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Database: PDB
Entry: 5PA7
LinkDB: 5PA7
Original site: 5PA7 
HEADER    TRANSFERASE                             19-OCT-16   5PA7              
TITLE     HUMANIZED RAT COMT IN COMPLEX WITH 6-BROMO-3-CHLOROQUINOLIN-8-OL      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SOLUBLE FORM, RESIDUES 44-264;                             
COMPND   5 SYNONYM: HUMANIZED RAT COMT;                                         
COMPND   6 EC: 2.1.1.6;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: COMT;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.EHLER,C.LERNER,M.G.RUDOLPH                                          
REVDAT   3   17-NOV-21 5PA7    1       LINK                                     
REVDAT   2   21-FEB-18 5PA7    1       REMARK                                   
REVDAT   1   22-NOV-17 5PA7    0                                                
JRNL        AUTH   C.LERNER,R.JAKOB-ROETNE,K.GROEBKE-ZBINDEN,B.BUETTELMANN,     
JRNL        AUTH 2 M.G.RUDOLPH                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF A COMT COMPLEX                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_764                                       
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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29565                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1502                            
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 45.2147 -  4.7134    1.00     2731   155  0.1548 0.1910        
REMARK   3     2  4.7134 -  3.7417    1.00     2591   154  0.1405 0.2025        
REMARK   3     3  3.7417 -  3.2689    1.00     2585   121  0.1755 0.2356        
REMARK   3     4  3.2689 -  2.9701    1.00     2569   101  0.2121 0.2870        
REMARK   3     5  2.9701 -  2.7572    1.00     2565   115  0.2176 0.2884        
REMARK   3     6  2.7572 -  2.5947    1.00     2493   161  0.2203 0.2809        
REMARK   3     7  2.5947 -  2.4648    1.00     2554   134  0.2575 0.3055        
REMARK   3     8  2.4648 -  2.3575    1.00     2522   128  0.2711 0.3429        
REMARK   3     9  2.3575 -  2.2667    0.99     2503   125  0.2904 0.3357        
REMARK   3    10  2.2667 -  2.1885    0.99     2465   159  0.3035 0.3591        
REMARK   3    11  2.1885 -  2.1201    1.00     2485   149  0.3314 0.3387        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 43.93                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.630            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 21.62930                                             
REMARK   3    B22 (A**2) : -11.28300                                            
REMARK   3    B33 (A**2) : -10.34630                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3446                                  
REMARK   3   ANGLE     :  1.067           4674                                  
REMARK   3   CHIRALITY :  0.069            531                                  
REMARK   3   PLANARITY :  0.004            593                                  
REMARK   3   DIHEDRAL  : 15.813           1302                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 3:16)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0800 -11.2625  21.8405              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2843 T22:   0.4613                                     
REMARK   3      T33:   0.3423 T12:   0.0442                                     
REMARK   3      T13:   0.0228 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9965 L22:   3.9319                                     
REMARK   3      L33:   3.6031 L12:  -0.1910                                     
REMARK   3      L13:  -0.2576 L23:   2.2136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0839 S12:  -0.2401 S13:  -0.3489                       
REMARK   3      S21:   0.2776 S22:   0.5247 S23:  -0.0861                       
REMARK   3      S31:   0.5423 S32:   0.8510 S33:  -0.3892                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 17:35)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7136  -0.7362  18.7742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4248 T22:   0.3786                                     
REMARK   3      T33:   0.4352 T12:  -0.0531                                     
REMARK   3      T13:  -0.0019 T23:   0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7305 L22:   4.9749                                     
REMARK   3      L33:   5.1609 L12:  -1.6246                                     
REMARK   3      L13:  -1.6292 L23:   0.9148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0925 S12:   0.3275 S13:   0.9566                       
REMARK   3      S21:  -0.2017 S22:   0.1983 S23:  -0.8248                       
REMARK   3      S31:  -0.9884 S32:   0.4174 S33:  -0.2420                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 36:57)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5826  -0.2904   7.4578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5086 T22:   0.4632                                     
REMARK   3      T33:   0.3903 T12:  -0.0315                                     
REMARK   3      T13:   0.0173 T23:   0.0610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8844 L22:   4.1259                                     
REMARK   3      L33:   2.1689 L12:  -1.2970                                     
