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LongText Report for: 2WFL-pdb

Name Class
2WFL-pdb
HEADER    HYDROLASE                               08-APR-09   2WFL              
TITLE     CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE ESTERASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYNEURIDINE-ALDEHYDE ESTERASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.78;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: POLYNEURIDINE-ALDEHYDE ESTERASE;                           
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 3.1.1.78;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;                           
SOURCE   3 ORGANISM_COMMON: SERPENTWOOD;                                        
SOURCE   4 ORGANISM_TAXID: 4060;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: M15PREP4;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE-2;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;                           
SOURCE  12 ORGANISM_COMMON: SERPENTWOOD;                                        
SOURCE  13 ORGANISM_TAXID: 4060;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: M15PREP4;                                  
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PQE-2                                     
KEYWDS    ALKALOID METABOLISM, MONOTERPENOID INDOLE ALKALOIDS, PNAE,            
KEYWDS   2 HYDROLASE, SERINE ESTERASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.YANG,M.HILL,S.PANJIKAR,M.WANG,J.STOECKIGT                           
REVDAT   1   18-AUG-09 2WFL    0                                                
JRNL        AUTH   L.YANG,M.HILL,M.WANG,S.PANJIKAR,J.STOCKIGT                   
JRNL        TITL   STRUCTURAL BASIS AND ENZYMATIC MECHANISM OF THE              
JRNL        TITL 2 BIOSYNTHESIS OF C9- FROM C10-MONOTERPENOID INDOLE            
JRNL        TITL 3 ALKALOIDS.                                                   
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  48  5211 2009              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   19496101                                                     
JRNL        DOI    10.1002/ANIE.200900150                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
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) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 35684                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1046                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2599                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4034                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 303                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.17000                                              
REMARK   3    B22 (A**2) : -1.32000                                             
REMARK   3    B33 (A**2) : -1.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.188         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.780         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4146 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5566 ; 1.897 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   502 ; 7.550 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;34.099 ;24.659       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   741 ;15.995 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;20.104 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   590 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3072 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2548 ; 0.899 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4086 ; 1.626 ; 2.500       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1598 ; 3.630 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1480 ; 5.229 ;10.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      9       A      54      2                      
REMARK   3           1     B      9       B      54      2                      
REMARK   3           2     A     60       A     113      2                      
REMARK   3           2     B     60       B     113      2                      
REMARK   3           3     A    157       A     262      2                      
REMARK   3           3     B    157       B     262      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    820 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    820 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    797 ;  0.22 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    797 ;  0.22 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    820 ;  0.22 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    820 ;  0.22 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    797 ;  0.30 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    797 ;  0.30 ;  2.00           
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     9        A    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3615 104.6133  18.9323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1091 T22:  -0.1664                                     
REMARK   3      T33:  -0.1489 T12:   0.0724                                     
REMARK   3      T13:  -0.0301 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2627 L22:   2.6489                                     
REMARK   3      L33:   2.7434 L12:   0.6366                                     
REMARK   3      L13:  -0.2349 L23:  -0.6094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0846 S12:   0.1758 S13:  -0.3988                       
REMARK   3      S21:  -0.3401 S22:  -0.1053 S23:  -0.1132                       
REMARK   3      S31:   0.3845 S32:   0.0049 S33:   0.0207                       
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    60        A   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0912 106.5370   9.0303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0262 T22:  -0.0420                                     
