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HEADER    TRANSFERASE/TRANSFERASE INHBITOR        31-AUG-17   6AUD              
TITLE     PI3K-GAMMA K802T IN COMPLEX WITH CPD 8 10-((1-(TERT-BUTYL)PIPERIDIN-4-
TITLE    2 YL)SULFINYL)-2-(1-ISOPROPYL-1H-1,2,4-TRIAZOL-5-YL)-5,6-              
TITLE    3 DIHYDROBENZO[F]IMIDAZO[1,2-D][1,4]OXAZEPINE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: P110 GAMMA, RESIDUES 144-1102;                             
COMPND   6 SYNONYM: PTDINS-3-KINASE SUBUNIT GAMMA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   7 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT GAMMA,P110GAMMA,     
COMPND   8 PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,               
COMPND   9 SERINE/THREONINE PROTEIN KINASE PIK3CG,P120-PI3K;                    
COMPND  10 EC: 2.7.1.153,2.7.11.1;                                              
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CG;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    P110 DELTA, SBDD, TRANSFERASE-TRANSFERASE INHBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.MURRAY,M.ULTSCH                                                   
REVDAT   1   15-NOV-17 6AUD    0                                                
JRNL        AUTH   B.S.SAFINA,R.L.ELLIOTT,A.K.FORREST,R.A.HEALD,J.M.MURRAY,     
JRNL        AUTH 2 J.NONOMIYA,J.PANG,L.SALPHATI,E.M.SEWARD,S.T.STABEN,M.ULTSCH, 
JRNL        AUTH 3 B.WEI,W.YANG,D.P.SUTHERLIN                                   
JRNL        TITL   DESIGN OF SELECTIVE BENZOXAZEPIN PI3K DELTA INHIBITORS       
JRNL        TITL 2 THROUGH CONTROL OF DIHEDRAL ANGLES.                          
JRNL        REF    ACS MED CHEM LETT             V.   8   936 2017              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   28947940                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.7B00170                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12-2829_FINAL)                             
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) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 60446                          
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) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3017                            
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 28.1214 -  5.6312    0.99     2730   140  0.1796 0.1945        
REMARK   3     2  5.6312 -  4.4755    1.00     2648   142  0.1674 0.1999        
REMARK   3     3  4.4755 -  3.9115    1.00     2628   160  0.1660 0.1849        
REMARK   3     4  3.9115 -  3.5546    1.00     2676   136  0.1761 0.2105        
REMARK   3     5  3.5546 -  3.3002    1.00     2609   149  0.1967 0.2346        
REMARK   3     6  3.3002 -  3.1059    1.00     2644   125  0.2120 0.2439        
REMARK   3     7  3.1059 -  2.9506    1.00     2642   151  0.2259 0.2622        
REMARK   3     8  2.9506 -  2.8222    1.00     2640   141  0.2261 0.2262        
REMARK   3     9  2.8222 -  2.7137    1.00     2595   152  0.2294 0.2799        
REMARK   3    10  2.7137 -  2.6201    1.00     2645   124  0.2278 0.2837        
REMARK   3    11  2.6201 -  2.5382    1.00     2625   128  0.2291 0.2915        
REMARK   3    12  2.5382 -  2.4657    1.00     2641   142  0.2293 0.2592        
REMARK   3    13  2.4657 -  2.4009    1.00     2589   143  0.2316 0.2879        
REMARK   3    14  2.4009 -  2.3423    1.00     2653   123  0.2266 0.2785        
REMARK   3    15  2.3423 -  2.2891    1.00     2621   139  0.2232 0.2813        
REMARK   3    16  2.2891 -  2.2404    1.00     2645   137  0.2381 0.3057        
REMARK   3    17  2.2404 -  2.1956    1.00     2581   135  0.2501 0.2671        
REMARK   3    18  2.1956 -  2.1542    1.00     2665   129  0.2471 0.2992        
REMARK   3    19  2.1542 -  2.1157    1.00     2602   140  0.2515 0.2644        
REMARK   3    20  2.1157 -  2.0799    1.00     2584   139  0.2598 0.2637        
REMARK   3    21  2.0799 -  2.0463    1.00     2664   131  0.2667 0.3190        
REMARK   3    22  2.0463 -  2.0149    0.82     2102   111  0.2804 0.3090        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6983                                  
REMARK   3   ANGLE     :  0.593           9454                                  
REMARK   3   CHIRALITY :  0.042           1062                                  
REMARK   3   PLANARITY :  0.004           1196                                  
REMARK   3   DIHEDRAL  : 16.218           4199                                  
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 144:190)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6206 -38.2775   7.7210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4332 T22:   0.3918                                     
REMARK   3      T33:   0.3738 T12:   0.0380                                     
REMARK   3      T13:  -0.0412 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5933 L22:   0.7651                                     
REMARK   3      L33:   0.4692 L12:  -0.4619                                     
REMARK   3      L13:   0.1790 L23:   0.2285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0994 S12:   0.5107 S13:  -0.3895                       
REMARK   3      S21:  -0.2409 S22:  -0.0140 S23:   0.0321                       
