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Database: PDB
Entry: 5NI4
LinkDB: 5NI4
Original site: 5NI4 
HEADER    HYDROLASE                               23-MAR-17   5NI4              
TITLE     CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT E271A IN COMPLEX WITH LTA4    
TITLE    2 (CRYSTAL FORM II)                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT3MB4                                    
KEYWDS    METALLOPEPTIDASE, EPOXIDE HYDROLASE, LEUKOTRIENE A4, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA                                                         
REVDAT   3   13-SEP-17 5NI4    1       JRNL                                     
REVDAT   2   06-SEP-17 5NI4    1       JRNL                                     
REVDAT   1   23-AUG-17 5NI4    0                                                
JRNL        AUTH   A.STSIAPANAVA,B.SAMUELSSON,J.Z.HAEGGSTROM                    
JRNL        TITL   CAPTURING LTA4 HYDROLASE IN ACTION: INSIGHTS TO THE          
JRNL        TITL 2 CHEMISTRY AND DYNAMICS OF CHEMOTACTIC LTB4 SYNTHESIS.        
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114  9689 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28827365                                                     
JRNL        DOI    10.1073/PNAS.1710850114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 152057                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.330                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8107                            
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 49.8242 -  5.8856    1.00     4787   272  0.1649 0.1757        
REMARK   3     2  5.8856 -  4.6727    1.00     4815   256  0.1185 0.1537        
REMARK   3     3  4.6727 -  4.0823    1.00     4812   248  0.1099 0.1416        
REMARK   3     4  4.0823 -  3.7092    1.00     4838   279  0.1298 0.1492        
REMARK   3     5  3.7092 -  3.4434    1.00     4746   285  0.1345 0.1854        
REMARK   3     6  3.4434 -  3.2404    1.00     4791   285  0.1405 0.1719        
REMARK   3     7  3.2404 -  3.0782    1.00     4808   276  0.1436 0.1849        
REMARK   3     8  3.0782 -  2.9442    1.00     4774   258  0.1476 0.2003        
REMARK   3     9  2.9442 -  2.8309    1.00     4822   295  0.1451 0.1931        
REMARK   3    10  2.8309 -  2.7332    1.00     4750   269  0.1461 0.1929        
REMARK   3    11  2.7332 -  2.6477    1.00     4852   257  0.1462 0.1974        
REMARK   3    12  2.6477 -  2.5721    1.00     4775   291  0.1502 0.2018        
REMARK   3    13  2.5721 -  2.5043    1.00     4792   268  0.1641 0.2028        
REMARK   3    14  2.5043 -  2.4433    1.00     4836   260  0.1664 0.2207        
REMARK   3    15  2.4433 -  2.3877    1.00     4788   264  0.1687 0.2169        
REMARK   3    16  2.3877 -  2.3369    1.00     4789   272  0.1729 0.2166        
REMARK   3    17  2.3369 -  2.2902    1.00     4806   279  0.1769 0.2157        
REMARK   3    18  2.2902 -  2.2469    1.00     4777   254  0.2050 0.2688        
REMARK   3    19  2.2469 -  2.2068    1.00     4823   281  0.2106 0.2538        
REMARK   3    20  2.2068 -  2.1694    1.00     4802   246  0.2080 0.2623        
REMARK   3    21  2.1694 -  2.1344    1.00     4828   282  0.2091 0.2396        
REMARK   3    22  2.1344 -  2.1016    1.00     4794   272  0.2159 0.2740        
REMARK   3    23  2.1016 -  2.0707    1.00     4849   275  0.2274 0.2682        
REMARK   3    24  2.0707 -  2.0415    1.00     4747   263  0.2340 0.2531        
REMARK   3    25  2.0415 -  2.0139    1.00     4835   266  0.2392 0.2543        
REMARK   3    26  2.0139 -  1.9877    1.00     4709   272  0.2483 0.3054        
REMARK   3    27  1.9877 -  1.9629    1.00     4800   280  0.2682 0.3185        
REMARK   3    28  1.9629 -  1.9392    1.00     4795   264  0.2815 0.3302        
REMARK   3    29  1.9392 -  1.9167    1.00     4821   272  0.3116 0.3484        
REMARK   3    30  1.9167 -  1.8952    0.99     4789   266  0.3231 0.3642        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          15519                                  
REMARK   3   ANGLE     :  0.844          21095                                  
REMARK   3   CHIRALITY :  0.048           2339                                  
REMARK   3   PLANARITY :  0.005           2709                                  
REMARK   3   DIHEDRAL  : 17.503           5847                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 3:209                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0169  21.8693 -11.1124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2470 T22:   0.1825                                     
REMARK   3      T33:   0.2253 T12:  -0.0204                                     
REMARK   3      T13:   0.0041 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2170 L22:   0.4398                                     
REMARK   3      L33:   0.4534 L12:  -0.0337                                     
REMARK   3      L13:  -0.0789 L23:  -0.0461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:   0.0510 S13:  -0.0021                       
REMARK   3      S21:  -0.1204 S22:   0.0144 S23:  -0.0412                       
REMARK   3      S31:  -0.1332 S32:   0.0688 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 210:465                               
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5836  13.1460   9.8759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1770 T22:   0.1674                                     
REMARK   3      T33:   0.2098 T12:   0.0084                                     
REMARK   3      T13:   0.0006 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4042 L22:   0.2467                                     
REMARK   3      L33:   0.4807 L12:  -0.0639                                     
REMARK   3      L13:  -0.0320 L23:   0.1754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0006 S12:  -0.0171 S13:  -0.0186                       
REMARK   3      S21:   0.0395 S22:  -0.0227 S23:   0.0270                       
REMARK   3      S31:   0.0006 S32:  -0.0603 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9941  31.0275  27.6865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2936 T22:   0.2016                                     
