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LongText Report for: 2EEP-pdb

Name Class
2EEP-pdb
HEADER    HYDROLASE                               16-FEB-07   2EEP              
TITLE     PROLYL TRIPEPTIDYL AMINOPEPTIDASE COMPLEXED WITH AN                   
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE IV, PUTATIVE;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 39-732;                                           
COMPND   5 SYNONYM: PROLYL TRIPEPTIDYL AMINOPEPTIDASE;                          
COMPND   6 EC: 3.4.14.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;                       
SOURCE   3 STRAIN: W83;                                                         
SOURCE   4 GENE: PG1361;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    PEPTIDASE FAMILY S9, PROLYL OLIGOPEPTIDASE FAMILY, SERINE             
KEYWDS   2 PEPTIDASE, INHIBITOR COMPLEX, HYDROLASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XU,Y.NAKAJIMA,K.ITO,T.YOSHIMOTO                                     
REVDAT   1   19-FEB-08 2EEP    0                                                
JRNL        AUTH   Y.XU,Y.NAKAJIMA,K.ITO,H.ZHENG,H.OYAMA,U.HEISER,              
JRNL        AUTH 2 T.HOFFMANN,U.T.GARTNER,H.U.DEMUTH,T.YOSHIMOTO                
JRNL        TITL   NOVEL INHIBITOR FOR PROLYL TRIPEPTIDYL                       
JRNL        TITL 2 AMINOPEPTIDASE FROM PORPHYROMONAS GINGIVALIS AND             
JRNL        TITL 3 DETAILS OF SUBSTRATE-RECOGNITION MECHANISM                   
JRNL        REF    J.MOL.BIOL.                   V. 375   708 2008              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 51058                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2718                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3686                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 188                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 5592                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.04000                                             
REMARK   3    B22 (A**2) : -1.04000                                             
REMARK   3    B33 (A**2) : 1.57000                                              
REMARK   3    B12 (A**2) : -0.52000                                             
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): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.302         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5399 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7340 ; 1.617 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   654 ; 6.940 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;33.740 ;23.268       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   840 ;14.458 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;17.170 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   785 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4181 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2322 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3612 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   431 ; 0.135 ; 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):    43 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.112 ; 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):  3368 ; 1.176 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5265 ; 1.792 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2382 ; 2.774 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2075 ; 3.953 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EEP COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB026572.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 9.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54747                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 20.700                             
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 79.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 19.80                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.27700                            
REMARK 200   FOR SHELL         : 14.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2D5L                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M POTASSIUM SODIUM TARTRATE,          
REMARK 280  0.2M LITHIUM SULFATE, 0.1M CHES BUFFER, PH 9.0, VAPOR               
