410 OR RESSEQ      
REMARK   3                          412:416 OR (RESID 417 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD1 OR NAME    
REMARK   3                          HE1 OR NAME HZ )) OR RESSEQ 418:469 OR      
REMARK   3                          (RESID 470 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3)) OR RESSEQ 471:504 OR RESSEQ   
REMARK   3                          600:601))                                   
REMARK   3     SELECTION          : (CHAIN B AND ((RESID 36 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD1)  
REMARK   3                          ) OR (RESID 38 AND (NAME N OR NAME CA OR    
REMARK   3                          NAME C )) OR (RESID 39 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME CB OR NAME OG )) OR         
REMARK   3                          (RESID 40 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          CB OR NAME CG OR NAME CD1 OR NAME CD2))     
REMARK   3                          OR (RESID 41 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME CB OR NAME CG OR NAME CD )) OR         
REMARK   3                          RESSEQ 47:155 OR RESSEQ 157:210 OR RESSEQ   
REMARK   3                          213:214 OR (RESID 217 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME CD2)) OR (RESID 219 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD )  
REMARK   3                          ) OR (RESID 221 AND (NAME N OR NAME CA OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD1 OR NAME      
REMARK   3                          CD2)) OR (RESID 222 AND (NAME N OR NAME     
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD OR      
REMARK   3                          NAME CE OR NAME NZ )) OR RESSEQ 227:228     
REMARK   3                          OR RESSEQ 231:247 OR RESSEQ 249:254 OR      
REMARK   3                          RESSEQ 256:270 OR RESSEQ 272:273 OR         
REMARK   3                          (RESID 274 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME OD2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 275 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME ND2 OR NAME C OR NAME   
REMARK   3                          O )) OR (RESID 281 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME CB OR NAME CG OR NAME OD1 OR NAME   
REMARK   3                          OD2 OR NAME C OR NAME O )) OR (RESID 282    
REMARK   3                          AND (NAME N OR NAME CA OR NAME CB OR NAME   
REMARK   3                          CG OR NAME CD OR NAME OE1 OR NAME NE2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 283 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME OD2 OR NAME C OR NAME   
REMARK   3                          O )) OR RESSEQ 284:337 OR (RESID 338 AND    
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME CD2 OR NAME C OR NAME O OR NAME H   
REMARK   3                          OR NAME HA OR NAME HB2 OR NAME HB3 OR       
REMARK   3                          NAME HD2 OR NAME HE2 OR NAME HZ )) OR       
REMARK   3                          RESSEQ 339:365 OR RESSEQ 367:383 OR         
REMARK   3                          (RESID 384 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 385:410 OR RESSEQ      
REMARK   3                          412:416 OR (RESID 417 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD1 OR NAME    
REMARK   3                          HE1 OR NAME HZ )) OR RESSEQ 418:469 OR      
REMARK   3                          (RESID 470 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3)) OR RESSEQ 471:504 OR RESSEQ   
REMARK   3                          600:601))                                   
REMARK   3     ATOM PAIRS NUMBER  : 10725                                       
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND ((RESID 36 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD1)  
REMARK   3                          ) OR (RESID 38 AND (NAME N OR NAME CA OR    
REMARK   3                          NAME C )) OR (RESID 39 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME CB OR NAME OG )) OR         
REMARK   3                          (RESID 40 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          CB OR NAME CG OR NAME CD1 OR NAME CD2))     
REMARK   3                          OR (RESID 41 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME CB OR NAME CG OR NAME CD )) OR         
REMARK   3                          RESSEQ 47:155 OR RESSEQ 157:210 OR RESSEQ   
REMARK   3                          213:214 OR (RESID 217 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME CD2)) OR (RESID 219 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD )  
REMARK   3                          ) OR (RESID 221 AND (NAME N OR NAME CA OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD1 OR NAME      
REMARK   3                          CD2)) OR (RESID 222 AND (NAME N OR NAME     
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD OR      
REMARK   3                          NAME CE OR NAME NZ )) OR RESSEQ 227:228     
REMARK   3                          OR RESSEQ 231:247 OR RESSEQ 249:254 OR      
REMARK   3                          RESSEQ 256:270 OR RESSEQ 272:273 OR         
REMARK   3                          (RESID 274 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME OD2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 275 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME ND2 OR NAME C OR NAME   
REMARK   3                          O )) OR (RESID 281 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME CB OR NAME CG OR NAME OD1 OR NAME   
REMARK   3                          OD2 OR NAME C OR NAME O )) OR (RESID 282    
REMARK   3                          AND (NAME N OR NAME CA OR NAME CB OR NAME   
REMARK   3                          CG OR NAME CD OR NAME OE1 OR NAME NE2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 283 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME OD2 OR NAME C OR NAME   
REMARK   3                          O )) OR RESSEQ 284:337 OR (RESID 338 AND    
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME CD2 OR NAME C OR NAME O OR NAME H   
REMARK   3                          OR NAME HA OR NAME HB2 OR NAME HB3 OR       
REMARK   3                          NAME HD2 OR NAME HE2 OR NAME HZ )) OR       
REMARK   3                          RESSEQ 339:365 OR RESSEQ 367:383 OR         
REMARK   3                          (RESID 384 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 385:410 OR RESSEQ      
REMARK   3                          412:416 OR (RESID 417 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD1 OR NAME    
REMARK   3                          HE1 OR NAME HZ )) OR RESSEQ 418:469 OR      
REMARK   3                          (RESID 470 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3)) OR RESSEQ 471:504 OR RESSEQ   
REMARK   3                          600:601))                                   
REMARK   3     SELECTION          : (CHAIN C AND ((RESID 36 AND (NAME O OR      
