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LongText Report for: 3DDU-pdb

Name Class
3DDU-pdb
HEADER    HYDROLASE                               06-JUN-08   3DDU              
TITLE     PROLYL OLIGOPEPTIDASE WITH GSK552                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL ENDOPEPTIDASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROLYL OLIGOPEPTIDASE; POST-PROLINE CLEAVING                
COMPND   5 ENZYME; PE;                                                          
COMPND   6 EC: 3.4.21.26;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: PREP, PEP;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    POP, PROLYL OLIGOPEPTIDASE, ENDOPEPTIDASE, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.P.MADAUSS,R.A.REID,C.D.HAFFNER,A.B.MILLER                           
REVDAT   1   19-AUG-08 3DDU    0                                                
JRNL        AUTH   C.D.HAFFNER,C.J.DIAZ,A.B.MILLER,R.A.REID,                    
JRNL        AUTH 2 K.P.MADAUSS,A.HASSELL,M.H.HANLON,D.J.PORTER,                 
JRNL        AUTH 3 J.D.BECHERER,L.H.CARTER                                      
JRNL        TITL   PYRROLIDINYL PYRIDONE AND PYRAZINONE ANALOGUES AS            
JRNL        TITL 2 POTENT INHIBITORS OF PROLYL OLIGOPEPTIDASE (POP)             
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  4360 2008              
JRNL        REFN   ASTM BMCLE8  UK ISSN 0960-894X                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.56 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3                                           
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) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 113121                         
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) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.172                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8217                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7624                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 586                          
REMARK   3   BIN FREE R VALUE                    : 0.1810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 6933                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.08                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.036         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.952         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5866 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3946 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7958 ; 1.298 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9604 ; 0.879 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   710 ; 6.062 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   277 ;31.908 ;24.152       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   950 ;10.957 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;12.752 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   848 ; 0.135 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6560 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1229 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1105 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4247 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2867 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2915 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   884 ; 0.126 ; 0.200       
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):    24 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.209 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    68 ; 0.159 ; 0.200       
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):  3747 ; 0.827 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1444 ; 0.168 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5702 ; 1.153 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2615 ; 2.040 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2256 ; 2.822 ; 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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
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 3DDU COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB047914.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-2007                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113251                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 42.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.06400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
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   (%): 50.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0 .2M NAOAC 4.6, 9% PEG 4000, VAPOR      
REMARK 280  DIFFUSION, TEMPERATURE 277K                                         
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.61050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.92650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.94150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.92650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.61050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.94150            
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: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     THR A   426                                                      
REMARK 465     GLY A   429                                                      