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X-Y,X,1/2+Z                                             
REMARK 290       3555   -Y,X-Y,Z                                                
REMARK 290       4555   -X,-Y,1/2+Z                                             
REMARK 290       5555   -X+Y,-X,Z                                               
REMARK 290       6555   Y,-X+Y,1/2+Z                                            
REMARK 290       7555   X-Y,-Y,-Z                                               
REMARK 290       8555   -Y,-X,1/2-Z                                             
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -X+Y,Y,1/2-Z                                            
REMARK 290      11555   Y,X,-Z                                                  
REMARK 290      12555   X,X-Y,1/2-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.49250            
REMARK 290   SMTRY1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       80.49250            
REMARK 290   SMTRY1   5 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       80.49250            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       80.49250            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       80.49250            
REMARK 290   SMTRY1  11 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       80.49250            
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: DIMER                             
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      160.98500            
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     MET A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     LEU A    39                                                      
REMARK 465     MET A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     TYR A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     ASN A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     LYS A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLN A    83                                                      
REMARK 465     GLU A    98                                                      
REMARK 465     GLY A    99                                                      
REMARK 465     CYS A   100                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     PHE A   102                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     THR A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     ASP A   106                                                      
REMARK 465     ALA A   107                                                      
REMARK 465     PRO A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     THR A   474                                                      
REMARK 465     GLY A   475                                                      
REMARK 465     TYR A   476                                                      
REMARK 465     SER A   532                                                      
REMARK 465     SER A   533                                                      
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     TYR A  50    CG    CD1   CD2   CE1   CE2   CZ    OH              
REMARK 470     LYS A  76    CG    CD    CE    NZ                                
REMARK 470     LYS A 470    CG    CD    CE    NZ                                
REMARK 470     ASN A 471    CG    OD1   ND2                                     
REMARK 470     ARG A 531    CG    CD    NE    CZ    NH1   NH2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 126      -34.82    -36.11                                   
REMARK 500    THR A 140      -76.02    -94.50                                   
REMARK 500    ASN A 146       47.76     39.03                                   
REMARK 500    GLU A 147      -13.82     86.25                                   
REMARK 500    HIS A 167       -8.66     79.63                                   
REMARK 500    HIS A 333      -66.03   -107.04                                   
REMARK 500    ARG A 374      136.21   -171.99                                   
REMARK 500    SER A 404      147.59   -170.16                                   
REMARK 500    ARG A 452      119.27   -171.76                                   
REMARK 500    LYS A 461       38.00   -142.25                                   