REMARK   3      T33:   0.2154 T12:   0.0359                                     
REMARK   3      T13:   0.0033 T23:  -0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1596 L22:   0.4988                                     
REMARK   3      L33:   0.3968 L12:  -0.0159                                     
REMARK   3      L13:  -0.0354 L23:   0.3609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:  -0.1131 S13:   0.0279                       
REMARK   3      S21:   0.1138 S22:   0.0735 S23:   0.0428                       
REMARK   3      S31:  -0.2010 S32:   0.0281 S33:   0.0016                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 2:209                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5153  64.7706  -5.4531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1688 T22:   0.2067                                     
REMARK   3      T33:   0.2000 T12:   0.0427                                     
REMARK   3      T13:   0.0048 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3622 L22:   0.3234                                     
REMARK   3      L33:   0.4750 L12:  -0.1597                                     
REMARK   3      L13:   0.2478 L23:  -0.1868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:  -0.1310 S13:   0.0282                       
REMARK   3      S21:  -0.0180 S22:   0.0141 S23:  -0.0423                       
REMARK   3      S31:   0.0761 S32:   0.0393 S33:   0.0016                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 210:465                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7776  59.7246 -26.5050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2388 T22:   0.1709                                     
REMARK   3      T33:   0.1900 T12:  -0.0090                                     
REMARK   3      T13:   0.0008 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1784 L22:   0.2364                                     
REMARK   3      L33:   0.3958 L12:   0.0841                                     
REMARK   3      L13:  -0.1348 L23:  -0.1349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0023 S12:   0.0005 S13:   0.0237                       
REMARK   3      S21:  -0.0581 S22:  -0.0092 S23:  -0.0135                       
REMARK   3      S31:   0.1141 S32:  -0.0350 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4305  53.2137 -44.4656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4164 T22:   0.2231                                     
REMARK   3      T33:   0.2474 T12:   0.0563                                     
REMARK   3      T13:   0.0740 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3839 L22:   0.3028                                     
REMARK   3      L33:   0.2273 L12:  -0.0874                                     
REMARK   3      L13:  -0.1199 L23:  -0.0797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0632 S12:   0.0564 S13:  -0.0395                       
REMARK   3      S21:  -0.1900 S22:   0.0081 S23:  -0.0701                       
REMARK   3      S31:   0.1691 S32:   0.0498 S33:  -0.0006                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 2:209                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7741  59.5234 -19.9433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2495 T22:   0.1934                                     
REMARK   3      T33:   0.1980 T12:   0.0158                                     
REMARK   3      T13:  -0.0071 T23:   0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5390 L22:   0.3848                                     
REMARK   3      L33:   0.3273 L12:  -0.1315                                     
REMARK   3      L13:  -0.0803 L23:  -0.2511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0018 S12:   0.1477 S13:   0.0408                       
REMARK   3      S21:  -0.0871 S22:   0.0023 S23:  -0.0128                       
REMARK   3      S31:  -0.0793 S32:  -0.0160 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 210:465                               
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4598  44.1792   0.8624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1740 T22:   0.1896                                     
REMARK   3      T33:   0.1923 T12:   0.0185                                     
REMARK   3      T13:  -0.0019 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5231 L22:   0.1181                                     
REMARK   3      L33:   0.4289 L12:   0.0504                                     
REMARK   3      L13:   0.1162 L23:   0.0383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0195 S12:  -0.0527 S13:  -0.0417                       
REMARK   3      S21:   0.0121 S22:   0.0227 S23:   0.0113                       
REMARK   3      S31:  -0.0268 S32:  -0.0486 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN C AND RESI 466:609                               
REMARK   3    ORIGIN FOR THE GROUP (A):  47.6673  63.5141  18.6823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3077 T22:   0.3532                                     
REMARK   3      T33:   0.2139 T12:   0.1136                                     
REMARK   3      T13:  -0.0021 T23:  -0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4592 L22:   0.2993                                     
REMARK   3      L33:   0.4763 L12:  -0.1713                                     
REMARK   3      L13:  -0.1610 L23:   0.1959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0422 S12:  -0.2523 S13:   0.1112                       
REMARK   3      S21:   0.0540 S22:   0.0799 S23:  -0.0369                       
REMARK   3      S31:  -0.1954 S32:  -0.1996 S33:   0.0659                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NI4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004019.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 152082                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.895                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.18850                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.60900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.930                              
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: 5NI2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% (W/V) PEG 20 000, 15% (W/V) PEG MME   