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     GLN A   5    CG    CD    OE1   NE2                               
REMARK 470     GLN A  56    CD    OE1   NE2                                     
REMARK 470     GLU A  65    OE1   OE2                                           
REMARK 470     GLU A  69    CD    OE1   OE2                                     
REMARK 470     GLU A 107    CG    CD    OE1   OE2                               
REMARK 470     GLU A 163    CD    OE1   OE2                                     
REMARK 470     GLN A 192    CD    OE1   NE2                                     
REMARK 470     ASP A 256    CG    OD1   OD2                                     
REMARK 470     LYS A 335    CD    CE    NZ                                      
REMARK 470     GLN A 388    CD    OE1   NE2                                     
REMARK 470     LYS A 428    CG    CD    CE    NZ                                
REMARK 470     ASN A 483    CG    OD1   ND2                                     
REMARK 470     ILE A 498    CG1   CG2   CD1                                     
REMARK 470     LYS A 546    CD    CE    NZ                                      
REMARK 470     GLU A 624    CD    OE1   OE2                                     
REMARK 470     ARG A 664    CG    CD    NE    CZ    NH1   NH2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A   267     O    HOH A  1464     4456     2.15            
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    SER A 271       57.45   -152.04                                   
REMARK 500    ASP A 284       51.21   -112.34                                   
REMARK 500    TYR A 311      150.20     75.61                                   
REMARK 500    ASP A 320       67.19   -152.16                                   
REMARK 500    SER A 346      -55.66     69.56                                   
REMARK 500    TYR A 473      -78.66   -127.24                                   
REMARK 500    LEU A 520     -126.76     59.22                                   
REMARK 500    SER A 554     -118.80     71.44                                   
REMARK 500    VAL A 578       48.62     39.55                                   
REMARK 500    THR A 590     -113.19     33.97                                   
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     GOL A 1000                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 801                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 802                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 803                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 804                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 805                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: 552 BINDING SITE FOR RESIDUE A 901                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 1000                
DBREF  3DDU A    2   710  UNP    P48147   PPCE_HUMAN       2    710             
SEQADV 3DDU HIS A  307  UNP  P48147    GLN   307 ENGINEERED                     
SEQADV 3DDU THR A  319  UNP  P48147    TRP   319 ENGINEERED                     
SEQADV 3DDU THR A  360  UNP  P48147    ILE   360 ENGINEERED                     
SEQADV 3DDU ILE A  374  UNP  P48147    THR   374 ENGINEERED                     
SEQADV 3DDU ASN A  667  UNP  P48147    SER   667 ENGINEERED                     
SEQRES   1 A  709  LEU SER PHE GLN TYR PRO ASP VAL TYR ARG ASP GLU THR          
SEQRES   2 A  709  ALA VAL GLN ASP TYR HIS GLY HIS LYS ILE CYS ASP PRO          
SEQRES   3 A  709  TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN THR LYS          
SEQRES   4 A  709  ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL PRO PHE          
SEQRES   5 A  709  LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS GLU ARG          
SEQRES   6 A  709  MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER CYS HIS          
SEQRES   7 A  709  PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR ASN THR          
SEQRES   8 A  709  GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN ASP SER          
SEQRES   9 A  709  LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO ASN ILE          
SEQRES  10 A  709  LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY TYR ALA          
SEQRES  11 A  709  PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY LEU SER          
SEQRES  12 A  709  ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE MET LYS          
SEQRES  13 A  709  VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU GLU ARG          
SEQRES  14 A  709  VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP GLY LYS          
SEQRES  15 A  709  GLY MET PHE TYR ASN SER TYR PRO GLN GLN ASP GLY LYS          
SEQRES  16 A  709  SER ASP GLY THR GLU THR SER THR ASN LEU HIS GLN LYS          
SEQRES  17 A  709  LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER GLU ASP          
SEQRES  18 A  709  ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS TRP MET          
SEQRES  19 A  709  GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR VAL LEU          
SEQRES  20 A  709  LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN ARG LEU          
SEQRES  21 A  709  TRP TYR CYS ASP LEU GLN GLN GLU SER SER GLY ILE ALA          
SEQRES  22 A  709  GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN PHE GLU          