REMARK 500    TYR A 518      -75.66   -117.00                                   
REMARK 500    ARG A 570       42.63   -144.25                                   
REMARK 500    SER A 603     -120.27     78.21                                   
REMARK 500    ASP A 645     -176.59     64.82                                   
REMARK 500    ASN A 650       57.61   -142.22                                   
REMARK 500    VAL A 680      -65.35   -103.71                                   
REMARK 500    GLN A 684      -36.93    -34.84                                   
REMARK 500    GLU A 709     -133.03    -91.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TRP A  530    ARG A  531                 -148.68                     
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 802                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: AIO BINDING SITE FOR RESIDUE A 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2D5L   RELATED DB: PDB                                   
REMARK 900 THE LIGAND-FREE TYPE OF THE SAME ENZYME                              
REMARK 900 RELATED ID: 2DCM   RELATED DB: PDB                                   
REMARK 900 THE S603A MUTANT ENZYME COMPLEXED WITH AN SUBSTRATE                  
DBREF  2EEP A   39   732  UNP    Q7MUW6   Q7MUW6_PORGI    39    732             
SEQADV 2EEP MET A   27  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP ARG A   28  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP GLY A   29  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP SER A   30  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   31  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   32  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   33  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   34  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   35  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP HIS A   36  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP GLY A   37  UNP  Q7MUW6              EXPRESSION TAG                 
SEQADV 2EEP SER A   38  UNP  Q7MUW6              EXPRESSION TAG                 
SEQRES   1 A  706  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER LEU          
SEQRES   2 A  706  MET PRO GLY GLY LYS GLU PHE TYR ASN PHE TYR PRO GLU          
SEQRES   3 A  706  TYR VAL VAL GLY LEU GLN TRP MET GLY ASP ASN TYR VAL          
SEQRES   4 A  706  PHE ILE GLU GLY ASP ASP LEU VAL PHE ASN LYS ALA ASN          
SEQRES   5 A  706  GLY LYS SER ALA GLN THR THR ARG PHE SER ALA ALA ASP          
SEQRES   6 A  706  LEU ASN ALA LEU MET PRO GLU GLY CYS LYS PHE GLN THR          
SEQRES   7 A  706  THR ASP ALA PHE PRO SER PHE ARG THR LEU ASP ALA GLY          
SEQRES   8 A  706  ARG GLY LEU VAL VAL LEU PHE THR GLN GLY GLY LEU VAL          
SEQRES   9 A  706  GLY PHE ASP MET LEU ALA ARG LYS VAL THR TYR LEU PHE          
SEQRES  10 A  706  ASP THR ASN GLU GLU THR ALA SER LEU ASP PHE SER PRO          
SEQRES  11 A  706  VAL GLY ASP ARG VAL ALA TYR VAL ARG ASN HIS ASN LEU          
SEQRES  12 A  706  TYR ILE ALA ARG GLY GLY LYS LEU GLY GLU GLY MET SER          
SEQRES  13 A  706  ARG ALA ILE ALA VAL THR ILE ASP GLY THR GLU THR LEU          
SEQRES  14 A  706  VAL TYR GLY GLN ALA VAL HIS GLN ARG GLU PHE GLY ILE          
SEQRES  15 A  706  GLU LYS GLY THR PHE TRP SER PRO LYS GLY SER CYS LEU          
SEQRES  16 A  706  ALA PHE TYR ARG MET ASP GLN SER MET VAL LYS PRO THR          
SEQRES  17 A  706  PRO ILE VAL ASP TYR HIS PRO LEU GLU ALA GLU SER LYS          
SEQRES  18 A  706  PRO LEU TYR TYR PRO MET ALA GLY THR PRO SER HIS HIS          
SEQRES  19 A  706  VAL THR VAL GLY ILE TYR HIS LEU ALA THR GLY LYS THR          
SEQRES  20 A  706  VAL TYR LEU GLN THR GLY GLU PRO LYS GLU LYS PHE LEU          
SEQRES  21 A  706  THR ASN LEU SER TRP SER PRO ASP GLU ASN ILE LEU TYR          
SEQRES  22 A  706  VAL ALA GLU VAL ASN ARG ALA GLN ASN GLU CYS LYS VAL          
SEQRES  23 A  706  ASN ALA TYR ASP ALA GLU THR GLY ARG PHE VAL ARG THR          
SEQRES  24 A  706  LEU PHE VAL GLU THR ASP LYS HIS TYR VAL GLU PRO LEU          
SEQRES  25 A  706  HIS PRO LEU THR PHE LEU PRO GLY SER ASN ASN GLN PHE          
SEQRES  26 A  706  ILE TRP GLN SER ARG ARG ASP GLY TRP ASN HIS LEU TYR          
SEQRES  27 A  706  LEU TYR ASP THR THR GLY ARG LEU ILE ARG GLN VAL THR          
