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LongText Report for: 1ODT-pdb

Name Class
1ODT-pdb
HEADER    HYDROLASE                               20-FEB-03   1ODT              
TITLE     CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH                  
TITLE    2 ACETATE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CEPHALOSPORIN C DEACETYLASE;                               
COMPND   3 SYNONYM: MULTI-FUNCTIONAL ESTERASE, CAH;                             
COMPND   4 CHAIN: C, H;                                                         
COMPND   5 EC: 3.1.1.41;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: COMPLEX WITH ACETATE                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   4 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   5 EXPRESSION_SYSTEM_VECTOR: PET26B;                                    
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PET26B                                    
KEYWDS    ALPHA/BETA HYDROLASE, ACETYLXYLAN, CARBOHYDRATE ESTERASE,             
KEYWDS   2 CEPHALOSPORIN, X-RAY STRUCTURE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VINCENT,S.J.CHARNOCK,K.H.G.VERSCHUEREN,J.P.TURKENBURG,              
AUTHOR   2 D.J.SCOTT,W.A.OFFEN,S.ROBERTS,G.PELL,H.J.GILBERT,                    
AUTHOR   3 J.A.BRANNIGAN,G.J.DAVIES                                             
REVDAT   1   10-JUL-03 1ODT    0                                                
JRNL        AUTH   F.VINCENT,S.CHARNOCK,K.VERSCHUEREN,J.TURKENBURG,             
JRNL        AUTH 2 D.SCOTT,W.OFFEN,S.ROBERTS,G.PELL,H.GILBERT,G.DAVIES,         
JRNL        AUTH 3 J.BRANNIGAN                                                  
JRNL        TITL   MULTIFUNCTIONAL XYLOOLIGOSACCHARIDE/CEPHALOSPORIN C          
JRNL        TITL 2 DEACETYLASE REVEALED BY THE HEXAMERIC STRUCTURE OF           
JRNL        TITL 3 THE BACILLUS SUBTILIS ENZYME AT 1.9A RESOLUTION              
JRNL        REF    J.MOL.BIOL.                   V. 330   593 2003              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.7  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
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) :   1.70                         
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) :  95.35                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) :  97.53                         
REMARK   3   NUMBER OF REFLECTIONS             :   63610                        
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) : 0.15752                         
REMARK   3   R VALUE            (WORKING SET) :  0.15569                        
REMARK   3   FREE R VALUE                     :  0.19120                        
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      :  3376                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           :      20                      
REMARK   3   BIN RESOLUTION RANGE HIGH           :    1.699                     
REMARK   3   BIN RESOLUTION RANGE LOW            :    1.743                     
REMARK   3   REFLECTION IN BIN     (WORKING SET) :     4548                     
REMARK   3   BIN R VALUE           (WORKING SET) :    0.224                     
REMARK   3   BIN FREE R VALUE SET COUNT          :      241                     
REMARK   3   BIN FREE R VALUE                    :    0.284                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5065                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 563                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  10.564                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) :    -0.94                                             
REMARK   3    B22 (A**2) :    -0.94                                             
REMARK   3    B33 (A**2) :     1.41                                             
REMARK   3    B12 (A**2) :    -0.47                                             
REMARK   3    B13 (A**2) :     0.00                                             
REMARK   3    B23 (A**2) :     0.00                                             
REMARK   3                                                                      
REMARK   3 ESTIMATED OVERALL COORDINATE ERROR.                                  
