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LongText Report for: 3IA2-pdb

Name Class
3IA2-pdb
HEADER    HYDROLASE                               13-JUL-09   3IA2              
TITLE     PSEUDOMONAS FLUORESCENS ESTERASE COMPLEXED TO THE R-ENANTIOMER OF A   
TITLE    2 SULFONATE TRANSITION STATE ANALOG                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARYLESTERASE;                                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: ARYL-ESTER HYDROLASE, PFE, PUTATIVE BROMOPEROXIDASE;        
COMPND   5 EC: 3.1.1.2, 1.-.-.-;                                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;                        
SOURCE   3 ORGANISM_TAXID: 294;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJOE2792                                  
KEYWDS    ALPHA-BETA HYDROLASE FOLD, TRANSITION STATE ANALOG, HYDROLASE,        
KEYWDS   2 OXIDOREDUCTASE, PEROXIDASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.SCHRAG,R.J.KAZLAUSKAS,Y.JIANG,K.MORLEY                            
REVDAT   1   21-JUL-10 3IA2    0                                                
JRNL        AUTH   Y.JIANG,K.MORLEY,J.D.SCHRAG,R.J.KAZLAUSKAS                   
JRNL        TITL   ACTIVE SITE LOOP ORIENTATION DIFFERS IN ESTERASE/LIPASES AND 
JRNL        TITL 2 ACYLTRANSFERASES: MOLECULAR BASIS FOR CONTROLLING THE        
JRNL        TITL 3 REACTIVITY OF WATER                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 345685                         
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 18410                           
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 23296                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1263                         
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12720                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 217                                     
REMARK   3   SOLVENT ATOMS            : 1419                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.07000                                             
REMARK   3    B22 (A**2) : -1.07000                                             
REMARK   3    B33 (A**2) : 1.61000                                              
REMARK   3    B12 (A**2) : -0.54000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.056         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.712         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
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 ATOMS        (A): 13585 ; 0.003 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18452 ; 0.775 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1710 ; 4.286 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   627 ;31.499 ;24.099       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2173 ;10.607 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;15.867 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2017 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10414 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8283 ; 0.289 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13348 ; 0.565 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5302 ; 0.859 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5086 ; 1.487 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     271      6                      
REMARK   3           1     B      1       B     271      6                      
REMARK   3           1     C      1       C     271      6                      
REMARK   3           1     D      1       D     271      6                      
REMARK   3           1     E      1       E     271      6                      
REMARK   3           1     F      1       F     271      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1993 ;  0.24 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1993 ;  0.27 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1993 ;  0.21 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1993 ;  0.18 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   1993 ;  0.21 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   1993 ;  0.29 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1993 ;  1.46 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1993 ;  1.03 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1993 ;  0.74 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1993 ;  0.50 ; 10.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   1993 ;  1.41 ; 10.00           
REMARK   3   LOOSE THERMAL      1    F (A**2):   1993 ;  1.29 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3IA2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054153.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : SI(111) MONOCHROMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 364141                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.650                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200   FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.57                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34300                            
REMARK 200   FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: O                                                     
REMARK 200 STARTING MODEL: PDB ENTRY 1VA4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULFATE, 3%  PEG 400,     