REMARK   3      L13:  -0.3460 L23:  -0.2249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:  -0.0772 S13:  -0.1067                       
REMARK   3      S21:  -0.4996 S22:   0.0418 S23:   0.2047                       
REMARK   3      S31:  -0.4243 S32:   0.5394 S33:  -0.0326                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 58:70)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1472  -5.3832  10.9645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3542 T22:   0.4116                                     
REMARK   3      T33:   0.3530 T12:   0.0701                                     
REMARK   3      T13:  -0.0155 T23:  -0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0087 L22:   1.3190                                     
REMARK   3      L33:   0.9755 L12:   0.0656                                     
REMARK   3      L13:   0.8072 L23:  -0.4294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1673 S12:   0.3224 S13:   0.5010                       
REMARK   3      S21:  -0.0966 S22:  -0.2960 S23:  -0.0868                       
REMARK   3      S31:  -0.3706 S32:   0.1999 S33:   0.0966                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 71:118)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5112  -6.1539  17.5702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3440 T22:   0.3368                                     
REMARK   3      T33:   0.3388 T12:   0.0325                                     
REMARK   3      T13:   0.0012 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9588 L22:   0.8040                                     
REMARK   3      L33:   1.3318 L12:   0.7192                                     
REMARK   3      L13:   0.1725 L23:  -0.4445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0005 S12:  -0.1364 S13:   0.1192                       
REMARK   3      S21:  -0.0516 S22:   0.0351 S23:  -0.0186                       
REMARK   3      S31:  -0.2005 S32:  -0.0461 S33:  -0.0213                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 119:136)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -15.3570 -11.2626  10.0358              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2990 T22:   0.4844                                     
REMARK   3      T33:   0.4283 T12:   0.0471                                     
REMARK   3      T13:  -0.0491 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0817 L22:   2.7447                                     
REMARK   3      L33:   0.8902 L12:  -0.3624                                     
REMARK   3      L13:   0.1756 L23:  -0.4088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0177 S12:  -0.1957 S13:  -0.0062                       
REMARK   3      S21:   0.2482 S22:  -0.0181 S23:   0.3475                       
REMARK   3      S31:  -0.1434 S32:  -0.3261 S33:   0.0265                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 137:156)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2557 -12.0728   0.9101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4511 T22:   0.3272                                     
REMARK   3      T33:   0.2715 T12:   0.0364                                     
REMARK   3      T13:  -0.0632 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6647 L22:   2.2466                                     
REMARK   3      L33:   1.7173 L12:   0.0509                                     
REMARK   3      L13:   0.1913 L23:   0.5885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0297 S12:   0.1565 S13:  -0.1831                       
REMARK   3      S21:  -0.5479 S22:   0.1008 S23:  -0.0795                       
REMARK   3      S31:   0.4138 S32:  -0.1275 S33:  -0.1367                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 157:188)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7924  -6.3117  -4.2401              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5114 T22:   0.3481                                     
REMARK   3      T33:   0.3419 T12:   0.0152                                     
REMARK   3      T13:  -0.0880 T23:   0.0640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5527 L22:   0.8313                                     
REMARK   3      L33:   1.2800 L12:   0.4046                                     
REMARK   3      L13:  -0.1307 L23:   0.4505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1497 S12:   0.1763 S13:   0.0461                       
REMARK   3      S21:  -0.5584 S22:   0.1567 S23:   0.2599                       
REMARK   3      S31:  -0.0166 S32:  -0.1548 S33:   0.0027                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 189:215)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7477  -2.2715  -3.3855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6038 T22:   0.3651                                     
REMARK   3      T33:   0.3478 T12:  -0.0036                                     
REMARK   3      T13:  -0.0202 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5481 L22:   1.8864                                     
REMARK   3      L33:   1.0019 L12:  -0.8402                                     
REMARK   3      L13:  -0.4455 L23:  -0.0849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2475 S12:   0.2332 S13:   0.4815                       
REMARK   3      S21:  -0.6161 S22:   0.2009 S23:   0.0425                       
