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LongText Report for: 3EQ9-pdb

Name Class
3EQ9-pdb
HEADER    HYDROLASE                               30-SEP-08   3EQ9              
TITLE     PROLYL OLIGOPEPTIDASE COMPLEXED WITH R-PRO-(DECARBOXY-PRO)-           
TITLE    2 TYPE INHIBITORS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL ENDOPEPTIDASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROLYL OLIGOPEPTIDASE, PE, POST-PROLINE CLEAVING            
COMPND   5 ENZYME;                                                              
COMPND   6 EC: 3.4.21.26                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 TISSUE: MUSCLE                                                       
KEYWDS    PROTEASE-INHIBITOR COMPLEX, CYTOPLASM, HYDROLASE, PROTEASE,           
KEYWDS   2 SERINE PROTEASE                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KANAI,P.ARANYI,Z.BOCSKEI,G.FERENCZY,V.HARMAT,K.SIMON,               
AUTHOR   2 G.NARAY-SZABO,I.HERMECZ                                              
REVDAT   1   25-AUG-09 3EQ9    0                                                
JRNL        AUTH   K.KANAI,P.ARANYI,Z.BOCSKEI,G.FERENCZY,V.HARMAT,              
JRNL        AUTH 2 K.SIMON,S.BATORI,G.NARAY-SZABO,I.HERMECZ                     
JRNL        TITL   PROLYL OLIGOPEPTIDASE INHIBITION BY                          
JRNL        TITL 2 N-ACYL-PRO-PYRROLIDINE-TYPE MOLECULES                        
JRNL        REF    J.MED.CHEM.                   V.  51  7514 2008              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19006380                                                     
JRNL        DOI    10.1021/JM800944X                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28372                          
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 SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2819                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5675                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 132                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.18                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.18                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.95                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUPED ISOTROPIC B-FACTORS, 2 B-         
REMARK   3                            VALUES/RESIDUE                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3EQ9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049640.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : CAPILLARY COLLIMATOR               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28405                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44100                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1QFS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% MPEG 5000, 15% GLYCEROL, 20MM        
REMARK 280  CALCIUM ACETATE, 0.1M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, 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   -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       36.27500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.16500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.73000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.16500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.27500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.73000            
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LEU 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     GLN A   5    OE1  NE2                                            
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 192    OE1  NE2                                            
REMARK 470     GLN A 193    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 194    CG   OD1  OD2                                       
REMARK 470     GLU A 416    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 546    CD   CE   NZ                                        
REMARK 470     GLU A 624    CG   CD   OE1  OE2                                  
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 A   187     OD2  ASP A   222              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  13        4.46    -67.57                                   
REMARK 500    ASP A 159      106.76    -58.18                                   
REMARK 500    MET A 176       86.22   -160.67                                   
REMARK 500    HIS A 180       -9.66    -56.56                                   
REMARK 500    SER A 197       58.57   -149.33                                   
REMARK 500    ASP A 222      150.22    -45.45                                   
REMARK 500    LEU A 282      -71.26    -54.84                                   
REMARK 500    ASP A 284       53.99    -96.81                                   
REMARK 500    VAL A 293      -61.20   -107.58                                   
REMARK 500    TYR A 311      159.65     70.25                                   
REMARK 500    ASP A 320       70.05   -159.33                                   
REMARK 500    SER A 324        2.10    -57.37                                   
REMARK 500    LYS A 335      -54.16   -129.25                                   
