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LongText Report for: 4BCC-pdb

Name Class
4BCC-pdb
HEADER    HYDROLASE                               01-OCT-12   4BCC              
TITLE     PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A COVALENTLY            
TITLE    2 BOUND P2-SUBSTITUTED N-ACYL-PROLYLPYRROLIDINE INHIBITOR              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL ENDOPEPTIDASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PE, POST-PROLINE CLEAVING ENZYME;                           
COMPND   5 EC: 3.4.21.26;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM105                                      
KEYWDS    ALPHA-BETA-HYDROLASE, AMNESIA, HYDROLASE, PARKINSONS DISEASE,         
KEYWDS   2 ALZHEIMERS DISEASE, INHIBITOR                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.VANDERVEKEN,V.FULOP,D.REA,M.GERARD,R.VANELZEN,J.JOOSSENS,J.D.CHENG, 
AUTHOR   2 V.BAEKELANDT,I.DEMEESTER,A.M.LAMBEIR,K.AUGUSTYNS                     
REVDAT   1   13-MAR-13 4BCC    0                                                
JRNL        AUTH   P.VAN DER VEKEN,V.FULOP,D.REA,M.GERARD,R.VAN ELZEN,          
JRNL        AUTH 2 J.JOOSSENS,J.D.CHENG,V.BAEKELANDT,I.DE MEESTER,A.M.LAMBEIR,  
JRNL        AUTH 3 K.AUGUSTYNS                                                  
JRNL        TITL   P2-SUBSTITUTED N-ACYLPROLYLPYRROLIDINE INHIBITORS OF PROLYL  
JRNL        TITL 2 OLIGOPEPTIDASE: BIOCHEMICAL EVALUATION, BINDING MODE         
JRNL        TITL 3 DETERMINATION, AND ASSESSMENT IN A CELLULAR MODEL OF         
JRNL        TITL 4 SYNUCLEINOPATHY.                                             
JRNL        REF    J.MED.CHEM.                   V.  55  9856 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23121075                                                     
JRNL        DOI    10.1021/JM301060G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.37                          
REMARK   3   NUMBER OF REFLECTIONS             : 81079                          
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) : 0.15746                         
REMARK   3   R VALUE            (WORKING SET) : 0.15609                         
REMARK   3   FREE R VALUE                     : 0.18954                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3405                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.650                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.693                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6124                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.228                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 239                          
REMARK   3   BIN FREE R VALUE                    : 0.275                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5701                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 817                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.512                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32                                                 
REMARK   3    B22 (A**2) : -0.97                                                
REMARK   3    B33 (A**2) : 0.65                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.094         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.157         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5953 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8057 ; 1.508 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   709 ; 6.232 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   285 ;33.213 ;24.316       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   972 ;13.101 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;16.988 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   847 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4547 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3528 ; 0.844 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5696 ; 1.519 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2425 ; 2.665 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2361 ; 4.102 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    72                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9420  49.0730  65.5420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0891 T22:   0.0420                                     
REMARK   3      T33:   0.0391 T12:  -0.0126                                     
REMARK   3      T13:  -0.0052 T23:   0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5499 L22:   0.0854                                     
REMARK   3      L33:   0.6647 L12:  -0.0443                                     
REMARK   3      L13:  -0.4015 L23:   0.0548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:   0.0447 S13:   0.0608                       
REMARK   3      S21:  -0.0755 S22:   0.0236 S23:   0.0054                       
REMARK   3      S31:  -0.0218 S32:  -0.0069 S33:   0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    73        A   427                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0010  40.6050 101.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0622 T22:   0.0662                                     
REMARK   3      T33:   0.0175 T12:   0.0059                                     
REMARK   3      T13:   0.0000 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1549 L22:   0.2925                                     
REMARK   3      L33:   0.1929 L12:   0.0127                                     
REMARK   3      L13:   0.0062 L23:  -0.0052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:  -0.0278 S13:   0.0075                       