REMARK   3      S31:  -0.1469 S32:  -0.2168 S33:  -0.0283                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 300:300)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9257 -13.7917   8.9488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5386 T22:   0.3779                                     
REMARK   3      T33:   0.3061 T12:   0.0763                                     
REMARK   3      T13:   0.1328 T23:   0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0738 L22:   0.0998                                     
REMARK   3      L33:   0.0165 L12:   0.0673                                     
REMARK   3      L13:  -0.0114 L23:   0.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0926 S12:  -0.1772 S13:   0.0594                       
REMARK   3      S21:   0.1038 S22:  -0.0577 S23:  -0.1010                       
REMARK   3      S31:  -0.0955 S32:   0.3277 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 301:302)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7554 -11.8315   3.4989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4109 T22:   1.0326                                     
REMARK   3      T33:   0.5625 T12:   0.0215                                     
REMARK   3      T13:   0.1269 T23:  -0.1873                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5548 L22:   0.2907                                     
REMARK   3      L33:   0.0611 L12:  -0.1150                                     
REMARK   3      L13:   0.0722 L23:  -0.1321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1755 S12:   0.0444 S13:  -0.0907                       
REMARK   3      S21:  -0.0288 S22:  -0.2264 S23:  -0.1984                       
REMARK   3      S31:   0.0921 S32:   0.0729 S33:  -0.0091                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 3:35)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0059 -20.5750  29.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3690 T22:   0.7066                                     
REMARK   3      T33:   0.7242 T12:   0.3326                                     
REMARK   3      T13:  -0.0185 T23:   0.1366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0571 L22:   1.0780                                     
REMARK   3      L33:   4.0335 L12:   1.2727                                     
REMARK   3      L13:  -0.2703 L23:  -0.4973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:   0.4509 S13:   1.1863                       
REMARK   3      S21:   0.0396 S22:   0.5880 S23:   0.7927                       
REMARK   3      S31:  -0.8690 S32:  -0.5398 S33:  -0.2138                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 36:57)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1258 -25.1654  20.8891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4605 T22:   0.4692                                     
REMARK   3      T33:   0.3761 T12:   0.0555                                     
REMARK   3      T13:   0.0561 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6076 L22:   1.5666                                     
REMARK   3      L33:   1.1767 L12:   0.6251                                     
REMARK   3      L13:   0.6343 L23:  -1.1335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1713 S12:  -0.2295 S13:   0.1909                       
REMARK   3      S21:  -0.0929 S22:  -0.2810 S23:   0.5160                       
REMARK   3      S31:  -0.1189 S32:  -0.3432 S33:  -0.0070                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 58:143)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1408 -37.7280  29.1447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3330 T22:   0.3628                                     
REMARK   3      T33:   0.4166 T12:  -0.0818                                     
REMARK   3      T13:  -0.0753 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4546 L22:   1.4540                                     
REMARK   3      L33:   2.8722 L12:  -1.0414                                     
REMARK   3      L13:  -0.0362 L23:  -1.0817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0739 S12:   0.0532 S13:   0.0059                       
REMARK   3      S21:  -0.3753 S22:   0.1351 S23:   0.4599                       
REMARK   3      S31:   0.4137 S32:  -0.5802 S33:  -0.0775                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 144:216)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6139 -33.0800  28.5592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2930 T22:   0.2779                                     
REMARK   3      T33:   0.3005 T12:   0.0619                                     
REMARK   3      T13:   0.0144 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8778 L22:   1.4144                                     
REMARK   3      L33:   1.7971 L12:   0.9981                                     
REMARK   3      L13:  -0.1658 L23:  -0.5351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0584 S12:   0.0299 S13:  -0.1221                       
REMARK   3      S21:  -0.0715 S22:  -0.0919 S23:  -0.1596                       
REMARK   3      S31:   0.1204 S32:   0.1179 S33:   0.1495                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 300:300)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2707 -31.3110  36.5609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4695 T22:   0.4437                                     
