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Database: PDB
Entry: 5K0K
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       17-MAY-16   5K0K              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTO-ONCOGENE       
TITLE    2 TYROSINE-PROTEIN KINASE MER IN COMPLEX WITH INHIBITOR UNC2434        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE MER;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 570-864;                    
COMPND   5 SYNONYM: PROTO-ONCOGENE C-MER,RECEPTOR TYROSINE KINASE MERTK;        
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MERTK, MER;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MACROCYCLIC, PYRROLOPYRIMIDINES, DRUG DESIGN, FIBRINOLYTIC AGENTS,    
KEYWDS   2 PROTEIN KINASE INHIBITORS, PROTO-ONCOGENE PROTEINS, PYRIMIDINES,     
KEYWDS   3 RECEPTOR PROTEIN-TYROSINE KINASES, STRUCTURE-ACTIVITY RELATIONSHIP,  
KEYWDS   4 THROMBOSIS, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.WANG,J.LIU,W.ZHANG,M.A.STASHKO,J.NICHOLS,D.DERYCKERE,M.J.MILEY,     
AUTHOR   2 J.NORRIS-DROUIN,Z.CHEN,M.MACHIUS,E.WOOD,D.K.GRAHAM,H.S.EARP,         
AUTHOR   3 K.GRAHAM,D.KIREEV,S.V.FRYE                                           
REVDAT   2   27-SEP-23 5K0K    1       COMPND HETNAM                            
REVDAT   1   11-JAN-17 5K0K    0                                                
JRNL        AUTH   X.WANG,J.LIU,W.ZHANG,M.A.STASHKO,J.NICHOLS,M.J.MILEY,        
JRNL        AUTH 2 J.NORRIS-DROUIN,Z.CHEN,M.MACHIUS,D.DERYCKERE,E.WOOD,         
JRNL        AUTH 3 D.K.GRAHAM,H.S.EARP,D.KIREEV,S.V.FRYE                        
JRNL        TITL   DESIGN AND SYNTHESIS OF NOVEL MACROCYCLIC MER TYROSINE       
JRNL        TITL 2 KINASE INHIBITORS.                                           
JRNL        REF    ACS MED CHEM LETT             V.   7  1044 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   27994735                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00221                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1261                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 17714                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1772                            
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 34.5498 -  5.9736    1.00     1461   163  0.1925 0.2354        
REMARK   3     2  5.9736 -  4.7454    1.00     1434   159  0.1762 0.2076        
REMARK   3     3  4.7454 -  4.1466    1.00     1427   158  0.1599 0.1831        
REMARK   3     4  4.1466 -  3.7680    1.00     1428   159  0.1684 0.2240        
REMARK   3     5  3.7680 -  3.4982    1.00     1438   160  0.1857 0.2256        
REMARK   3     6  3.4982 -  3.2921    1.00     1413   157  0.1995 0.2789        
REMARK   3     7  3.2921 -  3.1274    1.00     1423   158  0.2323 0.3457        
REMARK   3     8  3.1274 -  2.9913    0.98     1380   154  0.2415 0.3189        
REMARK   3     9  2.9913 -  2.8762    0.85     1197   133  0.2394 0.3258        
REMARK   3    10  2.8762 -  2.7770    0.73     1045   116  0.2365 0.2935        
REMARK   3    11  2.7770 -  2.6902    0.65      910   101  0.2399 0.3192        
REMARK   3    12  2.6902 -  2.6134    0.54      769    85  0.2458 0.3441        
REMARK   3    13  2.6134 -  2.5446    0.44      617    69  0.2387 0.2717        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           4276                                  
REMARK   3   ANGLE     :  0.720           5782                                  
REMARK   3   CHIRALITY :  0.043            640                                  
REMARK   3   PLANARITY :  0.003            722                                  
REMARK   3   DIHEDRAL  : 13.799           1650                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 577 THROUGH 612 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8882  -9.3694  19.0199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3393 T22:   0.4068                                     
REMARK   3      T33:   0.3344 T12:   0.0389                                     
REMARK   3      T13:  -0.0479 T23:  -0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1120 L22:   8.9855                                     
REMARK   3      L33:   9.4433 L12:   0.0587                                     
REMARK   3      L13:   1.7826 L23:   0.5027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1617 S12:  -0.6049 S13:  -0.4162                       
REMARK   3      S21:  -0.0165 S22:  -0.0011 S23:  -0.5112                       
REMARK   3      S31:   0.3193 S32:   0.6197 S33:  -0.1983                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 613 THROUGH 628 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4194  -2.0477  25.3059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3393 T22:   0.8161                                     
REMARK   3      T33:   0.5253 T12:   0.0619                                     
REMARK   3      T13:  -0.1457 T23:  -0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7053 L22:   0.3790                                     
REMARK   3      L33:   3.9801 L12:   0.8658                                     
REMARK   3      L13:   4.1486 L23:   0.4601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6445 S12:  -0.3191 S13:   0.3293                       
REMARK   3      S21:   0.0186 S22:  -0.0298 S23:  -0.5604                       
REMARK   3      S31:   0.0784 S32:   0.9512 S33:   0.2963                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 629 THROUGH 651 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6430  -4.3540  33.4314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5409 T22:   0.5161                                     
REMARK   3      T33:   0.4675 T12:   0.0142                                     
REMARK   3      T13:   0.0457 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5886 L22:   7.0578                                     