SEQRES  23 A  709  GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR VAL PHE          
SEQRES  24 A  709  THR PHE LYS THR ASN ARG HIS SER PRO ASN TYR ARG VAL          
SEQRES  25 A  709  ILE ASN ILE ASP PHE THR ASP PRO GLU GLU SER LYS TRP          
SEQRES  26 A  709  LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL LEU GLU          
SEQRES  27 A  709  TRP ILE ALA CYS VAL ARG SER ASN PHE LEU VAL LEU CYS          
SEQRES  28 A  709  TYR LEU HIS ASP VAL LYS ASN THR LEU GLN LEU HIS ASP          
SEQRES  29 A  709  LEU THR THR GLY ALA LEU LEU LYS ILE PHE PRO LEU ASP          
SEQRES  30 A  709  VAL GLY SER ILE VAL GLY TYR SER GLY GLN LYS LYS ASP          
SEQRES  31 A  709  THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU SER PRO          
SEQRES  32 A  709  GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU GLU LEU          
SEQRES  33 A  709  GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS GLY ILE          
SEQRES  34 A  709  ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE TYR PRO          
SEQRES  35 A  709  SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL HIS          
SEQRES  36 A  709  LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO ALA PHE          
SEQRES  37 A  709  LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE THR PRO          
SEQRES  38 A  709  ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG HIS MET          
SEQRES  39 A  709  GLY GLY ILE LEU ALA VAL ALA ASN ILE ARG GLY GLY GLY          
SEQRES  40 A  709  GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE LEU ALA          
SEQRES  41 A  709  ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS ALA ALA          
SEQRES  42 A  709  GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO LYS ARG          
SEQRES  43 A  709  LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU LEU VAL          
SEQRES  44 A  709  ALA ALA CYS ALA ASN GLN ARG PRO ASP LEU PHE GLY CYS          
SEQRES  45 A  709  VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU LYS PHE          
SEQRES  46 A  709  HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR ASP TYR          
SEQRES  47 A  709  GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP LEU VAL          
SEQRES  48 A  709  LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO GLU ALA          
SEQRES  49 A  709  ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU THR ALA          
SEQRES  50 A  709  ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER LEU LYS          
SEQRES  51 A  709  PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG SER ARG          
SEQRES  52 A  709  LYS GLN ASN ASN PRO LEU LEU ILE HIS VAL ASP THR LYS          
SEQRES  53 A  709  ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS VAL ILE          
SEQRES  54 A  709  GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA ARG CYS          
SEQRES  55 A  709  LEU ASN VAL ASP TRP ILE PRO                                  
HET    ACT  A 801       4                                                       
HET    ACT  A 802       4                                                       
HET    ACT  A 803       4                                                       
HET    ACT  A 804       4                                                       
HET    ACT  A 805       4                                                       
HET    552  A 901      27                                                       
HET    GOL  A1000       5                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     552 (6S)-1-CHLORO-3-[(4-FLUOROBENZYL)OXY]-6-(PYRROLIDIN-1-           
HETNAM   2 552  YLCARBONYL)PYRROLO[1,2-A]PYRAZIN-4(6H)-ONE                      
HETNAM     GOL GLYCEROL                                                         
FORMUL   2  ACT    5(C2 H3 O2 1-)                                               
FORMUL   7  552    C19 H17 CL F N3 O3                                           
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *1234(H2 O)                                                   
HELIX    1   1 TYR A   28  ASP A   33  5                                   6    
HELIX    2   2 SER A   36  GLN A   56  1                                  21    
HELIX    3   3 PRO A   58  TYR A   71  1                                  14    
HELIX    4   4 ASP A  115  SER A  120  5                                   6    
HELIX    5   5 ASP A  218  ASP A  222  5                                   5    
HELIX    6   6 GLN A  267  GLU A  269  5                                   3    
HELIX    7   7 GLU A  322  TRP A  326  5                                   5    
HELIX    8   8 ASP A  431  SER A  433  5                                   3    
HELIX    9   9 SER A  485  GLY A  496  1                                  12    
HELIX   10  10 TYR A  510  GLY A  517  1                                   8    
HELIX   11  11 GLY A  518  ASN A  522  5                                   5    
HELIX   12  12 LYS A  523  GLU A  540  1                                  18    
HELIX   13  13 SER A  544  LYS A  546  5                                   3    
HELIX   14  14 SER A  554  ARG A  567  1                                  14    
HELIX   15  15 PRO A  568  PHE A  571  5                                   4    
HELIX   16  16 LYS A  585  TYR A  589  5                                   5    
HELIX   17  17 ILE A  591  ALA A  594  5                                   4    