REMARK   3      S31:   0.4207 S32:   0.1279 S33:   0.0016                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 191:321)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0114 -33.0973  32.4045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3197 T22:   0.5244                                     
REMARK   3      T33:   0.4527 T12:  -0.0331                                     
REMARK   3      T13:   0.0803 T23:   0.1112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1607 L22:   1.9530                                     
REMARK   3      L33:   2.1779 L12:   0.0982                                     
REMARK   3      L13:   0.6150 L23:  -0.5508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1327 S12:  -0.4345 S13:  -0.0345                       
REMARK   3      S21:   0.2055 S22:   0.0401 S23:   0.3534                       
REMARK   3      S31:  -0.0779 S32:  -0.7603 S33:   0.0139                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 350:488)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2157 -22.8730  12.1194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2231 T22:   0.2808                                     
REMARK   3      T33:   0.2180 T12:   0.0250                                     
REMARK   3      T13:  -0.0077 T23:  -0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1376 L22:   0.7172                                     
REMARK   3      L33:   2.5899 L12:   0.2462                                     
REMARK   3      L13:   0.0162 L23:  -0.2898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0534 S12:  -0.2633 S13:   0.1010                       
REMARK   3      S21:   0.0722 S22:  -0.0565 S23:   0.0639                       
REMARK   3      S31:  -0.0697 S32:   0.3311 S33:  -0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 495:533)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  52.8618 -25.5946  10.2434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3542 T22:   0.3423                                     
REMARK   3      T33:   0.2886 T12:   0.0397                                     
REMARK   3      T13:   0.0487 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5590 L22:   0.4133                                     
REMARK   3      L33:   0.9086 L12:   0.4464                                     
REMARK   3      L13:  -0.1583 L23:   0.4737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0028 S12:  -0.1897 S13:  -0.0306                       
REMARK   3      S21:  -0.2121 S22:  -0.0536 S23:   0.2426                       
REMARK   3      S31:   0.2706 S32:   0.1116 S33:  -0.0139                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 544:725)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8489 -30.7099  31.5402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2703 T22:   0.2854                                     
REMARK   3      T33:   0.2814 T12:   0.0357                                     
REMARK   3      T13:   0.0004 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2380 L22:   0.1613                                     
REMARK   3      L33:   1.4775 L12:  -0.2134                                     
REMARK   3      L13:   1.5525 L23:  -0.1448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0134 S12:  -0.3163 S13:  -0.1045                       
REMARK   3      S21:   0.0715 S22:   0.0100 S23:  -0.0482                       
REMARK   3      S31:   0.0395 S32:   0.0015 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 726:836)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0051 -14.4440   8.8709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3479 T22:   0.3088                                     
REMARK   3      T33:   0.3323 T12:   0.0067                                     
REMARK   3      T13:  -0.0299 T23:   0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5016 L22:   2.0334                                     
REMARK   3      L33:   1.4914 L12:  -1.3744                                     
REMARK   3      L13:   0.6186 L23:  -0.8162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0257 S12:   0.1857 S13:   0.1006                       
REMARK   3      S21:  -0.2487 S22:   0.0413 S23:   0.0560                       
REMARK   3      S31:  -0.2002 S32:  -0.0939 S33:   0.0004                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 837:866)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8379 -15.9339  32.5812              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3578 T22:   0.2670                                     
REMARK   3      T33:   0.2927 T12:   0.0563                                     
REMARK   3      T13:   0.0408 T23:   0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7556 L22:   0.7883                                     
REMARK   3      L33:   0.4514 L12:  -0.0080                                     
REMARK   3      L13:   0.4869 L23:   0.3958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0876 S12:   0.0763 S13:  -0.2321                       
REMARK   3      S21:   0.3863 S22:  -0.0608 S23:   0.1867                       