REMARK   3      L33:   8.8664 L12:  -4.6811                                     
REMARK   3      L13:   4.4333 L23:  -3.9487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3731 S12:   0.6518 S13:   0.0627                       
REMARK   3      S21:   0.6522 S22:  -0.2473 S23:  -0.8100                       
REMARK   3      S31:  -0.1660 S32:   1.4965 S33:  -0.1297                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 652 THROUGH 763 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4818   4.1131  23.8314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2118 T22:   0.2423                                     
REMARK   3      T33:   0.2538 T12:  -0.0362                                     
REMARK   3      T13:  -0.0190 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5908 L22:   4.2866                                     
REMARK   3      L33:   2.9471 L12:  -1.0789                                     
REMARK   3      L13:  -1.2147 L23:  -0.2191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0311 S12:  -0.1054 S13:  -0.2210                       
REMARK   3      S21:  -0.2559 S22:   0.1455 S23:   0.1037                       
REMARK   3      S31:   0.2046 S32:   0.1161 S33:  -0.1978                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 764 THROUGH 814 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4686  19.7738  32.6040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2444 T22:   0.3360                                     
REMARK   3      T33:   0.3794 T12:  -0.0726                                     
REMARK   3      T13:  -0.0235 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5398 L22:   5.5246                                     
REMARK   3      L33:   5.6827 L12:  -0.1019                                     
REMARK   3      L13:  -0.6500 L23:  -0.1334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1998 S12:  -0.3504 S13:   0.3940                       
REMARK   3      S21:   0.4138 S22:  -0.0403 S23:  -0.6326                       
REMARK   3      S31:  -0.6994 S32:   0.5306 S33:  -0.1567                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 815 THROUGH 863 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1189  16.5468  34.6716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2245 T22:   0.3238                                     
REMARK   3      T33:   0.2554 T12:   0.0302                                     
REMARK   3      T13:   0.1101 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9423 L22:   5.9934                                     
REMARK   3      L33:   3.9837 L12:   0.9277                                     
REMARK   3      L13:  -0.0050 L23:  -0.7666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0484 S12:  -0.2144 S13:  -0.0136                       
REMARK   3      S21:   0.2252 S22:   0.1802 S23:   0.1548                       
REMARK   3      S31:  -0.4129 S32:  -0.5894 S33:  -0.1961                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 577 THROUGH 643 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7316  51.4224  17.7656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3275 T22:   0.5010                                     
REMARK   3      T33:   0.3098 T12:  -0.1135                                     
REMARK   3      T13:  -0.0387 T23:  -0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6950 L22:   3.9328                                     
REMARK   3      L33:   5.8155 L12:   0.3533                                     
REMARK   3      L13:  -2.4181 L23:  -1.5327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0953 S12:   0.3173 S13:   0.2254                       
REMARK   3      S21:  -0.3162 S22:   0.1542 S23:  -0.0873                       
REMARK   3      S31:  -0.4202 S32:   0.7967 S33:  -0.2492                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 644 THROUGH 678 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7642  47.7370  15.2608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3380 T22:   0.5414                                     
REMARK   3      T33:   0.2394 T12:  -0.0523                                     
REMARK   3      T13:   0.0029 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5040 L22:   4.5110                                     
REMARK   3      L33:   2.6625 L12:   2.7875                                     
REMARK   3      L13:   2.6588 L23:   1.4333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1736 S12:   0.0143 S13:   0.0607                       
REMARK   3      S21:   0.0482 S22:   0.1085 S23:  -0.0171                       
REMARK   3      S31:   0.0967 S32:   0.9189 S33:   0.0904                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 679 THROUGH 862 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1040  29.2947   3.7596              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1986 T22:   0.2601                                     
REMARK   3      T33:   0.2486 T12:  -0.0427                                     
REMARK   3      T13:  -0.0093 T23:   0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4004 L22:   5.0714                                     
REMARK   3      L33:   5.2733 L12:  -0.2269                                     
REMARK   3      L13:  -0.1218 L23:  -1.0100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0163 S12:   0.0676 S13:  -0.0195                       
REMARK   3      S21:  -0.1005 S22:  -0.0100 S23:  -0.1426                       
REMARK   3      S31:   0.1548 S32:   0.1222 S33:   0.0109                       
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 5K0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220286.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.545                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 3BRB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 32.5 MG/ML (IN 20 MM TRIS     
