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Database: PDB
Entry: 4DJ2
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HEADER    PROTEIN BINDING                         01-FEB-12   4DJ2              
TITLE     UNWINDING THE DIFFERENCES OF THE MAMMALIAN PERIOD CLOCK PROTEINS FROM 
TITLE    2 CRYSTAL STRUCTURE TO CELLULAR FUNCTION                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PERIOD CIRCADIAN PROTEIN HOMOLOG 1;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MPER1, CIRCADIAN CLOCK PROTEIN PERIOD 1, CIRCADIAN PACEMAKER
COMPND   5 PROTEIN RIGUI;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PER1, PER, RIGUI;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PAS DOMAINS, CIRCADIAN CLOCK PROTEIN, PROTEIN BINDING                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.KUCERA,I.SCHMALEN,S.HENNIG,R.OELLINGER,H.M.STRAUSS,A.GRUDZIECKI,    
AUTHOR   2 C.WIECZOREK,A.KRAMER,E.WOLF                                          
REVDAT   2   14-MAR-12 4DJ2    1       JRNL                                     
REVDAT   1   29-FEB-12 4DJ2    0                                                
JRNL        AUTH   N.KUCERA,I.SCHMALEN,S.HENNIG,R.OLLINGER,H.M.STRAUSS,         
JRNL        AUTH 2 A.GRUDZIECKI,C.WIECZOREK,A.KRAMER,E.WOLF                     
JRNL        TITL   UNWINDING THE DIFFERENCES OF THE MAMMALIAN PERIOD CLOCK      
JRNL        TITL 2 PROTEINS FROM CRYSTAL STRUCTURE TO CELLULAR FUNCTION.        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  3311 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22331899                                                     
JRNL        DOI    10.1073/PNAS.1113280109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29744                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.5565 -  6.6230    0.96     2017   146  0.2192 0.2293        
REMARK   3     2  6.6230 -  5.2588    0.98     1966   144  0.2059 0.2400        
REMARK   3     3  5.2588 -  4.5946    0.98     1992   145  0.1761 0.2748        
REMARK   3     4  4.5946 -  4.1747    0.99     1999   150  0.1564 0.2660        
REMARK   3     5  4.1747 -  3.8756    0.99     1942   140  0.1691 0.2257        
REMARK   3     6  3.8756 -  3.6472    0.99     2009   145  0.1883 0.2801        
REMARK   3     7  3.6472 -  3.4646    0.99     1973   142  0.2013 0.3053        
REMARK   3     8  3.4646 -  3.3138    0.99     1953   133  0.2091 0.3077        
REMARK   3     9  3.3138 -  3.1863    0.99     2005   145  0.2328 0.3532        
REMARK   3    10  3.1863 -  3.0763    1.00     2000   138  0.2311 0.3559        
REMARK   3    11  3.0763 -  2.9802    1.00     1956   143  0.2485 0.3321        
REMARK   3    12  2.9802 -  2.8950    1.00     1953   143  0.2428 0.3575        
REMARK   3    13  2.8950 -  2.8188    1.00     1994   138  0.2819 0.3288        
REMARK   3    14  2.8188 -  2.7500    1.00     1989   144  0.3061 0.4205        
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              : 0.33                                          
REMARK   3   B_SOL              : 73.33                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.190           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.89540                                             
REMARK   3    B22 (A**2) : -1.90240                                             
REMARK   3    B33 (A**2) : 9.79780                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.43220                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           8306                                  
REMARK   3   ANGLE     :  1.291          11338                                  
REMARK   3   CHIRALITY :  0.079           1300                                  
REMARK   3   PLANARITY :  0.007           1467                                  
REMARK   3   DIHEDRAL  : 16.415           2933                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 210:342 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3818 -13.7086  28.9073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2885 T22:   0.3542                                     
REMARK   3      T33:   0.5064 T12:  -0.0062                                     
REMARK   3      T13:  -0.0118 T23:  -0.0799                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9548 L22:   3.3899                                     
REMARK   3      L33:   1.8737 L12:  -0.7883                                     
REMARK   3      L13:  -0.5332 L23:   0.4361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1308 S12:   0.1954 S13:  -0.2171                       
REMARK   3      S21:   0.0584 S22:  -0.0365 S23:   0.5851                       
REMARK   3      S31:   0.4557 S32:   0.2325 S33:   0.0004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 358:502 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1830  13.6116  38.5380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3044 T22:   0.2724                                     
REMARK   3      T33:   0.2911 T12:   0.0429                                     
REMARK   3      T13:  -0.0015 T23:  -0.0822                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0037 L22:   1.1574                                     
REMARK   3      L33:   2.0553 L12:   0.0970                                     
REMARK   3      L13:   0.9105 L23:  -0.1008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0740 S12:   0.1019 S13:   0.3632                       
REMARK   3      S21:   0.0456 S22:  -0.0935 S23:   0.0987                       
REMARK   3      S31:  -0.2822 S32:  -0.2154 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN B AND RESSEQ 210:342 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2275  13.7104  21.1700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2432 T22:   0.2957                                     
REMARK   3      T33:   0.4261 T12:   0.0102                                     
REMARK   3      T13:   0.0139 T23:  -0.0898                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3509 L22:   4.0859                                     
REMARK   3      L33:   2.3348 L12:   2.1032                                     
REMARK   3      L13:   0.5302 L23:   0.8603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2181 S12:  -0.1252 S13:   0.2617                       
REMARK   3      S21:  -0.1025 S22:   0.2205 S23:   0.6341                       
REMARK   3      S31:   0.0931 S32:  -0.0030 S33:   0.0004                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESSEQ 358:502 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0758 -13.9382  11.9389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2531 T22:   0.2767                                     
REMARK   3      T33:   0.2193 T12:  -0.0482                                     
REMARK   3      T13:  -0.0131 T23:  -0.0940                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8500 L22:   1.2818                                     
REMARK   3      L33:   1.8337 L12:  -0.2882                                     
REMARK   3      L13:  -1.5977 L23:  -0.3582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1354 S12:   0.1674 S13:  -0.5833                       
REMARK   3      S21:  -0.1117 S22:  -0.0237 S23:  -0.2218                       
REMARK   3      S31:   0.2345 S32:  -0.1226 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN C AND RESSEQ 210:342 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1832 -13.1986  22.3411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4317 T22:   0.5086                                     
REMARK   3      T33:   0.5055 T12:  -0.2758                                     
REMARK   3      T13:  -0.3061 T23:   0.3510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9208 L22:   2.9219                                     
REMARK   3      L33:   1.6019 L12:   1.0905                                     
REMARK   3      L13:   0.2625 L23:   1.5683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9661 S12:  -0.5170 S13:  -0.6847                       
REMARK   3      S21:   0.3213 S22:  -0.4924 S23:  -1.1480                       
REMARK   3      S31:   0.1311 S32:  -0.0268 S33:   0.1906                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN C AND RESSEQ 358:502 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.6286  11.1387   9.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3183 T22:   0.2885                                     
REMARK   3      T33:   0.1386 T12:  -0.1476                                     
REMARK   3      T13:  -0.0295 T23:   0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1943 L22:   3.0436                                     
REMARK   3      L33:   0.3374 L12:   1.5953                                     
REMARK   3      L13:   0.5752 L23:   0.5588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3433 S12:   0.5077 S13:  -0.2685                       
REMARK   3      S21:  -0.7007 S22:   0.4030 S23:   0.3203                       
REMARK   3      S31:   0.2972 S32:  -0.0671 S33:  -0.0015                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN D AND RESSEQ 212:342 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7543  12.0363  28.2397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4303 T22:   0.6426                                     