REMARK   3      T33:   0.4815 T12:   0.0342                                     
REMARK   3      T13:   0.0954 T23:   0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0264 L22:   0.0372                                     
REMARK   3      L33:   0.0340 L12:   0.0089                                     
REMARK   3      L13:  -0.0232 L23:  -0.0242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0564 S12:   0.2040 S13:   0.2594                       
REMARK   3      S21:  -0.0285 S22:  -0.0073 S23:   0.1975                       
REMARK   3      S31:   0.0232 S32:  -0.1469 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PARTIAL RADIOLYSIS OF BROMINE. NO SIGMA   
REMARK   3  -HOLE EFFECT OF CHLORINE AND AMIDE CARBONYL. LYSINE BINDS TO        
REMARK   3  SAID CARBONYL.                                                      
REMARK   4                                                                      
REMARK   4 5PA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1001400412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
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   : 29641                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.610                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : 0.12400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.83400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.230                              
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: INHOUSE MODEL                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CHES, PH 9, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
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       28.59250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.80700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.05250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.80700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.59250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.05250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     PRO A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     TRP B    38                                                      
REMARK 465     ALA B    39                                                      
REMARK 465     MET B    40                                                      
REMARK 465     ASN B    41                                                      
REMARK 465     SER B   217                                                      
REMARK 465     PRO B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     LYS B   220                                                      
REMARK 465     SER B   221                                                      
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   430     O    HOH B   433              1.87            
REMARK 500   O    HOH A   433     O    HOH A   436              1.98            
REMARK 500   O    HOH B   427     O    HOH B   443              2.14            
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    MET A  40       35.82    -78.63                                   
REMARK 500    TYR A  68     -115.01     60.39                                   
REMARK 500    ASP A 133      -75.28    -90.10                                   
REMARK 500    ASP A 141       27.31   -158.24                                   
REMARK 500    HIS A 142     -153.76    -97.68                                   
REMARK 500    ASP A 205     -164.61   -122.51                                   
REMARK 500    GLN B  15      -62.94    -93.02                                   
REMARK 500    TYR B  68     -115.20     56.61                                   
REMARK 500    ASP B 133      -77.31    -98.64                                   
REMARK 500    ASP B 141       25.46   -141.87                                   
REMARK 500    HIS B 142     -146.27   -107.14                                   
REMARK 500    ASP B 205     -157.15    -93.66                                   
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                              MG A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 141   OD1                                                    
REMARK 620 2 ASP A 169   OD2  94.6                                              
REMARK 620 3 ASN A 170   OD1  84.3  88.3                                        
REMARK 620 4 7JX A 302   O12 160.7 104.7  97.8                                  
REMARK 620 5 HOH A 412   O    87.1  97.2 170.1  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 303  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 183   O                                                      
REMARK 620 2 ARG A 184   O    78.1                                              
REMARK 620 3 SER A 186   O    72.1  98.6                                        
REMARK 620 4 PHE A 189   O    90.0 158.9  60.8                                  
REMARK 620 5 HOH A 437   O   133.2 102.0  61.6  73.5                            
REMARK 620 6 HOH A 441   O   115.8  88.2 170.7 112.7 110.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL B 183   O                                                      
REMARK 620 2 ARG B 184   O    81.1                                              
REMARK 620 3 SER B 186   O    82.9 115.0                                        