HELIX   18  18 TRP A  595  GLY A  600  1                                   6    
HELIX   19  19 SER A  604  SER A  615  1                                  12    
HELIX   20  20 PRO A  616  ASN A  619  5                                   4    
HELIX   21  21 PRO A  646  VAL A  660  1                                  15    
HELIX   22  22 PRO A  685  ASN A  705  1                                  21    
SHEET    1   A 2 VAL A  16  TYR A  19  0                                        
SHEET    2   A 2 HIS A  22  CYS A  25 -1  O  HIS A  22   N  TYR A  19           
SHEET    1   B 3 LYS A  75  TYR A  76  0                                        
SHEET    2   B 3 ARG A  85  ASN A  91 -1  O  ASN A  91   N  LYS A  75           
SHEET    3   B 3 PHE A  80  LYS A  82 -1  N  PHE A  80   O  PHE A  87           
SHEET    1   C 4 LYS A  75  TYR A  76  0                                        
SHEET    2   C 4 ARG A  85  ASN A  91 -1  O  ASN A  91   N  LYS A  75           
SHEET    3   C 4 VAL A  99  GLN A 103 -1  O  TYR A 101   N  TYR A  88           
SHEET    4   C 4 ARG A 111  LEU A 114 -1  O  PHE A 113   N  LEU A 100           
SHEET    1   D 4 VAL A 125  PHE A 132  0                                        
SHEET    2   D 4 TYR A 138  ALA A 145 -1  O  GLY A 142   N  GLY A 129           
SHEET    3   D 4 VAL A 151  LYS A 157 -1  O  LYS A 154   N  TYR A 141           
SHEET    4   D 4 LYS A 162  VAL A 171 -1  O  VAL A 171   N  VAL A 151           
SHEET    1   E 4 MET A 176  TRP A 178  0                                        
SHEET    2   E 4 GLY A 184  SER A 189 -1  O  PHE A 186   N  ALA A 177           
SHEET    3   E 4 LYS A 209  VAL A 214 -1  O  HIS A 213   N  MET A 185           
SHEET    4   E 4 ILE A 223  ALA A 226 -1  O  CYS A 225   N  LEU A 210           
SHEET    1   F 4 MET A 235  LEU A 240  0                                        
SHEET    2   F 4 TYR A 246  ARG A 252 -1  O  LEU A 248   N  GLU A 239           
SHEET    3   F 4 ARG A 260  ASP A 265 -1  O  TRP A 262   N  LEU A 249           
SHEET    4   F 4 VAL A 280  ILE A 283 -1  O  VAL A 280   N  TYR A 263           
SHEET    1   G 4 TYR A 290  GLU A 296  0                                        
SHEET    2   G 4 VAL A 299  THR A 304 -1  O  THR A 301   N  THR A 294           
SHEET    3   G 4 ARG A 312  ASP A 317 -1  O  ILE A 316   N  PHE A 300           
SHEET    4   G 4 LYS A 327  VAL A 330 -1  O  LYS A 327   N  ASN A 315           
SHEET    1   H 4 VAL A 337  VAL A 344  0                                        
SHEET    2   H 4 PHE A 348  HIS A 355 -1  O  VAL A 350   N  ALA A 342           
SHEET    3   H 4 LYS A 358  ASP A 365 -1  O  LYS A 358   N  HIS A 355           
SHEET    4   H 4 LEU A 371  PHE A 375 -1  O  LEU A 372   N  LEU A 363           
SHEET    1   I 4 SER A 381  SER A 386  0                                        
SHEET    2   I 4 GLU A 393  THR A 399 -1  O  GLN A 397   N  VAL A 383           
SHEET    3   I 4 ILE A 406  ASP A 411 -1  O  TYR A 408   N  TYR A 396           
SHEET    4   I 4 ARG A 420  ARG A 423 -1  O  PHE A 422   N  ILE A 407           
SHEET    1   J 8 TYR A 435  PRO A 443  0                                        
SHEET    2   J 8 LYS A 449  LYS A 457 -1  O  ILE A 450   N  TYR A 442           
SHEET    3   J 8 ILE A 498  ALA A 502 -1  O  LEU A 499   N  VAL A 455           
SHEET    4   J 8 ALA A 468  TYR A 471  1  N  TYR A 471   O  ALA A 500           
SHEET    5   J 8 LEU A 548  GLY A 553  1  O  THR A 549   N  LEU A 470           
SHEET    6   J 8 CYS A 573  GLN A 577  1  O  ILE A 575   N  ILE A 550           
SHEET    7   J 8 SER A 632  ALA A 638  1  O  LEU A 634   N  VAL A 574           
SHEET    8   J 8 LEU A 670  ASP A 675  1  O  LEU A 671   N  MET A 633           
SITE     1 AC1  4 TYR A 473  SER A 554  HIS A 680  HOH A1213                    
SITE     1 AC2  5 PHE A 401  ARG A 488  LEU A 499  HOH A1543                    
SITE     2 AC2  5 HOH A2062                                                     
SITE     1 AC3  6 PRO A   7  GLN A 657  ARG A 662  HOH A1153                    
SITE     2 AC3  6 HOH A1587  HOH A2116                                          
SITE     1 AC4  5 SER A 485  SER A 487  HOH A1175  HOH A1695                    
SITE     2 AC4  5 HOH A1827                                                     
SITE     1 AC5  9 LEU A  70  ILE A 430  TYR A 435  LEU A 489                    
SITE     2 AC5  9 ILE A 490  ARG A 493  HIS A 494  HOH A1456                    
SITE     3 AC5  9 HOH A2236                                                     
SITE     1 AC6  8 PHE A 173  MET A 235  ARG A 252  GLY A 254                    
SITE     2 AC6  8 PHE A 476  SER A 554  TRP A 595  ARG A 643                    
SITE     1 AC7  7 ALA A 226  GLU A 227  PHE A 228  ILE A 276                    
SITE     2 AC7  7 HOH A1001  HOH A1244  HOH A1581                               
CRYST1   71.221   99.883  111.853  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      0.014041  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010012  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008940        0.00000                         
TER    5646      PRO A 710                                                      
MASTER      327    0    7   22   41    0   14    6 6931    1   52   55          
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
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