REMARK   3      T33:   0.4125 T12:   0.2968                                     
REMARK   3      T13:   0.2423 T23:   0.2359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3251 L22:   4.0990                                     
REMARK   3      L33:   1.0052 L12:  -1.5224                                     
REMARK   3      L13:  -0.3243 L23:   0.2208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7579 S12:   0.5181 S13:   0.3966                       
REMARK   3      S21:  -0.3287 S22:  -0.4931 S23:  -1.3540                       
REMARK   3      S31:  -0.4585 S32:  -0.0960 S33:   0.0718                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN D AND RESSEQ 358:502 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4330 -11.5401  40.4643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3665 T22:   0.2630                                     
REMARK   3      T33:   0.1565 T12:   0.1493                                     
REMARK   3      T13:   0.0464 T23:   0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2244 L22:   3.0877                                     
REMARK   3      L33:   0.1067 L12:  -1.7282                                     
REMARK   3      L13:  -0.0963 L23:   0.4137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3590 S12:  -0.5437 S13:   0.1144                       
REMARK   3      S21:   0.7641 S22:   0.4546 S23:   0.3781                       
REMARK   3      S31:  -0.0506 S32:  -0.2362 S33:   0.0052                       
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 4DJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9807                             
REMARK 200  MONOCHROMATOR                  : SILICIUM 111                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29780                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, 0.15 M NH4OAC, 16% PEG      
REMARK 280  3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
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       28.43500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   183                                                      
REMARK 465     PRO A   184                                                      
REMARK 465     LEU A   185                                                      
REMARK 465     GLY A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     PHE A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     PRO A   192                                                      
REMARK 465     CYS A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     MET A   195                                                      
REMARK 465     GLY A   281                                                      
REMARK 465     THR A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     ALA A   284                                                      
REMARK 465     GLY A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     LEU A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     PHE A   291                                                      
REMARK 465     THR A   292                                                      
REMARK 465     GLN A   293                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     ASP A   306                                                      
REMARK 465     ARG A   307                                                      
REMARK 465     ASP A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     SER A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     GLY A   330                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     PRO A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     PRO A   478                                                      
REMARK 465     ALA A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     SER A   481                                                      
REMARK 465     LEU A   482                                                      
REMARK 465     GLY B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     LEU B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     SER B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     GLU B   189                                                      
REMARK 465     PHE B   190                                                      
REMARK 465     GLU B   191                                                      
REMARK 465     PRO B   192                                                      
REMARK 465     CYS B   193                                                      
REMARK 465     ALA B   194                                                      
REMARK 465     MET B   195                                                      
REMARK 465     THR B   280                                                      
REMARK 465     GLY B   281                                                      
REMARK 465     THR B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 465     ALA B   284                                                      
REMARK 465     GLY B   285                                                      
REMARK 465     SER B   286                                                      
REMARK 465     GLY B   287                                                      
REMARK 465     LEU B   288                                                      
REMARK 465     LYS B   289                                                      
REMARK 465     ASP B   290                                                      
REMARK 465     PHE B   291                                                      
REMARK 465     THR B   292                                                      
REMARK 465     GLN B   293                                                      
REMARK 465     ASP B   306                                                      
REMARK 465     ARG B   307                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     ASP B   329                                                      
REMARK 465     ALA B   475                                                      
REMARK 465     PRO B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     PRO B   478                                                      
REMARK 465     ALA B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     LEU B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     GLY C   183                                                      
REMARK 465     PRO C   184                                                      
REMARK 465     LEU C   185                                                      
REMARK 465     GLY C   186                                                      
REMARK 465     SER C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     GLU C   189                                                      
REMARK 465     PHE C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     PRO C   192                                                      
REMARK 465     CYS C   193                                                      
REMARK 465     ALA C   194                                                      
REMARK 465     MET C   195                                                      
REMARK 465     ASP C   196                                                      
REMARK 465     MET C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     THR C   199                                                      
REMARK 465     TYR C   200                                                      
REMARK 465     THR C   201                                                      
REMARK 465     LEU C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     THR C   280                                                      
REMARK 465     GLY C   281                                                      
REMARK 465     THR C   282                                                      
REMARK 465     SER C   283                                                      
REMARK 465     ALA C   284                                                      
REMARK 465     GLY C   285                                                      
REMARK 465     SER C   286                                                      
REMARK 465     GLY C   287                                                      
REMARK 465     LEU C   288                                                      
REMARK 465     LYS C   289                                                      
REMARK 465     ASP C   290                                                      
REMARK 465     PHE C   291                                                      
REMARK 465     THR C   292                                                      
REMARK 465     GLN C   293                                                      
REMARK 465     GLU C   294                                                      
REMARK 465     ARG C   307                                                      
REMARK 465     ASP C   308                                                      
REMARK 465     PRO C   309                                                      
REMARK 465     GLY C   310                                                      