REMARK   3      S21:   0.0444 S22:   0.0067 S23:  -0.0018                       
REMARK   3      S31:  -0.0160 S32:   0.0079 S33:  -0.0048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   428        A   710                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2960  39.0950  76.0540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0537 T22:   0.0589                                     
REMARK   3      T33:   0.0339 T12:  -0.0030                                     
REMARK   3      T13:  -0.0118 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2659 L22:   0.3998                                     
REMARK   3      L33:   0.2590 L12:  -0.0016                                     
REMARK   3      L13:  -0.0562 L23:  -0.0599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0318 S12:   0.0004 S13:   0.0094                       
REMARK   3      S21:  -0.0515 S22:   0.0227 S23:   0.0500                       
REMARK   3      S31:   0.0045 S32:  -0.0303 S33:   0.0091                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   791        A   791                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4740  37.0840  84.6860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0780 T22:   0.0451                                     
REMARK   3      T33:   0.0613 T12:  -0.0349                                     
REMARK   3      T13:   0.0344 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3767 L22:   9.3240                                     
REMARK   3      L33:   7.4204 L12:   5.4618                                     
REMARK   3      L13:   5.6198 L23:   0.9494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3660 S12:  -0.4111 S13:   0.3121                       
REMARK   3      S21:  -0.0152 S22:  -0.1756 S23:   0.1759                       
REMARK   3      S31:   0.0222 S32:  -0.1430 S33:  -0.1904                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. U VALUES RESIDUAL ONLY                           
REMARK   4                                                                      
REMARK   4 4BCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54277.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9702                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 375210                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.65                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : 4.4                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.39                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1QFS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% METHOXY-POLYETHYLENE              
REMARK 280  GLYCOL (MPEG) 5K, 20 MM CA(OAC)2, 0.1 M TRIS                        
REMARK 280  PH 8.5, 15% GLYCEROL                                                
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       35.24500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.13000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.57000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.13000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.24500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.57000            
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 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   OD1  ASP A   707     O    HOH A  2804              2.19            
REMARK 500   O4   TAM A  1711     O    HOH A  2640              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 351   CB  -  CG  -  CD2 ANGL. DEV. =  12.3 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    SER A   3       39.26    -97.68                                   
REMARK 500    ASN A 271       50.41   -157.76                                   
REMARK 500    ASP A 284       50.54   -115.72                                   
REMARK 500    SER A 308       79.31   -154.01                                   
REMARK 500    TYR A 311      152.18     77.03                                   
REMARK 500    ASP A 320       67.92   -151.72                                   
REMARK 500    LYS A 335      -37.76   -133.31                                   
REMARK 500    SER A 346      -57.96     67.07                                   
REMARK 500    TYR A 473      -79.28   -129.16                                   
REMARK 500    LEU A 520     -126.33     52.18                                   
REMARK 500    SER A 554     -117.97     69.74                                   
REMARK 500    VAL A 578       54.18     39.15                                   
REMARK 500    THR A 590     -113.97     35.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JKT A 791                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A1711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1720                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E5T   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT                    
REMARK 900 RELATED ID: 1E8M   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT,                   
REMARK 900  COMPLEXED WITH INHIBITOR                                            
REMARK 900 RELATED ID: 1E8N   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT,                   
REMARK 900  COMPLEXED WITH PEPTIDE                                              
REMARK 900 RELATED ID: 1H2W   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN                            
REMARK 900 RELATED ID: 1H2X   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT              