REMARK   3  ESU BASED ON R VALUE                            (A): 0.101          
REMARK   3  ESU BASED ON FREE R VALUE                       (A): 0.099          
REMARK   3  ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066          
REMARK   3  ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.004          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      :   0.967                       
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE :   0.958                       
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  5211 ; 0.016 ; 0.021          
REMARK   3   BOND LENGTHS OTHERS            (A):  4618 ; 0.002 ; 0.020          
REMARK   3   BOND ANGLES REFINED      (DEGREES):  7074 ; 1.589 ; 1.954          
REMARK   3   BOND ANGLES OTHERS       (DEGREES): 10775 ; 1.075 ; 3.000          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):   632 ; 5.869 ; 5.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):   755 ; 0.131 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  5800 ; 0.008 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  1078 ; 0.004 ; 0.020          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  1109 ; 0.227 ; 0.200          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  5575 ; 0.246 ; 0.200          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  2835 ; 0.089 ; 0.200          
REMARK   3   H-BOND (X...Y) REFINED         (A):   445 ; 0.188 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):    24 ; 0.218 ; 0.200          
REMARK   3   SYMMETRY VDW OTHERS            (A):    60 ; 0.330 ; 0.200          
REMARK   3   SYMMETRY H-BOND REFINED        (A):    37 ; 0.208 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  3164 ; 0.783 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  5096 ; 1.352 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  2047 ; 2.413 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  1978 ; 3.793 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  :    2                                       
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 :   C     1        C   317                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3370  77.9850  43.4120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0892 T22:   0.1150                                     
REMARK   3      T33:   0.0072 T12:   0.0058                                     
REMARK   3      T13:   0.0150 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3932 L22:   0.6111                                     
REMARK   3      L33:   0.3823 L12:  -0.0330                                     
REMARK   3      L13:   0.0887 L23:  -0.0952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:   0.0493 S13:  -0.0175                       
REMARK   3      S21:  -0.0398 S22:  -0.0017 S23:  -0.0373                       
REMARK   3      S31:   0.0179 S32:   0.0377 S33:   0.0054                       
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 :   H     1        H   317                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4900 106.8960  66.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0837 T22:   0.0979                                     
REMARK   3      T33:   0.0154 T12:  -0.0108                                     
REMARK   3      T13:  -0.0122 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4109 L22:   0.6824                                     
REMARK   3      L33:   0.3956 L12:  -0.0219                                     
REMARK   3      L13:  -0.0522 L23:  -0.1084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0033 S12:  -0.0236 S13:   0.0227                       
REMARK   3      S21:   0.0347 S22:  -0.0118 S23:  -0.0481                       
REMARK   3      S31:  -0.0368 S32:   0.0492 S33:   0.0150                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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              
REMARK   3   THE RIDING POSITIONS                                               
REMARK   4                                                                      
REMARK   4 1ODT COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 21-FEB-2003.                
REMARK 100 THE EBI ID CODE IS EBI-12218.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-2002                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
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   : 63610                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.69                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 95                                 
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.1                                
REMARK 200  R MERGE                    (I) : 0.048                              
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.9                               
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) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.393                              
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.7                                
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ODS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 43.1                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.5                         
REMARK 280  0.2 M NA ACETATE 30% MPD , 0.1M MGCL2,                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   Y-X,-X,Z                                                
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,Y-X,-Z                                               
REMARK 290       7555   2/3+X,1/3+Y,1/3+Z                                       
REMARK 290       8555   2/3-Y,1/3+X-Y,1/3+Z                                     
REMARK 290       9555   2/3+Y-X,1/3-X,1/3+Z                                     
REMARK 290      10555   2/3+Y,1/3+X,1/3-Z                                       
REMARK 290      11555   2/3+X-Y,1/3-Y,1/3-Z                                     
REMARK 290      12555   2/3-X,1/3+Y-X,1/3-Z                                     
REMARK 290      13555   1/3+X,2/3+Y,2/3+Z                                       
REMARK 290      14555   1/3-Y,2/3+X-Y,2/3+Z                                     
REMARK 290      15555   1/3+Y-X,2/3-X,2/3+Z                                     
REMARK 290      16555   1/3+Y,2/3+X,2/3-Z                                       
REMARK 290      17555   1/3+X-Y,2/3-Y,2/3-Z                                     