REMARK 280  550, 100 MM MES/IMIDAZOLE PH 6.9, 20 MM OF EACH ALCOHOL (1,6-       
REMARK 280  HEXANEDIOL, 1-BUTANOL, (RS)-1,2-PROPANEDIOL, 2-PROPANOL, 1,4-       
REMARK 280  BUTANEDIOL, 1,3-PROPANEDIOL), VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.63333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.31667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 68900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A   610                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     ASP B   610                                                      
REMARK 465     MET C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     ASP C   610                                                      
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    HOH B   844     O    HOH B  1489              2.08            
REMARK 500   O    HOH A  1023     O    HOH A  1335              2.08            
REMARK 500   O    HOH B  1177     O    HOH B  1436              2.12            
REMARK 500   O    HOH B   907     O    HOH B  1380              2.12            
REMARK 500   O    HOH B  1360     O    HOH B  1387              2.13            
REMARK 500   O    HOH C   989     O    HOH C  1069              2.13            
REMARK 500   CAH  DJ3 A   705     O    HOH A   801              2.14            
REMARK 500   O    HOH A   813     O    HOH A  1110              2.14            
REMARK 500   O    HOH C   884     O    HOH C  1230              2.15            
REMARK 500   O    HOH C  1336     O    HOH C  1440              2.16            
REMARK 500   O    HOH C   812     O    HOH C   908              2.16            
REMARK 500   O    HOH A  1252     O    HOH A  1371              2.16            
REMARK 500   O    HOH A  1184     O    HOH A  1290              2.16            
REMARK 500   O    HOH A  1447     O    HOH A  1467              2.16            
REMARK 500   O    HOH C  1089     O    HOH C  1292              2.17            
REMARK 500   OE1  GLU B   412     O    HOH B   802              2.17            
REMARK 500   CAH  DJ3 A   705     O    HOH A   801              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   HZ3  LYS C   518     O    HOH B   813     2665     1.59            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  79       68.20   -119.85                                   
REMARK 500    SER A  80     -121.40     38.36                                   
REMARK 500    ASN A  97       -5.54     83.09                                   
REMARK 500    LYS A 126       -3.01     72.94                                   
REMARK 500    SER A 222     -177.12   -170.23                                   
REMARK 500    CYS A 274      -11.17     74.02                                   
REMARK 500    LEU A 275       82.30   -153.80                                   
REMARK 500    PHE A 432       52.07   -101.23                                   
REMARK 500    LYS A 546       31.66     72.58                                   
REMARK 500    LYS A 546       30.94     73.18                                   
REMARK 500    GLN B  79       71.04   -112.62                                   
REMARK 500    SER B  80     -117.61     38.28                                   
REMARK 500    ASN B  97       -6.08     79.89                                   
REMARK 500    LYS B 126       -1.37     70.38                                   
REMARK 500    ASP B 183      103.50   -162.90                                   
REMARK 500    CYS B 274       -8.93     77.42                                   
REMARK 500    LEU B 275       80.47   -157.17                                   
REMARK 500    PHE B 432       49.82   -100.74                                   
REMARK 500    GLN C  79       62.28   -113.48                                   
REMARK 500    SER C  80     -129.39     51.94                                   
REMARK 500    SER C  80     -129.55     52.30                                   
REMARK 500    ASN C  97       -7.70     83.29                                   
REMARK 500    ASP C 183      107.81   -163.10                                   
REMARK 500    SER C 222     -179.30   -170.39                                   
REMARK 500    CYS C 274       -9.44     75.23                                   
REMARK 500    LEU C 275       83.00   -156.45                                   
REMARK 500    TRP C 301      -60.55   -109.90                                   
REMARK 500    PHE C 432       42.41   -100.53                                   
REMARK 500    LYS C 546       38.02     71.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1475        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH B1518        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH B1519        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B1520        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B1521        DISTANCE =  6.31 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH B   801                                                      
REMARK 615     HOH B   895                                                      
REMARK 615     HOH C   801                                                      
REMARK 615     HOH C   832                                                      
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                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 103.4                                              
REMARK 620 3 GLU A 318   OE1  95.4 107.5                                        
REMARK 620 4 GLU A 318   OE2 151.8  89.0  56.5                                  
REMARK 620 5 DJ3 A 705   OAT  94.9 133.6 112.8  94.4                            
REMARK 620 6 DJ3 A 705   OAT  95.4 137.1 108.6  92.1   4.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 295   NE2                                                    
REMARK 620 2 HIS B 299   NE2  97.3                                              
REMARK 620 3 GLU B 318   OE1  96.8 106.3                                        
REMARK 620 4 GLU B 318   OE2 151.5  90.4  54.7                                  
REMARK 620 5 DJ3 B 705   OAT  98.6 132.6 115.7  96.2                            
