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LongText Report for: 4WCV-pdb

Name Class
4WCV-pdb
HEADER    HYDROLASE                               05-SEP-14   4WCV              
TITLE     HALOALKANE DEHALOGENASE DHAA MUTANT FROM RHODOCOCCUS RHODOCHROUS      
TITLE    2 (T148L+G171Q+A172V+C176G)                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;                        
SOURCE   3 ORGANISM_TAXID: 1829;                                                
SOURCE   4 GENE: DHAA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PAQN                                      
KEYWDS    HYDROLASE, MUTATION IN TUNNEL ACCESS                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HOLUBEVA,T.PRUDNIKOVA,I.KUTA-SMATANOVA,P.REZACOVA                   
REVDAT   1   15-OCT-14 4WCV    0                                                
JRNL        AUTH   V.LISKOVA,D.BEDNAR,T.PRUDNIKOVA,P.REZACOVA,T.KOUDELAKOVA,    
JRNL        AUTH 2 E.SEBESTOVA,I.KUTA-SMATANOVA,J.BREZOVSKY,R.CHALOUPKOVA,      
JRNL        AUTH 3 J.DAMBORSKY                                                  
JRNL        TITL   BALANCING THE STABILITY-ACTIVITY TRADE-OFF BY FINE-TUNING    
JRNL        TITL 2 DEHALOGENASE ACCESS TUNNELS                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26995                          
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) : 0.123                           
REMARK   3   R VALUE            (WORKING SET) : 0.120                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1421                            
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) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1882                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.1850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2365                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 477                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : -0.01000                                             
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.01000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.208         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.179         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2557 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3510 ; 1.846 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   314 ; 5.774 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   129 ;30.920 ;23.566       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   386 ;12.812 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.548 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   363 ; 0.137 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2061 ; 0.013 ; 0.022       
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):  1210 ; 1.103 ; 0.695       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1520 ; 1.408 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1347 ; 2.244 ; 0.798       
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):  4567 ; 3.449 ;  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):  2531 ; 4.112 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2436 ;10.696 ; 5.000       
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  : 9                                          
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     4        A   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0760   1.4900  -6.6560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0146 T22:   0.0049                                     
REMARK   3      T33:   0.0088 T12:  -0.0075                                     
REMARK   3      T13:  -0.0107 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0941 L22:   0.0728                                     
REMARK   3      L33:   0.0877 L12:  -0.0263                                     
REMARK   3      L13:  -0.0414 L23:   0.0127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0025 S12:   0.0065 S13:  -0.0028                       
REMARK   3      S21:  -0.0024 S22:  -0.0038 S23:   0.0099                       
REMARK   3      S31:  -0.0005 S32:  -0.0077 S33:   0.0013                       
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   133        A   144                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5120  -8.9670  14.4840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0260 T22:   0.0178                                     
REMARK   3      T33:   0.0130 T12:  -0.0077                                     
REMARK   3      T13:   0.0056 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2545 L22:   0.5393                                     
REMARK   3      L33:   0.4698 L12:   0.3681                                     
REMARK   3      L13:   0.3436 L23:   0.4913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0265 S12:   0.0105 S13:  -0.0039                       
REMARK   3      S21:  -0.0517 S22:   0.0252 S23:  -0.0091                       
REMARK   3      S31:  -0.0276 S32:   0.0102 S33:   0.0014                       
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   145        A   158                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3500  -0.4640  20.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0197 T22:   0.0174                                     
REMARK   3      T33:   0.0106 T12:  -0.0032                                     
REMARK   3      T13:  -0.0097 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2300 L22:   0.5915                                     
REMARK   3      L33:   0.2655 L12:  -0.3543                                     
REMARK   3      L13:  -0.2384 L23:   0.3545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0149 S12:  -0.0132 S13:  -0.0022                       
REMARK   3      S21:   0.0269 S22:   0.0072 S23:   0.0078                       
REMARK   3      S31:   0.0085 S32:   0.0087 S33:   0.0077                       
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 :   A   159        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2890   9.0380  18.0270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0179 T22:   0.0079                                     
REMARK   3      T33:   0.0070 T12:  -0.0050                                     
REMARK   3      T13:  -0.0064 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8467 L22:   0.1587                                     
REMARK   3      L33:   0.2509 L12:  -0.3209                                     
REMARK   3      L13:  -0.4356 L23:   0.1336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0062 S12:  -0.0330 S13:   0.0231                       
REMARK   3      S21:   0.0035 S22:   0.0105 S23:  -0.0195                       
REMARK   3      S31:  -0.0011 S32:   0.0173 S33:  -0.0042                       
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 :   A   168        A   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2970  11.6440   7.6700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0175 T22:   0.0089                                     