REMARK 290      18555   1/3-X,2/3+Y-X,2/3-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 -0.500010 -0.866009  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866042 -0.499990  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.499990  0.866009  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866042 -0.500010  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500010  0.865998  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866042  0.500010  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000022  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.499990 -0.866020  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866042  0.499990  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       78.58300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.37107            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       44.03267            
REMARK 290   SMTRY1   8 -0.500010 -0.866009  0.000000       78.58300            
REMARK 290   SMTRY2   8  0.866042 -0.499990  0.000000       45.37107            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       44.03267            
REMARK 290   SMTRY1   9 -0.499990  0.866009  0.000000       78.58300            
REMARK 290   SMTRY2   9 -0.866042 -0.500010  0.000000       45.37107            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       44.03267            
REMARK 290   SMTRY1  10 -0.500010  0.865998  0.000000       78.58300            
REMARK 290   SMTRY2  10  0.866042  0.500010  0.000000       45.37107            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       44.03267            
REMARK 290   SMTRY1  11  1.000000  0.000022  0.000000       78.58300            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       45.37107            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       44.03267            
REMARK 290   SMTRY1  12 -0.499990 -0.866020  0.000000       78.58300            
REMARK 290   SMTRY2  12 -0.866042  0.499990  0.000000       45.37107            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       44.03267            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       -0.00100            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       90.74214            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       88.06533            
REMARK 290   SMTRY1  14 -0.500010 -0.866009  0.000000       -0.00100            
REMARK 290   SMTRY2  14  0.866042 -0.499990  0.000000       90.74214            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       88.06533            
REMARK 290   SMTRY1  15 -0.499990  0.866009  0.000000       -0.00100            
REMARK 290   SMTRY2  15 -0.866042 -0.500010  0.000000       90.74214            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       88.06533            
REMARK 290   SMTRY1  16 -0.500010  0.865998  0.000000       -0.00100            
REMARK 290   SMTRY2  16  0.866042  0.500010  0.000000       90.74214            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       88.06533            
REMARK 290   SMTRY1  17  1.000000  0.000022  0.000000       -0.00100            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       90.74214            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       88.06533            
REMARK 290   SMTRY1  18 -0.499990 -0.866020  0.000000       -0.00100            
REMARK 290   SMTRY2  18 -0.866042  0.499990  0.000000       90.74214            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       88.06533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 295                                                                      
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY                                        
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW             
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS              
REMARK 295 IN THIS ENTRY.  APPLYING THE APPROPRIATE MTRIX                       
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD               
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.              
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH             
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.                                   
REMARK 295                                                                      
REMARK 295               APPLIED TO          TRANSFORMED TO                     
REMARK 295   TRANSFORM CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD           
REMARK 295     SSS                                                              
REMARK 295    M  1       C    1 .. 317         H    1 .. 317     0.153          
REMARK 295                                                                      
REMARK 295    WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS                        
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   3 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: HEXAMERIC                       
REMARK 300                                                                      
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350                        
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER                        
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR                        
REMARK 300 THE CHAIN IN THE COMPLEX IS     2821.8 ANGSTROM**2                   
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 APPLY THE FOLLOWING TO CHAINS: C, H                                  
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   BIOMT1   2 -0.500010 -0.866009  0.000000       78.58200            
REMARK 350   BIOMT2   2  0.866042 -0.499990  0.000000      136.11321            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.499990  0.866009  0.000000      -78.58500            
REMARK 350   BIOMT2   3 -0.866042 -0.500010  0.000000      136.11321            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH S  59  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH X  52  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION IN CHAIN C, SER 181 TO ALA 181                  
REMARK 400  ENGINEERED MUTATION IN CHAIN H, SER 181 TO ALA 181                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY C   318                                                      
REMARK 465     GLY H   318                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU C 316    O                                                   
REMARK 470     LEU H 316    O                                                   
