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LongText Report for: 3R41-pdb

Name Class
3R41-pdb
HEADER    HYDROLASE                               17-MAR-11   3R41              
TITLE     CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -         
TITLE    2 HIS280ASN/APO                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.8.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;                     
SOURCE   3 ORGANISM_TAXID: 1076;                                                
SOURCE   4 STRAIN: CGA009;                                                      
SOURCE   5 GENE: RPA1163;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P15TV-L                                   
KEYWDS    FACD, DEFLUORINASE, ALPHA/BETA HYDROLASE, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.W.Y.CHAN,A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI                            
REVDAT   1   04-MAY-11 3R41    0                                                
JRNL        AUTH   P.W.CHAN,A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI                     
JRNL        TITL   MAPPING THE REACTION COORDINATES OF ENZYMATIC                
JRNL        TITL 2 DEFLUORINATION.                                              
JRNL        REF    J.AM.CHEM.SOC.                             2011              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   21510690                                                     
JRNL        DOI    10.1021/JA200277D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 238331                         
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) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11952                           
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) : 1.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15308                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 847                          
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4729                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 455                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.65000                                              
REMARK   3    B33 (A**2) : -0.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.10000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.028         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.018         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.782         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5202 ; 0.026 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3553 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7123 ; 2.189 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8588 ; 1.176 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   659 ; 6.621 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   251 ;36.658 ;22.869       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   792 ;13.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;19.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   714 ; 0.159 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6053 ; 0.015 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1169 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3183 ; 2.563 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1260 ; 0.923 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5124 ; 3.498 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2019 ; 4.844 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1999 ; 6.547 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  8755 ; 2.222 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3R41 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064461.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978700                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 238333                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.9800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.420                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-24% PEG3350, 0.1-0.2M CACL2 AND       
REMARK 280  0.1M TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.05000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     SER B   304                                                      
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   OH   TYR B   141     O    ILE B   253              1.85            
REMARK 500   OH   TYR B   149     O    HOH B   452              1.87            
REMARK 500   O    HOH B   364     O    HOH B   403              1.89            
REMARK 500   CE2  TYR A   141     CE   MET A   145              1.96            
REMARK 500   CE2  PHE A   176     O    HOH B   399              2.00            
REMARK 500   O    MET B   145     O    HOH B   450              2.11            
REMARK 500   O    HOH A   513     O    HOH A   551              2.12            
REMARK 500   OD1  ASN A   280     O    HOH A   551              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A 145   N     MET A 145   CA      0.124                       
REMARK 500    TYR A 149   CB    TYR A 149   CG     -0.101                       
REMARK 500    TRP B  15   CB    TRP B  15   CG      0.220                       
REMARK 500    VAL B  45   CB    VAL B  45   CG2    -0.159                       
REMARK 500    VAL B  50   CB    VAL B  50   CG2    -0.181                       
REMARK 500    ARG B 144   CZ    ARG B 144   NH1    -0.092                       
REMARK 500    VAL B 271   CB    VAL B 271   CG1    -0.145                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  49   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    VAL A  50   CA  -  CB  -  CG1 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 149   CG  -  CD1 -  CE1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TYR A 149   CD1 -  CE1 -  CZ  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG A 220   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    MET A 244   CG  -  SD  -  CE  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 288   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    VAL B  45   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG B  49   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR B 149   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    MET B 244   CG  -  SD  -  CE  ANGL. DEV. = -17.1 DEGREES          
REMARK 500    GLN B 272   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 110     -127.27     58.14                                   
REMARK 500    MET A 145       77.32    -47.05                                   
REMARK 500    ASP A 173       67.21   -153.80                                   
REMARK 500    TYR A 224     -100.35   -120.44                                   
REMARK 500    ALA A 257       46.10   -146.09                                   
REMARK 500    SER A 278      159.11    178.16                                   