REMARK   3      T33:   0.0163 T12:  -0.0101                                     
REMARK   3      T13:  -0.0121 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3429 L22:   0.1439                                     
REMARK   3      L33:   0.1033 L12:  -0.1738                                     
REMARK   3      L13:  -0.0734 L23:   0.1066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:  -0.0159 S13:   0.0154                       
REMARK   3      S21:   0.0029 S22:   0.0106 S23:  -0.0113                       
REMARK   3      S31:  -0.0042 S32:   0.0087 S33:  -0.0037                       
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 :   A   186        A   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2980  15.6270   5.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0195 T22:   0.0094                                     
REMARK   3      T33:   0.0100 T12:  -0.0041                                     
REMARK   3      T13:  -0.0098 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4548 L22:   0.6742                                     
REMARK   3      L33:   0.5109 L12:   0.0982                                     
REMARK   3      L13:  -0.4538 L23:  -0.0386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:   0.0245 S13:   0.0314                       
REMARK   3      S21:   0.0091 S22:   0.0082 S23:   0.0147                       
REMARK   3      S31:  -0.0104 S32:  -0.0065 S33:  -0.0237                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   197        A   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7930  -7.6330   7.7960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0159 T22:   0.0068                                     
REMARK   3      T33:   0.0123 T12:  -0.0074                                     
REMARK   3      T13:  -0.0099 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0590 L22:   0.2971                                     
REMARK   3      L33:   0.0915 L12:  -0.0146                                     
REMARK   3      L13:  -0.0473 L23:   0.0486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:   0.0034 S13:  -0.0120                       
REMARK   3      S21:   0.0065 S22:  -0.0081 S23:   0.0181                       
REMARK   3      S31:   0.0056 S32:  -0.0021 S33:   0.0092                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   231        A   263                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4000 -11.1430  -1.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0200 T22:   0.0175                                     
REMARK   3      T33:   0.0126 T12:   0.0010                                     
REMARK   3      T13:  -0.0079 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0117 L22:   0.3266                                     
REMARK   3      L33:   0.1324 L12:   0.0471                                     
REMARK   3      L13:   0.0132 L23:   0.1181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0048 S12:  -0.0065 S13:  -0.0026                       
REMARK   3      S21:   0.0150 S22:   0.0070 S23:  -0.0061                       
REMARK   3      S31:   0.0227 S32:   0.0092 S33:  -0.0022                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   264        A   295                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2010  -0.5740  -7.9940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0167 T22:   0.0049                                     
REMARK   3      T33:   0.0117 T12:  -0.0060                                     
REMARK   3      T13:  -0.0094 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1278 L22:   0.0874                                     
REMARK   3      L33:   0.2371 L12:   0.0108                                     
REMARK   3      L13:  -0.0120 L23:   0.1034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0053 S12:  -0.0047 S13:  -0.0060                       
REMARK   3      S21:  -0.0077 S22:   0.0028 S23:  -0.0151                       
REMARK   3      S31:  -0.0037 S32:   0.0081 S33:  -0.0081                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4WCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202749.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OTHER                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541790                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : DIFFRACTOMETER                     
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28416                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 9.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3G9X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE TRIHYDRATE, AMMONIUM      
REMARK 280  ACETATE, PEG 4000                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
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 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     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1008     O    HOH A  1020              1.92            
REMARK 500   O    HOH A   701     O    HOH A  1008              1.98            
REMARK 500   O4   PGE A   502     O    HOH A  1076              2.09            
REMARK 500   OE2  GLU A   183     O    HOH A   601              2.15            
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   O    HOH A   653     O    HOH A   665     1565     2.08            
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  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 133   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 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                                                                      
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    PRO A  42       51.00   -107.80                                   
REMARK 500    THR A  43     -158.68   -105.26                                   
REMARK 500    GLU A  98      -92.24   -107.96                                   
REMARK 500    GLU A  98      -88.28   -111.07                                   
REMARK 500    ASP A 106     -130.44     50.16                                   
REMARK 500    ARG A 153       46.14    -91.23                                   
REMARK 500    ASP A 156      -71.73   -102.85                                   
REMARK 500    GLN A 171      -63.95   -107.22                                   
REMARK 500    VAL A 245      -77.22   -134.67                                   
REMARK 500    LEU A 271      -92.65   -120.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 875        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A 938        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A1041        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH A1042        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH A1052        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH A1053        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH A1056        DISTANCE =  7.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4F5Z   RELATED DB: PDB                                   