REMARK 620 6 DJ3 B 705   OAT 103.1 129.2 116.7  93.0   4.9                      
REMARK 620 7 HOH B 808   O    83.5  78.0 175.6 125.0  59.9  59.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 295   NE2                                                    
REMARK 620 2 HIS C 299   NE2  99.1                                              
REMARK 620 3 GLU C 318   OE1  95.3 105.2                                        
REMARK 620 4 GLU C 318   OE2 150.5  88.5  55.2                                  
REMARK 620 5 DJ3 C 703   OAT  97.4 142.1 107.0  93.6                            
REMARK 620 6 DJ3 C 703   OAT  97.3 140.7 108.6  94.5   1.7                      
REMARK 620 7 HOH C 805   O    89.6  87.6 165.3 119.3  58.6  56.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 C 703                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MS6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DPR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NI2   RELATED DB: PDB                                   
DBREF  5NI4 A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
DBREF  5NI4 B    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
DBREF  5NI4 C    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 5NI4 MET A   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NI4 HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 ALA A  271  UNP  P09960    GLU   272 ENGINEERED MUTATION            
SEQADV 5NI4 MET B   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NI4 HIS B   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS B   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS B   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS B   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS B   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS B    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 ALA B  271  UNP  P09960    GLU   272 ENGINEERED MUTATION            
SEQADV 5NI4 MET C   -6  UNP  P09960              INITIATING METHIONINE          
SEQADV 5NI4 HIS C   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS C   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS C   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS C   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS C   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 HIS C    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 5NI4 ALA C  271  UNP  P09960    GLU   272 ENGINEERED MUTATION            
SEQRES   1 A  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 A  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 A  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 A  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 A  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 A  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 A  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 A  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 A  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 A  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 A  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 A  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 A  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 A  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 A  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 A  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 A  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 A  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 A  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 A  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 A  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 A  617  TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 A  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 A  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 A  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 A  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 A  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 A  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 A  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 A  617  ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 A  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 A  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 A  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 A  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 A  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 A  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 A  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 A  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 A  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 A  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 A  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 A  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 A  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 A  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS          
SEQRES  45 A  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 A  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 A  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 A  617  LYS ASP LEU LYS VAL ASP                                      
SEQRES   1 B  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 B  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 B  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 B  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 B  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 B  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 B  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 B  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 B  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 B  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 B  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 B  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 B  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 B  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 B  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 B  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 B  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 B  