REMARK   3      S31:   0.0662 S32:   0.0052 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 867:881)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9547 -14.5983  16.2317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3175 T22:   0.2536                                     
REMARK   3      T33:   0.3165 T12:   0.0508                                     
REMARK   3      T13:   0.0232 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1295 L22:   0.2189                                     
REMARK   3      L33:   0.2125 L12:  -0.0694                                     
REMARK   3      L13:   0.1672 L23:   0.0184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0503 S12:   0.1281 S13:   0.2697                       
REMARK   3      S21:  -0.3596 S22:   0.1298 S23:  -0.2965                       
REMARK   3      S31:   0.0072 S32:   0.4546 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 882:1090)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6445  -1.9535  35.3057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3437 T22:   0.2640                                     
REMARK   3      T33:   0.2748 T12:   0.0143                                     
REMARK   3      T13:  -0.0046 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0161 L22:   2.1889                                     
REMARK   3      L33:   2.0447 L12:  -0.9143                                     
REMARK   3      L13:   0.3258 L23:  -0.6019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:  -0.1668 S13:   0.3078                       
REMARK   3      S21:   0.2300 S22:   0.0441 S23:  -0.2112                       
REMARK   3      S31:  -0.3431 S32:   0.0740 S33:  -0.0020                       
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 6AUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229853.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-10                          
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) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60464                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3R7R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 0.2M NH4SO4, 0.1M TRIS-HCL     
REMARK 280  8.5, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 289K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       69.52550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       69.52550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.03250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: MONOMER AS DETERMINED BYGEL FILTRATION                       
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1557  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1589  LIES ON A SPECIAL POSITION.                          
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     LYS A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     MET A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     ILE A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     TRP A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     TRP A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     VAL A   458                                                      
REMARK 465     GLN A   459                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     SER A   496                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     LEU A   529                                                      
REMARK 465     PRO A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     HIS A   532                                                      
REMARK 465     GLN A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     THR A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     VAL A   543                                                      
REMARK 465     ARG A   544                                                      
REMARK 465     ALA A   545                                                      
REMARK 465     LEU A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     LYS A   980                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     ILE A  1094                                                      
REMARK 465     LYS A  1095                                                      
REMARK 465     GLN A  1096                                                      
REMARK 465     GLY A  1097                                                      
REMARK 465     GLU A  1098                                                      
REMARK 465     LYS A  1099                                                      
REMARK 465     HIS A  1100                                                      
REMARK 465     SER A  1101                                                      
REMARK 465     ALA A  1102                                                      
REMARK 465     HIS A  1103                                                      
REMARK 465     HIS A  1104                                                      
REMARK 465     HIS A  1105                                                      
REMARK 465     HIS A  1106                                                      
REMARK 465     HIS A  1107                                                      
REMARK 465     HIS A  1108                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A 143    CG   SD   CE                                        