REMARK 280  100 MM SODIUM-POTASSIUM PHOSPHATE, PH 7.5, VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.64267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.32133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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 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   OG   SER C    94     O3   J6Z C   272              2.14            
REMARK 500   OG   SER E    94     O3   J6Z E   272              2.16            
REMARK 500   OG   SER B    94     O3   J6Z B   272              2.17            
REMARK 500   OG   SER D    94     O3   J6Z D   272              2.18            
REMARK 500   OG   SER F    94     O3   J6Z F   272              2.18            
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    LEU A  29      -28.00     83.51                                   
REMARK 500    SER A  94     -122.10     55.66                                   
REMARK 500    PHE A 125      -61.11   -100.14                                   
REMARK 500    ASP A 150       83.98   -160.95                                   
REMARK 500    THR A 230      -95.31   -120.32                                   
REMARK 500    LEU B  29      -30.14     82.83                                   
REMARK 500    SER B  94     -123.10     56.25                                   
REMARK 500    PHE B 125      -61.14   -101.44                                   
REMARK 500    ASP B 150       84.72   -157.87                                   
REMARK 500    THR B 230      -92.72   -123.73                                   
REMARK 500    ASP B 248       -5.20     71.88                                   
REMARK 500    LEU C  29      -28.79     84.96                                   
REMARK 500    SER C  94     -120.24     53.90                                   
REMARK 500    PHE C 125      -60.07   -105.10                                   
REMARK 500    TYR C 131       59.16   -141.25                                   
REMARK 500    ASP C 150       84.05   -156.73                                   
REMARK 500    THR C 230      -90.94   -124.08                                   
REMARK 500    LEU D  29      -25.68     84.15                                   
REMARK 500    SER D  94     -121.81     54.88                                   
REMARK 500    PHE D 125      -62.12   -104.45                                   
REMARK 500    ASP D 150       84.05   -156.46                                   
REMARK 500    THR D 230      -91.30   -123.45                                   
REMARK 500    LEU E  29      -26.87     83.77                                   
REMARK 500    SER E  94     -122.86     57.00                                   
REMARK 500    PHE E 125      -62.57   -101.86                                   
REMARK 500    ASP E 150       82.74   -160.47                                   
REMARK 500    THR E 230      -89.36   -122.13                                   
REMARK 500    LEU F  29      -30.70     83.43                                   
REMARK 500    GLN F  62       71.03   -119.69                                   
REMARK 500    SER F  94     -120.41     53.32                                   
REMARK 500    TYR F 131       58.48   -140.06                                   
REMARK 500    ASP F 150       84.61   -159.57                                   
REMARK 500    THR F 230      -91.44   -123.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     J6Z A  272                                                       
REMARK 610     J6Z B  272                                                       
REMARK 610     J6Z C  272                                                       
REMARK 610     J6Z D  272                                                       
REMARK 610     J6Z E  272                                                       
REMARK 610     J6Z F  272                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z A 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z B 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z C 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z D 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z E 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J6Z F 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 277                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VA4   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE UNCOMPLEXED P. FLUORESCENS ESTERASE                        
REMARK 900 RELATED ID: 3HEA   RELATED DB: PDB                                   
REMARK 900 THE L29P MUTANT OF P. FLUORESCENS ESTERASE                           
DBREF  3IA2 A    1   271  UNP    P22862   ESTE_PSEFL       2    272             
DBREF  3IA2 B    1   271  UNP    P22862   ESTE_PSEFL       2    272             
DBREF  3IA2 C    1   271  UNP    P22862   ESTE_PSEFL       2    272             
DBREF  3IA2 D    1   271  UNP    P22862   ESTE_PSEFL       2    272             
DBREF  3IA2 E    1   271  UNP    P22862   ESTE_PSEFL       2    272             
DBREF  3IA2 F    1   271  UNP    P22862   ESTE_PSEFL       2    272             