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 B  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 B  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 B  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 B  617  TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 B  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 B  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 B  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 B  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 B  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 B  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 B  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 B  617  ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 B  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 B  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 B  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 B  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 B  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 B  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 B  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 B  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 B  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 B  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 B  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 B  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 B  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 B  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS          
SEQRES  45 B  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 B  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 B  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 B  617  LYS ASP LEU LYS VAL ASP                                      
SEQRES   1 C  617  MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR          
SEQRES   2 C  617  CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS          
SEQRES   3 C  617  HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG          
SEQRES   4 C  617  THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN          
SEQRES   5 C  617  GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP          
SEQRES   6 C  617  LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL          
SEQRES   7 C  617  LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER          
SEQRES   8 C  617  PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN          
SEQRES   9 C  617  GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO          
SEQRES  10 C  617  LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR          
SEQRES  11 C  617  SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN          
SEQRES  12 C  617  ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR          
SEQRES  13 C  617  PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL          
SEQRES  14 C  617  PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP          
SEQRES  15 C  617  GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE          
SEQRES  16 C  617  TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU          
SEQRES  17 C  617  ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE          
SEQRES  18 C  617  GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL          
SEQRES  19 C  617  GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET          
SEQRES  20 C  617  LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP          
SEQRES  21 C  617  GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO          
SEQRES  22 C  617  TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR          
SEQRES  23 C  617  PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL          
SEQRES  24 C  617  ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU          
SEQRES  25 C  617  VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU          
SEQRES  26 C  617  GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG          
SEQRES  27 C  617  LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY          
SEQRES  28 C  617  GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY          
SEQRES  29 C  617  GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR          
SEQRES  30 C  617  ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR          
SEQRES  31 C  617  GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU          
SEQRES  32 C  617  LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA          
SEQRES  33 C  617  TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP          
SEQRES  34 C  617  ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS          
SEQRES  35 C  617  VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU          
SEQRES  36 C  617  TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP          
SEQRES  37 C  617  MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG          
SEQRES  38 C  617  TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN          
SEQRES  39 C  617  ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN          
SEQRES  40 C  617  GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO          
SEQRES  41 C  617  LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE          
SEQRES  42 C  617  ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU          
SEQRES  43 C  617  ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO          
SEQRES  44 C  617  LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS          
SEQRES  45 C  617  PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP          
SEQRES  46 C  617  LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS          
SEQRES  47 C  617  LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY          
SEQRES  48 C  617  LYS ASP LEU LYS VAL ASP                                      
HET     ZN  A 701       1                                                       
HET    IMD  A 702      10                                                       
HET    IMD  A 703      10                                                       
HET    IMD  A 704      10                                                       
HET    DJ3  A 705     104                                                       