REMARK 500    SER A 346      -51.10     65.78                                   
REMARK 500    GLU A 378     -173.32    -68.41                                   
REMARK 500    LYS A 428      153.45    -49.94                                   
REMARK 500    TYR A 473      -79.73   -119.23                                   
REMARK 500    SER A 485       88.64   -152.11                                   
REMARK 500    ASN A 503       58.93    -94.18                                   
REMARK 500    LEU A 520     -113.15     50.23                                   
REMARK 500    SER A 554     -113.53     57.75                                   
REMARK 500    VAL A 578       66.07     23.54                                   
REMARK 500    THR A 590     -111.83     32.21                                   
REMARK 500    SER A 615      113.84    -39.68                                   
REMARK 500    VAL A 645      140.03    -38.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: 3-{4-OXO-4-[(2S)-2-(PYRROLIDIN-1-YLCARBONYL)          
REMARK 630 PYRROLIDIN-1-YL]BUTYL}-5,5-DIPHENYLIMIDAZOLIDINE-2,4-DIONE           
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     X97 A     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 SUBCOMP:    FIM PRO PRU                                              
REMARK 630 STRUCTURE DETAILS: NULL                                              
REMARK 630 OTHER DETAILS: NULL                                                  
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X97 A 711                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EQ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EQ8   RELATED DB: PDB                                   
DBREF  3EQ9 A    1   710  UNP    P23687   PPCE_PIG         1    710             
SEQRES   1 A  710  MET LEU SER PHE GLN TYR PRO ASP VAL TYR ARG ASP GLU          
SEQRES   2 A  710  THR ALA ILE GLN ASP TYR HIS GLY HIS LYS VAL CYS ASP          
SEQRES   3 A  710  PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN THR          
SEQRES   4 A  710  LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL PRO          
SEQRES   5 A  710  PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS GLU          
SEQRES   6 A  710  ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER CYS          
SEQRES   7 A  710  HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR ASN          
SEQRES   8 A  710  THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN ASP          
SEQRES   9 A  710  SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO ASN          
SEQRES  10 A  710  ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY TYR          
SEQRES  11 A  710  ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY LEU          
SEQRES  12 A  710  SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE MET          
SEQRES  13 A  710  LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU GLU          
SEQRES  14 A  710  ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP GLY          
SEQRES  15 A  710  LYS GLY MET PHE TYR ASN ALA TYR PRO GLN GLN ASP GLY          
SEQRES  16 A  710  LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS GLN          
SEQRES  17 A  710  LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER GLU          
SEQRES  18 A  710  ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS TRP          
SEQRES  19 A  710  MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR VAL          
SEQRES  20 A  710  LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN ARG          
SEQRES  21 A  710  LEU TRP TYR CYS ASP LEU GLN GLN GLU SER ASN GLY ILE          
SEQRES  22 A  710  THR GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN PHE          
SEQRES  23 A  710  GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR VAL          
SEQRES  24 A  710  PHE THR PHE LYS THR ASN ARG HIS SER PRO ASN TYR ARG          
SEQRES  25 A  710  LEU ILE ASN ILE ASP PHE THR ASP PRO GLU GLU SER LYS          
SEQRES  26 A  710  TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL LEU          
SEQRES  27 A  710  GLU TRP VAL ALA CYS VAL ARG SER ASN PHE LEU VAL LEU          
SEQRES  28 A  710  CYS TYR LEU HIS ASP VAL LYS ASN THR LEU GLN LEU HIS          
SEQRES  29 A  710  ASP LEU ALA THR GLY ALA LEU LEU LYS ILE PHE PRO LEU          
SEQRES  30 A  710  GLU VAL GLY SER VAL VAL GLY TYR SER GLY GLN LYS LYS          
SEQRES  31 A  710  ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU SER          
SEQRES  32 A  710  PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU GLU          
SEQRES  33 A  710  LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS GLY          
SEQRES  34 A  710  ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE TYR          
SEQRES  35 A  710  PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL          
SEQRES  36 A  710  HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO ALA          
SEQRES  37 A  710  PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE THR          
SEQRES  38 A  710  PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG HIS          
SEQRES  39 A  710  MET GLY GLY VAL LEU ALA VAL ALA ASN ILE ARG GLY GLY          