SEQRES   1 A  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 A  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 A  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 A  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 A  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 A  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 A  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 A  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 A  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 A  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 A  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 A  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 A  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 A  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 A  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 A  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 A  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 A  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 A  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 A  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 A  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
SEQRES   1 B  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 B  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 B  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 B  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 B  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 B  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 B  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 B  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 B  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 B  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 B  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 B  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 B  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 B  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 B  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 B  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 B  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 B  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 B  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 B  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 B  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
SEQRES   1 C  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 C  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 C  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 C  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 C  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 C  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 C  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 C  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 C  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 C  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 C  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 C  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 C  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 C  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 C  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 C  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 C  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 C  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 C  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 C  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 C  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
SEQRES   1 D  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 D  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 D  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 D  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 D  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 D  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 D  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 D  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 D  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 D  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 D  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 D  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 D  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 D  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 D  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 D  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 D  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 D  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 D  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 D  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 D  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
SEQRES   1 E  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 E  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 E  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 E  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 E  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 E  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 E  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 E  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 E  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 E  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 E  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 E  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 E  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 E  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 E  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 E  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 E  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 E  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 E  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 E  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 E  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
SEQRES   1 F  271  SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE          
SEQRES   2 F  271  LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS          
SEQRES   3 F  271  GLY TRP LEU LEU ASP ALA ASP MET TRP GLU TYR GLN MET          
SEQRES   4 F  271  GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE          
SEQRES   5 F  271  ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR          
SEQRES   6 F  271  GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN          
SEQRES   7 F  271  LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL          
SEQRES   8 F  271  GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE          
SEQRES   9 F  271  ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU          
SEQRES  10 F  271  LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP          
SEQRES  11 F  271  TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE          
SEQRES  12 F  271  LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER          
SEQRES  13 F  271  ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN          
SEQRES  14 F  271  VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE          
SEQRES  15 F  271  ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL          
SEQRES  16 F  271  THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA          
SEQRES  17 F  271  LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY          
SEQRES  18 F  271  ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA          
SEQRES  19 F  271  ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS          
SEQRES  20 F  271  ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN          
SEQRES  21 F  271  LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG                  
HET    J6Z  A 272       7                                                       
HET    GOL  A 273       6                                                       
HET    GOL  A 274       6                                                       
HET    GOL  A 275       6                                                       
HET    GOL  A 276       6                                                       
HET    SO4  A 277       5                                                       
HET    J6Z  B 272       7                                                       
HET    GOL  B 273       6                                                       
HET    GOL  B 274       6                                                       
HET    GOL  B 275       6                                                       
HET    GOL  B 276       6                                                       
HET    SO4  B 277       5                                                       
HET    J6Z  C 272       7                                                       
HET    GOL  C 273       6                                                       
HET    GOL  C 274       6                                                       
HET    GOL  C 275       6                                                       
HET    GOL  C 276       6                                                       
HET    SO4  C 277       5                                                       
HET    J6Z  D 272       7                                                       
HET    GOL  D 273       6                                                       
HET    GOL  D 274       6                                                       
HET    GOL  D 275       6                                                       
HET    GOL  D 276       6                                                       
HET    SO4  D 277       5                                                       
HET    J6Z  E 272       7                                                       
HET    GOL  E 273       6                                                       
HET    GOL  E 274       6                                                       
HET    GOL  E 275       6                                                       
HET    GOL  E 276       6                                                       
HET    GOL  E 277       6                                                       
HET    SO4  E 278       5                                                       
HET    J6Z  F 272       7                                                       
HET    GOL  F 273       6                                                       
HET    GOL  F 274       6                                                       
HET    GOL  F 275       6                                                       
HET    GOL  F 276       6                                                       
HETNAM     J6Z (2R)-BUTANE-2-SULFONATE                                          
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  J6Z    6(C4 H9 O3 S 1-)                                             
FORMUL   8  GOL    25(C3 H8 O3)                                                 
FORMUL  12  SO4    5(O4 S 2-)                                                   
FORMUL  43  HOH   *1419(H2 O)                                                   
HELIX    1   1 ASP A   31  MET A   34  5                                   4    
HELIX    2   2 TRP A   35  SER A   44  1                                  10    
HELIX    3   3 ASP A   68  ASP A   84  1                                  17    
HELIX    4   4 MET A   95  GLY A  108  1                                  14    
HELIX    5   5 PRO A  136  GLY A  164  1                                  29    
HELIX    6   6 ILE A  165  GLY A  168  5                                   4    