SEQRES  28 A  706  LYS GLY GLU TRP GLU VAL THR ASN PHE ALA GLY PHE ASP          
SEQRES  29 A  706  PRO LYS GLY THR ARG LEU TYR PHE GLU SER THR GLU ALA          
SEQRES  30 A  706  SER PRO LEU GLU ARG HIS PHE TYR CYS ILE ASP ILE LYS          
SEQRES  31 A  706  GLY GLY LYS THR LYS ASP LEU THR PRO GLU SER GLY MET          
SEQRES  32 A  706  HIS ARG THR GLN LEU SER PRO ASP GLY SER ALA ILE ILE          
SEQRES  33 A  706  ASP ILE PHE GLN SER PRO THR VAL PRO ARG LYS VAL THR          
SEQRES  34 A  706  VAL THR ASN ILE GLY LYS GLY SER HIS THR LEU LEU GLU          
SEQRES  35 A  706  ALA LYS ASN PRO ASP THR GLY TYR ALA MET PRO GLU ILE          
SEQRES  36 A  706  ARG THR GLY THR ILE MET ALA ALA ASP GLY GLN THR PRO          
SEQRES  37 A  706  LEU TYR TYR LYS LEU THR MET PRO LEU HIS PHE ASP PRO          
SEQRES  38 A  706  ALA LYS LYS TYR PRO VAL ILE VAL TYR VAL TYR GLY GLY          
SEQRES  39 A  706  PRO HIS ALA GLN LEU VAL THR LYS THR TRP ARG SER SER          
SEQRES  40 A  706  VAL GLY GLY TRP ASP ILE TYR MET ALA GLN LYS GLY TYR          
SEQRES  41 A  706  ALA VAL PHE THR VAL ASP SER ARG GLY SER ALA ASN ARG          
SEQRES  42 A  706  GLY ALA ALA PHE GLU GLN VAL ILE HIS ARG ARG LEU GLY          
SEQRES  43 A  706  GLN THR GLU MET ALA ASP GLN MET CYS GLY VAL ASP PHE          
SEQRES  44 A  706  LEU LYS SER GLN SER TRP VAL ASP ALA ASP ARG ILE GLY          
SEQRES  45 A  706  VAL HIS GLY TRP SER TYR GLY GLY PHE MET THR THR ASN          
SEQRES  46 A  706  LEU MET LEU THR HIS GLY ASP VAL PHE LYS VAL GLY VAL          
SEQRES  47 A  706  ALA GLY GLY PRO VAL ILE ASP TRP ASN ARG TYR GLU ILE          
SEQRES  48 A  706  MET TYR GLY GLU ARG TYR PHE ASP ALA PRO GLN GLU ASN          
SEQRES  49 A  706  PRO GLU GLY TYR ASP ALA ALA ASN LEU LEU LYS ARG ALA          
SEQRES  50 A  706  GLY ASP LEU LYS GLY ARG LEU MET LEU ILE HIS GLY ALA          
SEQRES  51 A  706  ILE ASP PRO VAL VAL VAL TRP GLN HIS SER LEU LEU PHE          
SEQRES  52 A  706  LEU ASP ALA CYS VAL LYS ALA ARG THR TYR PRO ASP TYR          
SEQRES  53 A  706  TYR VAL TYR PRO SER HIS GLU HIS ASN VAL MET GLY PRO          
SEQRES  54 A  706  ASP ARG VAL HIS LEU TYR GLU THR ILE THR ARG TYR PHE          
SEQRES  55 A  706  THR ASP HIS LEU                                              
HET    SO4  A 802       5                                                       
HET    AIO  A 801      21                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     AIO [(2R)-1-(L-ALANYL-L-ISOLEUCYL)PYRROLIDIN-2-YL]BORONIC            
HETNAM   2 AIO  ACID                                                            
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  AIO    C13 H26 B N3 O4                                              
FORMUL   4  HOH   *336(H2 O)                                                    
HELIX    1   1 ALA A   89  MET A   96  1                                   8    
HELIX    2   2 VAL A  201  GLU A  205  5                                   5    
HELIX    3   3 GLY A  536  LYS A  544  1                                   9    
HELIX    4   4 GLY A  560  VAL A  566  1                                   7    
HELIX    5   5 GLY A  572  SER A  588  1                                  17    
HELIX    6   6 SER A  603  HIS A  616  1                                  14    
HELIX    7   7 ASP A  631  TYR A  635  5                                   5    
HELIX    8   8 GLU A  636  ASP A  645  1                                  10    
HELIX    9   9 ASN A  650  ASN A  658  1                                   9    
HELIX   10  10 LEU A  659  LEU A  666  5                                   8    
HELIX   11  11 TRP A  683  ARG A  697  1                                  15    
HELIX   12  12 PRO A  715  LEU A  732  1                                  18    
SHEET    1   A 4 GLN A  58  MET A  60  0                                        
SHEET    2   A 4 ASN A  63  GLU A  68 -1  O  ASN A  63   N  MET A  60           
SHEET    3   A 4 ASP A  71  ASN A  75 -1  O  VAL A  73   N  PHE A  66           
SHEET    4   A 4 THR A  85  SER A  88 -1  O  THR A  85   N  PHE A  74           
SHEET    1   B 4 PHE A 111  ASP A 115  0                                        
SHEET    2   B 4 LEU A 120  THR A 125 -1  O  VAL A 122   N  ARG A 112           
SHEET    3   B 4 GLY A 128  ASP A 133 -1  O  PHE A 132   N  VAL A 121           