REMARK   3      T33:  -0.1585 T12:   0.1528                                     
REMARK   3      T13:   0.0274 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7223 L22:   3.7300                                     
REMARK   3      L33:   3.8214 L12:   1.0544                                     
REMARK   3      L13:   0.1782 L23:   1.8193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:   0.3797 S13:  -0.2945                       
REMARK   3      S21:  -0.4545 S22:  -0.0530 S23:  -0.3066                       
REMARK   3      S31:   0.4997 S32:   0.3896 S33:  -0.0502                       
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   157        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4344 113.9559  10.5591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0427 T22:  -0.0870                                     
REMARK   3      T33:  -0.1386 T12:   0.0881                                     
REMARK   3      T13:  -0.0550 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7187 L22:   2.0522                                     
REMARK   3      L33:   2.5049 L12:  -0.4033                                     
REMARK   3      L13:  -0.1870 L23:   0.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2003 S12:   0.4894 S13:  -0.0610                       
REMARK   3      S21:  -0.5389 S22:  -0.0689 S23:   0.1235                       
REMARK   3      S31:   0.1420 S32:  -0.1995 S33:  -0.1314                       
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     9        B    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7378 115.6252  38.9784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2079 T22:  -0.2150                                     
REMARK   3      T33:  -0.1875 T12:   0.0329                                     
REMARK   3      T13:   0.0060 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5010 L22:   2.8942                                     
REMARK   3      L33:   2.4192 L12:  -1.2803                                     
REMARK   3      L13:   1.0910 L23:   0.0314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:  -0.0206 S13:   0.2493                       
REMARK   3      S21:   0.1103 S22:   0.0129 S23:   0.2217                       
REMARK   3      S31:  -0.1706 S32:  -0.2348 S33:   0.0540                       
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    60        B   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9437 117.9304  50.1232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1109 T22:  -0.1389                                     
REMARK   3      T33:  -0.1866 T12:   0.0574                                     
REMARK   3      T13:   0.0136 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5215 L22:   3.0241                                     
REMARK   3      L33:   2.8976 L12:   0.0487                                     
REMARK   3      L13:  -0.4362 L23:   1.2552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0390 S12:  -0.2987 S13:   0.1972                       
REMARK   3      S21:   0.3201 S22:   0.0898 S23:   0.0239                       
REMARK   3      S31:  -0.1515 S32:  -0.0205 S33:  -0.0508                       
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   157        B   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3270 104.0289  46.6786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1122 T22:  -0.1009                                     
REMARK   3      T33:  -0.0764 T12:   0.0103                                     
REMARK   3      T13:   0.0351 T23:   0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6015 L22:   2.4848                                     
REMARK   3      L33:   2.0707 L12:  -0.1884                                     
REMARK   3      L13:   0.0305 L23:   0.5384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:  -0.3765 S13:  -0.1749                       
REMARK   3      S21:   0.4148 S22:   0.0590 S23:   0.3250                       
REMARK   3      S31:   0.2978 S32:  -0.2524 S33:  -0.0633                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2WFL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-APR-09.                 
REMARK 100 THE PDBE ID CODE IS EBI-39424.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : SILICON 111                        
REMARK 200  OPTICS                         : DOUBLE CRYSTAL SI 111              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36861                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.6                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 32.50                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW,MOLREP                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1XKL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M BIS-TRIS, 0.25M LI2SO4,            
REMARK 280  25%POLYETHYLENE GLYCOL 3350, PH6.30.                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       46.37900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       88.45850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.37900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       88.45850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.37900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       88.45850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.37900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       88.45850            
REMARK 290   SMTRY3   8  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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     SER A   264                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     SER B   264                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG B    54  -  O    HOH B  2035              1.87            