REMARK 465     VAL C   327                                                      
REMARK 465     SER C   328                                                      
REMARK 465     ASP C   329                                                      
REMARK 465     GLY C   330                                                      
REMARK 465     ALA C   331                                                      
REMARK 465     PRO C   332                                                      
REMARK 465     ALA C   333                                                      
REMARK 465     GLN C   334                                                      
REMARK 465     PRO C   335                                                      
REMARK 465     CYS C   336                                                      
REMARK 465     PRO C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     PRO C   478                                                      
REMARK 465     ALA C   479                                                      
REMARK 465     PRO C   480                                                      
REMARK 465     SER C   481                                                      
REMARK 465     GLY D   183                                                      
REMARK 465     PRO D   184                                                      
REMARK 465     LEU D   185                                                      
REMARK 465     GLY D   186                                                      
REMARK 465     SER D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     GLU D   189                                                      
REMARK 465     PHE D   190                                                      
REMARK 465     GLU D   191                                                      
REMARK 465     PRO D   192                                                      
REMARK 465     CYS D   193                                                      
REMARK 465     ALA D   194                                                      
REMARK 465     MET D   195                                                      
REMARK 465     ASP D   196                                                      
REMARK 465     MET D   197                                                      
REMARK 465     SER D   198                                                      
REMARK 465     THR D   199                                                      
REMARK 465     TYR D   200                                                      
REMARK 465     THR D   201                                                      
REMARK 465     LEU D   202                                                      
REMARK 465     GLU D   203                                                      
REMARK 465     GLU D   204                                                      
REMARK 465     LEU D   205                                                      
REMARK 465     GLU D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     ILE D   208                                                      
REMARK 465     THR D   209                                                      
REMARK 465     SER D   210                                                      
REMARK 465     GLU D   211                                                      
REMARK 465     SER D   225                                                      
REMARK 465     PHE D   226                                                      
REMARK 465     THR D   280                                                      
REMARK 465     GLY D   281                                                      
REMARK 465     THR D   282                                                      
REMARK 465     SER D   283                                                      
REMARK 465     ALA D   284                                                      
REMARK 465     GLY D   285                                                      
REMARK 465     SER D   286                                                      
REMARK 465     GLY D   287                                                      
REMARK 465     LEU D   288                                                      
REMARK 465     LYS D   289                                                      
REMARK 465     ASP D   290                                                      
REMARK 465     PHE D   291                                                      
REMARK 465     THR D   292                                                      
REMARK 465     GLN D   293                                                      
REMARK 465     GLY D   304                                                      
REMARK 465     PRO D   305                                                      
REMARK 465     ASP D   306                                                      
REMARK 465     ARG D   307                                                      
REMARK 465     ASP D   308                                                      
REMARK 465     PRO D   309                                                      
REMARK 465     GLY D   310                                                      
REMARK 465     PRO D   311                                                      
REMARK 465     THR D   323                                                      
REMARK 465     LYS D   324                                                      
REMARK 465     ILE D   325                                                      
REMARK 465     ARG D   326                                                      
REMARK 465     VAL D   327                                                      
REMARK 465     SER D   328                                                      
REMARK 465     ASP D   329                                                      
REMARK 465     GLY D   330                                                      
REMARK 465     ALA D   331                                                      
REMARK 465     PRO D   332                                                      
REMARK 465     ALA D   333                                                      
REMARK 465     GLN D   334                                                      
REMARK 465     PRO D   335                                                      
REMARK 465     ALA D   475                                                      
REMARK 465     PRO D   476                                                      
REMARK 465     SER D   477                                                      
REMARK 465     PRO D   478                                                      
REMARK 465     ALA D   479                                                      
REMARK 465     PRO D   480                                                      
REMARK 465     SER D   481                                                      
REMARK 465     LEU D   482                                                      
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     SER A 198    OG                                                  
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 211    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 212    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 214    CG   CD1  CD2                                       
REMARK 470     GLN A 217    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     ASP A 247    CG   OD1  OD2                                       
REMARK 470     VAL A 248    CG1  CG2                                            
REMARK 470     ARG A 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 280    OG1  CG2                                            
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 411    CG   CD   CE   NZ                                   
REMARK 470     GLN A 418    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 450    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 451    CG   CD   CE   NZ                                   
REMARK 470     GLU A 468    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 483    CG   OD1  OD2                                       
REMARK 470     ASP A 485    CG   OD1  OD2                                       
REMARK 470     GLN A 487    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 488    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 499    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 502    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 196    CG   OD1  OD2                                       
REMARK 470     SER B 198    OG                                                  
REMARK 470     GLU B 206    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 207    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 211    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 212    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B 214    CG   CD1  CD2                                       
REMARK 470     ASN B 216    CG   OD1  ND2                                       
REMARK 470     GLN B 217    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     ASP B 247    CG   OD1  OD2                                       
REMARK 470     VAL B 248    CG1  CG2                                            
