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LongText Report for: 4RE6-pdb

Name Class
4RE6-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           22-SEP-14   4RE6              
TITLE     ACYLAMINOACYL PEPTIDASE COMPLEXED WITH A CHLOROMETHYLKETONE INHIBITOR 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-PEPTIDASE; 
COMPND   5 EC: 3.4.19.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 272557;                                              
SOURCE   4 STRAIN: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;       
SOURCE   5 GENE: APE_1547.1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    BETA-PROPELLER, ALPHA-BETA-HYDROLASE FOLD, CHLOROMETHYL-KETONE        
KEYWDS   2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.K.MENYHARD,Z.ORGOVAN,Z.SZELTNER,I.SZAMOSI,V.HARMAT                  
REVDAT   1   28-JAN-15 4RE6    0                                                
JRNL        AUTH   D.K.MENYHARD,Z.ORGOVAN,Z.SZELTNER,I.SZAMOSI,V.HARMAT         
JRNL        TITL   CATALYTICALLY DISTINCT STATES CAPTURED IN A CRYSTAL LATTICE: 
JRNL        TITL 2 THE SUBSTRATE-BOUND AND SCAVENGER STATES OF ACYLAMINOACYL    
JRNL        TITL 3 PEPTIDASE AND THEIR IMPLICATIONS FOR FUNCTIONALITY           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71       2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        DOI    10.1107/S1399004714026819                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 64833                          
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, IMPORTED FROM           
REMARK   3                                      ISOSTRUCTURAL DATA SET OF PDB   
REMARK   3                                      ENTRY 3O4H.                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3441                            
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) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2782                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17267                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 674                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : 0.63000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.42000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.14000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.373         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.256         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.075        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.861                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17786 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 16844 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24181 ; 1.470 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 38682 ; 1.294 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2335 ; 5.844 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   725 ;32.251 ;22.510       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2787 ;15.060 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   163 ;17.548 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2704 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20342 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4003 ; 0.006 ; 0.020       
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):  9270 ; 1.881 ; 2.390       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9270 ; 1.881 ; 2.390       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11584 ; 3.012 ; 3.582       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 11609 ; 2.969 ; 3.544       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8516 ; 2.226 ; 2.563       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  8587 ; 2.184 ; 2.534       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 12674 ; 3.458 ; 3.721       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 19574 ; 5.192 ;18.969       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 19480 ; 5.151 ;18.918       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     6   579       B     6    579    31212  0.14  0.05    
REMARK   3    2      A     5   581       C     5    581    35308  0.06  0.05    
REMARK   3    3      A     5   581       D     5    581    31290  0.14  0.05    
REMARK   3    4      B     6   579       C     6    579    31308  0.14  0.05    
REMARK   3    5      B     6   579       D     6    579    33346  0.08  0.05    
REMARK   3    6      C     5   581       D     5    581    31172  0.14  0.05    
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     5        A   581                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2054 -20.2746  -1.2164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0097 T22:   0.0650                                     
REMARK   3      T33:   0.0110 T12:   0.0087                                     
REMARK   3      T13:  -0.0045 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5338 L22:   0.8416                                     
REMARK   3      L33:   0.7022 L12:   0.1838                                     
REMARK   3      L13:   0.2122 L23:   0.0664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0466 S12:  -0.0353 S13:   0.0572                       
REMARK   3      S21:  -0.0520 S22:  -0.0064 S23:   0.0429                       
REMARK   3      S31:  -0.0402 S32:  -0.0882 S33:   0.0530                       
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 :   B     6        B   580                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2702  19.2386  12.2314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.1044                                     
REMARK   3      T33:   0.0612 T12:   0.0096                                     
REMARK   3      T13:   0.0261 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3788 L22:   0.8701                                     
REMARK   3      L33:   0.6759 L12:   0.3173                                     
REMARK   3      L13:   0.3624 L23:   0.0609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0185 S12:   0.1309 S13:  -0.0227                       
REMARK   3      S21:  -0.0535 S22:   0.0627 S23:   0.0682                       
REMARK   3      S31:  -0.0003 S32:   0.1382 S33:  -0.0442                       
