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LongText Report for: 4X6Y-pdb

Name Class
4X6Y-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           09-DEC-14   4X6Y              
TITLE     HUMAN SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH A CYCLOPROPYL UREA    
TITLE    2 DERIVATIVE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HYDROLASE DOMAIN, UNP RESIDUES 230-555;                    
COMPND   5 EC: 3.3.2.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPHX2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.CHIYO,K.TAKAI,T.ISHII                                               
REVDAT   1   08-APR-15 4X6Y    0                                                
JRNL        AUTH   K.TAKAI,N.CHIYO,T.NAKAJIMA,T.NARIAI,C.ISHIKAWA,S.NAKATANI,   
JRNL        AUTH 2 A.IKENO,S.YAMAMOTO,T.SONE                                    
JRNL        TITL   THREE-DIMENSIONAL RATIONAL APPROACH TO THE DISCOVERY OF      
JRNL        TITL 2 POTENT SUBSTITUTED CYCLOPROPYL UREA SOLUBLE EPOXIDE          
JRNL        TITL 3 HYDROLASE INHIBITORS                                         
JRNL        REF    BIOORG.MED.CHEM.LETT.                      2015              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   25800114                                                     
JRNL        DOI    10.1016/J.BMCL.2015.02.076                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33454                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1781                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1449                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5092                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : -0.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.290         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.219         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.166         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.448        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5302 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4912 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7194 ; 1.256 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11348 ; 0.781 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   630 ; 6.149 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;33.332 ;23.934       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   884 ;14.772 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;15.468 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   738 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5990 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1274 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2526 ; 1.031 ; 2.600       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2525 ; 1.031 ; 2.599       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3154 ; 1.794 ; 3.895       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   230        A   368                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7091  -6.4235  24.4039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1560 T22:   0.1551                                     
REMARK   3      T33:   0.1050 T12:   0.0034                                     
REMARK   3      T13:  -0.0014 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4769 L22:   2.2290                                     
REMARK   3      L33:   1.2706 L12:  -0.4533                                     
REMARK   3      L13:  -0.1276 L23:   0.5494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0351 S12:  -0.1060 S13:  -0.1127                       
REMARK   3      S21:   0.1976 S22:  -0.0076 S23:   0.0033                       
REMARK   3      S31:   0.0412 S32:  -0.1115 S33:   0.0427                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   369        A   430                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3623   9.4191  27.8115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2263 T22:   0.2540                                     
REMARK   3      T33:   0.1997 T12:   0.1394                                     
REMARK   3      T13:   0.0478 T23:  -0.0571                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7932 L22:   4.6582                                     
REMARK   3      L33:   2.3806 L12:   1.0671                                     
REMARK   3      L13:  -0.3635 L23:  -0.3096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1390 S12:  -0.2046 S13:   0.3702                       
REMARK   3      S21:   0.5680 S22:  -0.1226 S23:   0.5699                       
REMARK   3      S31:  -0.2406 S32:  -0.4040 S33:  -0.0164                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   431        A   545                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4663   3.9876  30.3573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1787 T22:   0.1530                                     
REMARK   3      T33:   0.0551 T12:   0.0416                                     
REMARK   3      T13:  -0.0078 T23:  -0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4274 L22:   1.8716                                     
REMARK   3      L33:   1.3886 L12:  -0.1320                                     
REMARK   3      L13:  -0.2869 L23:   0.4266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0204 S12:  -0.3023 S13:   0.1852                       
REMARK   3      S21:   0.2652 S22:  -0.0074 S23:  -0.0265                       
REMARK   3      S31:  -0.0515 S32:  -0.0335 S33:   0.0278                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   230        B   368                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5594 -16.7360   3.5389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0916 T22:   0.1314                                     
REMARK   3      T33:   0.1882 T12:   0.0101                                     
REMARK   3      T13:   0.0180 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3153 L22:   2.2996                                     
REMARK   3      L33:   1.5379 L12:  -0.0330                                     
