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LongText Report for: 2V9Z-pdb

Name Class
2V9Z-pdb
HEADER    HYDROLASE                               28-AUG-07   2V9Z              
TITLE     STRUCTURE OF THE RHODOCOCCUS HALOALKANE DEHALOGENASE MUTANT           
TITLE    2 WITH ENHANCED ENANTIOSELECTIVITY                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HALOALKANE DEHALOGENASE DHAA12;                             
COMPND   5 EC: 3.8.1.5;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;                        
SOURCE   3 STRAIN: NCIMB13064;                                                  
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR: PET21B                                     
KEYWDS    PLASMID, HYDROLASE, DETOXIFICATION                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KOUDELAKOVA,Z.PROKOP,Y.SATO,M.LAPKOUSKI,E.CHOVANCOVA,               
AUTHOR   2 M.MONINCOVA,A.JESENSKA,J.EMMER,T.SENDA,Y.NAGATA,                     
AUTHOR   3 I.KUTA SMATANOVA,J.DAMBORSKY                                         
REVDAT   1   16-SEP-08 2V9Z    0                                                
JRNL        AUTH   T.KOUDELAKOVA,Z.PROKOP,Y.SATO,M.LAPKOUSKI,                   
JRNL        AUTH 2 E.CHOVANCOVA,M.MONINCOVA,A.JESENSKA,J.EMMER,                 
JRNL        AUTH 3 T.SENDA,Y.NAGATA,I.KUTA SMATANOVA,J.DAMBORSKY                
JRNL        TITL   RATIONAL ENGINEERING OF RHODOCOCCUS HALOALKANE               
JRNL        TITL 2 DEHALOGENASE WITH ENHANCED ENANTIOSELECTIVITY                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. 3.0  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.13                          
REMARK   3   NUMBER OF REFLECTIONS             : 5648                           
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) : 0.20252                         
REMARK   3   R VALUE            (WORKING SET) : 0.19456                         
REMARK   3   FREE R VALUE                     : 0.26745                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 11.2                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 712                             
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) : 3.002                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.080                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 384                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.251                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.379                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2415                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.456                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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): 0.602         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.422         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.618        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.796                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  2497 ; 0.010 ; 0.022          
REMARK   3   BOND LENGTHS OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   BOND ANGLES REFINED      (DEGREES):  3416 ; 1.601 ; 1.954          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):   302 ;22.208 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):   122 ;37.308 ;23.361          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):   370 ;25.372 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):    18 ;23.471 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):   360 ; 0.281 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  1987 ; 0.004 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  1330 ; 0.304 ; 0.200          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION REFINED     (A):  1664 ; 0.340 ; 0.200          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  NULL ;  NULL ;  NULL          
REMARK   3   H-BOND (X...Y) REFINED         (A):   104 ; 0.224 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):    26 ; 0.169 ; 0.200          
REMARK   3   SYMMETRY VDW OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY H-BOND REFINED        (A):     5 ; 0.239 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  1537 ; 1.039 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  2466 ; 1.833 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  1058 ; 2.786 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):   950 ; 4.396 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. RESIDUES MET A 1 AND SER A 2 ARE                 
REMARK   3   DISORDERED. GLU A 3 DUE TO DISORDERED SIDE CHAIN IS                
REMARK   3   SUBSTITUTED BY ALA. SIDE CHAINS OF ASP A 167 AND VAL               
REMARK   3   A 168 WERE MODELLED STEREOCHEMICALLY                               
REMARK   4                                                                      
REMARK   4 2V9Z COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 28-AUG-2007.                
REMARK 100 THE EBI ID CODE IS EBI-33584.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-2007                        
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NONIUS FR591                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6389                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.45                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.7                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.20                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BN6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL OF PROTEIN (5 MG/ML IN 25           
REMARK 280  MM TRIS-HCL PH 7.5, 150 MM AMMONIUM SULPHATE, 1 MM EDTA)            
REMARK 280  WAS MIXED 1:1 WITH THE RESERVOIR (1 ML) CONSISTED OF 20 %           
REMARK 280   PEG 6000, 0.1 M SODIUM ACETATE, 0.2 M AMMONIUM SULPHATE,           
REMARK 280   0.1 M TRIS-HCL PH 8.5-9.0. SITTING-DROP 281K.                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.36950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.34750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.34750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.36950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.45000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TRP 141 TO PHE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PRO 142 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 144 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 171 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ALA 172 TO VAL                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 175 TO GLY                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 176 TO GLY                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 245 TO ALA                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   3    CB   CG   CD   OE1  OE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1999                                
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 221   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  18       49.09     39.86                                   
REMARK 500    ARG A  30       35.52    105.03                                   
REMARK 500    ASP A  31     -135.09   -176.22                                   
REMARK 500    PRO A  42       64.48   -103.34                                   
REMARK 500    THR A  43     -142.00   -104.55                                   