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 :   C     5        C   581                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9273  38.0016 -36.2516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0230 T22:   0.0457                                     
REMARK   3      T33:   0.0272 T12:  -0.0049                                     
REMARK   3      T13:   0.0041 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7452 L22:   0.9372                                     
REMARK   3      L33:   0.6743 L12:   0.1194                                     
REMARK   3      L13:   0.0801 L23:  -0.1843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0315 S12:   0.0708 S13:  -0.0353                       
REMARK   3      S21:   0.0646 S22:  -0.0323 S23:  -0.1117                       
REMARK   3      S31:  -0.0391 S32:   0.1302 S33:   0.0008                       
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 :   D     5        D   581                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5429  -0.9279 -49.0863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0612 T22:   0.0388                                     
REMARK   3      T33:   0.0253 T12:   0.0147                                     
REMARK   3      T13:   0.0324 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8248 L22:   0.8258                                     
REMARK   3      L33:   0.6143 L12:   0.3214                                     
REMARK   3      L13:   0.2936 L23:   0.1536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0256 S12:  -0.0460 S13:  -0.0218                       
REMARK   3      S21:   0.0338 S22:   0.0558 S23:  -0.0201                       
REMARK   3      S31:   0.0465 S32:  -0.0651 S33:  -0.0302                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4RE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087234.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : SAGITALLY FOCUSING GE(220) AND A   
REMARK 200                                   MULTILAYER                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY                : 2.180                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 11.40                    
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 20.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 39.030                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3O4H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 78 MM SODIUM ACETATE BUFFER, 2.2% W/V    
REMARK 280  PEG MW4000, 5.2 MM DITHIOTHREITOL, 0.34 MM EDTA. PROTEIN CRYSTALS   
REMARK 280  WERE SOAKED IN THE INHIBITOR SOLUTION., PH 5.0, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 80350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       17.33062            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -95.74414            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ARG A   582                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     ARG B   581                                                      
REMARK 465     ARG B   582                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     ILE C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     ARG C   582                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     ARG D   582                                                      
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     MET A   5    CG   SD   CE                                        
REMARK 470     LYS A 110    CD   CE   NZ                                        
REMARK 470     ARG A 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     ARG A 244    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     ARG A 327    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 479    CD   OE1  OE2                                       
REMARK 470     LYS A 513    CD   CE   NZ                                        
REMARK 470     ASP B  52    CG   OD1  OD2                                       
REMARK 470     VAL B  83    CG1  CG2                                            
REMARK 470     LYS B  85    CG   CD   CE   NZ                                   
REMARK 470     GLU B  88    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  89    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 131    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 174    CZ   NH1  NH2                                       
REMARK 470     GLU B 234    OE1  OE2                                            
REMARK 470     LYS B 294    CG   CD   CE   NZ                                   
REMARK 470     ARG B 345    CZ   NH1  NH2                                       
REMARK 470     LYS B 410    CE   NZ                                             
REMARK 470     ARG B 431    CZ   NH1  NH2                                       
REMARK 470     LEU B 480    CG   CD1  CD2                                       
REMARK 470     ASN B 487    CG   OD1  ND2                                       
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 491    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 497    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE B 499    CG1  CG2  CD1                                       
REMARK 470     ARG B 501    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 513    CD   CE   NZ                                        
REMARK 470     ARG B 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 530    CD   CE   NZ                                        
REMARK 470     ARG B 542    CZ   NH1  NH2                                       
REMARK 470     HIS B 556    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C   8    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  32    CG   OD1  OD2                                       
REMARK 470     LYS C  35    NZ                                                  
REMARK 470     GLU C  43    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  61    CZ   NH1  NH2                                       
REMARK 470     GLN C  89    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 122    CD   OE1  OE2                                       
REMARK 470     GLU C 131    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 217    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 330    CD1                                                 