REMARK 280  PH 8.0, 500 MM NACL, 2MM BME) WAS INCUBATED OVERNIGHT WITH          
REMARK 280  INHIBITOR AT 2.5 MM FINAL CONCENTRATION, AND THEN WAS MIXED 1:1     
REMARK 280  WITH CRYSTALLIZATION SOLUTION (27-33% (V/V) PEG 400, 200 MM         
REMARK 280  MGCL2, 100 MM TRIS PH 8.5)., VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 285.2K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.65750            
REMARK 290   SMTRY3   2  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   552                                                      
REMARK 465     GLY A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     SER A   555                                                      
REMARK 465     HIS A   556                                                      
REMARK 465     HIS A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     HIS A   561                                                      
REMARK 465     SER A   562                                                      
REMARK 465     SER A   563                                                      
REMARK 465     GLY A   564                                                      
REMARK 465     LEU A   565                                                      
REMARK 465     VAL A   566                                                      
REMARK 465     PRO A   567                                                      
REMARK 465     ARG A   568                                                      
REMARK 465     GLY A   569                                                      
REMARK 465     SER A   570                                                      
REMARK 465     GLU A   571                                                      
REMARK 465     GLU A   572                                                      
REMARK 465     LEU A   573                                                      
REMARK 465     GLN A   574                                                      
REMARK 465     ASN A   575                                                      
REMARK 465     LYS A   576                                                      
REMARK 465     GLY A   596                                                      
REMARK 465     GLU A   597                                                      
REMARK 465     PHE A   598                                                      
REMARK 465     MET A   659                                                      
REMARK 465     SER A   660                                                      
REMARK 465     SER A   661                                                      
REMARK 465     GLN A   662                                                      
REMARK 465     GLY A   663                                                      
REMARK 465     ILE A   664                                                      
REMARK 465     SER A   745                                                      
REMARK 465     LYS A   746                                                      
REMARK 465     LYS A   747                                                      
REMARK 465     ILE A   748                                                      
REMARK 465     TYR A   749                                                      
REMARK 465     SER A   750                                                      
REMARK 465     GLY A   751                                                      
REMARK 465     ASP A   752                                                      
REMARK 465     TYR A   753                                                      
REMARK 465     TYR A   754                                                      
REMARK 465     ARG A   755                                                      
REMARK 465     GLN A   756                                                      
REMARK 465     GLY A   757                                                      
REMARK 465     ARG A   758                                                      
REMARK 465     ILE A   759                                                      
REMARK 465     ALA A   760                                                      
REMARK 465     LYS A   761                                                      
REMARK 465     MET A   762                                                      
REMARK 465     VAL A   864                                                      
REMARK 465     MET B   552                                                      
REMARK 465     GLY B   553                                                      
REMARK 465     SER B   554                                                      
REMARK 465     SER B   555                                                      
REMARK 465     HIS B   556                                                      
REMARK 465     HIS B   557                                                      
REMARK 465     HIS B   558                                                      
REMARK 465     HIS B   559                                                      
REMARK 465     HIS B   560                                                      
REMARK 465     HIS B   561                                                      
REMARK 465     SER B   562                                                      
REMARK 465     SER B   563                                                      
REMARK 465     GLY B   564                                                      
REMARK 465     LEU B   565                                                      
REMARK 465     VAL B   566                                                      
REMARK 465     PRO B   567                                                      
REMARK 465     ARG B   568                                                      
REMARK 465     GLY B   569                                                      
REMARK 465     SER B   570                                                      