REMARK 470     ARG B 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 294    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 295    CG   CD   CE   NZ                                   
REMARK 470     PRO B 305    CG   CD                                             
REMARK 470     PRO B 311    CG   CD                                             
REMARK 470     ARG B 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 327    CG1  CG2                                            
REMARK 470     SER B 328    OG                                                  
REMARK 470     ARG B 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 411    CG   CD   CE   NZ                                   
REMARK 470     LEU B 415    CG   CD1  CD2                                       
REMARK 470     ARG B 450    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 451    CG   CD   CE   NZ                                   
REMARK 470     SER B 484    OG                                                  
REMARK 470     GLN B 487    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 488    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 502    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C 204    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 205    CG   CD1  CD2                                       
REMARK 470     GLU C 206    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 212    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C 214    CG   CD1  CD2                                       
REMARK 470     ARG C 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 225    OG                                                  
REMARK 470     GLU C 236    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 245    CG   CD   CE   NZ                                   
REMARK 470     PHE C 249    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 256    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP C 278    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 278    CZ3  CH2                                            
REMARK 470     LYS C 295    CG   CD   CE   NZ                                   
REMARK 470     ASP C 306    CG   OD1  OD2                                       
REMARK 470     PRO C 311    CG   CD                                             
REMARK 470     ARG C 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 325    CG1  CG2  CD1                                       
REMARK 470     ARG C 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 411    CG   CD   CE   NZ                                   
REMARK 470     LEU C 466    CG   CD1  CD2                                       
REMARK 470     LEU C 482    CG   CD1  CD2                                       
REMARK 470     ASP C 483    CG   OD1  OD2                                       
REMARK 470     GLU C 491    CG   CD   OE1  OE2                                  
REMARK 470     TYR D 212    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR D 213    OG1  CG2                                            
REMARK 470     LEU D 214    CG   CD1  CD2                                       
REMARK 470     ARG D 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 216    CG   OD1  ND2                                       
REMARK 470     LEU D 227    CG   CD1  CD2                                       
REMARK 470     THR D 228    OG1  CG2                                            
REMARK 470     ARG D 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 231    CG1  CG2  CD1                                       
REMARK 470     ILE D 234    CG1  CG2  CD1                                       
REMARK 470     GLU D 236    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 245    CG   CD   CE   NZ                                   
REMARK 470     ASP D 247    CG   OD1  OD2                                       
REMARK 470     PHE D 249    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG D 250    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 256    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 294    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 295    CG   CD   CE   NZ                                   
REMARK 470     ARG D 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 322    CG1  CG2                                            
REMARK 470     CYS D 336    SG                                                  
REMARK 470     CYS D 337    SG                                                  
REMARK 470     GLU D 342    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 395    CG   CD1  CD2                                       
REMARK 470     LYS D 411    CG   CD   CE   NZ                                   
REMARK 470     ARG D 458    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 466    CG   CD1  CD2                                       
REMARK 470     ASP D 483    CG   OD1  OD2                                       
REMARK 470     GLN D 487    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 491    CG   CD   OE1  OE2                                  
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    SER A 210       13.05    -64.98                                   
REMARK 500    PHE A 249      -95.91   -128.27                                   
REMARK 500    ARG A 250      132.20    -38.06                                   
REMARK 500    THR A 270       33.21    -97.18                                   
REMARK 500    LYS A 295       89.14     88.68                                   
REMARK 500    ARG A 326      -67.26    -97.09                                   
REMARK 500    TYR A 348       37.72    -91.35                                   
REMARK 500    CYS A 368       41.64     72.03                                   
REMARK 500    ALA A 416       19.02    -59.91                                   
REMARK 500    HIS A 422       81.90   -158.18                                   
REMARK 500    ARG A 430       -6.49     72.28                                   
REMARK 500    SER A 484       36.43    -83.18                                   
REMARK 500    VAL A 501      158.38    112.28                                   
REMARK 500    LEU B 202       32.52    -73.39                                   
REMARK 500    GLU B 203      -41.64   -141.69                                   
REMARK 500    SER B 210       -1.05    -58.50                                   
REMARK 500    VAL B 248       40.41    -72.80                                   
REMARK 500    PHE B 249      -65.47   -124.91                                   
REMARK 500    THR B 270       41.31    -97.65                                   
REMARK 500    PRO B 272      -45.78    -28.18                                   
REMARK 500    TRP B 278       96.12    -56.73                                   
REMARK 500    PRO B 311     -178.17    178.85                                   
REMARK 500    ARG B 312     -163.67     91.57                                   
REMARK 500    TYR B 348       31.92    -94.57                                   
REMARK 500    CYS B 368       41.15     72.53                                   
REMARK 500    LEU B 413        6.06    -68.55                                   
REMARK 500    GLN B 414      -64.98   -109.18                                   
REMARK 500    LEU B 415        2.69    -58.31                                   
REMARK 500    GLN B 418      126.92     -4.79                                   
REMARK 500    HIS B 422       97.93   -163.37                                   
REMARK 500    ARG B 430      -29.89     69.44                                   
REMARK 500    ALA B 442     -109.54   -143.04                                   
REMARK 500    ARG B 450      -10.29     69.20                                   
REMARK 500    VAL B 501      137.37    126.66                                   
REMARK 500    LEU C 205     -161.42     68.02                                   
REMARK 500    GLU C 206      -40.87    112.62                                   
REMARK 500    SER C 210       41.88    -61.57                                   
REMARK 500    GLU C 211      -69.20   -105.83                                   
REMARK 500    THR C 228     -112.33    -76.46                                   
REMARK 500    ARG C 230     -111.68   -130.89                                   
REMARK 500    SER C 235      161.79    -49.24                                   
REMARK 500    ARG C 246        1.69    -64.67                                   
REMARK 500    ARG C 250     -134.57    -69.51                                   
REMARK 500    THR C 270       31.02    -97.59                                   
REMARK 500    PRO C 305      108.10    -47.95                                   
REMARK 500    ARG C 312       66.86     76.11                                   
REMARK 500    ARG C 358       71.48    -67.94                                   
REMARK 500    CYS C 368       43.80     71.21                                   
REMARK 500    LEU C 381      -23.13   -144.59                                   
REMARK 500    LEU C 415      -22.58     73.39                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 RAMACHANDRAN OUTLIERS.                        