REMARK 470     ARG C 501    NE   CZ   NH1  NH2                                  
REMARK 470     ILE C 558    CD1                                                 
REMARK 470     LYS D  35    CE   NZ                                             
REMARK 470     PHE D  41    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU D  55    CG   CD   OE1  OE2                                  
REMARK 470     ILE D  78    CD1                                                 
REMARK 470     VAL D  83    CG1  CG2                                            
REMARK 470     LYS D  85    CG   CD   CE   NZ                                   
REMARK 470     GLU D  88    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  89    CG   CD   OE1  NE2                                  
REMARK 470     ARG D  99    CZ   NH1  NH2                                       
REMARK 470     GLU D 102    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 110    CG   CD   CE   NZ                                   
REMARK 470     GLU D 131    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 164    CD1                                                 
REMARK 470     ARG D 174    NE   CZ   NH1  NH2                                  
REMARK 470     ASP D 191    CG   OD1  OD2                                       
REMARK 470     ARG D 216    NE   CZ   NH1  NH2                                  
REMARK 470     ARG D 431    CZ   NH1  NH2                                       
REMARK 470     ASP D 482    CG   OD1  OD2                                       
REMARK 470     ILE D 489    CD1                                                 
REMARK 470     GLN D 491    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 501    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 511    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D 513    CG   CD   CE   NZ                                   
REMARK 470     ARG D 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 530    CE   NZ                                             
REMARK 470     HIS D 556    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D 580    CD   OE1  OE2                                       
REMARK 470     ARG D 581    NE   CZ   NH1  NH2                                  
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   NH1  ARG C   174     O    HOH C   839              2.17            
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    ARG D 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    ASP A  32     -134.64     55.66                                   
REMARK 500    ARG A  61      -82.09   -103.19                                   
REMARK 500    PRO A 151       40.21    -82.51                                   
REMARK 500    THR A 214     -167.14   -106.02                                   
REMARK 500    SER A 445     -126.03     58.21                                   
REMARK 500    GLU A 580       43.13    -94.94                                   
REMARK 500    ARG B  61      -81.94   -102.57                                   
REMARK 500    THR B 130     -169.39   -124.33                                   
REMARK 500    PRO B 151       40.61    -78.59                                   
REMARK 500    THR B 214     -162.96   -108.96                                   
REMARK 500    ARG B 216      -83.74   -123.03                                   
REMARK 500    ASP B 414       49.06   -142.40                                   
REMARK 500    SER B 445     -123.53     54.90                                   
REMARK 500    ASN B 523       30.86   -143.69                                   
REMARK 500    HIS B 556       13.89    -67.96                                   
REMARK 500    ASP C  32     -132.60     54.61                                   
REMARK 500    ARG C  61      -81.05   -103.96                                   
REMARK 500    PRO C 151       39.42    -82.48                                   
REMARK 500    THR C 214     -168.37   -107.77                                   
REMARK 500    ARG C 216       24.57   -141.21                                   
REMARK 500    ASP C 227       -0.04   -145.77                                   
REMARK 500    ARG C 292       50.43     38.77                                   
REMARK 500    ASP C 414       49.09   -140.54                                   
REMARK 500    SER C 445     -126.13     57.35                                   
REMARK 500    GLU C 580       42.16    -95.65                                   
REMARK 500    ASP D  52      -67.64   -124.07                                   
REMARK 500    ARG D  61      -82.06   -102.33                                   
REMARK 500    PRO D 151       40.68    -81.52                                   
REMARK 500    THR D 214     -165.51   -108.56                                   
REMARK 500    ARG D 216      -84.89   -121.68                                   
REMARK 500    ASP D 414       48.98   -142.23                                   
REMARK 500    SER D 445     -121.97     55.32                                   
REMARK 500    ASN D 523       31.33   -143.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 708        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH D 737        DISTANCE =  5.39 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     Y3A A  601                                                       
REMARK 610     Y3A C  601                                                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR                         
REMARK 630 MOLECULE NAME: N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-    
REMARK 630 3-HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE                             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     Y3A A   601                                                      
REMARK 630     Y3A C   601                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    PHQ GLY GLY HPH 0QE                                      
REMARK 630 DETAILS: THE CHLORORMETHYL KETONE INHIBITOR LINKED TO THE PROTEIN    
REMARK 630 THROUGH TWO COVALENT BONDS WITH THE ACTIVE SITE SERINE AND           