REMARK   3                          NAME N OR NAME C OR NAME CB OR NAME CD2))   
REMARK   3                          OR (RESID 38 AND (NAME O OR NAME N OR       
REMARK   3                          NAME CA )) OR (RESID 39 AND (NAME O OR      
REMARK   3                          NAME N OR NAME C OR NAME CB )) OR (RESID    
REMARK   3                          40 AND (NAME O OR NAME N OR NAME C OR       
REMARK   3                          NAME CB OR NAME CG OR NAME CD1)) OR         
REMARK   3                          (RESID 41 AND (NAME O OR NAME N OR NAME C   
REMARK   3                          OR NAME CB OR NAME CG )) OR RESSEQ 47:155   
REMARK   3                          OR RESSEQ 157:210 OR RESSEQ 213:214 OR      
REMARK   3                          (RESID 217 AND (NAME O OR NAME N OR NAME    
REMARK   3                          C OR NAME CB OR NAME CG OR NAME CD1)) OR    
REMARK   3                          (RESID 219 AND (NAME O OR NAME N OR NAME    
REMARK   3                          C OR NAME CB OR NAME CG )) OR (RESID 221    
REMARK   3                          AND (NAME O OR NAME N OR NAME C OR NAME     
REMARK   3                          CB OR NAME CG OR NAME CD1)) OR (RESID 222   
REMARK   3                          AND (NAME O OR NAME N OR NAME C OR NAME     
REMARK   3                          CB OR NAME CG OR NAME CD OR NAME CE )) OR   
REMARK   3                          RESSEQ 227:228 OR RESSEQ 231:247 OR         
REMARK   3                          RESSEQ 249:254 OR RESSEQ 256:270 OR         
REMARK   3                          RESSEQ 272:275 OR RESSEQ 281:337 OR         
REMARK   3                          (RESID 338 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 339:365 OR RESSEQ      
REMARK   3                          367:383 OR (RESID 384 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD2 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD2 OR NAME    
REMARK   3                          HE2 OR NAME HZ )) OR RESSEQ 385:410 OR      
REMARK   3                          RESSEQ 412:416 OR (RESID 417 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME CB OR NAME CG OR NAME    
REMARK   3                          CD1 OR NAME C OR NAME O OR NAME H OR NAME   
REMARK   3                          HA OR NAME HB2 OR NAME HB3 OR NAME HD1 OR   
REMARK   3                          NAME HE1 OR NAME HZ )) OR RESSEQ 418:469    
REMARK   3                          OR (RESID 470 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME CB OR NAME CG OR NAME OD1 OR NAME C    
REMARK   3                          OR NAME O OR NAME H OR NAME HA OR NAME      
REMARK   3                          HB2 OR NAME HB3)) OR RESSEQ 471:504 OR      
REMARK   3                          RESSEQ 600:601))                            
REMARK   3     ATOM PAIRS NUMBER  : 10725                                       
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND ((RESID 36 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD1)  
REMARK   3                          ) OR (RESID 38 AND (NAME N OR NAME CA OR    
REMARK   3                          NAME C )) OR (RESID 39 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME CB OR NAME OG )) OR         
REMARK   3                          (RESID 40 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          CB OR NAME CG OR NAME CD1 OR NAME CD2))     
REMARK   3                          OR (RESID 41 AND (NAME N OR NAME CA OR      
REMARK   3                          NAME CB OR NAME CG OR NAME CD )) OR         
REMARK   3                          RESSEQ 47:155 OR RESSEQ 157:210 OR RESSEQ   
REMARK   3                          213:214 OR (RESID 217 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME CD2)) OR (RESID 219 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME CB OR NAME CG OR NAME CD )  
REMARK   3                          ) OR (RESID 221 AND (NAME N OR NAME CA OR   
REMARK   3                          NAME CB OR NAME CG OR NAME CD1 OR NAME      
REMARK   3                          CD2)) OR (RESID 222 AND (NAME N OR NAME     
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD OR      
REMARK   3                          NAME CE OR NAME NZ )) OR RESSEQ 227:228     
REMARK   3                          OR RESSEQ 231:247 OR RESSEQ 249:254 OR      
REMARK   3                          RESSEQ 256:270 OR RESSEQ 272:273 OR         
REMARK   3                          (RESID 274 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME OD2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 275 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME ND2 OR NAME C OR NAME   
REMARK   3                          O )) OR (RESID 281 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME CB OR NAME CG OR NAME OD1 OR NAME   
REMARK   3                          OD2 OR NAME C OR NAME O )) OR (RESID 282    
REMARK   3                          AND (NAME N OR NAME CA OR NAME CB OR NAME   
REMARK   3                          CG OR NAME CD OR NAME OE1 OR NAME NE2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 283 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME OD2 OR NAME C OR NAME   
REMARK   3                          O )) OR RESSEQ 284:337 OR (RESID 338 AND    
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME CD2 OR NAME C OR NAME O OR NAME H   
REMARK   3                          OR NAME HA OR NAME HB2 OR NAME HB3 OR       
REMARK   3                          NAME HD2 OR NAME HE2 OR NAME HZ )) OR       
REMARK   3                          RESSEQ 339:365 OR RESSEQ 367:383 OR         
REMARK   3                          (RESID 384 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 385:410 OR RESSEQ      
REMARK   3                          412:416 OR (RESID 417 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD1 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD1 OR NAME    
REMARK   3                          HE1 OR NAME HZ )) OR RESSEQ 418:469 OR      
REMARK   3                          (RESID 470 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3)) OR RESSEQ 471:504 OR RESSEQ   
REMARK   3                          600:601))                                   
REMARK   3     SELECTION          : (CHAIN D AND ((RESID 36 AND (NAME O OR      
REMARK   3                          NAME N OR NAME C OR NAME CB OR NAME CG ))   
REMARK   3                          OR (RESID 38 AND (NAME O OR NAME N OR       
REMARK   3                          NAME CA )) OR (RESID 39 AND (NAME O OR      
REMARK   3                          NAME N OR NAME C OR NAME CB )) OR (RESID    
REMARK   3                          40 AND (NAME O OR NAME N OR NAME C OR       
REMARK   3                          NAME CB OR NAME CG OR NAME CD1)) OR         
REMARK   3                          (RESID 41 AND (NAME O OR NAME N OR NAME C   
REMARK   3                          OR NAME CB OR NAME CG )) OR RESSEQ 47:155   