REMARK 470     GLU A 322    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN A 376    CG   OD1  ND2                                       
REMARK 470     LEU A1042    CG   CD1  CD2                                       
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    ASN A 167       53.07   -147.36                                   
REMARK 500    HIS A 199       61.47     38.74                                   
REMARK 500    SER A 227     -122.98     59.56                                   
REMARK 500    LYS A 251       41.80    -76.19                                   
REMARK 500    MET A 252      -75.45   -127.11                                   
REMARK 500    ASP A 269       43.08   -144.71                                   
REMARK 500    THR A 377     -179.14     72.37                                   
REMARK 500    TRP A 410      -52.54   -127.23                                   
REMARK 500    PRO A 526     -170.69    -64.19                                   
REMARK 500    PHE A 578       37.70    -91.30                                   
REMARK 500    GLN A 705       -6.28   -147.53                                   
REMARK 500    ALA A 901       79.31   -101.98                                   
REMARK 500    HIS A 967      -64.50   -136.47                                   
REMARK 500    LYS A1001      100.50   -160.60                                   
REMARK 500    GLU A1046      -55.73   -141.43                                   
REMARK 500    THR A1056       59.58     32.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1590        DISTANCE =  7.07 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BWY A 1201                
DBREF  6AUD A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 6AUD MET A  143  UNP  P48736              INITIATING METHIONINE          
SEQADV 6AUD THR A  802  UNP  P48736    LYS   802 ENGINEERED MUTATION            
SEQADV 6AUD HIS A 1103  UNP  P48736              EXPRESSION TAG                 
SEQADV 6AUD HIS A 1104  UNP  P48736              EXPRESSION TAG                 
SEQADV 6AUD HIS A 1105  UNP  P48736              EXPRESSION TAG                 
SEQADV 6AUD HIS A 1106  UNP  P48736              EXPRESSION TAG                 
SEQADV 6AUD HIS A 1107  UNP  P48736              EXPRESSION TAG                 
SEQADV 6AUD HIS A 1108  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  966  MET SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR          
SEQRES   2 A  966  ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL          
SEQRES   3 A  966  HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL          
SEQRES   4 A  966  THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS          
SEQRES   5 A  966  LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU          
SEQRES   6 A  966  PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE          
SEQRES   7 A  966  PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE          
SEQRES   8 A  966  LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN          
SEQRES   9 A  966  SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET          
SEQRES  10 A  966  ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU          
SEQRES  11 A  966  ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR          
SEQRES  12 A  966  PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS          
SEQRES  13 A  966  ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO          
SEQRES  14 A  966  ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO          
SEQRES  15 A  966  LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU          
SEQRES  16 A  966  GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE          
SEQRES  17 A  966  THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL          
SEQRES  18 A  966  LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN          
SEQRES  19 A  966  THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS          
SEQRES  20 A  966  GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS          
SEQRES  21 A  966  PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU          
SEQRES  22 A  966  PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU          
SEQRES  23 A  966  LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU          
SEQRES  24 A  966  SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER          
SEQRES  25 A  966  LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU          
SEQRES  26 A  966  LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR          
SEQRES  27 A  966  VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP          
SEQRES  28 A  966  GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR          
SEQRES  29 A  966  ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU          
SEQRES  30 A  966  LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS          
SEQRES  31 A  966  GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA          
SEQRES  32 A  966  GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE          
SEQRES  33 A  966  ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP          
SEQRES  34 A  966  LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS          