HELIX    7   7 SER A  172  ALA A  186  1                                  15    
HELIX    8   8 SER A  187  THR A  201  1                                  15    
HELIX    9   9 PHE A  203  ALA A  208  1                                   6    
HELIX   10  10 PRO A  226  THR A  229  5                                   4    
HELIX   11  11 THR A  230  ILE A  238  1                                   9    
HELIX   12  12 GLY A  252  HIS A  257  1                                   6    
HELIX   13  13 HIS A  257  LYS A  270  1                                  14    
HELIX   14  14 ASP B   31  MET B   34  5                                   4    
HELIX   15  15 TRP B   35  SER B   44  1                                  10    
HELIX   16  16 ASP B   68  LEU B   83  1                                  16    
HELIX   17  17 MET B   95  GLY B  108  1                                  14    
HELIX   18  18 PRO B  136  GLY B  164  1                                  29    
HELIX   19  19 ILE B  165  GLY B  168  5                                   4    
HELIX   20  20 SER B  172  ALA B  186  1                                  15    
HELIX   21  21 SER B  187  THR B  201  1                                  15    
HELIX   22  22 PHE B  203  ALA B  208  1                                   6    
HELIX   23  23 PRO B  226  THR B  229  5                                   4    
HELIX   24  24 THR B  230  ILE B  238  1                                   9    
HELIX   25  25 GLY B  252  HIS B  257  1                                   6    
HELIX   26  26 HIS B  257  LYS B  270  1                                  14    
HELIX   27  27 ASP C   31  MET C   34  5                                   4    
HELIX   28  28 TRP C   35  SER C   44  1                                  10    
HELIX   29  29 ASP C   68  ASP C   84  1                                  17    
HELIX   30  30 MET C   95  GLY C  108  1                                  14    
HELIX   31  31 PRO C  136  GLY C  164  1                                  29    
HELIX   32  32 ILE C  165  GLY C  168  5                                   4    
HELIX   33  33 SER C  172  ALA C  186  1                                  15    
HELIX   34  34 SER C  187  THR C  201  1                                  15    
HELIX   35  35 PHE C  203  LYS C  209  1                                   7    
HELIX   36  36 PRO C  226  THR C  229  5                                   4    
HELIX   37  37 THR C  230  ILE C  238  1                                   9    
HELIX   38  38 GLY C  252  HIS C  257  1                                   6    
HELIX   39  39 HIS C  257  ARG C  271  1                                  15    
HELIX   40  40 ASP D   31  MET D   34  5                                   4    
HELIX   41  41 TRP D   35  SER D   44  1                                  10    
HELIX   42  42 ASP D   68  ASP D   84  1                                  17    
HELIX   43  43 MET D   95  GLY D  108  1                                  14    
HELIX   44  44 PRO D  136  GLY D  164  1                                  29    
HELIX   45  45 ILE D  165  GLY D  168  5                                   4    
HELIX   46  46 SER D  172  ALA D  186  1                                  15    
HELIX   47  47 SER D  187  THR D  201  1                                  15    
HELIX   48  48 PHE D  203  LYS D  209  1                                   7    
HELIX   49  49 PRO D  226  THR D  229  5                                   4    
HELIX   50  50 THR D  230  ILE D  238  1                                   9    
HELIX   51  51 GLY D  252  HIS D  257  1                                   6    
HELIX   52  52 HIS D  257  LYS D  270  1                                  14    
HELIX   53  53 ASP E   31  MET E   34  5                                   4    
HELIX   54  54 TRP E   35  SER E   44  1                                  10    
HELIX   55  55 ASP E   68  ASP E   84  1                                  17    
HELIX   56  56 MET E   95  GLY E  108  1                                  14    
HELIX   57  57 PRO E  136  GLY E  164  1                                  29    
HELIX   58  58 ILE E  165  GLY E  168  5                                   4    
HELIX   59  59 SER E  172  ALA E  186  1                                  15    
HELIX   60  60 SER E  187  THR E  201  1                                  15    
HELIX   61  61 PHE E  203  ILE E  210  1                                   8    
HELIX   62  62 PRO E  226  THR E  229  5                                   4    
HELIX   63  63 THR E  230  ILE E  238  1                                   9    
HELIX   64  64 GLY E  252  HIS E  257  1                                   6    
HELIX   65  65 HIS E  257  ARG E  271  1                                  15    
HELIX   66  66 ASP F   31  MET F   34  5                                   4    
HELIX   67  67 TRP F   35  SER F   44  1                                  10    
HELIX   68  68 ASP F   68  ASP F   84  1                                  17    
HELIX   69  69 MET F   95  GLY F  108  1                                  14    
HELIX   70  70 PRO F  136  GLY F  164  1                                  29    
HELIX   71  71 ILE F  165  GLY F  168  5                                   4    
HELIX   72  72 SER F  172  ALA F  186  1                                  15    
HELIX   73  73 SER F  187  THR F  201  1                                  15    
HELIX   74  74 PHE F  203  LYS F  209  1                                   7    
HELIX   75  75 PRO F  226  THR F  229  5                                   4    