REMARK   3                          OR RESSEQ 157:210 OR RESSEQ 213:214 OR      
REMARK   3                          (RESID 217 AND (NAME O OR NAME N OR NAME    
REMARK   3                          C OR NAME CB OR NAME CG OR NAME CD1)) OR    
REMARK   3                          (RESID 219 AND (NAME O OR NAME N OR NAME    
REMARK   3                          C OR NAME CB OR NAME CG )) OR (RESID 221    
REMARK   3                          AND (NAME O OR NAME N OR NAME C OR NAME     
REMARK   3                          CB OR NAME CG OR NAME CD1)) OR (RESID 222   
REMARK   3                          AND (NAME O OR NAME N OR NAME C OR NAME     
REMARK   3                          CB OR NAME CG OR NAME CD OR NAME CE )) OR   
REMARK   3                          RESSEQ 227:228 OR RESSEQ 231:247 OR         
REMARK   3                          RESSEQ 249:254 OR RESSEQ 256:270 OR         
REMARK   3                          RESSEQ 272:273 OR (RESID 274 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME CB OR NAME CG OR NAME    
REMARK   3                          OD1 OR NAME OD2 OR NAME C OR NAME O )) OR   
REMARK   3                          (RESID 275 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME ND2 OR    
REMARK   3                          NAME C OR NAME O )) OR (RESID 281 AND       
REMARK   3                          (NAME N OR NAME CA OR NAME CB OR NAME CG    
REMARK   3                          OR NAME OD1 OR NAME OD2 OR NAME C OR NAME   
REMARK   3                          O )) OR (RESID 282 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME CB OR NAME CG OR NAME CD OR NAME    
REMARK   3                          OE1 OR NAME NE2 OR NAME C OR NAME O )) OR   
REMARK   3                          (RESID 283 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME OD1 OR NAME OD2 OR    
REMARK   3                          NAME C OR NAME O )) OR RESSEQ 284:337 OR    
REMARK   3                          (RESID 338 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          CB OR NAME CG OR NAME CD2 OR NAME C OR      
REMARK   3                          NAME O OR NAME H OR NAME HA OR NAME HB2     
REMARK   3                          OR NAME HB3 OR NAME HD2 OR NAME HE2 OR      
REMARK   3                          NAME HZ )) OR RESSEQ 339:365 OR RESSEQ      
REMARK   3                          367:383 OR (RESID 384 AND (NAME N OR NAME   
REMARK   3                          CA OR NAME CB OR NAME CG OR NAME CD2 OR     
REMARK   3                          NAME C OR NAME O OR NAME H OR NAME HA OR    
REMARK   3                          NAME HB2 OR NAME HB3 OR NAME HD2 OR NAME    
REMARK   3                          HE2 OR NAME HZ )) OR RESSEQ 385:410 OR      
REMARK   3                          RESSEQ 412:416 OR (RESID 417 AND (NAME N    
REMARK   3                          OR NAME CA OR NAME CB OR NAME CG OR NAME    
REMARK   3                          CD1 OR NAME C OR NAME O OR NAME H OR NAME   
REMARK   3                          HA OR NAME HB2 OR NAME HB3 OR NAME HD1 OR   
REMARK   3                          NAME HE1 OR NAME HZ )) OR RESSEQ 418:469    
REMARK   3                          OR (RESID 470 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME CB OR NAME CG OR NAME OD1 OR NAME C    
REMARK   3                          OR NAME O OR NAME H OR NAME HA OR NAME      
REMARK   3                          HB2 OR NAME HB3)) OR RESSEQ 471:504 OR      
REMARK   3                          RESSEQ 600:601))                            
REMARK   3     ATOM PAIRS NUMBER  : 10725                                       
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219336.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL, NON-FIXED-EXIT SLIT       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43069                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.098                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.441                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3SWZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE TRIHYDRATE,     
REMARK 280  PH 6.5, 200 MM AMMONIUM SULFATE, 30% W/V PEG8000, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.47700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.51750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.74950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.51750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.47700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.74950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     MET A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     ASN A   277                                                      
REMARK 465     ALA A   278                                                      
REMARK 465     GLU A   505                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     THR A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     HIS A   512                                                      
REMARK 465     MET B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     GLY B   276                                                      
REMARK 465     ASN B   277                                                      
REMARK 465     ALA B   278                                                      
REMARK 465     GLU B   505                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     THR B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     HIS B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     MET C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     LYS C    21                                                      
REMARK 465     LYS C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     LYS C    26                                                      
REMARK 465     TYR C    27                                                      
REMARK 465     PRO C    28                                                      
REMARK 465     LYS C    29                                                      
REMARK 465     GLU C   505                                                      
REMARK 465     GLY C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     THR C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     HIS C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     HIS C   512                                                      
REMARK 465     MET D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     TYR D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     GLY D   276                                                      
REMARK 465     ASN D   277                                                      
REMARK 465     ALA D   278                                                      
REMARK 465     GLU D   505                                                      
REMARK 465     GLY D   506                                                      
REMARK 465     SER D   507                                                      