REMARK 465     GLU B   571                                                      
REMARK 465     GLU B   572                                                      
REMARK 465     LEU B   573                                                      
REMARK 465     GLN B   574                                                      
REMARK 465     ASN B   575                                                      
REMARK 465     LYS B   576                                                      
REMARK 465     GLU B   597                                                      
REMARK 465     PHE B   598                                                      
REMARK 465     MET B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     LEU B   623                                                      
REMARK 465     ASP B   624                                                      
REMARK 465     ASN B   625                                                      
REMARK 465     SER B   626                                                      
REMARK 465     SER B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     ARG B   629                                                      
REMARK 465     GLU B   630                                                      
REMARK 465     ILE B   631                                                      
REMARK 465     GLU B   632                                                      
REMARK 465     GLU B   633                                                      
REMARK 465     PHE B   634                                                      
REMARK 465     LEU B   635                                                      
REMARK 465     SER B   636                                                      
REMARK 465     GLY B   743                                                      
REMARK 465     LEU B   744                                                      
REMARK 465     SER B   745                                                      
REMARK 465     LYS B   746                                                      
REMARK 465     LYS B   747                                                      
REMARK 465     ILE B   748                                                      
REMARK 465     TYR B   749                                                      
REMARK 465     SER B   750                                                      
REMARK 465     GLY B   751                                                      
REMARK 465     ASP B   752                                                      
REMARK 465     TYR B   753                                                      
REMARK 465     TYR B   754                                                      
REMARK 465     ARG B   755                                                      
REMARK 465     GLN B   756                                                      
REMARK 465     GLY B   757                                                      
REMARK 465     ARG B   758                                                      
REMARK 465     ILE B   759                                                      
REMARK 465     ALA B   760                                                      
REMARK 465     LYS B   761                                                      
REMARK 465     MET B   762                                                      
REMARK 465     ASP B   863                                                      
REMARK 465     VAL B   864                                                      
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    GLU A   689     HG1  THR A   690              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    THR A 690      -51.89     70.42                                   
REMARK 500    PRO A 692      152.21    -46.03                                   
REMARK 500    ASP A 723       43.54   -163.93                                   
REMARK 500    THR B 690      -56.31     70.85                                   
REMARK 500    ARG B 722       -7.68     74.51                                   
REMARK 500    ASP B 723       55.16   -155.02                                   
REMARK 500    ASN B 728       41.67   -106.19                                   
REMARK 500    ALA B 773      -68.58    -96.91                                   
REMARK 500    ASP B 824       67.03   -104.96                                   
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 B 903  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 728   OD1                                                    
REMARK 620 2 ASP B 741   OD1  85.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Q1 A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 905                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Q1 B 904                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5K0X   RELATED DB: PDB                                   
DBREF  5K0K A  570   864  UNP    Q12866   MERTK_HUMAN    570    864             
DBREF  5K0K B  570   864  UNP    Q12866   MERTK_HUMAN    570    864             
SEQADV 5K0K MET A  552  UNP  Q12866              INITIATING METHIONINE          
SEQADV 5K0K GLY A  553  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER A  554  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER A  555  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  556  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  557  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  558  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  559  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  560  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS A  561  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER A  562  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER A  563  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K GLY A  564  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K LEU A  565  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K VAL A  566  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K PRO A  567  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K ARG A  568  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K GLY A  569  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K MET B  552  UNP  Q12866              INITIATING METHIONINE          