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU C   3   CB  -  CG  -  CD1 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    LEU C  30   CA  -  CB  -  CG  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    LEU C 290   CB  -  CG  -  CD2 ANGL. DEV. =  12.1 DEGREES          
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL                
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 500 NUMBER; I=INSERTION CODE).                                           
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)           
REMARK 500                                                                      
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991                               
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET H 102  SD     MET H 102  CE      -0.249                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                                                                      
REMARK 500   O    ASP C   195     O    HOH X   185               2.18           
REMARK 500   OE2  GLU H    26     O    HOH S    42               1.97           
REMARK 500   O    HOH S   138     O    HOH X   140               2.16           
REMARK 500   O    HOH S   190     O    HOH S   192               2.09           
REMARK 500   O    HOH X   104     O    HOH X   186               2.10           
REMARK 500   O    HOH X   162     O    HOH X   169               2.19           
REMARK 500   O    HOH X   251     O    HOH X   271               2.16           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500                                                                      
REMARK 500    SER C 122      -51.67     65.84                                   
REMARK 500    ALA C 181     -118.69     62.96                                   
REMARK 500    SER H 122      -53.62     62.85                                   
REMARK 500    ALA H 181     -115.22     61.37                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO                 
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY            
REMARK 525 ASSOCIATED WITH:                                                     
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN                                       
REMARK 525     C              X                                                 
REMARK 525     H              S                                                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR CHAIN H                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L7A   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF                           
REMARK 900  CEPHALOSPORIN CDEACETYLASE                                          
REMARK 900 RELATED ID: 1ODS   RELATED DB: PDB                                   
REMARK 900  CEPHALOSPORIN C DEACETYLASE FROM BACILLUS                           
REMARK 900  SUBTILIS                                                            
DBREF  1ODT C    1   318  SWS    P94388   P94388           1    318             
DBREF  1ODT H    1   318  SWS    P94388   P94388           1    318             
SEQADV 1ODT ALA C  181  SWS  P94388    SER   181 ENGINEERED MUTATION            
SEQADV 1ODT ALA H  181  SWS  P94388    SER   181 ENGINEERED MUTATION            
SEQADV 1ODT GLU C  220  SWS  P94388    GLN   220 CONFLICT                       
SEQADV 1ODT GLU H  220  SWS  P94388    GLN   220 CONFLICT                       
SEQRES   1 C  318  MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR          
SEQRES   2 C  318  TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU          
SEQRES   3 C  318  PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN          
SEQRES   4 C  318  ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP          
SEQRES   5 C  318  GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY          
SEQRES   6 C  318  ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS          
SEQRES   7 C  318  GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR          
SEQRES   8 C  318  ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN          
SEQRES   9 C  318  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 C  318  ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO          
SEQRES  11 C  318  HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 C  318  ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 C  318  ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU          
SEQRES  14 C  318  VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY ALA GLN          
SEQRES  15 C  318  GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 C  318  ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 C  318  ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO          
SEQRES  18 C  318  TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER          
SEQRES  19 C  318  PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR          
SEQRES  20 C  318  PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO          
SEQRES  21 C  318  VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO          
SEQRES  22 C  318  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 C  318  LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 C  318  TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE          
SEQRES  25 C  318  LYS GLN HIS LEU LYS GLY                                      
SEQRES   1 H  318  MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR          
SEQRES   2 H  318  TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU          
SEQRES   3 H  318  PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN          
SEQRES   4 H  318  ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP          
SEQRES   5 H  318  GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY          
SEQRES   6 H  318  ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS          
SEQRES   7 H  318  GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR          
SEQRES   8 H  318  ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN          
SEQRES   9 H  318  TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL          
SEQRES  10 H  318  ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO          
SEQRES  11 H  318  HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU          
SEQRES  12 H  318  ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP          
SEQRES  13 H  318  ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU          