REMARK 465     THR D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     HIS D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     HIS D   512                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA C   115    HH22  ARG C   440              1.47            
REMARK 500   O    GLY C   303     HG1  THR C   307              1.48            
REMARK 500   O    ALA D   115    HH22  ARG D   440              1.49            
REMARK 500   O    ALA B   115    HH22  ARG B   440              1.53            
REMARK 500   O    ALA A   115    HH22  ARG A   440              1.59            
REMARK 500   O    ALA A   302     OG1  THR A   306              1.95            
REMARK 500   O    GLY B   303     OG1  THR B   307              1.99            
REMARK 500   O    GLY C   303     OG1  THR C   307              2.08            
REMARK 500   O    ALA C   302     OG1  THR C   306              2.10            
REMARK 500   O    ALA B   302     OG1  THR B   306              2.19            
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    LEU A  32     -174.58    -61.29                                   
REMARK 500    PRO A  35      157.99    -49.11                                   
REMARK 500    ILE A  87      -71.67   -114.58                                   
REMARK 500    LYS A  89       40.32   -106.45                                   
REMARK 500    PHE A  93       62.77   -115.77                                   
REMARK 500    ASN A 108       71.05     59.87                                   
REMARK 500    ILE A 112      -68.94   -131.81                                   
REMARK 500    PHE A 135       47.93   -109.18                                   
REMARK 500    GLN A 140       41.78    -89.87                                   
REMARK 500    ASP A 212     -157.47   -150.39                                   
REMARK 500    LEU A 214       41.21    -73.74                                   
REMARK 500    ASP A 274       31.41    -85.13                                   
REMARK 500    PRO A 368       -6.01    -59.32                                   
REMARK 500    MET A 369       32.91   -140.66                                   
REMARK 500    LEU A 370     -151.91     51.90                                   
REMARK 500    SER A 379     -167.16   -165.04                                   
REMARK 500    LYS A 481     -155.61   -127.66                                   
REMARK 500    LYS B  89       41.20   -106.11                                   
REMARK 500    PHE B  93       63.67   -115.82                                   
REMARK 500    ASN B 108       73.53     60.85                                   
REMARK 500    ILE B 112      -68.01   -132.43                                   
REMARK 500    GLN B 140       41.30    -88.47                                   
REMARK 500    ASP B 212     -156.51   -149.23                                   
REMARK 500    LEU B 214       45.52    -75.33                                   
REMARK 500    ASP B 274       34.10    -84.71                                   
REMARK 500    MET B 369       32.48   -140.26                                   
REMARK 500    LEU B 370     -150.99     50.54                                   
REMARK 500    SER B 379     -168.28   -164.79                                   
REMARK 500    LYS B 481     -157.09   -126.71                                   
REMARK 500    PHE C  42       99.18    -30.70                                   
REMARK 500    ARG C  45      -72.64    -45.26                                   
REMARK 500    LYS C  89       43.38   -108.05                                   
REMARK 500    PHE C  93       62.62   -114.92                                   
REMARK 500    ASN C 108       71.41     59.46                                   
REMARK 500    ILE C 112      -66.56   -133.04                                   
REMARK 500    PHE C 135       46.93   -109.72                                   
REMARK 500    GLN C 140       42.26    -89.08                                   
REMARK 500    SER C 288      170.11    -59.98                                   
REMARK 500    MET C 369       33.33   -141.08                                   
REMARK 500    LEU C 370     -149.19     51.03                                   
REMARK 500    SER C 379     -168.60   -163.50                                   
REMARK 500    GLU C 383      -23.53    113.89                                   
REMARK 500    LYS C 481     -157.55   -127.84                                   
REMARK 500    LEU D  31      -35.82     84.69                                   
REMARK 500    PHE D  42       90.29    -31.69                                   
REMARK 500    HIS D  46       -2.90   -159.90                                   
REMARK 500    LYS D  89       42.75   -109.79                                   
REMARK 500    PHE D  93       61.87   -116.70                                   
REMARK 500    ILE D 112      -65.29   -132.40                                   
REMARK 500    PHE D 135       43.18   -108.48                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6D8 A 601   N27                                                    
REMARK 620 2 HEM A 600   NA   84.2                                              
REMARK 620 3 HEM A 600   NB   89.6  86.6                                        
REMARK 620 4 HEM A 600   NC   96.1 179.5  93.0                                  
REMARK 620 5 HEM A 600   ND   90.9  94.6 178.7  85.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6D8 B 601   N26                                                    
REMARK 620 2 HEM B 600   NA  105.1                                              
REMARK 620 3 HEM B 600   NB   83.9  88.0                                        
REMARK 620 4 HEM B 600   NC   79.3 175.5  91.7                                  
REMARK 620 5 HEM B 600   ND  100.2  92.0 175.7  88.0                            
REMARK 620 6 6D8 B 601   N27  28.6  79.5  95.5 105.0  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6D8 C 601   N27                                                    
REMARK 620 2 HEM C 600   NA   87.5                                              
REMARK 620 3 HEM C 600   NB   89.6  86.8                                        
REMARK 620 4 HEM C 600   NC   94.4 178.0  92.4                                  
REMARK 620 5 HEM C 600   ND   93.6  93.7 176.8  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 600  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 6D8 D 601   N26                                                    
REMARK 620 2 HEM D 600   NA  100.2                                              
REMARK 620 3 HEM D 600   NB   73.9  88.9                                        
REMARK 620 4 HEM D 600   NC   86.3 172.8  90.1                                  
REMARK 620 5 HEM D 600   ND  114.0  91.4 171.8  88.6                            