REMARK   3      L13:  -0.4121 L23:   0.5527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:   0.1451 S13:  -0.0359                       
REMARK   3      S21:  -0.1125 S22:   0.0403 S23:  -0.2180                       
REMARK   3      S31:  -0.0135 S32:   0.0588 S33:  -0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   369        B   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7797 -31.6598 -14.4321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3026 T22:   0.2116                                     
REMARK   3      T33:   0.2094 T12:   0.0191                                     
REMARK   3      T13:   0.1068 T23:  -0.1786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5113 L22:   3.4868                                     
REMARK   3      L33:   3.5719 L12:   1.4562                                     
REMARK   3      L13:   0.1899 L23:  -1.0426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0859 S12:   0.4855 S13:  -0.4591                       
REMARK   3      S21:  -0.8859 S22:   0.0262 S23:  -0.3801                       
REMARK   3      S31:   0.4080 S32:   0.1786 S33:   0.0597                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   430        B   545                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9908 -27.4426  -0.6264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0922 T22:   0.0953                                     
REMARK   3      T33:   0.2163 T12:   0.0290                                     
REMARK   3      T13:   0.0692 T23:  -0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7144 L22:   2.7681                                     
REMARK   3      L33:   1.5599 L12:   0.0190                                     
REMARK   3      L13:   0.0538 L23:   0.0330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.1932 S13:  -0.2768                       
REMARK   3      S21:  -0.2348 S22:   0.0152 S23:  -0.4345                       
REMARK   3      S31:   0.2864 S32:   0.1155 S33:  -0.0233                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4X6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204761.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43406                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 78.4                               
REMARK 200  DATA REDUNDANCY                : 1.600                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: NULL                                                  
REMARK 200 STARTING MODEL: 3ANS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG8000, 200MM SODIUM IODIDE,   
REMARK 280  PH 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K             
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       64.61400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.36100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       64.61400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.36100            
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     LYS A   222                                                      
REMARK 465     GLY A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     ALA A   546                                                      
REMARK 465     ARG A   547                                                      
REMARK 465     ASN A   548                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     MET B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     LYS B   222                                                      
REMARK 465     GLY B   223                                                      
REMARK 465     HIS B   224                                                      
REMARK 465     HIS B   225                                                      
REMARK 465     HIS B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     ALA B   546                                                      
REMARK 465     ARG B   547                                                      
REMARK 465     ASN B   548                                                      
REMARK 465     PRO B   549                                                      
REMARK 465     PRO B   550                                                      
REMARK 465     VAL B   551                                                      
REMARK 465     VAL B   552                                                      
REMARK 465     SER B   553                                                      
REMARK 465     LYS B   554                                                      
REMARK 465     MET B   555                                                      
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    GLU A 269     -148.10   -120.21                                   
REMARK 500    ASP A 335     -125.81     62.96                                   
REMARK 500    ASN A 359      -45.06     80.69                                   
REMARK 500    PHE A 381       36.05    -87.75                                   
REMARK 500    MET A 419       76.30    -64.76                                   
REMARK 500    HIS A 420      -44.41   -151.69                                   
REMARK 500    ASN A 431       34.00   -142.02                                   
REMARK 500    SER A 544      -70.77   -104.35                                   
REMARK 500    SER B 231     -160.89   -120.81                                   
REMARK 500    GLU B 269     -143.27   -117.50                                   
REMARK 500    ASP B 335     -129.97     63.32                                   
REMARK 500    ASN B 359      -41.54     76.19                                   
REMARK 500    MET B 419       32.58    -99.81                                   
REMARK 500    HIS B 420      -72.27    -72.60                                   
REMARK 500    SER B 479       14.37   -145.82                                   
REMARK 500    SER B 544      -61.55    -94.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  247     VAL A  248                 -148.79                    
REMARK 500 MET A  291     ASP A  292                  146.88                    