REMARK 500    SER A  44     -165.64    174.23                                   
REMARK 500    SER A  72     -173.57    -65.74                                   
REMARK 500    LYS A  74       58.97   -107.53                                   
REMARK 500    PHE A  80     -159.76    -58.42                                   
REMARK 500    GLU A  98      -89.37    -94.61                                   
REMARK 500    HIS A 105     -145.58   -106.98                                   
REMARK 500    ASP A 106     -109.69    -42.15                                   
REMARK 500    ASN A 119       47.26   -143.00                                   
REMARK 500    GLU A 130       77.51     26.62                                   
REMARK 500    ASP A 139        0.06    -53.34                                   
REMARK 500    GLU A 141G      -4.61    -55.72                                   
REMARK 500    ASP A 156       95.78     39.77                                   
REMARK 500    VAL A 157      -33.74    165.63                                   
REMARK 500    ARG A 171      -52.61   -135.09                                   
REMARK 500    LEU A 173      -70.43    -52.90                                   
REMARK 500    PRO A 192       20.15    -71.92                                   
REMARK 500    PHE A 193       21.57   -148.08                                   
REMARK 500    ALA A 212        1.52     86.46                                   
REMARK 500    ALA A 216      -38.74    -20.88                                   
REMARK 500    ALA A 245      -86.35   -147.10                                   
REMARK 500    GLU A 257      -36.29   -137.29                                   
REMARK 500    LEU A 271     -103.53   -106.52                                   
REMARK 500    ALA A 292       26.20    -70.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2V9Z A    1   141  UNP    P0A3G2   DHAA_RHORH       1    141             
DBREF  2V9Z A  141A  141K PDB    2V9Z     2V9Z           141A   141K            
DBREF  2V9Z A  142   293  UNP    P0A3G2   DHAA_RHORH     142    293             
SEQADV 2V9Z PHE A  141  UNP  P0A3G2    TRP   141 ENGINEERED MUTATION            
SEQADV 2V9Z ALA A  142  UNP  P0A3G2    PRO   142 ENGINEERED MUTATION            
SEQADV 2V9Z ALA A  144  UNP  P0A3G2    PHE   144 ENGINEERED MUTATION            
SEQADV 2V9Z ARG A  171  UNP  P0A3G2    GLY   171 ENGINEERED MUTATION            
SEQADV 2V9Z VAL A  172  UNP  P0A3G2    ALA   172 ENGINEERED MUTATION            
SEQADV 2V9Z GLY A  175  UNP  P0A3G2    LYS   175 ENGINEERED MUTATION            
SEQADV 2V9Z GLY A  176  UNP  P0A3G2    CYS   176 ENGINEERED MUTATION            
SEQADV 2V9Z ALA A  245  UNP  P0A3G2    VAL   245 ENGINEERED MUTATION            
SEQRES   1 A  304  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 A  304  TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP          
SEQRES   3 A  304  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 A  304  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 A  304  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 A  304  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 A  304  TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 A  304  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 A  304  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 A  304  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU          
SEQRES  11 A  304  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU PHE HIS HIS          
SEQRES  12 A  304  THR GLU VAL ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA          
SEQRES  13 A  304  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY          
SEQRES  14 A  304  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU ARG          
SEQRES  15 A  304  VAL LEU PRO GLY GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  16 A  304  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL          
SEQRES  17 A  304  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  18 A  304  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  19 A  304  ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  20 A  304  LEU LEU PHE TRP GLY THR PRO GLY ALA LEU ILE PRO PRO          
SEQRES  21 A  304  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS          
SEQRES  22 A  304  LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR LEU GLN          
SEQRES  23 A  304  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  24 A  304  TRP LEU PRO ALA LEU                                          
HELIX    1   1 SER A   44  ARG A   49  5                                   6    
HELIX    2   2 ILE A   51  ALA A   56  1                                   6    
HELIX    3   3 PHE A   81  LEU A   95  1                                  15    
HELIX    4   4 TRP A  107  ARG A  118  1                                  12    
HELIX    5   5 ASN A  119  GLU A  121  5                                   3    
HELIX    6   6 VAL A  141E GLU A  141G 5                                   3    
HELIX    7   7 GLU A  141H ARG A  153  1                                  16    
HELIX    8   8 VAL A  157  ILE A  163  1                                   7    
HELIX    9   9 ASN A  166  ARG A  171  1                                   6    
HELIX   10  10 ARG A  171  GLY A  176  1                                   6    
HELIX   11  11 THR A  182  GLU A  191  1                                  10    
HELIX   12  12 PRO A  192  LEU A  194  5                                   3    
HELIX   13  13 LYS A  195  ASP A  198  5                                   4    
HELIX   14  14 ARG A  199  LEU A  209  1                                  11    
HELIX   15  15 PRO A  215  SER A  232  1                                  18    
HELIX   16  16 PRO A  248  LEU A  259  1                                  12    
HELIX   17  17 TYR A  273  ASP A  277  5                                   5    
HELIX   18  18 ASN A  278  LEU A  290  1                                  13    
SHEET    1  AA 2 HIS A  13  GLU A  16  0                                        
SHEET    2  AA 2 ARG A  21  TYR A  24 -1  O  MET A  22   N  VAL A  15           
SHEET    1  AB 7 ASP A  26  VAL A  27  0                                        
SHEET    2  AB 7 CYS A  61  ILE A  62 -1  O  CYS A  61   N  VAL A  27           
SHEET    3  AB 7 VAL A  35  LEU A  38  1  O  VAL A  35   N  ILE A  62           
SHEET    4  AB 7 VAL A 100  ILE A 104  1  O  VAL A 101   N  LEU A  36           
SHEET    5  AB 7 VAL A 123  MET A 129  1  N  LYS A 124   O  VAL A 100           
SHEET    6  AB 7 LYS A 236  PRO A 243  1  O  LEU A 237   N  CYS A 128           
SHEET    7  AB 7 CYS A 262  GLY A 270  1  O  LYS A 263   N  LEU A 238           
CISPEP   1 ASN A   41    PRO A   42          0        -6.98                     
CISPEP   2 GLU A  214    PRO A  215          0        -8.08                     
CISPEP   3 THR A  242    PRO A  243          0        11.92                     
CRYST1   52.739   68.900   84.695  90.00  90.00  90.00 P 21 21 21    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      0.018961  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011807        0.00000                         
TER    2416      LEU A 293                                                      
MASTER      312    0    0   18    9    0    0    6 2415    1    0   24          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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