REMARK 620 4 PHE B 189   O    93.4 166.5  76.2                                  
REMARK 620 5 HOH B 440   O   105.3  78.4 165.6  91.3                            
REMARK 620 6 HOH B 442   O   159.1  78.6 101.3 107.5  75.2                      
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 SAH A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7JX A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 302                  
DBREF  5PA7 A    1   221  UNP    P22734   COMT_RAT        44    264             
DBREF  5PA7 B    1   221  UNP    P22734   COMT_RAT        44    264             
SEQADV 5PA7 ILE A   91  UNP  P22734    MET   134 ENGINEERED MUTATION            
SEQADV 5PA7 CYS A   95  UNP  P22734    TYR   138 ENGINEERED MUTATION            
SEQADV 5PA7 ILE B   91  UNP  P22734    MET   134 ENGINEERED MUTATION            
SEQADV 5PA7 CYS B   95  UNP  P22734    TYR   138 ENGINEERED MUTATION            
SEQRES   1 A  221  MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL          
SEQRES   2 A  221  GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU          
SEQRES   3 A  221  GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA          
SEQRES   4 A  221  MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA          
SEQRES   5 A  221  VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU          
SEQRES   6 A  221  GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG          
SEQRES   7 A  221  LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE          
SEQRES   8 A  221  ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN          
SEQRES   9 A  221  PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY          
SEQRES  10 A  221  ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR          
SEQRES  11 A  221  ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP          
SEQRES  12 A  221  LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS          
SEQRES  13 A  221  CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP          
SEQRES  14 A  221  ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR          
SEQRES  15 A  221  VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER          
SEQRES  16 A  221  SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU          
SEQRES  17 A  221  LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER          
SEQRES   1 B  221  MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL          
SEQRES   2 B  221  GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU          
SEQRES   3 B  221  GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA          
SEQRES   4 B  221  MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA          
SEQRES   5 B  221  VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU          
SEQRES   6 B  221  GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG          
SEQRES   7 B  221  LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE          
SEQRES   8 B  221  ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN          
SEQRES   9 B  221  PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY          
SEQRES  10 B  221  ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR          
SEQRES  11 B  221  ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP          
SEQRES  12 B  221  LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS          
SEQRES  13 B  221  CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP          
SEQRES  14 B  221  ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR          
SEQRES  15 B  221  VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER          
SEQRES  16 B  221  SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU          
SEQRES  17 B  221  LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER          
HET    SAH  A 300      26                                                       
HET     MG  A 301       1                                                       
HET    7JX  A 302      13                                                       
HET     NA  A 303       1                                                       
HET    SAH  B 301      26                                                       
HET     NA  B 302       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     7JX 6-BROMANYL-3-CHLORANYL-QUINOLIN-8-OL                             
HETNAM      NA SODIUM ION                                                       
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  7JX    C9 H5 BR CL N O                                              
FORMUL   6   NA    2(NA 1+)                                                     
FORMUL   9  HOH   *91(H2 O)                                                     
HELIX    1 AA1 THR A    4  ALA A   17  1                                  14    
HELIX    2 AA2 ASP A   21  LYS A   36  1                                  16    
HELIX    3 AA3 GLY A   43  SER A   58  1                                  16    
HELIX    4 AA4 GLY A   70  ARG A   78  1                                   9    
HELIX    5 AA5 ASN A   92  GLY A  107  1                                  16    
HELIX    6 AA6 ALA A  118  ILE A  123  1                                   6    
HELIX    7 AA7 GLN A  125  TYR A  130  1                                   6    
HELIX    8 AA8 TRP A  143  ASP A  145  5                                   3    