SHEET    4   B 4 LYS A 138  PHE A 143 -1  O  TYR A 141   N  GLY A 131           
SHEET    1   C 4 ASP A 153  PHE A 154  0                                        
SHEET    2   C 4 ARG A 160  ARG A 165 -1  O  ALA A 162   N  ASP A 153           
SHEET    3   C 4 ASN A 168  ARG A 173 -1  O  ALA A 172   N  VAL A 161           
SHEET    4   C 4 ILE A 185  ALA A 186 -1  O  ILE A 185   N  ILE A 171           
SHEET    1   D 3 LEU A 195  TYR A 197  0                                        
SHEET    2   D 3 CYS A 220  ASP A 227 -1  O  MET A 226   N  VAL A 196           
SHEET    3   D 3 THR A 212  TRP A 214 -1  N  PHE A 213   O  ALA A 222           
SHEET    1   E 4 LEU A 195  TYR A 197  0                                        
SHEET    2   E 4 CYS A 220  ASP A 227 -1  O  MET A 226   N  VAL A 196           
SHEET    3   E 4 HIS A 260  HIS A 267 -1  O  TYR A 266   N  LEU A 221           
SHEET    4   E 4 LYS A 272  TYR A 275 -1  O  LYS A 272   N  HIS A 267           
SHEET    1   F 2 THR A 234  ASP A 238  0                                        
SHEET    2   F 2 GLU A 245  LEU A 249 -1  O  GLU A 245   N  ASP A 238           
SHEET    1   G 4 PHE A 285  TRP A 291  0                                        
SHEET    2   G 4 ILE A 297  VAL A 303 -1  O  TYR A 299   N  SER A 290           
SHEET    3   G 4 GLU A 309  ASP A 316 -1  O  LYS A 311   N  GLU A 302           
SHEET    4   G 4 PHE A 322  THR A 330 -1  O  LEU A 326   N  VAL A 312           
SHEET    1   H 4 THR A 342  PHE A 343  0                                        
SHEET    2   H 4 GLN A 350  SER A 355 -1  O  ILE A 352   N  THR A 342           
SHEET    3   H 4 HIS A 362  ASP A 367 -1  O  HIS A 362   N  SER A 355           
SHEET    4   H 4 LEU A 372  GLN A 375 -1  O  ARG A 374   N  LEU A 365           
SHEET    1   I 4 VAL A 383  PHE A 389  0                                        
SHEET    2   I 4 ARG A 395  SER A 400 -1  O  TYR A 397   N  GLY A 388           
SHEET    3   I 4 HIS A 409  ASP A 414 -1  O  ILE A 413   N  LEU A 396           
SHEET    4   I 4 LYS A 421  ASP A 422 -1  O  LYS A 421   N  CYS A 412           
SHEET    1   J 4 MET A 429  LEU A 434  0                                        
SHEET    2   J 4 ALA A 440  GLN A 446 -1  O  ILE A 444   N  ARG A 431           
SHEET    3   J 4 LYS A 453  ASN A 458 -1  O  THR A 455   N  ASP A 443           
SHEET    4   J 4 SER A 463  GLU A 468 -1  O  LEU A 466   N  VAL A 454           
SHEET    1   K 8 ILE A 481  MET A 487  0                                        
SHEET    2   K 8 PRO A 494  THR A 500 -1  O  LEU A 495   N  ILE A 486           
SHEET    3   K 8 ALA A 547  VAL A 551 -1  O  VAL A 548   N  THR A 500           
SHEET    4   K 8 TYR A 511  TYR A 516  1  N  ILE A 514   O  ALA A 547           
SHEET    5   K 8 VAL A 592  TRP A 602  1  O  GLY A 598   N  VAL A 515           
SHEET    6   K 8 VAL A 622  GLY A 626  1  O  GLY A 626   N  GLY A 601           
SHEET    7   K 8 ARG A 669  GLY A 675  1  O  MET A 671   N  ALA A 625           
SHEET    8   K 8 ASP A 701  TYR A 705  1  O  ASP A 701   N  LEU A 670           
LINK         B   AIO A 801                 OG  SER A 603   1555   1555    1.77  
CISPEP   1 TYR A   50    PRO A   51          0         9.28                     
CISPEP   2 GLU A  280    PRO A  281          0        -3.57                     
SITE     1 AC1  4 ARG A 321  SER A 347  ASN A 349  GLN A 350                    
SITE     1 AC2 13 GLN A 203  GLU A 205  TYR A 518  HIS A 522                    
SITE     2 AC2 13 SER A 603  TYR A 604  TYR A 635  GLU A 636                    
SITE     3 AC2 13 TYR A 639  HIS A 710  HOH A1134  HOH A1158                    
SITE     4 AC2 13 HOH A1184                                                     
CRYST1  150.103  150.103  160.985  90.00  90.00 120.00 P 63 2 2     12          
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      0.006662  0.003846  0.000000        0.00000                         
SCALE2      0.000000  0.007693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006212        0.00000                         
TER    5231      LEU A 732                                                      
MASTER      405    0    2   12   45    0    5    6 5592    1   27   55          
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.
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