REMARK 500   O    LYS B   196  -  O    HOH B  2126              2.16            
REMARK 500   O    HOH A  2007  -  O    HOH A  2095              2.15            
REMARK 500   O    HOH A  2019  -  O    HOH A  2023              1.81            
REMARK 500   O    HOH A  2042  -  O    HOH A  2082              2.12            
REMARK 500   O    HOH A  2061  -  O    HOH A  2069              2.05            
REMARK 500   O    HOH B  2041  -  O    HOH B  2151              2.16            
REMARK 500   O    HOH B  2098  -  O    HOH B  2153              1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   CA   ALA A   134     O    ALA B    73     6564      1.95           
REMARK 500   CB   ALA A   134     C    ALA B    73     6564      1.74           
REMARK 500   CB   ALA A   134     O    ALA B    73     6564      0.58           
REMARK 500   ND2  ASN A   147     CD   PRO A   148     3655      1.96           
REMARK 500   CD   PRO A   148     CD   PRO A   148     3655      2.10           
REMARK 500   CB   MET A   153     OD2  ASP B    78     6564      1.68           
REMARK 500   CG   MET A   153     CG   ASP B    78     6564      1.72           
REMARK 500   CG   MET A   153     OD2  ASP B    78     6564      0.53           
REMARK 500   SD   MET A   153     CG   ASP B    78     6564      0.85           
REMARK 500   SD   MET A   153     OD1  ASP B    78     6564      0.94           
REMARK 500   SD   MET A   153     OD2  ASP B    78     6564      1.49           
REMARK 500   CE   MET A   153     CA   ASP B    78     6564      1.84           
REMARK 500   CE   MET A   153     CB   ASP B    78     6564      0.55           
REMARK 500   CE   MET A   153     CG   ASP B    78     6564      1.22           
REMARK 500   CE   MET A   153     OD1  ASP B    78     6564      2.01           
REMARK 500   CA   SER A   199     OE1  GLU B   149     3655      1.73           
REMARK 500   C    SER A   199     CD   GLU B   149     3655      1.92           
REMARK 500   C    SER A   199     OE1  GLU B   149     3655      1.41           
REMARK 500   CB   SER A   199     OE1  GLU B   149     3655      1.76           
REMARK 500   N    THR A   200     CD   GLU B   149     3655      1.69           
REMARK 500   N    THR A   200     OE2  GLU B   149     3655      1.56           
REMARK 500   N    THR A   200     OE1  GLU B   149     3655      1.56           
REMARK 500   CA   THR A   200     CD   GLU B   149     3655      2.16           
REMARK 500   CA   THR A   200     OE2  GLU B   149     3655      1.10           
REMARK 500   C    THR A   200     CD   GLU B   149     3655      1.89           
REMARK 500   C    THR A   200     OE2  GLU B   149     3655      0.94           
REMARK 500   C    THR A   200     O    HOH B  2094     3655      2.04           
REMARK 500   O    THR A   200     OE2  GLU B   149     3655      2.14           
REMARK 500   O    THR A   200     O    HOH B  2094     3655      2.14           
REMARK 500   CB   THR A   200     O    HOH B  2091     3655      1.77           
REMARK 500   OG1  THR A   200     O    HOH B  2091     3655      0.75           
REMARK 500   N    GLU A   201     CD   GLU B   149     3655      1.32           
REMARK 500   N    GLU A   201     OE2  GLU B   149     3655      1.32           
REMARK 500   N    GLU A   201     CB   GLU B   149     3655      2.15           
REMARK 500   N    GLU A   201     CG   GLU B   149     3655      1.42           
REMARK 500   CA   GLU A   201     CB   GLU B   149     3655      1.83           
REMARK 500   CA   GLU A   201     CG   GLU B   149     3655      1.53           
REMARK 500   C    GLU A   201     CG   GLU B   149     3655      2.01           
REMARK 500   CB   GLU A   201     CA   GLU B   149     3655      1.05           
REMARK 500   CB   GLU A   201     C    GLU B   149     3655      2.08           
REMARK 500   CB   GLU A   201     CB   GLU B   149     3655      0.87           
REMARK 500   CB   GLU A   201     CG   GLU B   149     3655      1.86           
REMARK 500   CG   GLU A   201     O    GLU B   149     3655      1.67           
REMARK 500   CG   GLU A   201     CA   GLU B   149     3655      1.30           
REMARK 500   CG   GLU A   201     C    GLU B   149     3655      1.52           
REMARK 500   CD   GLU A   201     O    GLU B   149     3655      1.25           
REMARK 500   CD   GLU A   201     CA   GLU B   149     3655      1.83           
REMARK 500   CD   GLU A   201     C    GLU B   149     3655      0.66           
REMARK 500   CD   GLU A   201     N    ASN B   150     3655      1.44           
REMARK 500   OE1  GLU A   201     O    GLU B   149     3655      1.90           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 SYMMETRY CONTACTS                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A  30   CE    LYS A  30   NZ     -0.152                       
REMARK 500    VAL A  43   CB    VAL A  43   CG2    -0.166                       
REMARK 500    ARG A  53   CG    ARG A  53   CD     -0.194                       
REMARK 500    GLU A 102   CD    GLU A 102   OE1    -0.076                       
REMARK 500    VAL B  43   CB    VAL B  43   CG2    -0.131                       
REMARK 500    ARG B  53   CD    ARG B  53   NE     -0.116                       
REMARK 500    ARG B  53   CG    ARG B  53   CD     -0.222                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  53   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    GLU A 102   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    VAL B  43   CG1 -  CB  -  CG2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG B  53   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ASP B 234   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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    LEU A  21     -158.11   -121.06                                   
REMARK 500    ASP A  56        2.97    -66.40                                   