HELIX    9 AA9 ARG A  146  CYS A  157  1                                  12    
HELIX   10 AB1 THR A  176  SER A  186  1                                  11    
HELIX   11 AB2 THR B    4  ALA B   17  1                                  14    
HELIX   12 AB3 ASP B   21  LYS B   36  1                                  16    
HELIX   13 AB4 GLY B   43  SER B   58  1                                  16    
HELIX   14 AB5 GLY B   70  ARG B   78  1                                   9    
HELIX   15 AB6 ASN B   92  GLY B  107  1                                  16    
HELIX   16 AB7 ALA B  118  ILE B  123  1                                   6    
HELIX   17 AB8 GLN B  125  TYR B  130  1                                   6    
HELIX   18 AB9 TRP B  143  ASP B  145  5                                   3    
HELIX   19 AC1 ARG B  146  CYS B  157  1                                  12    
HELIX   20 AC2 THR B  176  SER B  186  1                                  11    
SHEET    1 AA1 7 VAL A 112  ASN A 116  0                                        
SHEET    2 AA1 7 ARG A  85  GLU A  90  1  N  THR A  88   O  LEU A 115           
SHEET    3 AA1 7 LEU A  61  LEU A  65  1  N  VAL A  62   O  LEU A  87           
SHEET    4 AA1 7 MET A 137  LEU A 140  1  O  PHE A 139   N  LEU A  65           
SHEET    5 AA1 7 VAL A 165  ALA A 168  1  O  LEU A 167   N  VAL A 138           
SHEET    6 AA1 7 VAL A 203  TYR A 212 -1  O  ALA A 210   N  LEU A 166           
SHEET    7 AA1 7 PHE A 189  LEU A 198 -1  N  SER A 196   O  ASP A 205           
SHEET    1 AA2 7 VAL B 112  ASN B 116  0                                        
SHEET    2 AA2 7 ARG B  85  GLU B  90  1  N  THR B  88   O  LEU B 115           
SHEET    3 AA2 7 LEU B  61  LEU B  65  1  N  GLU B  64   O  LEU B  87           
SHEET    4 AA2 7 LEU B 135  LEU B 140  1  O  PHE B 139   N  LEU B  63           
SHEET    5 AA2 7 LEU B 160  ALA B 168  1  O  LEU B 167   N  VAL B 138           
SHEET    6 AA2 7 VAL B 203  TYR B 212 -1  O  TYR B 212   N  GLY B 163           
SHEET    7 AA2 7 PHE B 189  LEU B 198 -1  N  LEU B 198   O  VAL B 203           
LINK         OD1 ASP A 141                MG    MG A 301     1555   1555  2.27  
LINK         OD2 ASP A 169                MG    MG A 301     1555   1555  2.23  
LINK         OD1 ASN A 170                MG    MG A 301     1555   1555  2.17  
LINK         O   VAL A 183                NA    NA A 303     1555   1555  2.80  
LINK         O   ARG A 184                NA    NA A 303     1555   1555  2.86  
LINK         O   SER A 186                NA    NA A 303     1555   1555  3.00  
LINK         O   PHE A 189                NA    NA A 303     1555   1555  2.75  
LINK        MG    MG A 301                 O12 7JX A 302     1555   1555  2.19  
LINK        MG    MG A 301                 O   HOH A 412     1555   1555  2.27  
LINK        NA    NA A 303                 O   HOH A 437     1555   1555  2.98  
LINK        NA    NA A 303                 O   HOH A 441     1555   1555  2.88  
LINK         O   VAL B 183                NA    NA B 302     1555   1555  2.76  
LINK         O   ARG B 184                NA    NA B 302     1555   1555  2.73  
LINK         O   SER B 186                NA    NA B 302     1555   1555  2.71  
LINK         O   PHE B 189                NA    NA B 302     1555   1555  2.59  
LINK        NA    NA B 302                 O   HOH B 440     1555   1555  2.90  
LINK        NA    NA B 302                 O   HOH B 442     1555   1555  2.91  
CISPEP   1 VAL A  173    PRO A  174          0        -2.26                     
CISPEP   2 VAL B  173    PRO B  174          0         6.85                     
SITE     1 AC1 19 MET A  40  VAL A  42  GLY A  66  ALA A  67                    
SITE     2 AC1 19 TYR A  68  TYR A  71  SER A  72  MET A  89                    
SITE     3 AC1 19 GLU A  90  ILE A  91  CYS A  95  GLY A 117                    
SITE     4 AC1 19 ALA A 118  SER A 119  ASP A 141  HIS A 142                    
SITE     5 AC1 19 TRP A 143  7JX A 302  HOH A 408                               
SITE     1 AC2  5 ASP A 141  ASP A 169  ASN A 170  7JX A 302                    
SITE     2 AC2  5 HOH A 412                                                     
SITE     1 AC3  8 ASP A 141  HIS A 142  LYS A 144  ASP A 169                    
SITE     2 AC3  8 ASN A 170  SAH A 300   MG A 301  HOH A 402                    
SITE     1 AC4  6 VAL A 183  ARG A 184  SER A 186  PHE A 189                    
SITE     2 AC4  6 HOH A 437  HOH A 441                                          
SITE     1 AC5 17 LYS B  46  GLY B  66  ALA B  67  TYR B  68                    
SITE     2 AC5 17 TYR B  71  SER B  72  GLU B  90  ILE B  91                    
SITE     3 AC5 17 GLY B 117  ALA B 118  SER B 119  GLN B 120                    
SITE     4 AC5 17 ASP B 141  TRP B 143  ARG B 146  HOH B 401                    
SITE     5 AC5 17 HOH B 414                                                     
SITE     1 AC6  6 VAL B 183  ARG B 184  SER B 186  PHE B 189                    
SITE     2 AC6  6 HOH B 440  HOH B 442                                          
CRYST1   57.185   60.105  147.614  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017487  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016638  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006774        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system