HELIX   76  76 THR F  230  ILE F  238  1                                   9    
HELIX   77  77 GLY F  252  HIS F  257  1                                   6    
HELIX   78  78 HIS F  257  LYS F  270  1                                  14    
SHEET    1   A 8 THR A   2  VAL A   4  0                                        
SHEET    2   A 8 GLN A  10  TRP A  16 -1  O  ILE A  11   N  PHE A   3           
SHEET    3   A 8 ARG A  48  PHE A  52 -1  O  THR A  49   N  TRP A  16           
SHEET    4   A 8 PRO A  21  SER A  25  1  N  PHE A  24   O  ILE A  50           
SHEET    5   A 8 VAL A  88  PHE A  93  1  O  VAL A  91   N  SER A  25           
SHEET    6   A 8 VAL A 112  LEU A 118  1  O  LEU A 118   N  GLY A  92           
SHEET    7   A 8 THR A 214  GLY A 219  1  O  LEU A 215   N  LEU A 117           
SHEET    8   A 8 GLU A 242  TYR A 246  1  O  GLU A 242   N  VAL A 216           
SHEET    1   B 8 THR B   2  VAL B   4  0                                        
SHEET    2   B 8 GLN B  10  TRP B  16 -1  O  ILE B  11   N  PHE B   3           
SHEET    3   B 8 ARG B  48  PHE B  52 -1  O  THR B  49   N  TRP B  16           
SHEET    4   B 8 PRO B  21  SER B  25  1  N  PHE B  24   O  ILE B  50           
SHEET    5   B 8 VAL B  88  PHE B  93  1  O  VAL B  91   N  SER B  25           
SHEET    6   B 8 VAL B 112  LEU B 118  1  O  LEU B 118   N  GLY B  92           
SHEET    7   B 8 THR B 214  GLY B 219  1  O  ILE B 217   N  LEU B 117           
SHEET    8   B 8 GLU B 242  TYR B 246  1  O  GLU B 242   N  VAL B 216           
SHEET    1   C 8 THR C   2  VAL C   4  0                                        
SHEET    2   C 8 GLN C  10  TRP C  16 -1  O  ILE C  11   N  PHE C   3           
SHEET    3   C 8 ARG C  48  PHE C  52 -1  O  THR C  49   N  TRP C  16           
SHEET    4   C 8 PRO C  21  SER C  25  1  N  PHE C  24   O  ILE C  50           
SHEET    5   C 8 VAL C  88  PHE C  93  1  O  VAL C  91   N  SER C  25           
SHEET    6   C 8 VAL C 112  LEU C 118  1  O  LEU C 118   N  GLY C  92           
SHEET    7   C 8 THR C 214  GLY C 219  1  O  ILE C 217   N  LEU C 117           
SHEET    8   C 8 GLU C 242  TYR C 246  1  O  GLU C 242   N  VAL C 216           
SHEET    1   D 8 THR D   2  VAL D   4  0                                        
SHEET    2   D 8 GLN D  10  TRP D  16 -1  O  ILE D  11   N  PHE D   3           
SHEET    3   D 8 ARG D  48  PHE D  52 -1  O  THR D  49   N  TRP D  16           
SHEET    4   D 8 PRO D  21  SER D  25  1  N  PHE D  24   O  ILE D  50           
SHEET    5   D 8 VAL D  88  PHE D  93  1  O  VAL D  91   N  SER D  25           
SHEET    6   D 8 VAL D 112  LEU D 118  1  O  LEU D 118   N  GLY D  92           
SHEET    7   D 8 THR D 214  GLY D 219  1  O  ILE D 217   N  LEU D 117           
SHEET    8   D 8 GLU D 242  TYR D 246  1  O  GLU D 242   N  VAL D 216           
SHEET    1   E 8 THR E   2  VAL E   4  0                                        
SHEET    2   E 8 GLN E  10  TRP E  16 -1  O  ILE E  11   N  PHE E   3           
SHEET    3   E 8 ARG E  48  PHE E  52 -1  O  THR E  49   N  TRP E  16           
SHEET    4   E 8 PRO E  21  SER E  25  1  N  PHE E  24   O  ILE E  50           
SHEET    5   E 8 VAL E  88  PHE E  93  1  O  VAL E  91   N  SER E  25           
SHEET    6   E 8 VAL E 112  LEU E 118  1  O  LEU E 118   N  GLY E  92           
SHEET    7   E 8 THR E 214  GLY E 219  1  O  LEU E 215   N  LEU E 117           
SHEET    8   E 8 GLU E 242  TYR E 246  1  O  GLU E 242   N  VAL E 216           
SHEET    1   F 8 THR F   2  VAL F   4  0                                        
SHEET    2   F 8 GLN F  10  TRP F  16 -1  O  ILE F  11   N  PHE F   3           
SHEET    3   F 8 ARG F  48  PHE F  52 -1  O  THR F  49   N  TRP F  16           
SHEET    4   F 8 PRO F  21  SER F  25  1  N  PHE F  24   O  ILE F  50           
SHEET    5   F 8 VAL F  88  PHE F  93  1  O  VAL F  91   N  SER F  25           
SHEET    6   F 8 VAL F 112  LEU F 118  1  O  LEU F 118   N  GLY F  92           
SHEET    7   F 8 THR F 214  GLY F 219  1  O  LEU F 215   N  LEU F 115           
SHEET    8   F 8 GLU F 242  TYR F 246  1  O  GLU F 242   N  VAL F 216           
LINK         OG  SER A  94                 S1  J6Z A 272     1555   1555  1.47  
LINK         OG  SER B  94                 S1  J6Z B 272     1555   1555  1.47  
LINK         OG  SER C  94                 S1  J6Z C 272     1555   1555  1.47  
LINK         OG  SER D  94                 S1  J6Z D 272     1555   1555  1.47  
LINK         OG  SER E  94                 S1  J6Z E 272     1555   1555  1.47  
LINK         OG  SER F  94                 S1  J6Z F 272     1555   1555  1.47  
CISPEP   1 THR A  122    PRO A  123          0         2.79                     
CISPEP   2 THR B  122    PRO B  123          0         2.39                     
CISPEP   3 THR C  122    PRO C  123          0         1.03                     
CISPEP   4 THR D  122    PRO D  123          0         1.72                     
CISPEP   5 THR E  122    PRO E  123          0         2.34                     
CISPEP   6 THR F  122    PRO F  123          0         2.70                     
SITE     1 AC1  5 TRP A  28  SER A  94  MET A  95  PHE A 198                    
SITE     2 AC1  5 HIS A 251                                                     
SITE     1 AC2  7 TRP B  28  SER B  94  MET B  95  VAL B 121                    
SITE     2 AC2  7 PHE B 198  ILE B 224  HIS B 251                               
SITE     1 AC3  7 TRP C  28  SER C  94  MET C  95  VAL C 121                    