SEQRES  35 A  966  HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS          
SEQRES  36 A  966  TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU          
SEQRES  37 A  966  LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP          
SEQRES  38 A  966  VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER          
SEQRES  39 A  966  ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU          
SEQRES  40 A  966  SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN          
SEQRES  41 A  966  LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER          
SEQRES  42 A  966  ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN          
SEQRES  43 A  966  LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER          
SEQRES  44 A  966  GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA          
SEQRES  45 A  966  VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA          
SEQRES  46 A  966  MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU          
SEQRES  47 A  966  MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER          
SEQRES  48 A  966  ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN          
SEQRES  49 A  966  LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU          
SEQRES  50 A  966  PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS          
SEQRES  51 A  966  ALA GLY ALA LEU ALA ILE GLU LYS CYS THR VAL MET ALA          
SEQRES  52 A  966  SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA          
SEQRES  53 A  966  ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE          
SEQRES  54 A  966  PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE          
SEQRES  55 A  966  LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR          
SEQRES  56 A  966  GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE          
SEQRES  57 A  966  SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS          
SEQRES  58 A  966  ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL          
SEQRES  59 A  966  GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS          
SEQRES  60 A  966  TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN          
SEQRES  61 A  966  ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR          
SEQRES  62 A  966  CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS          
SEQRES  63 A  966  ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE          
SEQRES  64 A  966  HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER          
SEQRES  65 A  966  PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU          
SEQRES  66 A  966  THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS          
SEQRES  67 A  966  LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS          
SEQRES  68 A  966  VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU          
SEQRES  69 A  966  LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET          
SEQRES  70 A  966  PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG          
SEQRES  71 A  966  ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS          
SEQRES  72 A  966  LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS          
SEQRES  73 A  966  GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL          
SEQRES  74 A  966  LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA HIS HIS          
SEQRES  75 A  966  HIS HIS HIS HIS                                              
HET    BWY  A1201      34                                                       
HETNAM     BWY 10-[(S)-(1-TERT-BUTYLPIPERIDIN-4-YL)SULFINYL]-2-[1-              
HETNAM   2 BWY  (PROPAN-2-YL)-1H-1,2,4-TRIAZOL-5-YL]-5,6-                       
HETNAM   3 BWY  DIHYDROIMIDAZO[1,2-D][1,4]BENZOXAZEPINE                         
FORMUL   2  BWY    C25 H34 N6 O2 S                                              
FORMUL   3  HOH   *290(H2 O)                                                    
HELIX    1 AA1 SER A  144  GLY A  159  1                                  16    
HELIX    2 AA2 ASP A  171  LEU A  180  1                                  10    
HELIX    3 AA3 LEU A  180  ARG A  191  1                                  12    
HELIX    4 AA4 ASP A  192  HIS A  199  1                                   8    
HELIX    5 AA5 PRO A  208  LYS A  213  1                                   6    
HELIX    6 AA6 THR A  240  LYS A  251  1                                  12    
HELIX    7 AA7 PRO A  286  ASN A  289  5                                   4    
HELIX    8 AA8 PHE A  290  GLY A  300  1                                  11    
HELIX    9 AA9 ASP A  312  GLU A  317  5                                   6    
HELIX   10 AB1 LYS A  421  LEU A  423  5                                   3    
HELIX   11 AB2 ASN A  498  THR A  503  5                                   6    
HELIX   12 AB3 PRO A  548  THR A  561  1                                  14    
HELIX   13 AB4 THR A  568  PHE A  578  1                                  11    
HELIX   14 AB5 PHE A  578  LEU A  583  1                                   6    
HELIX   15 AB6 LYS A  584  LYS A  587  5                                   4    
HELIX   16 AB7 ALA A  588  SER A  594  1                                   7    