REMARK 620 6 6D8 D 601   N27  29.4  94.2 102.5  92.9  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6D8 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6D8 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6D8 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6D8 D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IRQ   RELATED DB: PDB                                   
DBREF  5IRV A   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  5IRV B   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  5IRV C   24   508  UNP    P05093   CP17A_HUMAN     24    508             
DBREF  5IRV D   24   508  UNP    P05093   CP17A_HUMAN     24    508             
SEQADV 5IRV MET A   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV ALA A   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS A   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS A   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV THR A   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS A  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS A  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS A  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS A  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV MET B   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV ALA B   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS B   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS B   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV THR B   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS B  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS B  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS B  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS B  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV MET C   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV ALA C   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS C   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS C   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV THR C   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS C  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS C  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS C  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS C  512  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV MET D   19  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV ALA D   20  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS D   21  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV LYS D   22  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV THR D   23  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS D  509  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS D  510  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS D  511  UNP  P05093              EXPRESSION TAG                 
SEQADV 5IRV HIS D  512  UNP  P05093              EXPRESSION TAG                 
SEQRES   1 A  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 A  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 A  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 A  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 A  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 A  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 A  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 A  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 A  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 A  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 A  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 A  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 A  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 A  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 A  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 A  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 A  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 A  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 A  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 A  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 A  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 A  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 A  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 A  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 A  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 A  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 A  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 A  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 A  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 A  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 A  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 A  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 A  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 A  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 A  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 A  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 A  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 A  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 B  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 B  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 B  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 B  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 B  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 B  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 B  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 B  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 B  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 B  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 B  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 B  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 B  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 B  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 B  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 B  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 B  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 B  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 B  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 B  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 B  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 B  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 B  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 B  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 B  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 B  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 B  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 B  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 B  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 B  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 B  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 B  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 B  