REMARK 630 HISTIDINE                                                            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y3A A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y3A C 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RE5   RELATED DB: PDB                                   
DBREF  4RE6 A    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  4RE6 B    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  4RE6 C    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  4RE6 D    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
SEQRES   1 A  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 A  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 A  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 A  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 A  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 A  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 A  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 A  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 A  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 A  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 A  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 A  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 A  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 A  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 A  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 A  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 A  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 A  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 A  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 A  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 A  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 A  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 A  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 A  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 A  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 A  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 A  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 A  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 A  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 A  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 A  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 A  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 A  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 A  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 A  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 A  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 A  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 A  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 A  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 A  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 A  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 A  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 A  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 A  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 A  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 B  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 B  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 B  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 B  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 B  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 B  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 B  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 B  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 B  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 B  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 B  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 B  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 B  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 B  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 B  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 B  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 B  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 B  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 B  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 B  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 B  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 B  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 B  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 B  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 B  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 B  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 B  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 B  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 B  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 B  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 B  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 B  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 B  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 B  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 B  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 B  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 B  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 B  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 B  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 B  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 B  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 B  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 B  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 B  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 B  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 C  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 C  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 C  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 C  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 C  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 C  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 C  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 C  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 C  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 C  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 C  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 C  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 C  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 C  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 C  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 C  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 C  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 C  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 C  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 C  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 C  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 C  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 C  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 C  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 C  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 C  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 C  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 C  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 C  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 C  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 C  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 C  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 C  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 C  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 C  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 C  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 C  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 C  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 C  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 C  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 C  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 C  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 C  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 C  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 C  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 D  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 D  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 D  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 D  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 D  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 D  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 D  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 D  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 D  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 D  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 D  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 D  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 D  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 D  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 D  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 D  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 D  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 D  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 D  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 D  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 D  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 D  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 D  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 D  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 D  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 D  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 D  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 D  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 D  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 D  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 D  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 D  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 D  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 D  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 D  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 D  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 D  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 D  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 D  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 D  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 D  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 D  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 D  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 D  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 D  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
HET    Y3A  A 601      23                                                       
HET     CL  A 602       1                                                       
HET     CL  A 603       1                                                       
HET     CL  B 601       1                                                       
HET     CL  B 602       1                                                       
HET    Y3A  C 601      20                                                       
HET     CL  C 602       1                                                       
HET     CL  C 603       1                                                       
HETNAM     Y3A N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-3-             
HETNAM   2 Y3A  HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE                          
HETNAM      CL CHLORIDE ION                                                     
HETSYN     Y3A Z-GLY-GLY-PHE-CHLOROMETHYL KETONE (BOUND FORM)                   
FORMUL   5  Y3A    2(C22 H26 CL N3 O5)                                          
FORMUL   6   CL    6(CL 1-)                                                     
FORMUL  13  HOH   *674(H2 O)                                                    
HELIX    1   1 GLU A    8  VAL A   22  1                                  15    
HELIX    2   2 LYS A  238  ARG A  244  1                                   7    
HELIX    3   3 PRO A  323  SER A  329  1                                   7    
HELIX    4   4 ASP A  379  ALA A  388  1                                  10    
HELIX    5   5 GLY A  404  LYS A  410  1                                   7    
HELIX    6   6 GLY A  417  SER A  433  1                                  17    
HELIX    7   7 SER A  445  LYS A  458  1                                  14    