REMARK 500 MET B  291     ASP B  292                  147.04                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue S94 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue S94 B 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X6X   RELATED DB: PDB                                   
DBREF  4X6Y A  230   555  UNP    P34913   HYES_HUMAN     230    555             
DBREF  4X6Y B  230   555  UNP    P34913   HYES_HUMAN     230    555             
SEQADV 4X6Y MET A  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y LYS A  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y LYS A  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y GLY A  223  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  224  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  225  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  226  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  227  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  228  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS A  229  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y MET B  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y LYS B  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y LYS B  222  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y GLY B  223  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  224  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  225  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  226  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  227  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  228  UNP  P34913              EXPRESSION TAG                 
SEQADV 4X6Y HIS B  229  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  336  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS          
SEQRES   2 A  336  ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS          
SEQRES   3 A  336  PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY          
SEQRES   4 A  336  PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP          
SEQRES   5 A  336  TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA          
SEQRES   6 A  336  GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY          
SEQRES   7 A  336  GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET          
SEQRES   8 A  336  GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS          
SEQRES   9 A  336  LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP          
SEQRES  10 A  336  GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO          
SEQRES  11 A  336  GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE          
SEQRES  12 A  336  ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE          
SEQRES  13 A  336  LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN          
SEQRES  14 A  336  GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU          
SEQRES  15 A  336  SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU          
SEQRES  16 A  336  SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY          
SEQRES  17 A  336  LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG          
SEQRES  18 A  336  MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN          
SEQRES  19 A  336  PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR          
SEQRES  20 A  336  ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER          
SEQRES  21 A  336  LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR          
SEQRES  22 A  336  ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN          
SEQRES  23 A  336  HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS          
SEQRES  24 A  336  ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO          
SEQRES  25 A  336  THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER          
SEQRES  26 A  336  ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET                  
SEQRES   1 B  336  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS          
SEQRES   2 B  336  ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS          
SEQRES   3 B  336  PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY          
SEQRES   4 B  336  PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP          
SEQRES   5 B  336  TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA          
SEQRES   6 B  336  GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY          
SEQRES   7 B  336  GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET          
SEQRES   8 B  336  GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS          
SEQRES   9 B  336  LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP          
SEQRES  10 B  336  GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO          
SEQRES  11 B  336  GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE          
SEQRES  12 B  336  ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE          
SEQRES  13 B  336  LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN          
SEQRES  14 B  336  GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU          
SEQRES  15 B  336  SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU          
SEQRES  16 B  336  SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY          
SEQRES  17 B  336  LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG          
SEQRES  18 B  336  MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN          
SEQRES  19 B  336  PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR          
SEQRES  20 B  336  ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER          
SEQRES  21 B  336  LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR          
SEQRES  22 B  336  ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN          
SEQRES  23 B  336  HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS          
SEQRES  24 B  336  ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO          
SEQRES  25 B  336  THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER          
SEQRES  26 B  336  ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET                  
HET    S94  A 601      25                                                       
HET    S94  B 601      25                                                       