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 B  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 B  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 B  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 B  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 B  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 C  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 C  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 C  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 C  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 C  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 C  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 C  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 C  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 C  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 C  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 C  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 C  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 C  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 C  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 C  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 C  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 C  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 C  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 C  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 C  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 C  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 C  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 C  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 C  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 C  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 C  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 C  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 C  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 C  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 C  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 C  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 C  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 C  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 C  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 C  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 C  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 C  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 C  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
SEQRES   1 D  494  MET ALA LYS LYS THR GLY ALA LYS TYR PRO LYS SER LEU          
SEQRES   2 D  494  LEU SER LEU PRO LEU VAL GLY SER LEU PRO PHE LEU PRO          
SEQRES   3 D  494  ARG HIS GLY HIS MET HIS ASN ASN PHE PHE LYS LEU GLN          
SEQRES   4 D  494  LYS LYS TYR GLY PRO ILE TYR SER VAL ARG MET GLY THR          
SEQRES   5 D  494  LYS THR THR VAL ILE VAL GLY HIS HIS GLN LEU ALA LYS          
SEQRES   6 D  494  GLU VAL LEU ILE LYS LYS GLY LYS ASP PHE SER GLY ARG          
SEQRES   7 D  494  PRO GLN MET ALA THR LEU ASP ILE ALA SER ASN ASN ARG          
SEQRES   8 D  494  LYS GLY ILE ALA PHE ALA ASP SER GLY ALA HIS TRP GLN          
SEQRES   9 D  494  LEU HIS ARG ARG LEU ALA MET ALA THR PHE ALA LEU PHE          
SEQRES  10 D  494  LYS ASP GLY ASP GLN LYS LEU GLU LYS ILE ILE CYS GLN          
SEQRES  11 D  494  GLU ILE SER THR LEU CYS ASP MET LEU ALA THR HIS ASN          
SEQRES  12 D  494  GLY GLN SER ILE ASP ILE SER PHE PRO VAL PHE VAL ALA          
SEQRES  13 D  494  VAL THR ASN VAL ILE SER LEU ILE CYS PHE ASN THR SER          
SEQRES  14 D  494  TYR LYS ASN GLY ASP PRO GLU LEU ASN VAL ILE GLN ASN          
SEQRES  15 D  494  TYR ASN GLU GLY ILE ILE ASP ASN LEU SER LYS ASP SER          
SEQRES  16 D  494  LEU VAL ASP LEU VAL PRO TRP LEU LYS ILE PHE PRO ASN          
SEQRES  17 D  494  LYS THR LEU GLU LYS LEU LYS SER HIS VAL LYS ILE ARG          
SEQRES  18 D  494  ASN ASP LEU LEU ASN LYS ILE LEU GLU ASN TYR LYS GLU          
SEQRES  19 D  494  LYS PHE ARG SER ASP SER ILE THR ASN MET LEU ASP THR          
SEQRES  20 D  494  LEU MET GLN ALA LYS MET ASN SER ASP ASN GLY ASN ALA          
SEQRES  21 D  494  GLY PRO ASP GLN ASP SER GLU LEU LEU SER ASP ASN HIS          
SEQRES  22 D  494  ILE LEU THR THR ILE GLY ASP ILE PHE GLY ALA GLY VAL          
SEQRES  23 D  494  GLU THR THR THR SER VAL VAL LYS TRP THR LEU ALA PHE          
SEQRES  24 D  494  LEU LEU HIS ASN PRO GLN VAL LYS LYS LYS LEU TYR GLU          
SEQRES  25 D  494  GLU ILE ASP GLN ASN VAL GLY PHE SER ARG THR PRO THR          
SEQRES  26 D  494  ILE SER ASP ARG ASN ARG LEU LEU LEU LEU GLU ALA THR          
SEQRES  27 D  494  ILE ARG GLU VAL LEU ARG LEU ARG PRO VAL ALA PRO MET          
SEQRES  28 D  494  LEU ILE PRO HIS LYS ALA ASN VAL ASP SER SER ILE GLY          
SEQRES  29 D  494  GLU PHE ALA VAL ASP LYS GLY THR GLU VAL ILE ILE ASN          
SEQRES  30 D  494  LEU TRP ALA LEU HIS HIS ASN GLU LYS GLU TRP HIS GLN          
SEQRES  31 D  494  PRO ASP GLN PHE MET PRO GLU ARG PHE LEU ASN PRO ALA          
SEQRES  32 D  494  GLY THR GLN LEU ILE SER PRO SER VAL SER TYR LEU PRO          
SEQRES  33 D  494  PHE GLY ALA GLY PRO ARG SER CYS ILE GLY GLU ILE LEU          
SEQRES  34 D  494  ALA ARG GLN GLU LEU PHE LEU ILE MET ALA TRP LEU LEU          
SEQRES  35 D  494  GLN ARG PHE ASP LEU GLU VAL PRO ASP ASP GLY GLN LEU          
SEQRES  36 D  494  PRO SER LEU GLU GLY ILE PRO LYS VAL VAL PHE LEU ILE          
SEQRES  37 D  494  ASP SER PHE LYS VAL LYS ILE LYS VAL ARG GLN ALA TRP          
SEQRES  38 D  494  ARG GLU ALA GLN ALA GLU GLY SER THR HIS HIS HIS HIS          
HET    HEM  A 600      73                                                       
HET    6D8  A 601      45                                                       
HET    HEM  B 600      73                                                       
HET    6D8  B 601      45                                                       
HET    HEM  C 600      73                                                       
HET    6D8  C 601      45                                                       
HET    HEM  D 600      73                                                       
HET    6D8  D 601      45                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     6D8 VT-464                                                           
HETSYN     HEM HEME                                                             
HETSYN     6D8 (1S)-1-[6,7-BIS(DIFLUOROMETHOXY)NAPHTHALEN-2-YL]-2-              
HETSYN   2 6D8  METHYL-1-(2H-1,2,3-TRIAZOL-4-YL)PROPAN-1-OL                     
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  6D8    4(C18 H17 F4 N3 O3)                                          
HELIX    1 AA1 HIS A   48  LEU A   56  1                                   9    
HELIX    2 AA2 LEU A   56  GLY A   61  1                                   6    
HELIX    3 AA3 HIS A   78  ILE A   87  1                                  10    
HELIX    4 AA4 MET A   99  SER A  106  1                                   8    