REMARK 500    ASP B 110     -130.81     55.90                                   
REMARK 500    TYR B 224      -96.97   -122.02                                   
REMARK 500    SER B 278      156.34    175.81                                   
REMARK 500    PHE B 281       61.40   -101.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 114         0.10    SIDE CHAIN                              
REMARK 500    TYR A 154         0.08    SIDE CHAIN                              
REMARK 500    ARG B 114         0.10    SIDE CHAIN                              
REMARK 500    TYR B 154         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 349        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 461        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH A 487        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 423        DISTANCE =  5.04 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 494   O                                                      
REMARK 620 2 HOH A 408   O    78.9                                              
REMARK 620 3 HOH A 417   O    76.4 137.3                                        
REMARK 620 4 HOH A 510   O    90.2  73.5  72.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 255   OE1                                                    
REMARK 620 2 HOH B 322   O    78.0                                              
REMARK 620 3 HOH B 394   O   107.9 142.0                                        
REMARK 620 4 GLN B 255   O    75.1 142.3  72.6                                  
REMARK 620 5 HOH B 340   O    86.7  73.5 142.8  79.0                            
REMARK 620 6 HOH B 449   O    75.8  77.0  68.7 120.3 148.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 308                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 307                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3R3U   RELATED DB: PDB                                   
REMARK 900 THE WT/APO CRYSTAL STRUCTURE                                         
REMARK 900 RELATED ID: 3R3V   RELATED DB: PDB                                   
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH FLUOROACETATE                   
REMARK 900 RELATED ID: 3R3W   RELATED DB: PDB                                   
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH CHLOROACETATE                   
REMARK 900 RELATED ID: 3R3X   RELATED DB: PDB                                   
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH BROMOACETATE                    
REMARK 900 RELATED ID: 3R3Y   RELATED DB: PDB                                   
REMARK 900 THE HIS280ASN MUTANT IN COVALENT COMPLEX WITH FLUOROACETATE          
REMARK 900 RELATED ID: 3R3Z   RELATED DB: PDB                                   
REMARK 900 THE WT IN COMPLEX WITH GLYCOLATE                                     
REMARK 900 RELATED ID: 3R40   RELATED DB: PDB                                   
REMARK 900 THE ASP110ASN MUTANT/APO CRYSTAL STRUCTURE                           
DBREF  3R41 A    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
DBREF  3R41 B    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
SEQADV 3R41 GLY A   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 HIS A    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 ASN A  280  UNP  Q6NAM1    HIS   280 ENGINEERED MUTATION            
SEQADV 3R41 GLY A  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 SER A  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 GLY B   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 HIS B    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 ASN B  280  UNP  Q6NAM1    HIS   280 ENGINEERED MUTATION            
SEQADV 3R41 GLY B  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 3R41 SER B  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQRES   1 A  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 A  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 A  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 A  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 A  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 A  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 A  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 A  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 A  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 A  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 A  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 A  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 A  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 A  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 A  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 A  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 A  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 A  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 A  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 A  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 A  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 A  306  GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU          
SEQRES  23 A  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 A  306  PHE SER ALA ALA PRO GLY SER                                  
SEQRES   1 B  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 B  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 B  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 B  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 B  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 B  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 B  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 B  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 B  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 B  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 B  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 B  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 B  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 B  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 B  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 B  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 B  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 B  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 B  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 B  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 B  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 B  306  GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU          
SEQRES  23 B  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 B  306  PHE SER ALA ALA PRO GLY SER                                  
HET     CA  A 305       1                                                       
HET     CL  A 306       1                                                       