SEQADV 5K0K GLY B  553  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER B  554  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER B  555  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  556  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  557  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  558  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  559  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  560  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K HIS B  561  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER B  562  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K SER B  563  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K GLY B  564  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K LEU B  565  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K VAL B  566  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K PRO B  567  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K ARG B  568  UNP  Q12866              EXPRESSION TAG                 
SEQADV 5K0K GLY B  569  UNP  Q12866              EXPRESSION TAG                 
SEQRES   1 A  313  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  313  LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU          
SEQRES   3 A  313  GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY          
SEQRES   4 A  313  LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU          
SEQRES   5 A  313  GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL          
SEQRES   6 A  313  ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG          
SEQRES   7 A  313  GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS          
SEQRES   8 A  313  ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL          
SEQRES   9 A  313  CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET          
SEQRES  10 A  313  VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR          
SEQRES  11 A  313  TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS          
SEQRES  12 A  313  ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE          
SEQRES  13 A  313  ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU          
SEQRES  14 A  313  HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP          
SEQRES  15 A  313  ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS          
SEQRES  16 A  313  LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE          
SEQRES  17 A  313  ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU          
SEQRES  18 A  313  ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA          
SEQRES  19 A  313  PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET          
SEQRES  20 A  313  THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP          
SEQRES  21 A  313  TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP          
SEQRES  22 A  313  CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP          
SEQRES  23 A  313  ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU          
SEQRES  24 A  313  ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP          
SEQRES  25 A  313  VAL                                                          
SEQRES   1 B  313  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  313  LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU          
SEQRES   3 B  313  GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY          
SEQRES   4 B  313  LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU          
SEQRES   5 B  313  GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL          
SEQRES   6 B  313  ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG          
SEQRES   7 B  313  GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS          
SEQRES   8 B  313  ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL          
SEQRES   9 B  313  CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET          
SEQRES  10 B  313  VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR          
SEQRES  11 B  313  TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS          
SEQRES  12 B  313  ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE          
SEQRES  13 B  313  ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU          
SEQRES  14 B  313  HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP          
SEQRES  15 B  313  ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS          
SEQRES  16 B  313  LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE          
SEQRES  17 B  313  ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU          
SEQRES  18 B  313  ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA          
SEQRES  19 B  313  PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET          
SEQRES  20 B  313  THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP          
SEQRES  21 B  313  TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP          
SEQRES  22 B  313  CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP          
SEQRES  23 B  313  ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU          
SEQRES  24 B  313  ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP          
SEQRES  25 B  313  VAL                                                          
HET     CL  A 901       1                                                       
HET     CL  A 902       1                                                       
HET     CL  A 903       1                                                       