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 B 614        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH B 616        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH C 601        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH D 601        DISTANCE =  6.87 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GDI   RELATED DB: PDB                                   
REMARK 900 MOUSE PERIOD 2                                                       
REMARK 900 RELATED ID: 1WA9   RELATED DB: PDB                                   
REMARK 900 DROSOPHILA PERIOD                                                    
REMARK 900 RELATED ID: 4DJ3   RELATED DB: PDB                                   
DBREF  4DJ2 A  191   502  UNP    O35973   PER1_MOUSE     191    502             
DBREF  4DJ2 B  191   502  UNP    O35973   PER1_MOUSE     191    502             
DBREF  4DJ2 C  191   502  UNP    O35973   PER1_MOUSE     191    502             
DBREF  4DJ2 D  191   502  UNP    O35973   PER1_MOUSE     191    502             
SEQADV 4DJ2 GLY A  183  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO A  184  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 LEU A  185  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY A  186  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 SER A  187  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO A  188  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLU A  189  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PHE A  190  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY B  183  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO B  184  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 LEU B  185  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY B  186  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 SER B  187  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO B  188  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLU B  189  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PHE B  190  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY C  183  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO C  184  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 LEU C  185  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY C  186  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 SER C  187  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO C  188  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLU C  189  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PHE C  190  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY D  183  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO D  184  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 LEU D  185  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLY D  186  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 SER D  187  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PRO D  188  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 GLU D  189  UNP  O35973              EXPRESSION TAG                 
SEQADV 4DJ2 PHE D  190  UNP  O35973              EXPRESSION TAG                 
SEQRES   1 A  320  GLY PRO LEU GLY SER PRO GLU PHE GLU PRO CYS ALA MET          
SEQRES   2 A  320  ASP MET SER THR TYR THR LEU GLU GLU LEU GLU HIS ILE          
SEQRES   3 A  320  THR SER GLU TYR THR LEU ARG ASN GLN ASP THR PHE SER          
SEQRES   4 A  320  VAL ALA VAL SER PHE LEU THR GLY ARG ILE VAL TYR ILE          
SEQRES   5 A  320  SER GLU GLN ALA GLY VAL LEU LEU ARG CYS LYS ARG ASP          
SEQRES   6 A  320  VAL PHE ARG GLY ALA ARG PHE SER GLU LEU LEU ALA PRO          
SEQRES   7 A  320  GLN ASP VAL GLY VAL PHE TYR GLY SER THR THR PRO SER          
SEQRES   8 A  320  ARG LEU PRO THR TRP GLY THR GLY THR SER ALA GLY SER          
SEQRES   9 A  320  GLY LEU LYS ASP PHE THR GLN GLU LYS SER VAL PHE CYS          
SEQRES  10 A  320  ARG ILE ARG GLY GLY PRO ASP ARG ASP PRO GLY PRO ARG          
SEQRES  11 A  320  TYR GLN PRO PHE ARG LEU THR PRO TYR VAL THR LYS ILE          
SEQRES  12 A  320  ARG VAL SER ASP GLY ALA PRO ALA GLN PRO CYS CYS LEU          
SEQRES  13 A  320  LEU ILE ALA GLU ARG ILE HIS SER GLY TYR GLU ALA PRO          
SEQRES  14 A  320  ARG ILE PRO PRO ASP LYS ARG ILE PHE THR THR ARG HIS          
SEQRES  15 A  320  THR PRO SER CYS LEU PHE GLN ASP VAL ASP GLU ARG ALA          
SEQRES  16 A  320  ALA PRO LEU LEU GLY TYR LEU PRO GLN ASP LEU LEU GLY          
SEQRES  17 A  320  ALA PRO VAL LEU LEU PHE LEU HIS PRO GLU ASP ARG PRO          
SEQRES  18 A  320  LEU MET LEU ALA ILE HIS LYS LYS ILE LEU GLN LEU ALA          
SEQRES  19 A  320  GLY GLN PRO PHE ASP HIS SER PRO ILE ARG PHE CYS ALA          
SEQRES  20 A  320  ARG ASN GLY GLU TYR VAL THR MET ASP THR SER TRP ALA          
SEQRES  21 A  320  GLY PHE VAL HIS PRO TRP SER ARG LYS VAL ALA PHE VAL          
SEQRES  22 A  320  LEU GLY ARG HIS LYS VAL ARG THR ALA PRO LEU ASN GLU          
SEQRES  23 A  320  ASP VAL PHE THR PRO PRO ALA PRO SER PRO ALA PRO SER          
SEQRES  24 A  320  LEU ASP SER ASP ILE GLN GLU LEU SER GLU GLN ILE HIS          
SEQRES  25 A  320  ARG LEU LEU LEU GLN PRO VAL HIS                              
SEQRES   1 B  320  GLY PRO LEU GLY SER PRO GLU PHE GLU PRO CYS ALA MET          
SEQRES   2 B  320  ASP MET SER THR TYR THR LEU GLU GLU LEU GLU HIS ILE          