HELIX   17 AB8 GLN A  600  ARG A  613  1                                  14    
HELIX   18 AB9 ARG A  614  SER A  620  1                                   7    
HELIX   19 AC1 ASP A  623  LEU A  630  1                                   8    
HELIX   20 AC2 ASP A  637  GLU A  649  1                                  13    
HELIX   21 AC3 GLU A  652  VAL A  667  1                                  16    
HELIX   22 AC4 LYS A  668  GLU A  670  5                                   3    
HELIX   23 AC5 SER A  675  ASN A  688  1                                  14    
HELIX   24 AC6 ASN A  688  ALA A  704  1                                  17    
HELIX   25 AC7 TYR A  709  ARG A  722  1                                  14    
HELIX   26 AC8 GLY A  725  SER A  753  1                                  29    
HELIX   27 AC9 SER A  760  ASN A  776  1                                  17    
HELIX   28 AD1 ILE A  798  CYS A  801  5                                   4    
HELIX   29 AD2 ASP A  837  GLU A  858  1                                  22    
HELIX   30 AD3 ILE A  888  VAL A  896  1                                   9    
HELIX   31 AD4 GLU A  905  SER A  915  1                                  11    
HELIX   32 AD5 THR A  917  LEU A  942  1                                  26    
HELIX   33 AD6 HIS A  948  ASP A  950  5                                   3    
HELIX   34 AD7 THR A  988  MET A  995  1                                   8    
HELIX   35 AD8 SER A 1003  HIS A 1022  1                                  20    
HELIX   36 AD9 HIS A 1023  MET A 1039  1                                  17    
HELIX   37 AE1 GLU A 1046  ILE A 1048  5                                   3    
HELIX   38 AE2 GLU A 1049  LEU A 1055  1                                   7    
HELIX   39 AE3 ASN A 1060  GLY A 1079  1                                  20    
HELIX   40 AE4 TRP A 1080  LEU A 1090  1                                  11    
SHEET    1 AA1 5 THR A 229  VAL A 235  0                                        
SHEET    2 AA1 5 ILE A 220  ARG A 226 -1  N  ILE A 220   O  VAL A 235           
SHEET    3 AA1 5 ILE A 303  ASP A 308  1  O  VAL A 305   N  HIS A 225           
SHEET    4 AA1 5 VAL A 271  VAL A 274 -1  N  ARG A 273   O  VAL A 306           
SHEET    5 AA1 5 TYR A 280  LEU A 281 -1  O  LEU A 281   N  LEU A 272           
SHEET    1 AA2 4 GLU A 407  LYS A 419  0                                        
SHEET    2 AA2 4 LYS A 360  ASP A 369 -1  N  PHE A 361   O  PHE A 416           
SHEET    3 AA2 4 SER A 515  LEU A 520 -1  O  SER A 515   N  ASP A 369           
SHEET    4 AA2 4 GLY A 478  HIS A 483 -1  N  GLY A 478   O  LEU A 520           
SHEET    1 AA3 3 GLN A 392  ARG A 398  0                                        
SHEET    2 AA3 3 THR A 380  HIS A 389 -1  N  ALA A 385   O  ARG A 397           
SHEET    3 AA3 3 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1 AA4 5 GLN A 392  ARG A 398  0                                        
SHEET    2 AA4 5 THR A 380  HIS A 389 -1  N  ALA A 385   O  ARG A 397           
SHEET    3 AA4 5 LEU A 428  TYR A 434 -1  O  GLN A 432   N  GLU A 384           
SHEET    4 AA4 5 TYR A 462  LEU A 467 -1  O  LEU A 466   N  LEU A 429           
SHEET    5 AA4 5 TRP A 485  GLN A 486 -1  O  TRP A 485   N  TYR A 463           
SHEET    1 AA5 4 PHE A 783  VAL A 785  0                                        
SHEET    2 AA5 4 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3 AA5 4 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4 AA5 4 THR A 802  VAL A 803 -1  N  THR A 802   O  TRP A 812           
SHEET    1 AA6 6 PHE A 783  VAL A 785  0                                        
SHEET    2 AA6 6 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3 AA6 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4 AA6 6 ILE A 828  HIS A 834 -1  O  ILE A 828   N  PHE A 815           
SHEET    5 AA6 6 ILE A 876  GLU A 880 -1  O  ILE A 879   N  ILE A 831           
SHEET    6 AA6 6 CYS A 869  GLY A 873 -1  N  THR A 872   O  ILE A 876           
SHEET    1 AA7 3 ALA A 885  THR A 887  0                                        
SHEET    2 AA7 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3 AA7 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
CISPEP   1 ILE A  527    ALA A  528          0         0.75                     
CISPEP   2 ASN A  776    SER A  777          0         2.86                     
CISPEP   3 SER A  777    GLN A  778          0         4.29                     
CISPEP   4 HIS A  834    GLY A  835          0         2.97                     
CISPEP   5 THR A  899    GLY A  900          0        11.72                     
SITE     1 AC1 11 TRP A 812  LYS A 833  ILE A 879  GLU A 880                    
SITE     2 AC1 11 ILE A 881  VAL A 882  LYS A 890  MET A 953                    
SITE     3 AC1 11 ILE A 963  ASP A 964  HOH A1347                               
CRYST1  139.051   66.065  102.492  90.00  98.06  90.00 C 1 2 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      0.007192  0.000000  0.001019        0.00000                         
SCALE2      0.000000  0.015137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009854        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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