SEQRES  40 A  710  GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE LEU          
SEQRES  41 A  710  ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS ALA          
SEQRES  42 A  710  ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO LYS          
SEQRES  43 A  710  ARG LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU LEU          
SEQRES  44 A  710  VAL ALA THR CYS ALA ASN GLN ARG PRO ASP LEU PHE GLY          
SEQRES  45 A  710  CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU LYS          
SEQRES  46 A  710  PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR ASP          
SEQRES  47 A  710  TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP LEU          
SEQRES  48 A  710  ILE LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO GLU          
SEQRES  49 A  710  ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU THR          
SEQRES  50 A  710  ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER LEU          
SEQRES  51 A  710  LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG SER          
SEQRES  52 A  710  ARG LYS GLN ASN ASN PRO LEU LEU ILE HIS VAL ASP THR          
SEQRES  53 A  710  LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS VAL          
SEQRES  54 A  710  ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA ARG          
SEQRES  55 A  710  CYS LEU ASN ILE ASP TRP ILE PRO                              
HET    X97  A 711      36                                                       
HETNAM     X97 3-{4-OXO-4-[(2S)-2-(PYRROLIDIN-1-YLCARBONYL)PYRROLIDIN-          
HETNAM   2 X97  1-YL]BUTYL}-5,5-DIPHENYLIMIDAZOLIDINE-2,4-DIONE                 
FORMUL   2  X97    C28 H32 N4 O4                                                
FORMUL   3  HOH   *132(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  LEU A  119  5                                   5    
HELIX    5   5 ASP A  218  ASP A  222  5                                   5    
HELIX    6   6 GLU A  322  TRP A  326  5                                   5    
HELIX    7   7 ASP A  431  SER A  433  5                                   3    
HELIX    8   8 SER A  485  GLY A  496  1                                  12    
HELIX    9   9 GLY A  511  GLY A  517  1                                   7    
HELIX   10  10 GLY A  518  ASN A  522  5                                   5    
HELIX   11  11 LYS A  523  GLU A  540  1                                  18    
HELIX   12  12 SER A  544  LYS A  546  5                                   3    
HELIX   13  13 ASN A  555  ARG A  567  1                                  13    
HELIX   14  14 PRO A  568  PHE A  571  5                                   4    
HELIX   15  15 LYS A  585  TYR A  589  5                                   5    
HELIX   16  16 ILE A  591  ALA A  594  5                                   4    
HELIX   17  17 TRP A  595  GLY A  600  1                                   6    
HELIX   18  18 SER A  604  SER A  615  1                                  12    
HELIX   19  19 PRO A  616  ASN A  619  5                                   4    
HELIX   20  20 PRO A  646  VAL A  660  1                                  15    
HELIX   21  21 PRO A  685  LEU A  704  1                                  20    
SHEET    1   A 2 ILE 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  GLN A 103   N  TYR A  86           
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  ARG A 128           
SHEET    3   D 4 VAL A 151  LYS A 157 -1  O  MET A 156   N  PHE A 139           
SHEET    4   D 4 LYS A 162  VAL A 171 -1  O  LYS A 162   N  LYS A 157           
SHEET    1   E 4 ALA A 177  TRP A 178  0                                        
SHEET    2   E 4 GLY A 184  ALA 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  ARG A 252   N  MET A 235           
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  LYS A 303   N  ASP A 291           
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  LEU A 354 -1  O  VAL A 350   N  ALA A 342           
SHEET    3   H 4 ASN A 359  ASP A 365 -1  O  HIS A 364   N  LEU A 349           
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  THR A 399   N  SER A 381           
SHEET    3   I 4 ILE A 406  ASP A 411 -1  O  ILE A 406   N  PHE A 398           
SHEET    4   I 4 ARG A 420  GLU A 424 -1  O  ARG A 420   N  HIS A 409           
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 VAL 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  PHE A 469   O  VAL A 498           
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  GLN A 577   N  GLY A 552           
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 12 PHE A 173  MET A 235  ARG A 252  GLY A 254                    
SITE     2 AC1 12 PHE A 476  SER A 554  ALA A 594  TRP A 595                    
SITE     3 AC1 12 TYR A 599  ARG A 643  VAL A 644  HOH A 843                    
CRYST1   72.550  101.460  112.330  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      0.013780  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008900        0.00000                         
TER    5676      PRO A 710                                                      
MASTER      301    0    1   21   41    0    3    6 5843    1   36   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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