SEQRES   3 B  320  THR SER GLU TYR THR LEU ARG ASN GLN ASP THR PHE SER          
SEQRES   4 B  320  VAL ALA VAL SER PHE LEU THR GLY ARG ILE VAL TYR ILE          
SEQRES   5 B  320  SER GLU GLN ALA GLY VAL LEU LEU ARG CYS LYS ARG ASP          
SEQRES   6 B  320  VAL PHE ARG GLY ALA ARG PHE SER GLU LEU LEU ALA PRO          
SEQRES   7 B  320  GLN ASP VAL GLY VAL PHE TYR GLY SER THR THR PRO SER          
SEQRES   8 B  320  ARG LEU PRO THR TRP GLY THR GLY THR SER ALA GLY SER          
SEQRES   9 B  320  GLY LEU LYS ASP PHE THR GLN GLU LYS SER VAL PHE CYS          
SEQRES  10 B  320  ARG ILE ARG GLY GLY PRO ASP ARG ASP PRO GLY PRO ARG          
SEQRES  11 B  320  TYR GLN PRO PHE ARG LEU THR PRO TYR VAL THR LYS ILE          
SEQRES  12 B  320  ARG VAL SER ASP GLY ALA PRO ALA GLN PRO CYS CYS LEU          
SEQRES  13 B  320  LEU ILE ALA GLU ARG ILE HIS SER GLY TYR GLU ALA PRO          
SEQRES  14 B  320  ARG ILE PRO PRO ASP LYS ARG ILE PHE THR THR ARG HIS          
SEQRES  15 B  320  THR PRO SER CYS LEU PHE GLN ASP VAL ASP GLU ARG ALA          
SEQRES  16 B  320  ALA PRO LEU LEU GLY TYR LEU PRO GLN ASP LEU LEU GLY          
SEQRES  17 B  320  ALA PRO VAL LEU LEU PHE LEU HIS PRO GLU ASP ARG PRO          
SEQRES  18 B  320  LEU MET LEU ALA ILE HIS LYS LYS ILE LEU GLN LEU ALA          
SEQRES  19 B  320  GLY GLN PRO PHE ASP HIS SER PRO ILE ARG PHE CYS ALA          
SEQRES  20 B  320  ARG ASN GLY GLU TYR VAL THR MET ASP THR SER TRP ALA          
SEQRES  21 B  320  GLY PHE VAL HIS PRO TRP SER ARG LYS VAL ALA PHE VAL          
SEQRES  22 B  320  LEU GLY ARG HIS LYS VAL ARG THR ALA PRO LEU ASN GLU          
SEQRES  23 B  320  ASP VAL PHE THR PRO PRO ALA PRO SER PRO ALA PRO SER          
SEQRES  24 B  320  LEU ASP SER ASP ILE GLN GLU LEU SER GLU GLN ILE HIS          
SEQRES  25 B  320  ARG LEU LEU LEU GLN PRO VAL HIS                              
SEQRES   1 C  320  GLY PRO LEU GLY SER PRO GLU PHE GLU PRO CYS ALA MET          
SEQRES   2 C  320  ASP MET SER THR TYR THR LEU GLU GLU LEU GLU HIS ILE          
SEQRES   3 C  320  THR SER GLU TYR THR LEU ARG ASN GLN ASP THR PHE SER          
SEQRES   4 C  320  VAL ALA VAL SER PHE LEU THR GLY ARG ILE VAL TYR ILE          
SEQRES   5 C  320  SER GLU GLN ALA GLY VAL LEU LEU ARG CYS LYS ARG ASP          
SEQRES   6 C  320  VAL PHE ARG GLY ALA ARG PHE SER GLU LEU LEU ALA PRO          
SEQRES   7 C  320  GLN ASP VAL GLY VAL PHE TYR GLY SER THR THR PRO SER          
SEQRES   8 C  320  ARG LEU PRO THR TRP GLY THR GLY THR SER ALA GLY SER          
SEQRES   9 C  320  GLY LEU LYS ASP PHE THR GLN GLU LYS SER VAL PHE CYS          
SEQRES  10 C  320  ARG ILE ARG GLY GLY PRO ASP ARG ASP PRO GLY PRO ARG          
SEQRES  11 C  320  TYR GLN PRO PHE ARG LEU THR PRO TYR VAL THR LYS ILE          
SEQRES  12 C  320  ARG VAL SER ASP GLY ALA PRO ALA GLN PRO CYS CYS LEU          
SEQRES  13 C  320  LEU ILE ALA GLU ARG ILE HIS SER GLY TYR GLU ALA PRO          
SEQRES  14 C  320  ARG ILE PRO PRO ASP LYS ARG ILE PHE THR THR ARG HIS          
SEQRES  15 C  320  THR PRO SER CYS LEU PHE GLN ASP VAL ASP GLU ARG ALA          
SEQRES  16 C  320  ALA PRO LEU LEU GLY TYR LEU PRO GLN ASP LEU LEU GLY          
SEQRES  17 C  320  ALA PRO VAL LEU LEU PHE LEU HIS PRO GLU ASP ARG PRO          
SEQRES  18 C  320  LEU MET LEU ALA ILE HIS LYS LYS ILE LEU GLN LEU ALA          
SEQRES  19 C  320  GLY GLN PRO PHE ASP HIS SER PRO ILE ARG PHE CYS ALA          
SEQRES  20 C  320  ARG ASN GLY GLU TYR VAL THR MET ASP THR SER TRP ALA          
SEQRES  21 C  320  GLY PHE VAL HIS PRO TRP SER ARG LYS VAL ALA PHE VAL          
SEQRES  22 C  320  LEU GLY ARG HIS LYS VAL ARG THR ALA PRO LEU ASN GLU          
SEQRES  23 C  320  ASP VAL PHE THR PRO PRO ALA PRO SER PRO ALA PRO SER          
SEQRES  24 C  320  LEU ASP SER ASP ILE GLN GLU LEU SER GLU GLN ILE HIS          
SEQRES  25 C  320  ARG LEU LEU LEU GLN PRO VAL HIS                              
SEQRES   1 D  320  GLY PRO LEU GLY SER PRO GLU PHE GLU PRO CYS ALA MET          
SEQRES   2 D  320  ASP MET SER THR TYR THR LEU GLU GLU LEU GLU HIS ILE          
SEQRES   3 D  320  THR SER GLU TYR THR LEU ARG ASN GLN ASP THR PHE SER          
SEQRES   4 D  320  VAL ALA VAL SER PHE LEU THR GLY ARG ILE VAL TYR ILE          
SEQRES   5 D  320  SER GLU GLN ALA GLY VAL LEU LEU ARG CYS LYS ARG ASP          
SEQRES   6 D  320  VAL PHE ARG GLY ALA ARG PHE SER GLU LEU LEU ALA PRO          
SEQRES   7 D  320  GLN ASP VAL GLY VAL PHE TYR GLY SER THR THR PRO SER          
SEQRES   8 D  320  ARG LEU PRO THR TRP GLY THR GLY THR SER ALA GLY SER          
SEQRES   9 D  320  GLY LEU LYS ASP PHE THR GLN GLU LYS SER VAL PHE CYS          
SEQRES  10 D  320  ARG ILE ARG GLY GLY PRO ASP ARG ASP PRO GLY PRO ARG          
SEQRES  11 D  320  TYR GLN PRO PHE ARG LEU THR PRO TYR VAL THR LYS ILE          
SEQRES  12 D  320  ARG VAL SER ASP GLY ALA PRO ALA GLN PRO CYS CYS LEU          
SEQRES  13 D  320  LEU ILE ALA GLU ARG ILE HIS SER GLY TYR GLU ALA PRO          
SEQRES  14 D  320  ARG ILE PRO PRO ASP LYS ARG ILE PHE THR THR ARG HIS          
SEQRES  15 D  320  THR PRO SER CYS LEU PHE GLN ASP VAL ASP GLU ARG ALA          
SEQRES  16 D  320  ALA PRO LEU LEU GLY TYR LEU PRO GLN ASP LEU LEU GLY          
SEQRES  17 D  320  ALA PRO VAL LEU LEU PHE LEU HIS PRO GLU ASP ARG PRO          