REMARK 500    SER A  87     -131.41     57.00                                   
REMARK 500    LEU A 138     -119.58     60.73                                   
REMARK 500    ASN A 150       69.93   -163.73                                   
REMARK 500    LYS A 196      104.54     -3.15                                   
REMARK 500    ARG A 202      -75.13   -108.80                                   
REMARK 500    MET A 245       67.23   -107.09                                   
REMARK 500    LEU B  21     -156.06   -117.05                                   
REMARK 500    SER B  87     -129.59     48.76                                   
REMARK 500    PRO B 133      143.86    -37.73                                   
REMARK 500    ASP B 135       42.20   -108.45                                   
REMARK 500    LEU B 138     -119.60     53.86                                   
REMARK 500    ASN B 150       69.31   -152.62                                   
REMARK 500    ARG B 202      -79.87   -107.70                                   
REMARK 500    MET B 245       65.89   -108.03                                   
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 ALA A  195     LYS A  196                  109.54                    
REMARK 500 ALA B  195     LYS B  196                   70.29                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS B 256        -14.03                                           
REMARK 500    CME B 257        -15.95                                           
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1264                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1264                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WFM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE                         
REMARK 900  ESTERASE                                                            
DBREF  2WFL A    1   264  UNP    Q9SE93   PNAE_RAUSE       1    264             
DBREF  2WFL B    1   264  UNP    Q9SE93   PNAE_RAUSE       1    264             
SEQRES   1 A  264  MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE          
SEQRES   2 A  264  VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP          
SEQRES   3 A  264  TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS          
SEQRES   4 A  264  VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO          
SEQRES   5 A  264  ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER          
SEQRES   6 A  264  GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP          
SEQRES   7 A  264  GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET          
SEQRES   8 A  264  SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE          
SEQRES   9 A  264  SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO          
SEQRES  10 A  264  ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU          
SEQRES  11 A  264  LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER          
SEQRES  12 A  264  THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE          
SEQRES  13 A  264  LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN          
SEQRES  14 A  264  CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR          
SEQRES  15 A  264  ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA          
SEQRES  16 A  264  LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG          
SEQRES  17 A  264  ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL          
SEQRES  18 A  264  GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP          
SEQRES  19 A  264  LYS VAL LYS GLU ILE LYS GLU ALA ASP HIS MET GLY MET          
SEQRES  20 A  264  LEU SER GLN PRO ARG GLU VAL CME LYS CYS LEU LEU ASP          
SEQRES  21 A  264  ILE SER ASP SER                                              
SEQRES   1 B  264  MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE          
SEQRES   2 B  264  VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP          
SEQRES   3 B  264  TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS          
SEQRES   4 B  264  VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO          
SEQRES   5 B  264  ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER          
SEQRES   6 B  264  GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP          
SEQRES   7 B  264  GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET          
SEQRES   8 B  264  SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE          
SEQRES   9 B  264  SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO          
SEQRES  10 B  264  ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU          
SEQRES  11 B  264  LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER          
SEQRES  12 B  264  THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE          
SEQRES  13 B  264  LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN          
SEQRES  14 B  264  CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR          
SEQRES  15 B  264  ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA          
SEQRES  16 B  264  LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG          
SEQRES  17 B  264  ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL          
SEQRES  18 B  264  GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP          
SEQRES  19 B  264  LYS VAL LYS GLU ILE LYS GLU ALA ASP HIS MET GLY MET          
SEQRES  20 B  264  LEU SER GLN PRO ARG GLU VAL CME LYS CME LEU LEU ASP          
SEQRES  21 B  264  ILE SER ASP SER                                              
MODRES 2WFL CME A  255  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 2WFL CME B  255  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 2WFL CME B  257  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 255      10                                                       