HELIX    5 AA5 GLY A  118  LEU A  134  1                                  17    
HELIX    6 AA6 LYS A  141  THR A  159  1                                  19    
HELIX    7 AA7 ILE A  167  PHE A  184  1                                  18    
HELIX    8 AA8 ASP A  192  SER A  210  1                                  19    
HELIX    9 AA9 PRO A  219  PHE A  224  1                                   6    
HELIX   10 AB1 LYS A  227  PHE A  254  1                                  28    
HELIX   11 AB2 ASN A  261  ASP A  274  1                                  14    
HELIX   12 AB3 SER A  284  LEU A  287  5                                   4    
HELIX   13 AB4 SER A  288  ASN A  321  1                                  34    
HELIX   14 AB5 ASN A  321  VAL A  336  1                                  16    
HELIX   15 AB6 THR A  343  ARG A  349  5                                   7    
HELIX   16 AB7 LEU A  350  ARG A  364  1                                  15    
HELIX   17 AB8 ASN A  395  HIS A  401  1                                   7    
HELIX   18 AB9 MET A  413  LEU A  418  5                                   6    
HELIX   19 AC1 ALA A  437  SER A  441  5                                   5    
HELIX   20 AC2 GLY A  444  ARG A  462  1                                  19    
HELIX   21 AC3 ARG A  496  ALA A  502  1                                   7    
HELIX   22 AC4 HIS B   48  LEU B   56  1                                   9    
HELIX   23 AC5 LEU B   56  GLY B   61  1                                   6    
HELIX   24 AC6 HIS B   78  ILE B   87  1                                  10    
HELIX   25 AC7 MET B   99  SER B  106  1                                   8    
HELIX   26 AC8 GLY B  118  LEU B  134  1                                  17    
HELIX   27 AC9 LYS B  141  THR B  159  1                                  19    
HELIX   28 AD1 ILE B  167  PHE B  184  1                                  18    
HELIX   29 AD2 ASP B  192  SER B  210  1                                  19    
HELIX   30 AD3 PRO B  219  PHE B  224  1                                   6    
HELIX   31 AD4 LYS B  227  PHE B  254  1                                  28    
HELIX   32 AD5 ASN B  261  ASP B  274  1                                  14    
HELIX   33 AD6 ASP B  281  LEU B  287  5                                   7    
HELIX   34 AD7 SER B  288  ASN B  321  1                                  34    
HELIX   35 AD8 ASN B  321  VAL B  336  1                                  16    
HELIX   36 AD9 THR B  343  ASN B  348  5                                   6    
HELIX   37 AE1 LEU B  350  ARG B  364  1                                  15    
HELIX   38 AE2 ASN B  395  HIS B  401  1                                   7    
HELIX   39 AE3 MET B  413  LEU B  418  5                                   6    
HELIX   40 AE4 ALA B  437  SER B  441  5                                   5    
HELIX   41 AE5 GLY B  444  ARG B  462  1                                  19    
HELIX   42 AE6 ARG B  496  ALA B  502  1                                   7    
HELIX   43 AE7 HIS C   48  LEU C   56  1                                   9    
HELIX   44 AE8 LEU C   56  GLY C   61  1                                   6    
HELIX   45 AE9 HIS C   78  ILE C   87  1                                  10    
HELIX   46 AF1 MET C   99  SER C  106  1                                   8    
HELIX   47 AF2 GLY C  118  LEU C  134  1                                  17    
HELIX   48 AF3 LYS C  141  THR C  159  1                                  19    
HELIX   49 AF4 ILE C  167  PHE C  184  1                                  18    
HELIX   50 AF5 PRO C  193  SER C  210  1                                  18    
HELIX   51 AF6 LYS C  227  PHE C  254  1                                  28    
HELIX   52 AF7 ASN C  261  ASN C  275  1                                  15    
HELIX   53 AF8 SER C  284  LEU C  287  5                                   4    
HELIX   54 AF9 SER C  288  ASN C  321  1                                  34    
HELIX   55 AG1 ASN C  321  VAL C  336  1                                  16    
HELIX   56 AG2 THR C  343  ASN C  348  5                                   6    
HELIX   57 AG3 LEU C  350  ARG C  364  1                                  15    
HELIX   58 AG4 ASN C  395  ASN C  402  1                                   8    
HELIX   59 AG5 MET C  413  LEU C  418  5                                   6    
HELIX   60 AG6 ALA C  437  SER C  441  5                                   5    
HELIX   61 AG7 GLY C  444  ARG C  462  1                                  19    
HELIX   62 AG8 ARG C  496  ALA C  502  1                                   7    
HELIX   63 AG9 HIS D   48  LEU D   56  1                                   9    
HELIX   64 AH1 LEU D   56  GLY D   61  1                                   6    
HELIX   65 AH2 HIS D   78  ILE D   87  1                                  10    
HELIX   66 AH3 MET D   99  SER D  106  1                                   8    
HELIX   67 AH4 GLY D  118  LEU D  134  1                                  17    
HELIX   68 AH5 LYS D  141  THR D  159  1                                  19    
HELIX   69 AH6 ILE D  167  PHE D  184  1                                  18    
HELIX   70 AH7 ASP D  192  SER D  210  1                                  19    
HELIX   71 AH8 LYS D  227  PHE D  254  1                                  28    
HELIX   72 AH9 ASN D  261  ASP D  274  1                                  14    
HELIX   73 AI1 ASP D  281  GLU D  285  5                                   5    
HELIX   74 AI2 SER D  288  ASN D  321  1                                  34    
HELIX   75 AI3 ASN D  321  VAL D  336  1                                  16    
HELIX   76 AI4 THR D  343  ARG D  349  5                                   7    
HELIX   77 AI5 LEU D  350  ARG D  364  1                                  15    
HELIX   78 AI6 ASN D  395  HIS D  401  1                                   7    
HELIX   79 AI7 MET D  413  LEU D  418  5                                   6    
HELIX   80 AI8 ALA D  437  SER D  441  5                                   5    
HELIX   81 AI9 GLY D  444  ARG D  462  1                                  19    
HELIX   82 AJ1 ARG D  496  ALA D  502  1                                   7    
SHEET    1 AA1 5 LEU A  36  LEU A  40  0                                        
SHEET    2 AA1 5 ILE C  63  MET C  68  1  O  ARG C  67   N  LEU A  40           
SHEET    3 AA1 5 LYS C  71  VAL C  76 -1  O  ILE C  75   N  TYR C  64           
SHEET    4 AA1 5 GLU C 391  ILE C 394  1  O  GLU C 391   N  VAL C  74           
SHEET    5 AA1 5 HIS C 373  LYS C 374 -1  N  HIS C 373   O  VAL C 392           
SHEET    1 AA2 5 HIS A 373  LYS A 374  0                                        
SHEET    2 AA2 5 GLU A 391  ILE A 394 -1  O  VAL A 392   N  HIS A 373           