SEQRES  18 D  320  LEU MET LEU ALA ILE HIS LYS LYS ILE LEU GLN LEU ALA          
SEQRES  19 D  320  GLY GLN PRO PHE ASP HIS SER PRO ILE ARG PHE CYS ALA          
SEQRES  20 D  320  ARG ASN GLY GLU TYR VAL THR MET ASP THR SER TRP ALA          
SEQRES  21 D  320  GLY PHE VAL HIS PRO TRP SER ARG LYS VAL ALA PHE VAL          
SEQRES  22 D  320  LEU GLY ARG HIS LYS VAL ARG THR ALA PRO LEU ASN GLU          
SEQRES  23 D  320  ASP VAL PHE THR PRO PRO ALA PRO SER PRO ALA PRO SER          
SEQRES  24 D  320  LEU ASP SER ASP ILE GLN GLU LEU SER GLU GLN ILE HIS          
SEQRES  25 D  320  ARG LEU LEU LEU GLN PRO VAL HIS                              
FORMUL   5  HOH   *77(H2 O)                                                     
HELIX    1   1 THR A  201  THR A  213  1                                  13    
HELIX    2   2 GLU A  236  ARG A  243  1                                   8    
HELIX    3   3 ARG A  253  LEU A  258  5                                   6    
HELIX    4   4 ALA A  259  THR A  270  1                                  12    
HELIX    5   5 PRO A  354  LYS A  357  5                                   4    
HELIX    6   6 ARG A  376  GLY A  382  1                                   7    
HELIX    7   7 LEU A  384  LEU A  389  1                                   6    
HELIX    8   8 PRO A  392  LEU A  397  5                                   6    
HELIX    9   9 HIS A  398  GLU A  400  5                                   3    
HELIX   10  10 ASP A  401  LEU A  413  1                                  13    
HELIX   11  11 SER A  484  GLN A  499  1                                  16    
HELIX   12  12 GLU B  203  ASN B  216  1                                  14    
HELIX   13  13 GLU B  236  ARG B  243  1                                   8    
HELIX   14  14 ARG B  253  LEU B  258  5                                   6    
HELIX   15  15 ASP B  262  THR B  270  1                                   9    
HELIX   16  16 PRO B  354  LYS B  357  5                                   4    
HELIX   17  17 ARG B  376  GLY B  382  1                                   7    
HELIX   18  18 LEU B  384  LEU B  389  1                                   6    
HELIX   19  19 PRO B  392  LEU B  397  5                                   6    
HELIX   20  20 HIS B  398  GLU B  400  5                                   3    
HELIX   21  21 ASP B  401  ALA B  416  1                                  16    
HELIX   22  22 ASP B  485  LEU B  498  1                                  14    
HELIX   23  23 GLU C  236  ARG C  243  1                                   8    
HELIX   24  24 LYS C  245  PHE C  249  5                                   5    
HELIX   25  25 ARG C  253  LEU C  257  5                                   5    
HELIX   26  26 ALA C  259  THR C  270  1                                  12    
HELIX   27  27 THR C  271  LEU C  275  5                                   5    
HELIX   28  28 ARG C  376  GLY C  382  1                                   7    
HELIX   29  29 LEU C  384  LEU C  389  1                                   6    
HELIX   30  30 PRO C  392  LEU C  397  5                                   6    
HELIX   31  31 HIS C  398  PRO C  403  5                                   6    
HELIX   32  32 LEU C  404  GLN C  414  1                                  11    
HELIX   33  33 SER C  484  LEU C  498  1                                  15    
HELIX   34  34 GLN D  237  LEU D  242  1                                   6    
HELIX   35  35 LYS D  245  PHE D  249  5                                   5    
HELIX   36  36 ALA D  259  THR D  270  1                                  12    
HELIX   37  37 PRO D  354  LYS D  357  5                                   4    
HELIX   38  38 ARG D  376  GLY D  382  1                                   7    
HELIX   39  39 LEU D  384  LEU D  389  1                                   6    
HELIX   40  40 PRO D  392  LEU D  397  5                                   6    
HELIX   41  41 HIS D  398  PRO D  403  5                                   6    
HELIX   42  42 LEU D  404  LEU D  415  1                                  12    
HELIX   43  43 SER D  484  LEU D  498  1                                  15    
SHEET    1   A 5 THR A 199  TYR A 200  0                                        
SHEET    2   A 5 GLN A 314  ILE A 325  1  O  LYS A 324   N  TYR A 200           
SHEET    3   A 5 GLN A 334  ARG A 343 -1  O  LEU A 338   N  TYR A 321           
SHEET    4   A 5 THR A 219  SER A 225 -1  N  VAL A 224   O  CYS A 337           
SHEET    5   A 5 ILE A 231  ILE A 234 -1  O  TYR A 233   N  ALA A 223           
SHEET    1   B 3 THR A 199  TYR A 200  0                                        
SHEET    2   B 3 GLN A 314  ILE A 325  1  O  LYS A 324   N  TYR A 200           
SHEET    3   B 3 VAL A 297  ILE A 301 -1  N  ILE A 301   O  GLN A 314           
SHEET    1   C 5 PHE A 370  VAL A 373  0                                        
SHEET    2   C 5 ILE A 359  HIS A 364 -1  N  ARG A 363   O  GLN A 371           
SHEET    3   C 5 VAL A 452  VAL A 461 -1  O  VAL A 455   N  HIS A 364           
SHEET    4   C 5 SER A 440  VAL A 445 -1  N  PHE A 444   O  ALA A 453           
SHEET    5   C 5 PHE A 420  ASP A 421 -1  N  PHE A 420   O  TRP A 441           
SHEET    1   D 5 PHE A 370  VAL A 373  0                                        