HELIX    8   8 ASP A  473  SER A  481  1                                   9    
HELIX    9   9 ASP A  482  THR A  493  1                                  12    
HELIX   10  10 SER A  496  ARG A  503  1                                   8    
HELIX   11  11 SER A  504  ILE A  512  5                                   9    
HELIX   12  12 LEU A  529  ARG A  542  1                                  14    
HELIX   13  13 THR A  560  GLU A  580  1                                  21    
HELIX   14  14 GLU B    8  VAL B   22  1                                  15    
HELIX   15  15 LYS B  238  ARG B  244  1                                   7    
HELIX   16  16 PRO B  323  SER B  329  1                                   7    
HELIX   17  17 ASP B  379  GLY B  389  1                                  11    
HELIX   18  18 GLY B  404  LYS B  410  1                                   7    
HELIX   19  19 GLY B  417  SER B  433  1                                  17    
HELIX   20  20 SER B  445  LYS B  458  1                                  14    
HELIX   21  21 ASP B  473  SER B  481  1                                   9    
HELIX   22  22 ALA B  484  THR B  493  1                                  10    
HELIX   23  23 SER B  496  ARG B  503  1                                   8    
HELIX   24  24 SER B  504  ILE B  512  5                                   9    
HELIX   25  25 LEU B  529  ARG B  542  1                                  14    
HELIX   26  26 THR B  560  LEU B  568  1                                   9    
HELIX   27  27 LEU B  568  ARG B  579  1                                  12    
HELIX   28  28 GLU C    8  VAL C   22  1                                  15    
HELIX   29  29 LYS C  238  ARG C  244  1                                   7    
HELIX   30  30 PRO C  323  SER C  329  1                                   7    
HELIX   31  31 ASP C  379  GLY C  389  1                                  11    
HELIX   32  32 GLY C  404  LYS C  410  1                                   7    
HELIX   33  33 GLY C  417  SER C  433  1                                  17    
HELIX   34  34 SER C  445  LYS C  458  1                                  14    
HELIX   35  35 ASP C  473  SER C  481  1                                   9    
HELIX   36  36 ASP C  482  THR C  493  1                                  12    
HELIX   37  37 SER C  496  ARG C  503  1                                   8    
HELIX   38  38 SER C  504  ILE C  512  5                                   9    
HELIX   39  39 LEU C  529  ARG C  542  1                                  14    
HELIX   40  40 THR C  560  GLU C  580  1                                  21    
HELIX   41  41 GLU D    8  VAL D   22  1                                  15    
HELIX   42  42 LYS D  238  ARG D  244  1                                   7    
HELIX   43  43 PRO D  323  SER D  329  1                                   7    
HELIX   44  44 ASP D  379  GLY D  389  1                                  11    
HELIX   45  45 GLY D  404  LYS D  410  1                                   7    
HELIX   46  46 GLY D  417  SER D  433  1                                  17    
HELIX   47  47 SER D  445  LYS D  458  1                                  14    
HELIX   48  48 ASP D  473  SER D  481  1                                   9    
HELIX   49  49 ASP D  482  THR D  493  1                                  12    
HELIX   50  50 SER D  496  ARG D  503  1                                   8    
HELIX   51  51 SER D  504  ILE D  512  5                                   9    
HELIX   52  52 LEU D  529  ARG D  542  1                                  14    
HELIX   53  53 THR D  560  LEU D  568  1                                   9    
HELIX   54  54 LEU D  568  ARG D  579  1                                  12    
SHEET    1   A 4 LYS A  24  VAL A  31  0                                        
SHEET    2   A 4 LYS A  35  SER A  42 -1  O  LEU A  37   N  GLY A  29           
SHEET    3   A 4 SER A  45  ASP A  52 -1  O  TYR A  49   N  VAL A  38           
SHEET    4   A 4 GLU A  55  LYS A  58 -1  O  VAL A  57   N  LEU A  50           
SHEET    1   B 4 SER A  66  VAL A  67  0                                        
SHEET    2   B 4 ARG A  76  ASP A  82 -1  O  VAL A  80   N  SER A  66           
SHEET    3   B 4 HIS A  90  ASN A  96 -1  O  PHE A  93   N  LEU A  79           
SHEET    4   B 4 GLN A 104  ARG A 105 -1  O  GLN A 104   N  LYS A  94           
SHEET    1   C 5 ASP A  69  PRO A  70  0                                        
SHEET    2   C 5 ARG A 113  ASP A 119  1  O  ASP A 119   N  ASP A  69           
SHEET    3   C 5 VAL A 124  ALA A 129 -1  O  VAL A 125   N  VAL A 118           
SHEET    4   C 5 VAL A 134  ASP A 140 -1  O  TYR A 137   N  PHE A 126           
SHEET    5   C 5 GLY A 143  LEU A 150 -1  O  LEU A 150   N  VAL A 134           
SHEET    1   D 4 GLY A 154  ARG A 160  0                                        
SHEET    2   D 4 LEU A 163  GLY A 171 -1  O  LEU A 167   N  PHE A 155           
SHEET    3   D 4 ARG A 174  ASN A 181 -1  O  PHE A 178   N  GLY A 166           
SHEET    4   D 4 GLY A 185  PHE A 190 -1  O  PHE A 190   N  LEU A 177           
SHEET    1   E 4 GLY A 195  ILE A 202  0                                        
SHEET    2   E 4 VAL A 208  THR A 214 -1  O  GLU A 213   N  SER A 196           
SHEET    3   E 4 ALA A 218  VAL A 223 -1  O  ARG A 219   N  LEU A 212           
SHEET    4   E 4 VAL A 230  ASP A 232 -1  O  GLU A 231   N  THR A 222           
SHEET    1   F 4 ALA A 247  TYR A 253  0                                        
SHEET    2   F 4 LEU A 259  ARG A 265 -1  O  ALA A 260   N  GLY A 252           
SHEET    3   F 4 ARG A 268  ILE A 273 -1  O  PHE A 272   N  VAL A 261           
SHEET    4   F 4 GLU A 276  VAL A 278 -1  O  GLU A 276   N  ILE A 273           
SHEET    1   G 4 ASN A 284  TRP A 291  0                                        
SHEET    2   G 4 LYS A 294  SER A 301 -1  O  LYS A 294   N  TRP A 291           
SHEET    3   G 4 THR A 304  LEU A 311 -1  O  ARG A 307   N  HIS A 299           
SHEET    4   G 4 PRO A 316  LEU A 318 -1  O  LEU A 317   N  ILE A 308           
SHEET    1   H16 ILE A 330  GLU A 339  0                                        
SHEET    2   H16 ARG A 345  SER A 353 -1  O  VAL A 346   N  VAL A 338           