SITE     2 AC3  7 PHE C 198  ILE C 224  HIS C 251                               
SITE     1 AC4  5 TRP D  28  SER D  94  MET D  95  PHE D 198                    
SITE     2 AC4  5 HIS D 251                                                     
SITE     1 AC5  7 TRP E  28  SER E  94  MET E  95  VAL E 121                    
SITE     2 AC5  7 PHE E 198  ILE E 224  HIS E 251                               
SITE     1 AC6  6 TRP F  28  SER F  94  MET F  95  PHE F 198                    
SITE     2 AC6  6 ILE F 224  HIS F 251                                          
SITE     1 AC7  7 SER A   1  TYR A  12  LYS A  14  ASP A  15                    
SITE     2 AC7  7 HOH A 323  ASP C  61  GLN C  62                               
SITE     1 AC8  7 LEU D 137  ALA D 141  LYS D 144  THR D 196                    
SITE     2 AC8  7 GLU D 200  HOH D 883  HOH D1003                               
SITE     1 AC9  7 ASP B  61  GLN B  62  SER C   1  TYR C  12                    
SITE     2 AC9  7 LYS C  14  ASP C  15  HOH C 299                               
SITE     1 BC1  7 SER D   1  TYR D  12  LYS D  14  ASP D  15                    
SITE     2 BC1  7 HOH D 300  ASP E  61  GLN E  62                               
SITE     1 BC2  7 SER E   1  TYR E  12  LYS E  14  ASP E  15                    
SITE     2 BC2  7 HOH E 334  ASP F  61  GLN F  62                               
SITE     1 BC3  8 ASP D  61  GLN D  62  SER F   1  TYR F  12                    
SITE     2 BC3  8 PHE F  13  LYS F  14  ASP F  15  HOH F 317                    
SITE     1 BC4  5 ALA A 141  LYS A 144  THR A 196  GLU A 200                    
SITE     2 BC4  5 HOH A 584                                                     
SITE     1 BC5  8 LEU F  30  TYR F 163  GLN F 178  THR F 179                    
SITE     2 BC5  8 VAL F 255  HOH F 546  HOH F 631  HOH F 873                    
SITE     1 BC6  6 LEU B 137  ALA B 141  LYS B 144  THR B 196                    
SITE     2 BC6  6 GLU B 200  HOH B 815                                          
SITE     1 BC7  6 LEU C 137  ALA C 141  LYS C 144  THR C 196                    
SITE     2 BC7  6 GLU C 200  HOH C 723                                          
SITE     1 BC8  6 LEU E 137  ALA E 141  LYS E 144  THR E 196                    
SITE     2 BC8  6 GLU E 200  HOH E 730                                          
SITE     1 BC9  5 LEU F 137  LYS F 144  THR F 196  GLU F 200                    
SITE     2 BC9  5 HOH F 461                                                     
SITE     1 CC1  7 ASP A  61  GLN A  62  SER B   1  TYR B  12                    
SITE     2 CC1  7 LYS B  14  ASP B  15  HOH B 298                               
SITE     1 CC2  5 TYR D 163  VAL D 175  GLN D 178  THR D 179                    
SITE     2 CC2  5 HOH D 362                                                     
SITE     1 CC3  6 TYR C 163  VAL C 175  GLN C 178  THR C 179                    
SITE     2 CC3  6 ILE C 182  HOH C 500                                          
SITE     1 CC4  6 LEU E  30  TYR E 163  VAL E 175  GLN E 178                    
SITE     2 CC4  6 THR E 179  HOH E 429                                          
SITE     1 CC5  5 TYR A 163  GLN A 178  THR A 179  HOH A 373                    
SITE     2 CC5  5 HOH A 618                                                     
SITE     1 CC6  6 TYR B 163  GLN B 178  THR B 179  ILE B 182                    
SITE     2 CC6  6 HOH B 310  HOH B 420                                          
SITE     1 CC7  5 LYS E   6  GLU E  81  HIS E 107  HOH E1029                    
SITE     2 CC7  5 HOH E1228                                                     
SITE     1 CC8  2 GLN F 223  ILE F 224                                          
SITE     1 CC9  2 GLN A 223  ILE A 224                                          
SITE     1 DC1  2 GLN B 223  ILE B 224                                          
SITE     1 DC2  3 GLN C 223  ILE C 224  PRO C 226                               
SITE     1 DC3  2 GLN D 223  ILE D 224                                          
SITE     1 DC4  4 VAL E 135  GLN E 223  ILE E 224  PRO E 226                    
SITE     1 DC5  1 ARG E 106                                                     
SITE     1 DC6  1 ARG A 106                                                     
SITE     1 DC7  2 ASP B  70  ARG B 106                                          
SITE     1 DC8  1 ARG C 106                                                     
SITE     1 DC9  1 ARG D 106                                                     
CRYST1  146.215  146.215  129.964  90.00  90.00 120.00 P 32         18          
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      0.006839  0.003949  0.000000        0.00000                         
SCALE2      0.000000  0.007897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007694        0.00000                         
TER    2210      ARG A 271                                                      
TER    4376      ARG B 271                                                      
TER    6551      ARG C 271                                                      
TER    8716      ARG D 271                                                      
TER   10875      ARG E 271                                                      
TER   13054      ARG F 271                                                      
MASTER      492    0   36   78   48    0   61    614356    6  223  126          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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