HET     ZN  B 701       1                                                       
HET    IMD  B 702      10                                                       
HET    IMD  B 703      10                                                       
HET    IMD  B 704      10                                                       
HET    DJ3  B 705     104                                                       
HET     ZN  C 701       1                                                       
HET    IMD  C 702      10                                                       
HET    DJ3  C 703     104                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     DJ3 5S-5,6-OXIDO-7,9-TRANS-11,14-CIS-EICOSATETRAENOIC ACID           
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   5  IMD    7(C3 H5 N2 1+)                                               
FORMUL   8  DJ3    3(C20 H30 O3)                                                
FORMUL  17  HOH   *2056(H2 O)                                                   
HELIX    1 AA1 GLN A   79  GLY A   83  5                                   5    
HELIX    2 AA2 THR A  119  THR A  123  5                                   5    
HELIX    3 AA3 HIS A  139  ILE A  143  5                                   5    
HELIX    4 AA4 PRO A  198  ILE A  202  5                                   5    
HELIX    5 AA5 GLU A  223  PHE A  234  1                                  12    
HELIX    6 AA6 GLU A  236  GLY A  249  1                                  14    
HELIX    7 AA7 PRO A  280  LEU A  283  5                                   4    
HELIX    8 AA8 SER A  290  HIS A  299  1                                  10    
HELIX    9 AA9 THR A  310  ASP A  312  5                                   3    
HELIX   10 AB1 HIS A  313  GLY A  334  1                                  22    
HELIX   11 AB2 GLY A  334  GLY A  357  1                                  24    
HELIX   12 AB3 HIS A  360  LYS A  364  5                                   5    
HELIX   13 AB4 ASP A  373  TYR A  378  1                                   6    
HELIX   14 AB5 SER A  380  GLY A  398  1                                  19    
HELIX   15 AB6 GLY A  399  SER A  415  1                                  17    
HELIX   16 AB7 THR A  420  PHE A  432  1                                  13    
HELIX   17 AB8 LYS A  435  ASN A  440  1                                   6    
HELIX   18 AB9 ASP A  443  SER A  450  1                                   8    
HELIX   19 AC1 THR A  465  THR A  477  1                                  13    
HELIX   20 AC2 LYS A  479  PHE A  486  5                                   8    
HELIX   21 AC3 ASN A  487  LYS A  492  5                                   6    
HELIX   22 AC4 SER A  495  ARG A  509  1                                  15    
HELIX   23 AC5 PRO A  513  ASN A  525  1                                  13    
HELIX   24 AC6 PHE A  526  ILE A  529  5                                   4    
HELIX   25 AC7 ASN A  531  SER A  545  1                                  15    
HELIX   26 AC8 TRP A  547  ASP A  549  5                                   3    
HELIX   27 AC9 ALA A  550  GLN A  561  1                                  12    
HELIX   28 AD1 ARG A  563  PHE A  577  1                                  15    
HELIX   29 AD2 SER A  580  LYS A  592  1                                  13    
HELIX   30 AD3 ALA A  593  MET A  595  5                                   3    
HELIX   31 AD4 HIS A  596  LEU A  607  1                                  12    
HELIX   32 AD5 GLN B   79  GLY B   83  5                                   5    
HELIX   33 AD6 THR B  119  THR B  123  5                                   5    
HELIX   34 AD7 HIS B  139  ILE B  143  5                                   5    
HELIX   35 AD8 PRO B  198  ILE B  202  5                                   5    
HELIX   36 AD9 GLU B  223  PHE B  234  1                                  12    
HELIX   37 AE1 GLU B  236  GLY B  249  1                                  14    
HELIX   38 AE2 PRO B  280  LEU B  283  5                                   4    
HELIX   39 AE3 SER B  290  HIS B  299  1                                  10    
HELIX   40 AE4 THR B  310  ASP B  312  5                                   3    
HELIX   41 AE5 HIS B  313  GLY B  334  1                                  22    
HELIX   42 AE6 GLY B  334  GLY B  357  1                                  24    
HELIX   43 AE7 HIS B  360  LYS B  364  5                                   5    
HELIX   44 AE8 ASP B  373  TYR B  378  1                                   6    
HELIX   45 AE9 SER B  380  GLY B  398  1                                  19    
HELIX   46 AF1 GLY B  399  SER B  415  1                                  17    
HELIX   47 AF2 THR B  420  PHE B  432  1                                  13    
HELIX   48 AF3 LYS B  435  ASN B  440  1                                   6    
HELIX   49 AF4 ASP B  443  SER B  450  1                                   8    
HELIX   50 AF5 THR B  465  THR B  477  1                                  13    
HELIX   51 AF6 LYS B  479  PHE B  486  5                                   8    
HELIX   52 AF7 ASN B  487  LYS B  492  5                                   6    
HELIX   53 AF8 SER B  495  GLN B  508  1                                  14    
HELIX   54 AF9 PRO B  513  ASN B  525  1                                  13    
HELIX   55 AG1 PHE B  526  ILE B  529  5                                   4    
HELIX   56 AG2 ASN B  531  SER B  545  1                                  15    
HELIX   57 AG3 TRP B  547  ASP B  549  5                                   3    
HELIX   58 AG4 ALA B  550  GLN B  561  1                                  12    
HELIX   59 AG5 ARG B  563  PHE B  577  1                                  15    
HELIX   60 AG6 SER B  580  LYS B  592  1                                  13    
HELIX   61 AG7 ALA B  593  MET B  595  5                                   3    
HELIX   62 AG8 HIS B  596  LYS B  608  1                                  13    
HELIX   63 AG9 GLN C   79  GLY C   83  5                                   5    
HELIX   64 AH1 THR C  119  THR C  123  5                                   5    
HELIX   65 AH2 HIS C  139  ILE C  143  5                                   5    