SHEET    3   H16 HIS A 391  PRO A 395 -1  O  MET A 394   N  TYR A 349           
SHEET    4   H16 GLY A 360  VAL A 366  1  N  VAL A 363   O  HIS A 391           
SHEET    5   H16 ALA A 436  TYR A 444  1  O  TYR A 440   N  VAL A 364           
SHEET    6   H16 ALA A 464  GLY A 468  1  O  GLY A 468   N  GLY A 443           
SHEET    7   H16 LEU A 516  PRO A 521  1  O  ALA A 517   N  ALA A 467           
SHEET    8   H16 PHE A 546  ILE A 551  1  O  GLU A 547   N  LEU A 518           
SHEET    9   H16 PHE B 546  ILE B 551 -1  O  ALA B 548   N  ILE A 550           
SHEET   10   H16 LEU B 516  PRO B 521  1  N  LEU B 518   O  GLU B 547           
SHEET   11   H16 ALA B 464  GLY B 468  1  N  ALA B 467   O  ALA B 517           
SHEET   12   H16 ALA B 436  TYR B 444  1  N  GLY B 443   O  GLY B 468           
SHEET   13   H16 GLY B 360  VAL B 366  1  N  VAL B 364   O  TYR B 440           
SHEET   14   H16 HIS B 391  PRO B 395  1  O  HIS B 391   N  VAL B 363           
SHEET   15   H16 ARG B 345  SER B 353 -1  N  TYR B 349   O  MET B 394           
SHEET   16   H16 ILE B 330  GLU B 339 -1  N  VAL B 338   O  VAL B 346           
SHEET    1   I 4 LYS B  24  VAL B  31  0                                        
SHEET    2   I 4 LYS B  35  SER B  42 -1  O  LEU B  37   N  GLN B  28           
SHEET    3   I 4 SER B  45  ASP B  52 -1  O  SER B  45   N  SER B  42           
SHEET    4   I 4 GLU B  55  LYS B  58 -1  O  VAL B  57   N  LEU B  50           
SHEET    1   J 4 SER B  66  VAL B  67  0                                        
SHEET    2   J 4 ARG B  76  ASP B  82 -1  O  VAL B  80   N  SER B  66           
SHEET    3   J 4 HIS B  90  ASN B  96 -1  O  PHE B  93   N  LEU B  79           
SHEET    4   J 4 GLN B 104  ARG B 105 -1  O  GLN B 104   N  LYS B  94           
SHEET    1   K 5 ASP B  69  PRO B  70  0                                        
SHEET    2   K 5 ARG B 113  ASP B 119  1  O  ASP B 119   N  ASP B  69           
SHEET    3   K 5 VAL B 124  ALA B 129 -1  O  VAL B 125   N  VAL B 118           
SHEET    4   K 5 VAL B 134  ASP B 140 -1  O  TYR B 137   N  PHE B 126           
SHEET    5   K 5 GLY B 143  LEU B 150 -1  O  LEU B 150   N  VAL B 134           
SHEET    1   L 4 GLY B 154  ARG B 160  0                                        
SHEET    2   L 4 LEU B 163  PHE B 169 -1  O  LEU B 167   N  PHE B 155           
SHEET    3   L 4 VAL B 175  ASN B 181 -1  O  PHE B 178   N  GLY B 166           
SHEET    4   L 4 GLY B 185  PHE B 190 -1  O  PHE B 190   N  LEU B 177           
SHEET    1   M 4 SER B 196  ILE B 202  0                                        
SHEET    2   M 4 VAL B 208  GLU B 213 -1  O  GLU B 213   N  SER B 196           
SHEET    3   M 4 ARG B 219  VAL B 223 -1  O  ARG B 219   N  LEU B 212           
SHEET    4   M 4 VAL B 230  ASP B 232 -1  O  GLU B 231   N  THR B 222           
SHEET    1   N 4 ALA B 247  TYR B 253  0                                        
SHEET    2   N 4 LEU B 259  ARG B 265 -1  O  ALA B 260   N  GLY B 252           
SHEET    3   N 4 ARG B 268  ILE B 273 -1  O  PHE B 272   N  VAL B 261           
SHEET    4   N 4 GLU B 276  VAL B 278 -1  O  GLU B 276   N  ILE B 273           
SHEET    1   O 4 ASN B 284  TRP B 291  0                                        
SHEET    2   O 4 LYS B 294  SER B 301 -1  O  LYS B 294   N  TRP B 291           
SHEET    3   O 4 THR B 304  LEU B 311 -1  O  ARG B 307   N  HIS B 299           
SHEET    4   O 4 PRO B 316  LEU B 318 -1  O  LEU B 317   N  ILE B 308           
SHEET    1   P 4 LYS C  24  VAL C  31  0                                        
SHEET    2   P 4 LYS C  35  SER C  42 -1  O  LEU C  37   N  GLY C  29           
SHEET    3   P 4 SER C  45  ASP C  52 -1  O  TYR C  49   N  VAL C  38           
SHEET    4   P 4 GLU C  55  LYS C  58 -1  O  VAL C  57   N  LEU C  50           
SHEET    1   Q 4 SER C  66  VAL C  67  0                                        
SHEET    2   Q 4 ARG C  76  ASP C  82 -1  O  VAL C  80   N  SER C  66           
SHEET    3   Q 4 HIS C  90  ASN C  96 -1  O  PHE C  93   N  LEU C  79           
SHEET    4   Q 4 GLN C 104  ARG C 105 -1  O  GLN C 104   N  LYS C  94           
SHEET    1   R 5 ASP C  69  PRO C  70  0                                        
SHEET    2   R 5 ARG C 113  ASP C 119  1  O  ASP C 119   N  ASP C  69           
SHEET    3   R 5 VAL C 124  ALA C 129 -1  O  VAL C 125   N  VAL C 118           
SHEET    4   R 5 VAL C 134  ASP C 140 -1  O  TYR C 137   N  PHE C 126           
SHEET    5   R 5 GLY C 143  LEU C 150 -1  O  LEU C 150   N  VAL C 134           
SHEET    1   S 4 GLY C 154  ARG C 160  0                                        
SHEET    2   S 4 LEU C 163  GLY C 171 -1  O  LEU C 167   N  PHE C 155           
SHEET    3   S 4 ARG C 174  ASN C 181 -1  O  PHE C 178   N  GLY C 166           
SHEET    4   S 4 GLY C 185  PHE C 190 -1  O  PHE C 190   N  LEU C 177           
SHEET    1   T 4 SER C 196  ILE C 202  0                                        
SHEET    2   T 4 VAL C 208  GLU C 213 -1  O  GLU C 213   N  SER C 196           
SHEET    3   T 4 ALA C 218  VAL C 223 -1  O  ARG C 219   N  LEU C 212           
SHEET    4   T 4 VAL C 230  ASP C 232 -1  O  GLU C 231   N  THR C 222           
SHEET    1   U 4 ALA C 247  TYR C 253  0                                        
SHEET    2   U 4 LEU C 259  ARG C 265 -1  O  ALA C 260   N  GLY C 252           
SHEET    3   U 4 ARG C 268  ILE C 273 -1  O  PHE C 272   N  VAL C 261           
SHEET    4   U 4 GLU C 276  VAL C 278 -1  O  GLU C 276   N  ILE C 273           
SHEET    1   V 4 ASN C 284  TRP C 291  0                                        
SHEET    2   V 4 LYS C 294  SER C 301 -1  O  LYS C 294   N  TRP C 291           
SHEET    3   V 4 THR C 304  LEU C 311 -1  O  ARG C 307   N  HIS C 299           
SHEET    4   V 4 PRO C 316  LEU C 318 -1  O  LEU C 317   N  ILE C 308           
SHEET    1   W16 ILE C 330  GLU C 339  0                                        
SHEET    2   W16 ARG C 345  SER C 353 -1  O  VAL C 346   N  VAL C 338           
SHEET    3   W16 HIS C 391  PRO C 395 -1  O  MET C 394   N  TYR C 349           
SHEET    4   W16 GLY C 360  VAL C 366  1  N  VAL C 363   O  HIS C 391           
SHEET    5   W16 ALA C 436  TYR C 444  1  O  TYR C 440   N  VAL C 364           
SHEET    6   W16 ALA C 464  GLY C 468  1  O  GLY C 468   N  GLY C 443           