SHEET    2   D 5 ILE A 359  HIS A 364 -1  N  ARG A 363   O  GLN A 371           
SHEET    3   D 5 VAL A 452  VAL A 461 -1  O  VAL A 455   N  HIS A 364           
SHEET    4   D 5 TYR A 434  ASP A 438 -1  N  ASP A 438   O  LYS A 460           
SHEET    5   D 5 ILE A 425  CYS A 428 -1  N  ILE A 425   O  MET A 437           
SHEET    1   E 5 THR B 199  THR B 201  0                                        
SHEET    2   E 5 GLN B 314  ARG B 326  1  O  LYS B 324   N  TYR B 200           
SHEET    3   E 5 GLN B 334  ARG B 343 -1  O  GLU B 342   N  ARG B 317           
SHEET    4   E 5 THR B 219  SER B 225 -1  N  VAL B 222   O  LEU B 339           
SHEET    5   E 5 ILE B 231  ILE B 234 -1  O  VAL B 232   N  ALA B 223           
SHEET    1   F 3 THR B 199  THR B 201  0                                        
SHEET    2   F 3 GLN B 314  ARG B 326  1  O  LYS B 324   N  TYR B 200           
SHEET    3   F 3 VAL B 297  ILE B 301 -1  N  VAL B 297   O  LEU B 318           
SHEET    1   G 5 PHE B 370  VAL B 373  0                                        
SHEET    2   G 5 ILE B 359  HIS B 364 -1  N  ARG B 363   O  GLN B 371           
SHEET    3   G 5 VAL B 452  VAL B 461 -1  O  VAL B 455   N  HIS B 364           
SHEET    4   G 5 TYR B 434  TRP B 441 -1  N  ASP B 438   O  LYS B 460           
SHEET    5   G 5 PHE B 420  CYS B 428 -1  N  ILE B 425   O  MET B 437           
SHEET    1   H 4 PHE B 370  VAL B 373  0                                        
SHEET    2   H 4 ILE B 359  HIS B 364 -1  N  ARG B 363   O  GLN B 371           
SHEET    3   H 4 VAL B 452  VAL B 461 -1  O  VAL B 455   N  HIS B 364           
SHEET    4   H 4 PHE B 444  VAL B 445 -1  N  PHE B 444   O  ALA B 453           
SHEET    1   I 5 ILE C 231  ILE C 234  0                                        
SHEET    2   I 5 THR C 219  VAL C 224 -1  N  ALA C 223   O  VAL C 232           
SHEET    3   I 5 LEU C 338  ARG C 343 -1  O  ALA C 341   N  PHE C 220           
SHEET    4   I 5 GLN C 314  TYR C 321 -1  N  ARG C 317   O  GLU C 342           
SHEET    5   I 5 VAL C 297  ILE C 301 -1  N  VAL C 297   O  LEU C 318           
SHEET    1   J 5 PHE C 370  VAL C 373  0                                        
SHEET    2   J 5 ILE C 359  HIS C 364 -1  N  ARG C 363   O  GLN C 371           
SHEET    3   J 5 VAL C 452  VAL C 461 -1  O  HIS C 459   N  PHE C 360           
SHEET    4   J 5 TYR C 434  TRP C 441 -1  N  ASP C 438   O  LYS C 460           
SHEET    5   J 5 PHE C 420  CYS C 428 -1  N  HIS C 422   O  THR C 439           
SHEET    1   K 4 PHE C 370  VAL C 373  0                                        
SHEET    2   K 4 ILE C 359  HIS C 364 -1  N  ARG C 363   O  GLN C 371           
SHEET    3   K 4 VAL C 452  VAL C 461 -1  O  HIS C 459   N  PHE C 360           
SHEET    4   K 4 PHE C 444  VAL C 445 -1  N  PHE C 444   O  ALA C 453           
SHEET    1   L 5 TYR D 233  ILE D 234  0                                        
SHEET    2   L 5 THR D 219  ALA D 223 -1  O  ALA D 223   N  TYR D 233           
SHEET    3   L 5 LEU D 338  ARG D 343 -1  O  ALA D 341   N  PHE D 220           
SHEET    4   L 5 GLN D 314  TYR D 321 -1  N  ARG D 317   O  GLU D 342           
SHEET    5   L 5 VAL D 297  ILE D 301 -1  N  VAL D 297   O  LEU D 318           
SHEET    1   M 5 PHE D 370  VAL D 373  0                                        
SHEET    2   M 5 ILE D 359  HIS D 364 -1  N  ARG D 363   O  GLN D 371           
SHEET    3   M 5 VAL D 452  THR D 463 -1  O  VAL D 455   N  HIS D 364           
SHEET    4   M 5 TYR D 434  TRP D 441 -1  N  ASP D 438   O  LYS D 460           
SHEET    5   M 5 PHE D 420  CYS D 428 -1  N  ILE D 425   O  MET D 437           
SHEET    1   N 4 PHE D 370  VAL D 373  0                                        
SHEET    2   N 4 ILE D 359  HIS D 364 -1  N  ARG D 363   O  GLN D 371           
SHEET    3   N 4 VAL D 452  THR D 463 -1  O  VAL D 455   N  HIS D 364           
SHEET    4   N 4 PHE D 444  VAL D 445 -1  N  PHE D 444   O  ALA D 453           
CISPEP   1 ALA A  350    PRO A  351          0        -7.64                     
CISPEP   2 SER A  423    PRO A  424          0        -8.13                     
CISPEP   3 ASN A  431    GLY A  432          0       -19.48                     
CISPEP   4 ALA B  350    PRO B  351          0        -6.65                     
CISPEP   5 SER B  423    PRO B  424          0       -10.16                     
CISPEP   6 PHE C  226    LEU C  227          0        -7.96                     
CISPEP   7 ARG C  302    GLY C  303          0         5.61                     
CISPEP   8 PRO C  311    ARG C  312          0         5.61                     
CISPEP   9 ALA C  350    PRO C  351          0        -6.22                     
CISPEP  10 SER C  423    PRO C  424          0        -4.25                     
CISPEP  11 ALA D  350    PRO D  351          0        -7.75                     
CISPEP  12 SER D  423    PRO D  424          0        -7.30                     
CRYST1  100.340   56.870  100.950  90.00  90.07  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009966  0.000000  0.000011        0.00000                         
SCALE2      0.000000  0.017584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009906        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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