HET     CL  A 307       1                                                       
HET     CL  A 308       1                                                       
HET     CA  B 305       1                                                       
HET     CL  B 306       1                                                       
HET     CL  B 307       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4   CL    5(CL 1-)                                                     
FORMUL  10  HOH   *455(H2 O)                                                    
HELIX    1   1 THR A   43  HIS A   48  5                                   6    
HELIX    2   2 VAL A   50  GLU A   56  1                                   7    
HELIX    3   3 HIS A   80  TYR A   83  5                                   4    
HELIX    4   4 THR A   84  LEU A   99  1                                  16    
HELIX    5   5 ASP A  110  SER A  123  1                                  14    
HELIX    6   6 PRO A  137  ARG A  144  1                                   8    
HELIX    7   7 ASN A  146  ILE A  153  1                                   8    
HELIX    8   8 TYR A  154  ALA A  160  1                                   7    
HELIX    9   9 PRO A  164  GLY A  172  1                                   9    
HELIX   10  10 ASP A  173  TRP A  185  1                                  13    
HELIX   11  11 ASP A  195  ALA A  207  1                                  13    
HELIX   12  12 ASP A  208  TYR A  224  1                                  17    
HELIX   13  13 TYR A  224  GLY A  237  1                                  14    
HELIX   14  14 THR A  259  ALA A  268  1                                  10    
HELIX   15  15 PHE A  281  ALA A  286  1                                   6    
HELIX   16  16 ALA A  286  ALA A  300  1                                  15    
HELIX   17  17 THR B   43  ARG B   49  5                                   7    
HELIX   18  18 VAL B   50  ALA B   55  1                                   6    
HELIX   19  19 HIS B   80  TYR B   83  5                                   4    
HELIX   20  20 THR B   84  LEU B   99  1                                  16    
HELIX   21  21 ASP B  110  SER B  123  1                                  14    
HELIX   22  22 PRO B  137  ARG B  144  1                                   8    
HELIX   23  23 ASN B  146  ILE B  153  1                                   8    
HELIX   24  24 TYR B  154  LEU B  159  1                                   6    
HELIX   25  25 PRO B  164  GLY B  171  1                                   8    
HELIX   26  26 ASP B  173  TRP B  185  1                                  13    
HELIX   27  27 ASP B  195  ALA B  207  1                                  13    
HELIX   28  28 ASP B  208  TYR B  224  1                                  17    
HELIX   29  29 TYR B  224  GLY B  237  1                                  14    
HELIX   30  30 THR B  259  LYS B  266  1                                   8    
HELIX   31  31 PHE B  281  ALA B  286  1                                   6    
HELIX   32  32 ALA B  286  ALA B  300  1                                  15    
SHEET    1   A 8 GLY A  12  ILE A  16  0                                        
SHEET    2   A 8 ILE A  23  GLY A  29 -1  O  ILE A  23   N  ILE A  16           
SHEET    3   A 8 LYS A  59  ALA A  63 -1  O  VAL A  62   N  ARG A  26           
SHEET    4   A 8 PRO A  33  LEU A  37  1  N  LEU A  34   O  ILE A  61           
SHEET    5   A 8 PHE A 104  HIS A 109  1  O  ALA A 105   N  LEU A  35           
SHEET    6   A 8 LEU A 127  LEU A 133  1  O  ALA A 131   N  LEU A 106           
SHEET    7   A 8 MET A 244  GLY A 249  1  O  LEU A 245   N  VAL A 132           
SHEET    8   A 8 VAL A 271  ILE A 276  1  O  GLN A 272   N  ALA A 246           
SHEET    1   B 8 GLY B  12  ILE B  16  0                                        
SHEET    2   B 8 ILE B  23  GLY B  28 -1  O  ILE B  23   N  ILE B  16           
SHEET    3   B 8 LYS B  59  ALA B  63 -1  O  VAL B  62   N  ARG B  26           
SHEET    4   B 8 PRO B  33  LEU B  37  1  N  LEU B  34   O  ILE B  61           
SHEET    5   B 8 PHE B 104  HIS B 109  1  O  ALA B 105   N  LEU B  35           
SHEET    6   B 8 LEU B 127  LEU B 133  1  O  ALA B 131   N  LEU B 106           
SHEET    7   B 8 MET B 244  GLY B 249  1  O  LEU B 245   N  VAL B 132           
SHEET    8   B 8 VAL B 271  ILE B 276  1  O  ILE B 276   N  TRP B 248           
LINK        CA    CA A 305                 O   HOH A 494     1555   1555  2.35  
LINK        CA    CA A 305                 O   HOH A 408     1555   1555  2.36  
LINK         OE1 GLN B 255                CA    CA B 305     1555   1555  2.40  
LINK        CA    CA B 305                 O   HOH B 322     1555   1555  2.41  
LINK        CA    CA A 305                 O   HOH A 417     1555   1555  2.41  
LINK        CA    CA A 305                 O   HOH A 510     1555   1555  2.41  
LINK        CA    CA B 305                 O   HOH B 394     1555   1555  2.42  
LINK         O   GLN B 255                CA    CA B 305     1555   1555  2.47  
LINK        CA    CA B 305                 O   HOH B 340     1555   1555  2.47  
LINK        CA    CA B 305                 O   HOH B 449     1555   1555  2.51  
CISPEP   1 PHE A   40    PRO A   41          0        -1.59                     
CISPEP   2 ALA A  163    PRO A  164          0         8.03                     
CISPEP   3 PHE B   40    PRO B   41          0        -3.58                     
CISPEP   4 ALA B  163    PRO B  164          0         7.95                     
SITE     1 AC1  4 HOH A 408  HOH A 417  HOH A 494  HOH A 510                    
SITE     1 AC2  3 ARG A 114  LEU A 136  HOH A 558                               
SITE     1 AC3  4 ALA A 286  PRO A 287  ASP A 288  GLN A 289                    
SITE     1 AC4  2 LYS A  90  HOH A 464                                          
SITE     1 AC5  5 GLN B 255  HOH B 322  HOH B 340  HOH B 394                    
SITE     2 AC5  5 HOH B 449                                                     
SITE     1 AC6  3 ASP B 110  ARG B 111  ARG B 114                               
SITE     1 AC7  4 ARG B 114  LEU B 136  TYR B 141  HOH B 402                    
CRYST1   41.690   78.100   85.100  90.00 103.41  90.00 P 1 21 1      4          
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      0.023987  0.000000  0.005721        0.00000                         
SCALE2      0.000000  0.012804  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012080        0.00000                         
TER    2531      ALA A 300                                                      
TER    5015      ALA B 300                                                      
MASTER      451    0    7   32   16    0    8    6 5191    2   13   48          
END                                                                             

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