SHEET    3 AA2 5 LYS A  71  VAL A  76  1  N  VAL A  76   O  ILE A 393           
SHEET    4 AA2 5 ILE A  63  MET A  68 -1  N  TYR A  64   O  ILE A  75           
SHEET    5 AA2 5 LEU C  36  LEU C  40  1  O  GLY C  38   N  ARG A  67           
SHEET    1 AA3 3 GLN A 163  ILE A 165  0                                        
SHEET    2 AA3 3 VAL A 491  VAL A 495 -1  O  VAL A 491   N  ILE A 165           
SHEET    3 AA3 3 PHE A 463  GLU A 466 -1  N  ASP A 464   O  LYS A 494           
SHEET    1 AA4 2 SER A 379  ILE A 381  0                                        
SHEET    2 AA4 2 PHE A 384  VAL A 386 -1  O  VAL A 386   N  SER A 379           
SHEET    1 AA5 2 ILE A 479  PRO A 480  0                                        
SHEET    2 AA5 2 PHE A 484  LEU A 485 -1  O  LEU A 485   N  ILE A 479           
SHEET    1 AA6 5 LEU B  36  LEU B  40  0                                        
SHEET    2 AA6 5 ILE D  63  MET D  68  1  O  ARG D  67   N  LEU B  40           
SHEET    3 AA6 5 LYS D  71  VAL D  76 -1  O  ILE D  75   N  TYR D  64           
SHEET    4 AA6 5 GLU D 391  ILE D 394  1  O  GLU D 391   N  VAL D  74           
SHEET    5 AA6 5 HIS D 373  LYS D 374 -1  N  HIS D 373   O  VAL D 392           
SHEET    1 AA7 5 HIS B 373  LYS B 374  0                                        
SHEET    2 AA7 5 GLU B 391  ILE B 394 -1  O  VAL B 392   N  HIS B 373           
SHEET    3 AA7 5 LYS B  71  VAL B  76  1  N  VAL B  74   O  GLU B 391           
SHEET    4 AA7 5 ILE B  63  MET B  68 -1  N  TYR B  64   O  ILE B  75           
SHEET    5 AA7 5 LEU D  36  LEU D  40  1  O  VAL D  37   N  SER B  65           
SHEET    1 AA8 3 GLN B 163  ILE B 165  0                                        
SHEET    2 AA8 3 VAL B 491  VAL B 495 -1  O  VAL B 491   N  ILE B 165           
SHEET    3 AA8 3 PHE B 463  GLU B 466 -1  N  ASP B 464   O  LYS B 494           
SHEET    1 AA9 2 SER B 379  ILE B 381  0                                        
SHEET    2 AA9 2 PHE B 384  VAL B 386 -1  O  VAL B 386   N  SER B 379           
SHEET    1 AB1 2 ILE B 479  PRO B 480  0                                        
SHEET    2 AB1 2 PHE B 484  LEU B 485 -1  O  LEU B 485   N  ILE B 479           
SHEET    1 AB2 3 GLN C 163  ILE C 165  0                                        
SHEET    2 AB2 3 VAL C 491  VAL C 495 -1  O  VAL C 491   N  ILE C 165           
SHEET    3 AB2 3 PHE C 463  GLU C 466 -1  N  ASP C 464   O  LYS C 494           
SHEET    1 AB3 2 SER C 379  ILE C 381  0                                        
SHEET    2 AB3 2 PHE C 384  VAL C 386 -1  O  VAL C 386   N  SER C 379           
SHEET    1 AB4 2 ILE C 479  PRO C 480  0                                        
SHEET    2 AB4 2 PHE C 484  LEU C 485 -1  O  LEU C 485   N  ILE C 479           
SHEET    1 AB5 3 GLN D 163  ILE D 165  0                                        
SHEET    2 AB5 3 VAL D 491  VAL D 495 -1  O  VAL D 491   N  ILE D 165           
SHEET    3 AB5 3 PHE D 463  GLU D 466 -1  N  ASP D 464   O  LYS D 494           
SHEET    1 AB6 2 SER D 379  ILE D 381  0                                        
SHEET    2 AB6 2 PHE D 384  VAL D 386 -1  O  VAL D 386   N  SER D 379           
SHEET    1 AB7 2 ILE D 479  PRO D 480  0                                        
SHEET    2 AB7 2 PHE D 484  LEU D 485 -1  O  LEU D 485   N  ILE D 479           
LINK        FE   HEM A 600                 N27 6D8 A 601     1555   1555  2.23  
LINK        FE   HEM B 600                 N26 6D8 B 601     1555   1555  2.77  
LINK        FE   HEM B 600                 N27 6D8 B 601     1555   1555  2.09  
LINK        FE   HEM C 600                 N27 6D8 C 601     1555   1555  2.14  
LINK        FE   HEM D 600                 N26 6D8 D 601     1555   1555  2.74  
LINK        FE   HEM D 600                 N27 6D8 D 601     1555   1555  2.14  
SITE     1 AC1 17 ARG A  96  ILE A 112  ALA A 113  TRP A 121                    
SITE     2 AC1 17 ARG A 125  ILE A 299  GLY A 303  THR A 307                    
SITE     3 AC1 17 ILE A 371  HIS A 373  PRO A 434  PHE A 435                    
SITE     4 AC1 17 ARG A 440  CYS A 442  ILE A 443  ALA A 448                    
SITE     5 AC1 17 6D8 A 601                                                     
SITE     1 AC2 15 ALA A 105  ASN A 202  ILE A 205  ILE A 206                    
SITE     2 AC2 15 ARG A 239  ASP A 298  GLY A 301  ALA A 302                    
SITE     3 AC2 15 GLU A 305  THR A 306  ALA A 367  ILE A 371                    
SITE     4 AC2 15 VAL A 482  VAL A 483  HEM A 600                               
SITE     1 AC3 18 ARG B  96  ILE B 112  ALA B 113  TRP B 121                    
SITE     2 AC3 18 ARG B 125  GLY B 303  LEU B 361  VAL B 366                    
SITE     3 AC3 18 LEU B 370  ILE B 371  HIS B 373  PRO B 434                    
SITE     4 AC3 18 PHE B 435  ARG B 440  CYS B 442  ALA B 448                    
SITE     5 AC3 18 LEU B 452  6D8 B 601                                          
SITE     1 AC4 14 ALA B 105  PHE B 114  ASN B 202  ILE B 205                    
SITE     2 AC4 14 ILE B 206  ARG B 239  GLY B 301  ALA B 302                    
SITE     3 AC4 14 GLU B 305  THR B 306  ALA B 367  ILE B 371                    
SITE     4 AC4 14 VAL B 482  HEM B 600                                          
SITE     1 AC5 19 ARG C  96  ILE C 112  ALA C 113  TRP C 121                    
SITE     2 AC5 19 ARG C 125  ILE C 299  GLY C 303  VAL C 310                    
SITE     3 AC5 19 VAL C 366  ALA C 367  LEU C 370  ILE C 371                    
SITE     4 AC5 19 HIS C 373  PRO C 434  PHE C 435  ARG C 440                    
SITE     5 AC5 19 CYS C 442  ALA C 448  6D8 C 601                               
SITE     1 AC6 14 ALA C 105  PHE C 114  ASN C 202  ILE C 205                    
SITE     2 AC6 14 ILE C 206  ARG C 239  ASP C 298  ALA C 302                    
SITE     3 AC6 14 THR C 306  ALA C 367  ILE C 371  VAL C 482                    
SITE     4 AC6 14 VAL C 483  HEM C 600                                          
SITE     1 AC7 19 ARG D  96  ILE D 112  ALA D 113  TRP D 121                    
SITE     2 AC7 19 ARG D 125  ILE D 299  GLY D 303  THR D 306                    
SITE     3 AC7 19 THR D 307  VAL D 310  VAL D 366  LEU D 370                    
SITE     4 AC7 19 HIS D 373  PRO D 434  PHE D 435  ARG D 440                    
SITE     5 AC7 19 CYS D 442  ALA D 448  6D8 D 601                               
SITE     1 AC8 14 ALA D 105  ASN D 202  ILE D 205  ILE D 206                    
SITE     2 AC8 14 ARG D 239  GLY D 297  ASP D 298  GLY D 301                    
SITE     3 AC8 14 ALA D 302  THR D 306  ILE D 371  VAL D 482                    
SITE     4 AC8 14 VAL D 483  HEM D 600                                          
CRYST1   90.954  153.499  169.035  90.00  90.00  90.00 P 21 21 21   16          
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      0.010995  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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