REMARK 900 RELATED ID: 1H2Y   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT              
REMARK 900  WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL                      
REMARK 900 RELATED ID: 1H2Z   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO                               
REMARK 900 RELATED ID: 1O6F   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO                               
REMARK 900 RELATED ID: 1O6G   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641N MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO                               
REMARK 900 RELATED ID: 1QFM   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE                           
REMARK 900 RELATED ID: 1QFS   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY           
REMARK 900   BOUND INHIBITOR Z-PRO-PROLINAL                                     
REMARK 900 RELATED ID: 1UOO   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND GLY-PHE-ARG-PRO                           
REMARK 900 RELATED ID: 1UOP   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND GLY-PHE-GLU-PRO                           
REMARK 900 RELATED ID: 1UOQ   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT              
REMARK 900  WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO                           
REMARK 900 RELATED ID: 1VZ2   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/               
REMARK 900  C255T MUTANT                                                        
REMARK 900 RELATED ID: 1VZ3   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT              
REMARK 900 RELATED ID: 2XDW   RELATED DB: PDB                                   
REMARK 900  INHIBITION OF PROLYL OLIGOPEPTIDASE WITH A SYNTHETIC                
REMARK 900  UNNATURAL DIPEPTIDE                                                 
REMARK 900 RELATED ID: 4AMY   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A                     
REMARK 900  COVALENTLY BOUND INHIBITOR IC-1                                     
REMARK 900 RELATED ID: 4AMZ   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A                     
REMARK 900  COVALENTLY BOUND INHIBITOR IC-2                                     
REMARK 900 RELATED ID: 4AN0   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A                     
REMARK 900  COVALENTLY BOUND INHIBITOR IC-3                                     
REMARK 900 RELATED ID: 4AN1   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A                     
REMARK 900  COVALENTLY BOUND INHIBITOR IC-4                                     
REMARK 900 RELATED ID: 4AX4   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, H680A MUTANT              
REMARK 900 RELATED ID: 4BCB   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A                     
REMARK 900  COVALENTLY BOUND P2-SUBSTITUTED N-ACYL-PROLYLPYRROLIDINE            
REMARK 900  INHIBITOR                                                           
REMARK 900 RELATED ID: 4BCD   RELATED DB: PDB                                   
REMARK 900  PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A NON-                
REMARK 900  COVALENTLY BOUND P2-SUBSTITUTED N-ACYL-PROLYLPYRROLIDINE            
REMARK 900  INHIBITOR                                                           
DBREF  4BCC 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    JKT  A 791      39                                                       
HET    TAM  A1711      11                                                       
HET    GOL  A1712       6                                                       
HET    GOL  A1713       6                                                       
HET    GOL  A1714       6                                                       
HET    GOL  A1715       6                                                       
HET    GOL  A1716       6                                                       
HET    GOL  A1717       6                                                       
HET    GOL  A1718       6                                                       
HET    GOL  A1719       6                                                       
HET    GOL  A1720       6                                                       
HETNAM     JKT TERT-BUTYL N-[[1-[(3S,5S)-5-[(2S)-2-                             
HETNAM   2 JKT  [AZANYL(OXIDANYL)METHYL]PYRROLIDIN-1-YL]CARBONYL-1-(4-          
HETNAM   3 JKT  PHENYLBUTANOYL)PYRROLIDIN-3-YL]-1,2,3-                          
HETNAM   4 JKT  TRIAZOL-4-YL]METHYL]CARBAMATE                                   
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  JKT    C28 H39 N7 O5                                                
FORMUL   3  TAM    C7 H17 N O3                                                  
FORMUL   4  GOL    9(C3 H8 O3)                                                  
FORMUL   5  HOH   *817(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  AA 2 ILE A  16  TYR A  19  0                                        
SHEET    2  AA 2 HIS A  22  CYS A  25 -1  O  HIS A  22   N  TYR A  19           
SHEET    1  AB 2 LYS A  75  TYR A  76  0                                        
SHEET    2  AB 2 ARG A  85  ASN A  91 -1  O  ASN A  91   N  LYS A  75           
SHEET    1  AC 2 PHE A  80  LYS A  82  0                                        
SHEET    2  AC 2 ARG A  85  ASN A  91 -1  O  ARG A  85   N  LYS A  82           
SHEET    1  AD 4 ALA A 110  LEU A 114  0                                        
SHEET    2  AD 4 VAL A  99  GLN A 103 -1  O  LEU A 100   N  PHE A 113           
SHEET    3  AD 4 ARG A  85  ASN A  91 -1  O  TYR A  86   N  GLN A 103           