SEQRES  14 H  318  VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY ALA GLN          
SEQRES  15 H  318  GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP          
SEQRES  16 H  318  ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER          
SEQRES  17 H  318  ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO          
SEQRES  18 H  318  TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER          
SEQRES  19 H  318  PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR          
SEQRES  20 H  318  PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO          
SEQRES  21 H  318  VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO          
SEQRES  22 H  318  PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR          
SEQRES  23 H  318  LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU          
SEQRES  24 H  318  TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE          
SEQRES  25 H  318  LYS GLN HIS LEU LYS GLY                                      
HET    ACT  C1318       4                                                       
HET    ACT  H1318       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   4  HOH   *563(H2 O1)                                                   
HELIX    1   1 PRO C    7  GLN C   12  1                                   6    
HELIX    2   2 ASP C   23  LYS C   37  1                                  15    
HELIX    3   3 PHE C   64  ASN C   66  5                                   3    
HELIX    4   4 TYR C   95  GLY C   97  5                                   3    
HELIX    5   5 GLU C   98  HIS C  108  1                                  11    
HELIX    6   6 TYR C  148  SER C  166  1                                  19    
HELIX    7   7 ALA C  181  SER C  194  1                                  14    
HELIX    8   8 ASN C  209  ALA C  217  1                                   9    
HELIX    9   9 TYR C  222  ASN C  232  1                                  11    
HELIX   10  10 SER C  234  TYR C  247  1                                  14    
HELIX   11  11 ASP C  249  ALA C  254  1                                   6    
HELIX   12  12 ASP C  255  VAL C  257  5                                   3    
HELIX   13  13 PRO C  273  LEU C  284  1                                  12    
HELIX   14  14 ILE C  301  HIS C  315  1                                  15    
HELIX   15  15 PRO H    7  THR H   13  1                                   7    
HELIX   16  16 ASP H   23  LYS H   37  1                                  15    
HELIX   17  17 PHE H   64  ASN H   66  5                                   3    
HELIX   18  18 TYR H   95  GLY H   97  5                                   3    
HELIX   19  19 GLU H   98  HIS H  108  1                                  11    
HELIX   20  20 TYR H  148  SER H  166  1                                  19    
HELIX   21  21 ALA H  181  SER H  194  1                                  14    
HELIX   22  22 ASN H  209  ALA H  217  1                                   9    
HELIX   23  23 TYR H  222  ASN H  232  1                                  11    
HELIX   24  24 SER H  234  TYR H  247  1                                  14    
HELIX   25  25 ASP H  249  ALA H  254  1                                   6    
HELIX   26  26 ASP H  255  VAL H  257  5                                   3    
HELIX   27  27 PRO H  273  LEU H  284  1                                  12    
HELIX   28  28 ILE H  301  HIS H  315  1                                  15    
SHEET    1  CA 9 ASP C  43  VAL C  47  0                                        
SHEET    2  CA 9 VAL C  54  LYS C  62 -1  O  VAL C  56   N  VAL C  47           
SHEET    3  CA 9 ARG C  68  PRO C  76 -1  O  ILE C  69   N  TYR C  61           
SHEET    4  CA 9 ALA C 111  MET C 115 -1  O  THR C 112   N  ALA C  74           
SHEET    5  CA 9 HIS C  82  TYR C  88  1  O  PRO C  83   N  ALA C 111           
SHEET    6  CA 9 VAL C 170  GLY C 180  1  N  ASP C 171   O  HIS C  82           
SHEET    7  CA 9 ALA C 199  ASP C 203  1  O  ALA C 199   N  VAL C 177           
SHEET    8  CA 9 VAL C 261  GLY C 266  1  O  LEU C 262   N  ALA C 202           
SHEET    9  CA 9 LYS C 288  TYR C 293  1  O  GLU C 289   N  MET C 263           
SHEET    1  HA 9 ASP H  43  VAL H  47  0                                        
SHEET    2  HA 9 VAL H  54  SER H  63 -1  O  VAL H  56   N  VAL H  47           
SHEET    3  HA 9 ALA H  67  PRO H  76 -1  O  ALA H  67   N  SER H  63           
SHEET    4  HA 9 ALA H 111  MET H 115 -1  O  THR H 112   N  ALA H  74           
SHEET    5  HA 9 HIS H  82  TYR H  88  1  O  PRO H  83   N  ALA H 111           
SHEET    6  HA 9 VAL H 170  GLY H 180  1  N  ASP H 171   O  HIS H  82           
SHEET    7  HA 9 ALA H 199  ASP H 203  1  O  ALA H 199   N  VAL H 177           
SHEET    8  HA 9 VAL H 261  GLY H 266  1  O  LEU H 262   N  ALA H 202           
SHEET    9  HA 9 LYS H 288  TYR H 293  1  O  GLU H 289   N  MET H 263           
CISPEP   1 GLY C   80    PRO C   81          0         1.84                     
CISPEP   2 GLU C  220    PRO C  221          0         2.05                     
CISPEP   3 GLY H   80    PRO H   81          0        -4.37                     
CISPEP   4 GLU H  220    PRO H  221          0         3.25                     
SITE     1 AC1  7 GLY C  90  TYR C  91  ALA C 181  GLN C 182                    
SITE     2 AC1  7 TYR C 206  PRO C 221  HIS C 298                               
SITE     1 AC2  6 GLY H  90  TYR H  91  ALA H 181  GLN H 182                    
SITE     2 AC2  6 HIS H 298  HOH S 274                                          
CRYST1  157.167  157.170  132.098  90.00  90.00 120.00 H 3 2        36          
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      0.006363  0.003673  0.000000        0.00000                         
SCALE2      0.000000  0.007347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007570        0.00000                         
MTRIX1   1  0.991000  0.133000  0.000000      -11.98389    1                    
MTRIX2   1  0.133000 -0.991000  0.003000      180.54744    1                    
MTRIX3   1  0.001000 -0.003000 -1.000000      110.41402    1                    
TER    2531      LYS C 317                                                      
TER    5067      LYS H 317                                                      
MASTER      450    0    2   28   18    0    4    9 5636    2    8   50          
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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