REMARK 900 4F5Z CONTAINS L95V, A172V MUTATIONS IN ACCESS TUNNEL                 
REMARK 900 RELATED ID: 4F60   RELATED DB: PDB                                   
REMARK 900 4F60 CONTAINS T148L, G171Q, A172V, C176F MUTATIOSN IN ACCESS TUNNEL  
DBREF  4WCV A    1   293  UNP    P0A3G3   DHAA_RHOSO       1    293             
SEQADV 4WCV LEU A  148  UNP  P0A3G3    THR   148 ENGINEERED MUTATION            
SEQADV 4WCV GLN A  171  UNP  P0A3G3    GLY   171 ENGINEERED MUTATION            
SEQADV 4WCV VAL A  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION            
SEQADV 4WCV GLY A  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 4WCV HIS A  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4WCV HIS A  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4WCV HIS A  296  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4WCV HIS A  297  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4WCV HIS A  298  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 4WCV HIS A  299  UNP  P0A3G3              EXPRESSION TAG                 
SEQRES   1 A  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 A  299  TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP          
SEQRES   3 A  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 A  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 A  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 A  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 A  299  TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 A  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 A  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 A  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU          
SEQRES  11 A  299  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 A  299  PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR ALA ASP          
SEQRES  13 A  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 A  299  GLU GLN VAL LEU PRO LYS GLY VAL VAL ARG PRO LEU THR          
SEQRES  15 A  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 A  299  PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 A  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU          
SEQRES  18 A  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 A  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 A  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 A  299  ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 A  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 A  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
HET     CL  A 501       1                                                       
HET    PGE  A 502      10                                                       
HET    ACT  A 503       4                                                       
HET    ACT  A 504       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     ACT ACETATE ION                                                      
FORMUL   2   CL    CL 1-                                                        
FORMUL   3  PGE    C6 H14 O4                                                    
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6  HOH   *477(H2 O)                                                    
HELIX    1 AA1 SER A   44  ARG A   49  5                                   6    
HELIX    2 AA2 ILE A   51  ALA A   56  1                                   6    
HELIX    3 AA3 PHE A   80  LEU A   95  1                                  16    
HELIX    4 AA4 ASP A  106  ASN A  119  1                                  14    
HELIX    5 AA5 THR A  137  TRP A  141  5                                   5    
HELIX    6 AA6 PRO A  142  PHE A  144  5                                   3    
HELIX    7 AA7 ALA A  145  ARG A  153  1                                   9    
HELIX    8 AA8 ASP A  156  ILE A  163  1                                   8    
HELIX    9 AA9 ASN A  166  GLN A  171  1                                   6    
HELIX   10 AB1 GLN A  171  GLY A  176  1                                   6    
HELIX   11 AB2 THR A  182  GLU A  191  1                                  10    
HELIX   12 AB3 PRO A  192  LEU A  194  5                                   3    
HELIX   13 AB4 LYS A  195  ASP A  198  5                                   4    
HELIX   14 AB5 ARG A  199  LEU A  209  1                                  11    
HELIX   15 AB6 PRO A  215  SER A  232  1                                  18    
HELIX   16 AB7 PRO A  248  LEU A  259  1                                  12    
HELIX   17 AB8 TYR A  273  ASN A  278  1                                   6    
HELIX   18 AB9 ASN A  278  LEU A  290  1                                  13    
HELIX   19 AC1 PRO A  291  HIS A  294  5                                   4    
SHEET    1 AA1 8 HIS A  13  VAL A  17  0                                        
SHEET    2 AA1 8 GLU A  20  VAL A  27 -1  O  MET A  22   N  VAL A  15           
SHEET    3 AA1 8 CYS A  61  PRO A  64 -1  O  CYS A  61   N  VAL A  27           
SHEET    4 AA1 8 VAL A  35  LEU A  38  1  N  PHE A  37   O  ILE A  62           
SHEET    5 AA1 8 VAL A 100  HIS A 105  1  O  VAL A 101   N  LEU A  36           
SHEET    6 AA1 8 VAL A 123  MET A 129  1  O  ALA A 127   N  LEU A 102           
SHEET    7 AA1 8 LYS A 236  PRO A 243  1  O  LEU A 237   N  CYS A 128           
SHEET    8 AA1 8 CYS A 262  GLY A 270  1  O  LYS A 263   N  LEU A 238           
CISPEP   1 ASN A   41    PRO A   42          0        -3.19                     
CISPEP   2 GLU A  214    PRO A  215          0        -2.86                     
CISPEP   3 GLU A  214    PRO A  215          0        -7.75                     
CISPEP   4 THR A  242    PRO A  243          0         5.00                     
SITE     1 AC1  5 ASN A  41  TRP A 107  PRO A 206  PGE A 502                    
SITE     2 AC1  5 HOH A1076                                                     
SITE     1 AC2  6 ASP A 106  PHE A 144  PHE A 168  LYS A 175                    
SITE     2 AC2  6  CL A 501  HOH A1076                                          
SITE     1 AC3  8 PRO A  12  GLN A 231  PRO A 233  PRO A 260                    
SITE     2 AC3  8 HOH A 603  HOH A 628  HOH A 663  HOH A 689                    
SITE     1 AC4  7 THR A  33  HIS A  59  LYS A 124  LEU A 290                    
SITE     2 AC4  7 HIS A 294  HOH A 823  HOH A 982                               
CRYST1   42.585   44.477   46.508 115.47  98.79 109.12 P 1           1          
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      0.023482  0.008142  0.009113        0.00000                         
SCALE2      0.000000  0.023797  0.014263        0.00000                         
SCALE3      0.000000  0.000000  0.025366        0.00000                         
TER    2450      HIS A 296                                                      
MASTER      522    0    4   19    8    0    8    6 2861    1   18   23          
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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