SHEET    4  AD 4 PHE A  80  LYS A  82 -1  O  PHE A  80   N  PHE A  87           
SHEET    1  AE 4 ALA A 110  LEU A 114  0                                        
SHEET    2  AE 4 VAL A  99  GLN A 103 -1  O  LEU A 100   N  PHE A 113           
SHEET    3  AE 4 ARG A  85  ASN A  91 -1  O  TYR A  86   N  GLN A 103           
SHEET    4  AE 4 LYS A  75  TYR A  76 -1  O  LYS A  75   N  ASN A  91           
SHEET    1  AF 4 VAL A 125  PHE A 132  0                                        
SHEET    2  AF 4 TYR A 138  ALA A 145 -1  O  ALA A 140   N  ALA A 131           
SHEET    3  AF 4 VAL A 151  LYS A 157 -1  O  THR A 152   N  LEU A 143           
SHEET    4  AF 4 LYS A 162  VAL A 171 -1  O  LYS A 162   N  LYS A 157           
SHEET    1  AG 4 MET A 176  TRP A 178  0                                        
SHEET    2  AG 4 GLY A 184  ALA A 189 -1  O  PHE A 186   N  ALA A 177           
SHEET    3  AG 4 LYS A 209  VAL A 214 -1  O  LYS A 209   N  ALA A 189           
SHEET    4  AG 4 ILE A 223  ALA A 226 -1  O  ILE A 223   N  TYR A 212           
SHEET    1  AH 4 MET A 235  LEU A 240  0                                        
SHEET    2  AH 4 TYR A 246  ARG A 252 -1  O  LEU A 248   N  GLU A 239           
SHEET    3  AH 4 ARG A 260  ASP A 265 -1  O  ARG A 260   N  ILE A 251           
SHEET    4  AH 4 VAL A 280  ILE A 283 -1  O  VAL A 280   N  TYR A 263           
SHEET    1  AI 4 TYR A 290  GLU A 296  0                                        
SHEET    2  AI 4 VAL A 299  THR A 304 -1  O  VAL A 299   N  GLU A 296           
SHEET    3  AI 4 ARG A 312  ASP A 317 -1  O  ARG A 312   N  THR A 304           
SHEET    4  AI 4 LYS A 327  VAL A 330 -1  O  LYS A 327   N  ASN A 315           
SHEET    1  AJ 4 VAL A 337  VAL A 344  0                                        
SHEET    2  AJ 4 PHE A 348  HIS A 355 -1  O  PHE A 348   N  VAL A 344           
SHEET    3  AJ 4 LYS A 358  ASP A 365 -1  O  LYS A 358   N  HIS A 355           
SHEET    4  AJ 4 LEU A 371  PHE A 375 -1  N  LEU A 372   O  LEU A 363           
SHEET    1  AK 4 SER A 381  SER A 386  0                                        
SHEET    2  AK 4 GLU A 393  THR A 399 -1  O  PHE A 395   N  SER A 386           
SHEET    3  AK 4 ILE A 406  ASP A 411 -1  O  ILE A 406   N  PHE A 398           
SHEET    4  AK 4 ARG A 420  GLU A 424 -1  O  ARG A 420   N  HIS A 409           
SHEET    1  AL 8 TYR A 435  PRO A 443  0                                        
SHEET    2  AL 8 LYS A 449  LYS A 457 -1  O  ILE A 450   N  TYR A 442           
SHEET    3  AL 8 VAL A 498  ALA A 502 -1  O  LEU A 499   N  VAL A 455           
SHEET    4  AL 8 ALA A 468  TYR A 471  1  O  PHE A 469   N  ALA A 500           
SHEET    5  AL 8 LEU A 548  GLY A 553  1  O  THR A 549   N  LEU A 470           
SHEET    6  AL 8 CYS A 573  GLN A 577  1  O  CYS A 573   N  ILE A 550           
SHEET    7  AL 8 SER A 632  ALA A 638  1  O  SER A 632   N  VAL A 574           
SHEET    8  AL 8 LEU A 670  ASP A 675  1  O  LEU A 671   N  LEU A 635           
LINK         C1  JKT A 791                 OG  SER A 554     1555   1555  1.39  
SITE     1 AC1 14 PHE A 173  GLY A 254  TYR A 473  PHE A 476                    
SITE     2 AC1 14 SER A 554  ASN A 555  VAL A 580  TRP A 595                    
SITE     3 AC1 14 TYR A 599  ARG A 643  VAL A 644  HIS A 680                    
SITE     4 AC1 14 GOL A1714  HOH A2810                                          
SITE     1 AC2 11 ILE A 118  LEU A 119  SER A 120  ASP A 121                    
SITE     2 AC2 11 LYS A 445  ASP A 446  ASN A 522  ASN A 525                    
SITE     3 AC2 11 HOH A2234  HOH A2640  HOH A2687                               
SITE     1 AC3  5 LYS A  48  GLU A 323  TRP A 326  VAL A 328                    
SITE     2 AC3  5 HOH A2522                                                     
SITE     1 AC4  8 ALA A 226  GLU A 227  PHE A 228  TRP A 262                    
SITE     2 AC4  8 ILE A 276  LYS A 281  HOH A2811  HOH A2812                    
SITE     1 AC5  4 GLY A 553  SER A 554  HIS A 680  JKT A 791                    
SITE     1 AC6 10 PRO A 568  ASP A 569  PHE A 571  GLY A 572                    
SITE     2 AC6 10 ILE A 628  GLN A 629  PRO A 631  ASN A 668                    
SITE     3 AC6 10 HOH A2703  HOH A2779                                          
SITE     1 AC7  7 GLU A 239  ASP A 291  TYR A 292  HOH A2426                    
SITE     2 AC7  7 HOH A2492  HOH A2493  HOH A2495                               
SITE     1 AC8  5 VAL A 341  HOH A2493  HOH A2495  HOH A2814                    
SITE     2 AC8  5 HOH A2815                                                     
SITE     1 AC9  6 ASP A   8  GLN A  38  ALA A  41  PHE A  42                    
SITE     2 AC9  6 HOH A2024  HOH A2816                                          
SITE     1 BC1  7 VAL A 258  GLU A 287  ASN A 305  GLU A 512                    
SITE     2 BC1  7 LYS A 516  HOH A2506  HOH A2507                               
SITE     1 BC2  7 TYR A 190  PRO A 191  GLN A 193  THR A 204                    
SITE     2 BC2  7 ASN A 205  LEU A 206  HOH A2817                               
CRYST1   70.490   99.140  110.260  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      0.014186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010087  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009069        0.00000                         
TER    5702      PRO A 710                                                      
MASTER      478    0   11   22   46    0   25    6 6622    1  105   55          
END                                                                             

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