SHEET    7   W16 LEU C 516  PRO C 521  1  O  ALA C 517   N  ALA C 467           
SHEET    8   W16 PHE C 546  ILE C 551  1  O  GLU C 547   N  LEU C 518           
SHEET    9   W16 PHE D 546  ILE D 551 -1  O  ALA D 548   N  ILE C 550           
SHEET   10   W16 LEU D 516  PRO D 521  1  N  LEU D 518   O  GLU D 547           
SHEET   11   W16 ALA D 464  GLY D 468  1  N  ALA D 467   O  ALA D 517           
SHEET   12   W16 ALA D 436  TYR D 444  1  N  GLY D 443   O  GLY D 468           
SHEET   13   W16 GLY D 360  VAL D 366  1  N  VAL D 364   O  TYR D 440           
SHEET   14   W16 HIS D 391  PRO D 395  1  O  HIS D 391   N  VAL D 363           
SHEET   15   W16 ARG D 345  SER D 353 -1  N  TYR D 349   O  MET D 394           
SHEET   16   W16 ILE D 330  GLU D 339 -1  N  VAL D 338   O  VAL D 346           
SHEET    1   X 4 LYS D  24  VAL D  31  0                                        
SHEET    2   X 4 LYS D  35  SER D  42 -1  O  LEU D  37   N  GLY D  29           
SHEET    3   X 4 SER D  45  TYR D  51 -1  O  TYR D  49   N  VAL D  38           
SHEET    4   X 4 VAL D  57  LYS D  58 -1  O  VAL D  57   N  LEU D  50           
SHEET    1   Y 4 SER D  66  VAL D  67  0                                        
SHEET    2   Y 4 ARG D  76  ASP D  82 -1  O  VAL D  80   N  SER D  66           
SHEET    3   Y 4 HIS D  90  ASN D  96 -1  O  PHE D  93   N  LEU D  79           
SHEET    4   Y 4 GLN D 104  ARG D 105 -1  O  GLN D 104   N  LYS D  94           
SHEET    1   Z 5 ASP D  69  PRO D  70  0                                        
SHEET    2   Z 5 ARG D 113  ASP D 119  1  O  ASP D 119   N  ASP D  69           
SHEET    3   Z 5 VAL D 124  ALA D 129 -1  O  VAL D 125   N  VAL D 118           
SHEET    4   Z 5 VAL D 134  ASP D 140 -1  O  TYR D 137   N  PHE D 126           
SHEET    5   Z 5 GLY D 143  LEU D 150 -1  O  LEU D 150   N  VAL D 134           
SHEET    1  AA 4 GLY D 154  ARG D 160  0                                        
SHEET    2  AA 4 LEU D 163  PHE D 169 -1  O  LEU D 167   N  PHE D 155           
SHEET    3  AA 4 VAL D 175  ASN D 181 -1  O  PHE D 178   N  GLY D 166           
SHEET    4  AA 4 GLY D 185  PHE D 190 -1  O  PHE D 190   N  LEU D 177           
SHEET    1  AB 4 SER D 196  ILE D 202  0                                        
SHEET    2  AB 4 VAL D 208  GLU D 213 -1  O  GLU D 213   N  SER D 196           
SHEET    3  AB 4 ARG D 219  VAL D 223 -1  O  ARG D 219   N  LEU D 212           
SHEET    4  AB 4 VAL D 230  ASP D 232 -1  O  GLU D 231   N  THR D 222           
SHEET    1  AC 4 ALA D 247  TYR D 253  0                                        
SHEET    2  AC 4 LEU D 259  ARG D 265 -1  O  ALA D 260   N  GLY D 252           
SHEET    3  AC 4 ARG D 268  ILE D 273 -1  O  PHE D 272   N  VAL D 261           
SHEET    4  AC 4 GLU D 276  VAL D 278 -1  O  GLU D 276   N  ILE D 273           
SHEET    1  AD 4 ASN D 284  TRP D 291  0                                        
SHEET    2  AD 4 LYS D 294  SER D 301 -1  O  LYS D 294   N  TRP D 291           
SHEET    3  AD 4 THR D 304  LEU D 311 -1  O  ARG D 307   N  HIS D 299           
SHEET    4  AD 4 PRO D 316  LEU D 318 -1  O  LEU D 317   N  ILE D 308           
SSBOND   1 CYS A  416    CYS A  453                          1555   1555  2.04  
SSBOND   2 CYS B  416    CYS B  453                          1555   1555  2.02  
SSBOND   3 CYS C  416    CYS C  453                          1555   1555  2.03  
SSBOND   4 CYS D  416    CYS D  453                          1555   1555  2.04  
LINK         OG  SER A 445                 C4  Y3A A 601     1555   1555  1.40  
LINK         OG  SER C 445                 C4  Y3A C 601     1555   1555  1.41  
LINK         NE2 HIS A 556                 C15 Y3A A 601     1555   1555  1.44  
LINK         NE2 HIS C 556                 C15 Y3A C 601     1555   1555  1.44  
CISPEP   1 LEU A  311    PRO A  312          0         1.88                     
CISPEP   2 THR A  358    PRO A  359          0         0.82                     
CISPEP   3 GLY A  369    PRO A  370          0         9.06                     
CISPEP   4 LEU B  311    PRO B  312          0        11.59                     
CISPEP   5 THR B  358    PRO B  359          0        -0.31                     
CISPEP   6 GLY B  369    PRO B  370          0        10.71                     
CISPEP   7 LEU C  311    PRO C  312          0         2.08                     
CISPEP   8 THR C  358    PRO C  359          0        -2.50                     
CISPEP   9 GLY C  369    PRO C  370          0         7.79                     
CISPEP  10 LEU D  311    PRO D  312          0         8.22                     
CISPEP  11 THR D  358    PRO D  359          0        -0.05                     
CISPEP  12 GLY D  369    PRO D  370          0         7.10                     
SITE     1 AC1  8 GLY A 369  SER A 445  TYR A 446  PHE A 485                    
SITE     2 AC1  8 PHE A 488  ARG A 526  HIS A 556  HOH A 752                    
SITE     1 AC2  1 ARG A 345                                                     
SITE     1 AC3  1 ALA B 388                                                     
SITE     1 AC4  3 GLN B 282  SER B 301  THR B 304                               
SITE     1 AC5 10 PHE C 153  GLY C 368  GLY C 369  SER C 445                    
SITE     2 AC5 10 PHE C 485  PHE C 488  ARG C 526  HIS C 556                    
SITE     3 AC5 10 HOH C 711  HOH C 738                                          
CRYST1   71.580   97.300   99.160 105.15 103.96 100.26 P 1           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      0.013970  0.002529  0.004514        0.00000                         
SCALE2      0.000000  0.010445  0.003511        0.00000                         
SCALE3      0.000000  0.000000  0.010963        0.00000                         
TER    4384      ARG A 581                                                      
TER    8662      GLU B 580                                                      
TER   13039      ARG C 581                                                      
TER   17355      ARG D 581                                                      
MASTER      595    0    8   54  148    0    8    617990    4   55  180          
END                                                                             

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