HET    CME  B 255      10                                                       
HET    CME  B 257      10                                                       
HET    SO4  B1264       5                                                       
HET    SO4  A1264       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  CME    3(C5 H11 N O3 S2)                                            
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *303(H2 O1)                                                   
HELIX    1   1 GLY A   22  TYR A   27  5                                   6    
HELIX    2   2 LYS A   28  ALA A   36  1                                   9    
HELIX    3   3 ARG A   54  ILE A   58  5                                   5    
HELIX    4   4 THR A   60  ILE A   75  1                                  16    
HELIX    5   5 PHE A   88  TYR A  100  1                                  13    
HELIX    6   6 THR A  122  CYS A  132  1                                  11    
HELIX    7   7 GLY A  158  MET A  166  1                                   9    
HELIX    8   8 SER A  171  THR A  182  1                                  12    
HELIX    9   9 PHE A  188  ALA A  193  1                                   6    
HELIX   10  10 ARG A  202  VAL A  206  5                                   5    
HELIX   11  11 PRO A  220  GLY A  232  1                                  13    
HELIX   12  12 MET A  245  GLN A  250  1                                   6    
HELIX   13  13 LYS A  256  ASP A  263  1                                   8    
HELIX   14  14 GLY B   22  TYR B   27  5                                   6    
HELIX   15  15 LYS B   28  ALA B   36  1                                   9    
HELIX   16  16 ARG B   54  ILE B   58  5                                   5    
HELIX   17  17 THR B   60  ILE B   75  1                                  16    
HELIX   18  18 PHE B   88  TYR B  100  1                                  13    
HELIX   19  19 THR B  122  CYS B  132  1                                  11    
HELIX   20  20 GLY B  158  MET B  166  1                                   9    
HELIX   21  21 SER B  171  THR B  182  1                                  12    
HELIX   22  22 PHE B  188  ALA B  193  1                                   6    
HELIX   23  23 ARG B  202  VAL B  206  5                                   5    
HELIX   24  24 PRO B  220  GLY B  232  1                                  13    
HELIX   25  25 MET B  245  GLN B  250  1                                   6    
HELIX   26  26 LEU B  258  ASP B  263  1                                   6    
SHEET    1  AA 6 LYS A  39  VAL A  43  0                                        
SHEET    2  AA 6 HIS A  12  VAL A  16  1  O  PHE A  13   N  THR A  41           
SHEET    3  AA 6 VAL A  81  HIS A  86  1  O  VAL A  82   N  VAL A  14           
SHEET    4  AA 6 ILE A 104  MET A 110  1  N  SER A 105   O  VAL A  81           
SHEET    5  AA 6 ARG A 208  CYS A 213  1  O  ALA A 209   N  PHE A 109           
SHEET    6  AA 6 LYS A 235  ILE A 239  1  O  LYS A 235   N  TYR A 210           
SHEET    1  AB 3 GLN A 141  TYR A 145  0                                        
SHEET    2  AB 3 GLY A 152  ILE A 156 -1  O  GLY A 152   N  TYR A 145           
SHEET    3  AB 3 GLY A 185  SER A 186 -1  O  GLY A 185   N  MET A 155           
SHEET    1  BA 6 LYS B  39  VAL B  43  0                                        
SHEET    2  BA 6 HIS B  12  VAL B  16  1  O  PHE B  13   N  THR B  41           
SHEET    3  BA 6 VAL B  81  HIS B  86  1  O  VAL B  82   N  VAL B  14           
SHEET    4  BA 6 ILE B 104  MET B 110  1  N  SER B 105   O  VAL B  81           
SHEET    5  BA 6 ARG B 208  CYS B 213  1  O  ALA B 209   N  PHE B 109           
SHEET    6  BA 6 LYS B 235  ILE B 239  1  O  LYS B 235   N  TYR B 210           
SHEET    1  BB 2 GLN B 141  TYR B 145  0                                        
SHEET    2  BB 2 GLY B 152  ILE B 156 -1  O  GLY B 152   N  TYR B 145           
LINK         C   VAL A 254                 N   CME A 255     1555   1555  1.28  
LINK         C   CME A 255                 N   LYS A 256     1555   1555  1.27  
LINK         C   VAL B 254                 N   CME B 255     1555   1555  1.29  
LINK         C   CME B 255                 N   LYS B 256     1555   1555  1.29  
LINK         C   LYS B 256                 N   CME B 257     1555   1555  1.28  
LINK         C   CME B 257                 N   LEU B 258     1555   1555  1.26  
SITE     1 AC1 10 GLY B 152  MET B 153  SER B 186  PHE B 188                    
SITE     2 AC1 10 PHE B 189  GLN B 190  HOH B2099  HOH B2151                    
SITE     3 AC1 10 HOH B2152  HOH B2153                                          
SITE     1 AC2  5 SER A  87  SER A 218  HIS A 244  HOH A2001                    
SITE     2 AC2  5 HOH A2150                                                     
CRYST1   92.758  176.917   75.697  90.00  90.00  90.00 C 2 2 21     16          
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      0.010781  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005652  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013211        0.00000                         
MTRIX1   1  0.708500  0.681800  0.182000      -73.44000    1                    
MTRIX2   1  0.685800 -0.726000  0.050360      173.20000    1                    
MTRIX3   1  0.166500  0.089170 -0.982000       43.62000    1                    
TER    2016      ASP A 263                                                      
TER    4036      ASP B 263                                                      
MASTER      627    0    5   26   17    0    5    9 4347    2   46   42          
END                                                                             

Send your questions or comments to :
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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