HELIX   66 AH3 PRO C  198  ILE C  202  5                                   5    
HELIX   67 AH4 GLN C  226  PHE C  234  1                                   9    
HELIX   68 AH5 GLU C  236  GLY C  249  1                                  14    
HELIX   69 AH6 PRO C  280  LEU C  283  5                                   4    
HELIX   70 AH7 SER C  290  HIS C  299  1                                  10    
HELIX   71 AH8 THR C  310  ASP C  312  5                                   3    
HELIX   72 AH9 HIS C  313  GLY C  334  1                                  22    
HELIX   73 AI1 GLY C  334  GLY C  357  1                                  24    
HELIX   74 AI2 HIS C  360  LYS C  364  5                                   5    
HELIX   75 AI3 ASP C  373  TYR C  378  1                                   6    
HELIX   76 AI4 SER C  380  GLY C  398  1                                  19    
HELIX   77 AI5 GLY C  399  SER C  415  1                                  17    
HELIX   78 AI6 THR C  420  PHE C  432  1                                  13    
HELIX   79 AI7 LYS C  435  ASN C  440  1                                   6    
HELIX   80 AI8 ASP C  443  SER C  450  1                                   8    
HELIX   81 AI9 THR C  465  ALA C  478  1                                  14    
HELIX   82 AJ1 LYS C  479  PHE C  486  5                                   8    
HELIX   83 AJ2 ASN C  487  LYS C  492  5                                   6    
HELIX   84 AJ3 SER C  495  GLN C  508  1                                  14    
HELIX   85 AJ4 PRO C  513  ASN C  525  1                                  13    
HELIX   86 AJ5 PHE C  526  ILE C  529  5                                   4    
HELIX   87 AJ6 ASN C  531  SER C  545  1                                  15    
HELIX   88 AJ7 TRP C  547  ASP C  549  5                                   3    
HELIX   89 AJ8 ALA C  550  GLN C  561  1                                  12    
HELIX   90 AJ9 ARG C  563  PHE C  577  1                                  15    
HELIX   91 AK1 SER C  580  LYS C  592  1                                  13    
HELIX   92 AK2 ALA C  593  MET C  595  5                                   3    
HELIX   93 AK3 HIS C  596  LYS C  608  1                                  13    
SHEET    1 AA1 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA1 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA1 8 GLU A  99  THR A 108 -1  O  GLU A 103   N  VAL A  65           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  VAL A  42   O  ILE A 100           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6 AA1 8 LEU A 154  PRO A 163  1  O  THR A 157   N  LEU A  23           
SHEET    7 AA1 8 ARG A 186  ILE A 197 -1  O  GLN A 193   N  TYR A 156           
SHEET    8 AA1 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1 AA2 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA2 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA2 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA3 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA3 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3 AA3 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA3 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1 AA4 5 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 5 THR A 218  SER A 222 -1  O  SER A 222   N  GLU A 210           
SHEET    3 AA4 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5 AA4 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1 AA5 2 VAL A 306  ASN A 308  0                                        
SHEET    2 AA5 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
SHEET    1 AA6 8 GLN B  69  GLU B  70  0                                        
SHEET    2 AA6 8 THR B  60  ILE B  66 -1  N  ILE B  66   O  GLN B  69           
SHEET    3 AA6 8 GLU B  99  GLU B 107 -1  O  GLU B 103   N  VAL B  65           
SHEET    4 AA6 8 THR B  33  SER B  44 -1  N  LEU B  40   O  ILE B 102           
SHEET    5 AA6 8 CYS B  16  ASP B  28 -1  N  LYS B  19   O  THR B  41           
SHEET    6 AA6 8 LEU B 154  PRO B 163  1  O  SER B 161   N  VAL B  27           
SHEET    7 AA6 8 ARG B 186  ILE B 197 -1  O  LYS B 187   N  VAL B 162           
SHEET    8 AA6 8 ILE B 173  PRO B 179 -1  N  THR B 178   O  ILE B 188           
SHEET    1 AA7 3 LEU B  49  LEU B  54  0                                        
SHEET    2 AA7 3 MET B  86  LEU B  94 -1  O  ILE B  88   N  LEU B  52           
SHEET    3 AA7 3 TYR B  73  LEU B  75 -1  N  ALA B  74   O  GLU B  87           
SHEET    1 AA8 4 LEU B 115  LEU B 118  0                                        
SHEET    2 AA8 4 TYR B 130  SER B 133 -1  O  TYR B 130   N  LEU B 118           
SHEET    3 AA8 4 LEU B 204  GLY B 207 -1  O  VAL B 206   N  LEU B 131           
SHEET    4 AA8 4 VAL B 167  MET B 170 -1  N  VAL B 167   O  GLY B 207           
SHEET    1 AA9 5 GLU B 210  GLY B 215  0                                        
SHEET    2 AA9 5 THR B 218  SER B 222 -1  O  SER B 222   N  GLU B 210           
SHEET    3 AA9 5 ASP B 257  VAL B 260  1  O  LEU B 258   N  TRP B 221           
SHEET    4 AA9 5 LEU B 275  VAL B 278  1  O  THR B 276   N  LEU B 259           
SHEET    5 AA9 5 GLY B 269  MET B 270 -1  N  MET B 270   O  PHE B 277           
SHEET    1 AB1 2 THR B 307  ASN B 308  0                                        
SHEET    2 AB1 2 SER B 418  ILE B 419  1  O  ILE B 419   N  THR B 307           
SHEET    1 AB2 8 GLN C  69  GLU C  70  0                                        
SHEET    2 AB2 8 LEU C  59  ILE C  66 -1  N  ILE C  66   O  GLN C  69           
SHEET    3 AB2 8 GLU C  99  THR C 108 -1  O  GLU C 103   N  VAL C  65           
SHEET    4 AB2 8 THR C  33  SER C  44 -1  N  LEU C  40   O  ILE C 102           
SHEET    5 AB2 8 CYS C  16  ASP C  28 -1  N  LYS C  19   O  THR C  41           
SHEET    6 AB2 8 LEU C 154  PRO C 163  1  O  SER C 161   N  VAL C  27           
SHEET    7 AB2 8 ARG C 186  ILE C 197 -1  O  GLN C 193   N  TYR C 156           
SHEET    8 AB2 8 ILE C 173  PRO C 179 -1  N  THR C 178   O  ILE C 188           
SHEET    1 AB3 3 LEU C  49  LEU C  54  0                                        
SHEET    2 AB3 3 MET C  86  LEU C  94 -1  O  ILE C  88   N  LEU C  52           
SHEET    3 AB3 3 TYR C  73  LEU C  75 -1  N  ALA C  74   O  GLU C  87           