HETNAM     S94 4-PHENOXY-N-[(1S,2R)-2-PHENYLCYCLOPROPYL]PIPERIDINE-1-           
HETNAM   2 S94  CARBOXAMIDE                                                     
FORMUL   3  S94    2(C21 H24 N2 O2)                                             
FORMUL   5  HOH   *88(H2 O)                                                     
HELIX    1 AA1 ASN A  233  MET A  237  5                                   5    
HELIX    2 AA2 SER A  270  ARG A  275  5                                   6    
HELIX    3 AA3 GLN A  277  ALA A  284  1                                   8    
HELIX    4 AA4 GLU A  304  TYR A  308  5                                   5    
HELIX    5 AA5 CYS A  309  GLY A  325  1                                  17    
HELIX    6 AA6 ASP A  335  TYR A  348  1                                  14    
HELIX    7 AA7 PRO A  371  ALA A  377  1                                   7    
HELIX    8 AA8 ASN A  378  VAL A  380  5                                   3    
HELIX    9 AA9 PHE A  381  PHE A  387  1                                   7    
HELIX   10 AB1 GLY A  391  ASN A  400  1                                  10    
HELIX   11 AB2 ASN A  400  PHE A  409  1                                  10    
HELIX   12 AB3 ALA A  411  SER A  415  5                                   5    
HELIX   13 AB4 LYS A  421  GLY A  426  1                                   6    
HELIX   14 AB5 THR A  443  LYS A  455  1                                  13    
HELIX   15 AB6 PHE A  459  TRP A  465  1                                   7    
HELIX   16 AB7 ASN A  468  CYS A  477  1                                  10    
HELIX   17 AB8 LYS A  478  LEU A  480  5                                   3    
HELIX   18 AB9 VAL A  500  GLN A  505  5                                   6    
HELIX   19 AC1 HIS A  506  ILE A  511  5                                   6    
HELIX   20 AC2 TRP A  525  LYS A  530  1                                   6    
HELIX   21 AC3 LYS A  530  ASP A  545  1                                  16    
HELIX   22 AC4 ASN B  233  MET B  237  5                                   5    
HELIX   23 AC5 SER B  270  ARG B  275  5                                   6    
HELIX   24 AC6 GLN B  277  ALA B  284  1                                   8    
HELIX   25 AC7 GLU B  304  TYR B  308  5                                   5    
HELIX   26 AC8 CYS B  309  GLY B  325  1                                  17    
HELIX   27 AC9 ASP B  335  TYR B  348  1                                  14    
HELIX   28 AD1 SER B  370  LYS B  376  1                                   7    
HELIX   29 AD2 ALA B  377  VAL B  380  5                                   4    
HELIX   30 AD3 PHE B  381  PHE B  387  1                                   7    
HELIX   31 AD4 GLY B  391  ASN B  400  1                                  10    
HELIX   32 AD5 ASN B  400  PHE B  409  1                                  10    
HELIX   33 AD6 ALA B  411  SER B  415  5                                   5    
HELIX   34 AD7 LYS B  421  GLY B  426  1                                   6    
HELIX   35 AD8 THR B  443  GLY B  458  1                                  16    
HELIX   36 AD9 PHE B  459  TRP B  465  1                                   7    
HELIX   37 AE1 ASN B  468  CYS B  477  1                                  10    
HELIX   38 AE2 VAL B  500  GLN B  505  5                                   6    
HELIX   39 AE3 HIS B  506  TRP B  510  5                                   5    
HELIX   40 AE4 TRP B  525  LYS B  530  1                                   6    
HELIX   41 AE5 LYS B  530  ASP B  545  1                                  16    
SHEET    1 AA116 LYS A 515  ILE A 519  0                                        
SHEET    2 AA116 ALA A 488  ALA A 493  1  N  THR A 492   O  ILE A 519           
SHEET    3 AA116 VAL A 352  LEU A 358  1  N  SER A 357   O  VAL A 491           
SHEET    4 AA116 ALA A 329  HIS A 334  1  N  GLY A 333   O  LEU A 358           
SHEET    5 AA116 ALA A 260  CYS A 264  1  N  CYS A 262   O  VAL A 330           
SHEET    6 AA116 ARG A 287  MET A 291  1  O  LEU A 289   N  VAL A 261           
SHEET    7 AA116 VAL A 248  LEU A 255 -1  N  LEU A 255   O  VAL A 288           
SHEET    8 AA116 SER A 238  LYS A 245 -1  N  GLY A 240   O  PHE A 252           
SHEET    9 AA116 SER B 238  LYS B 245 -1  O  HIS B 239   N  TYR A 241           
SHEET   10 AA116 VAL B 248  LEU B 255 -1  O  PHE B 252   N  GLY B 240           
SHEET   11 AA116 ARG B 287  MET B 291 -1  O  VAL B 288   N  LEU B 255           
SHEET   12 AA116 ALA B 260  CYS B 264  1  N  LEU B 263   O  LEU B 289           
SHEET   13 AA116 ALA B 329  HIS B 334  1  O  VAL B 330   N  CYS B 262           
SHEET   14 AA116 VAL B 352  LEU B 358  1  O  LEU B 358   N  GLY B 333           
SHEET   15 AA116 ALA B 488  ALA B 493  1  O  LEU B 489   N  SER B 357           
SHEET   16 AA116 LYS B 515  ILE B 519  1  O  LYS B 515   N  ALA B 488           
CISPEP   1 PHE A  267    PRO A  268          0       -11.57                     
CISPEP   2 PHE B  267    PRO B  268          0       -13.48                     
SITE     1 AC1  9 PHE A 267  ASP A 335  MET A 339  TYR A 383                    
SITE     2 AC1  9 GLN A 384  LEU A 408  TYR A 466  LEU A 499                    
SITE     3 AC1  9 HIS A 524                                                     
SITE     1 AC2  8 PHE B 267  ASP B 335  TRP B 336  MET B 339                    
SITE     2 AC2  8 TYR B 383  LEU B 408  TYR B 466  HIS B 524                    
CRYST1  129.228   80.722   87.326  90.00 126.22  90.00 C 1 2 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      0.007738  0.000000  0.005668        0.00000                         
SCALE2      0.000000  0.012388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014194        0.00000                         
TER    2547      ASP A 545                                                      
TER    5094      ASP B 545                                                      
MASTER      448    0    2   41   16    0    5    6 5230    2   50   52          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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