HET    6Q1  A 904      69                                                       
HET     CL  A 905       1                                                       
HET     CL  B 901       1                                                       
HET     CL  B 902       1                                                       
HET     MG  B 903       1                                                       
HET    6Q1  B 904      69                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     6Q1 15-{4-[(4-METHYLPIPERAZIN-1-YL)METHYL]PHENYL}-4,5,6,7,           
HETNAM   2 6Q1  9,10,11,12-OCTAHYDRO-2,16-(AZENOMETHENO)PYRROLO[2,1-            
HETNAM   3 6Q1  D][1,3,5,9]TE TRAAZACYCLOTETRADECIN-8(3H)-ONE                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     6Q1 UNC2434                                                          
FORMUL   3   CL    6(CL 1-)                                                     
FORMUL   6  6Q1    2(C26 H35 N7 O)                                              
FORMUL  10   MG    MG 2+                                                        
FORMUL  12  HOH   *28(H2 O)                                                     
HELIX    1 AA1 ASP A  583  ASN A  585  5                                   3    
HELIX    2 AA2 GLN A  628  LYS A  642  1                                  15    
HELIX    3 AA3 ASP A  678  ARG A  687  1                                  10    
HELIX    4 AA4 PRO A  696  ARG A  717  1                                  22    
HELIX    5 AA5 ALA A  725  ARG A  727  5                                   3    
HELIX    6 AA6 PRO A  763  ILE A  767  5                                   5    
HELIX    7 AA7 ALA A  768  ASP A  774  1                                   7    
HELIX    8 AA8 THR A  778  THR A  795  1                                  18    
HELIX    9 AA9 GLN A  805  HIS A  807  5                                   3    
HELIX   10 AB1 GLU A  808  HIS A  815  1                                   8    
HELIX   11 AB2 LEU A  826  CYS A  836  1                                  11    
HELIX   12 AB3 THR A  846  SER A  860  1                                  15    
HELIX   13 AB4 ASP B  583  ASN B  585  5                                   3    
HELIX   14 AB5 ALA B  638  PHE B  644  1                                   7    
HELIX   15 AB6 ASP B  678  SER B  686  1                                   9    
HELIX   16 AB7 PRO B  696  ARG B  717  1                                  22    
HELIX   17 AB8 ALA B  725  ARG B  727  5                                   3    
HELIX   18 AB9 PRO B  763  ILE B  767  5                                   5    
HELIX   19 AC1 ALA B  768  ASP B  774  1                                   7    
HELIX   20 AC2 THR B  778  THR B  795  1                                  18    
HELIX   21 AC3 GLN B  805  HIS B  807  5                                   3    
HELIX   22 AC4 GLU B  808  HIS B  815  1                                   8    
HELIX   23 AC5 LEU B  826  SER B  835  1                                  10    
HELIX   24 AC6 CYS B  836  ARG B  838  5                                   3    
HELIX   25 AC7 ASP B  840  ARG B  844  5                                   5    
HELIX   26 AC8 THR B  846  LEU B  861  1                                  16    
SHEET    1 AA1 5 LEU A 587  GLY A 594  0                                        
SHEET    2 AA1 5 VAL A 601  LYS A 607 -1  O  VAL A 601   N  GLY A 594           
SHEET    3 AA1 5 SER A 613  THR A 620 -1  O  LEU A 614   N  LEU A 606           
SHEET    4 AA1 5 PRO A 667  PRO A 672 -1  O  LEU A 671   N  ALA A 617           
SHEET    5 AA1 5 GLY A 654  ILE A 657 -1  N  GLY A 654   O  ILE A 670           
SHEET    1 AA2 2 CYS A 729  LEU A 731  0                                        
SHEET    2 AA2 2 VAL A 737  VAL A 739 -1  O  CYS A 738   N  MET A 730           
SHEET    1 AA3 5 LEU B 587  GLY B 594  0                                        
SHEET    2 AA3 5 VAL B 601  LYS B 607 -1  O  VAL B 601   N  GLY B 594           
SHEET    3 AA3 5 SER B 613  LYS B 619 -1  O  LEU B 614   N  LEU B 606           
SHEET    4 AA3 5 PRO B 665  PRO B 672 -1  O  LEU B 671   N  ALA B 617           
SHEET    5 AA3 5 GLY B 654  MET B 659 -1  N  GLU B 658   O  LYS B 666           
SHEET    1 AA4 2 CYS B 729  LEU B 731  0                                        
SHEET    2 AA4 2 VAL B 737  VAL B 739 -1  O  CYS B 738   N  MET B 730           
LINK         OD1AASN B 728                MG    MG B 903     1555   1555  2.17  
LINK         OD1 ASP B 741                MG    MG B 903     1555   1555  2.26  
SITE     1 AC1  2 ARG A 651  ARG A 732                                          
SITE     1 AC2  2 PRO A 802  LYS A 820                                          
SITE     1 AC3  3 ARG A 584  ILE A 588  LEU A 589                               
SITE     1 AC4 10 ALA A 617  ILE A 650  LEU A 671  PRO A 672                    
SITE     2 AC4 10 PHE A 673  MET A 674  LYS A 675  ARG A 727                    
SITE     3 AC4 10 MET A 730  ALA A 740                                          
SITE     1 AC5  3 ARG A 687  HOH A1010  ARG B 687                               
SITE     1 AC6  3 ARG B 584  ILE B 588  LEU B 589                               
SITE     1 AC7  2 LEU B 819  LYS B 820                                          
SITE     1 AC8  2 ASN B 728  ASP B 741                                          
SITE     1 AC9  9 LYS B 591  VAL B 601  ALA B 617  PRO B 672                    
SITE     2 AC9  9 PHE B 673  MET B 674  LYS B 675  MET B 730                    
SITE     3 AC9  9 ASP B 741                                                     
CRYST1   51.072   91.315   69.203  90.00 100.42  90.00 P 1 21 1      4          
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      0.019580  0.000000  0.003599        0.00000                         
SCALE2      0.000000  0.010951  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system