SHEET    1 AB4 4 LEU C 115  LEU C 118  0                                        
SHEET    2 AB4 4 TYR C 130  SER C 133 -1  O  TYR C 130   N  LEU C 118           
SHEET    3 AB4 4 LEU C 204  GLY C 207 -1  O  VAL C 206   N  LEU C 131           
SHEET    4 AB4 4 VAL C 167  MET C 170 -1  N  VAL C 167   O  GLY C 207           
SHEET    1 AB5 5 GLU C 210  GLY C 215  0                                        
SHEET    2 AB5 5 THR C 218  SER C 222 -1  O  SER C 222   N  GLU C 210           
SHEET    3 AB5 5 ASP C 257  VAL C 260  1  O  LEU C 258   N  TRP C 221           
SHEET    4 AB5 5 LEU C 275  VAL C 278  1  O  VAL C 278   N  LEU C 259           
SHEET    5 AB5 5 GLY C 269  MET C 270 -1  N  MET C 270   O  PHE C 277           
SHEET    1 AB6 2 VAL C 306  ASN C 308  0                                        
SHEET    2 AB6 2 LYS C 417  ILE C 419  1  O  ILE C 419   N  THR C 307           
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.15  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.12  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.03  
LINK         OE2 GLU A 318                ZN    ZN A 701     1555   1555  2.52  
LINK         NE2 HIS B 295                ZN    ZN B 701     1555   1555  2.09  
LINK         NE2 HIS B 299                ZN    ZN B 701     1555   1555  2.03  
LINK         OE1 GLU B 318                ZN    ZN B 701     1555   1555  2.01  
LINK         OE2 GLU B 318                ZN    ZN B 701     1555   1555  2.60  
LINK         NE2 HIS C 295                ZN    ZN C 701     1555   1555  2.11  
LINK         NE2 HIS C 299                ZN    ZN C 701     1555   1555  2.08  
LINK         OE1 GLU C 318                ZN    ZN C 701     1555   1555  1.98  
LINK         OE2 GLU C 318                ZN    ZN C 701     1555   1555  2.59  
LINK        ZN    ZN A 701                 OATADJ3 A 705     1555   1555  2.07  
LINK        ZN    ZN A 701                 OATBDJ3 A 705     1555   1555  2.44  
LINK        ZN    ZN B 701                 OATADJ3 B 705     1555   1555  2.01  
LINK        ZN    ZN B 701                 OATBDJ3 B 705     1555   1555  1.85  
LINK        ZN    ZN B 701                 O   HOH B 808     1555   1555  2.65  
LINK        ZN    ZN C 701                 OATADJ3 C 703     1555   1555  2.02  
LINK        ZN    ZN C 701                 OATBDJ3 C 703     1555   1555  2.04  
LINK        ZN    ZN C 701                 O   HOH C 805     1555   1555  2.65  
CISPEP   1 GLN A  136    ALA A  137          0         4.18                     
CISPEP   2 ALA A  510    PRO A  511          0         2.64                     
CISPEP   3 GLN B  136    ALA B  137          0         4.43                     
CISPEP   4 ALA B  510    PRO B  511          0         1.44                     
CISPEP   5 GLN C  136    ALA C  137          0         4.10                     
CISPEP   6 ALA C  510    PRO C  511          0         1.71                     
SITE     1 AC1  5 HIS A 295  HIS A 299  GLU A 318  DJ3 A 705                    
SITE     2 AC1  5 HOH A 804                                                     
SITE     1 AC2  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC2  6 GLN A 508  HOH A1206                                          
SITE     1 AC3  7 GLY A 248  PRO A 250  VAL A 252  GLU A 412                    
SITE     2 AC3  7 SER A 415  HOH A1002  HOH A1152                               
SITE     1 AC4  4 ASP A 422  ASP A 426  HOH A1004  HOH A1385                    
SITE     1 AC5 20 GLN A 136  ALA A 137  TYR A 267  GLY A 268                    
SITE     2 AC5 20 GLY A 269  MET A 270  HIS A 295  GLU A 296                    
SITE     3 AC5 20 TRP A 311  PHE A 314  GLU A 318  VAL A 367                    
SITE     4 AC5 20 TYR A 378  TYR A 383  ARG A 563   ZN A 701                    
SITE     5 AC5 20 HOH A 801  HOH A 804  HOH A 810  HOH A1145                    
SITE     1 AC6  5 HIS B 295  HIS B 299  GLU B 318  DJ3 B 705                    
SITE     2 AC6  5 HOH B 808                                                     
SITE     1 AC7  6 GLY B 344  GLY B 347  GLU B 348  GLU B 501                    
SITE     2 AC7  6 ALA B 504  GLN B 508                                          
SITE     1 AC8  2 ASP B 422  ASP B 426                                          
SITE     1 AC9 10 GLY B 248  GLY B 249  PRO B 250  LEU B 305                    
SITE     2 AC9 10 VAL B 411  GLU B 412  SER B 415  HOH B 896                    
SITE     3 AC9 10 HOH B 988  HOH B1063                                          
SITE     1 AD1 21 GLN B 136  ALA B 137  TYR B 267  GLY B 268                    
SITE     2 AD1 21 GLY B 269  HIS B 295  GLU B 296  HIS B 299                    
SITE     3 AD1 21 TRP B 311  PHE B 314  GLU B 318  VAL B 367                    
SITE     4 AD1 21 PRO B 374  TYR B 378  TYR B 383  ARG B 563                    
SITE     5 AD1 21 LYS B 565   ZN B 701  HOH B 808  HOH B 870                    
SITE     6 AD1 21 HOH B1007                                                     
SITE     1 AD2  5 HIS C 295  HIS C 299  GLU C 318  DJ3 C 703                    
SITE     2 AD2  5 HOH C 805                                                     
SITE     1 AD3  7 GLY C 344  GLY C 347  GLU C 348  ASN C 351                    
SITE     2 AD3  7 GLU C 501  ALA C 504  GLN C 508                               
SITE     1 AD4 22 GLN C 136  ALA C 137  TYR C 267  GLY C 268                    
SITE     2 AD4 22 GLY C 269  MET C 270  HIS C 295  GLU C 296                    
SITE     3 AD4 22 TRP C 311  PHE C 314  GLU C 318  VAL C 367                    
SITE     4 AD4 22 PRO C 374  TYR C 383  ARG C 563  LYS C 565                    
SITE     5 AD4 22  ZN C 701  HOH C 805  HOH C 865  HOH C1025                    
SITE     6 AD4 22 HOH C1169  HOH C1203                                          
CRYST1  139.560  139.560   87.950  90.00  90.00 120.00 P 32          9          
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      0.007165  0.004137  0.000000        0.00000                         
SCALE2      0.000000  0.008274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011370        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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