GenomeNet

Database: PDB
Entry: 3SZ9
LinkDB: 3SZ9
Original site: 3SZ9 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 18-JUL-11   3SZ9              
TITLE     CRYSTAL STRUCTURE OF HUMAN ALDH2 MODIFIED WITH THE BETA-ELIMINATION   
TITLE    2 PRODUCT OF ALDI-3; 1-(4-ETHYLBENZENE)PROP-2-EN-1-ONE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL;                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: MATURE SEQUENCE, UNP RESIDUES 18-517;                      
COMPND   5 SYNONYM: ALDH CLASS 2, ALDH-E2, ALDHI;                               
COMPND   6 EC: 1.2.1.3;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALDH2, ALDM;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT-7-7                                    
KEYWDS    ALDH, ALDI-3, INHIBITOR, ROSSMANN FOLD, OXIDOREDUCTASE, COVALENT      
KEYWDS   2 ADDUCT, MITOCHONDRIA, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR        
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PEREZ-MILLER,T.D.HURLEY                                             
REVDAT   4   24-JAN-18 3SZ9    1       JRNL                                     
REVDAT   3   08-NOV-17 3SZ9    1       REMARK                                   
REVDAT   2   28-DEC-11 3SZ9    1       JRNL                                     
REVDAT   1   02-NOV-11 3SZ9    0                                                
JRNL        AUTH   M.KHANNA,C.H.CHEN,A.KIMBLE-HILL,B.PARAJULI,S.PEREZ-MILLER,   
JRNL        AUTH 2 S.BASKARAN,J.KIM,K.DRIA,V.VASILIOU,D.MOCHLY-ROSEN,T.D.HURLEY 
JRNL        TITL   DISCOVERY OF A NOVEL CLASS OF COVALENT INHIBITOR FOR         
JRNL        TITL 2 ALDEHYDE DEHYDROGENASES.                                     
JRNL        REF    J.BIOL.CHEM.                  V. 286 43486 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22021038                                                     
JRNL        DOI    10.1074/JBC.M111.293597                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.PEREZ-MILLER,H.YOUNUS,R.VANAM,C.-H.CHEN,D.MOCHLY-ROSEN,    
REMARK   1  AUTH 2 T.D.HURLEY                                                   
REMARK   1  TITL   ALDA-1 IS AN AGONIST AND CHEMICAL CHAPERONE FOR THE COMMON   
REMARK   1  TITL 2 HUMAN ALDEHYDE DEHYDROGENASE 2 VARIANT                       
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  17   159 2010              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.-H.CHEN,G.R.BUDAS,E.N.CHURCHILL,M.-H.DISATNIK,T.D.HURLEY,  
REMARK   1  AUTH 2 D.MOCHLY-ROSEN                                               
REMARK   1  TITL   ACTIVATION OF ALDEHYDE DEHYDROGENASE-2 REDUCES ISCHEMIC      
REMARK   1  TITL 2 DAMAGE TO THE HEART                                          
REMARK   1  REF    SCIENCE                       V. 321  1493 2008              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 217729                         
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5541                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15451                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 385                          
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30393                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 260                                     
REMARK   3   SOLVENT ATOMS            : 2594                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.01000                                              
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : -1.52000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.190         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.077         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31436 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 42595 ; 1.131 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3945 ; 7.188 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1426 ;36.762 ;24.727       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5102 ;14.656 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   160 ;18.825 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4673 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24164 ; 0.004 ; 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): 19683 ; 1.076 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31600 ; 1.772 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11753 ; 3.199 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10995 ; 4.820 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3SZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066837.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9869                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 217889                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.5.0109                                       
REMARK 200 STARTING MODEL: PDB ENTRY 1O05                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ACES (N-[2-ACETAMIDO]-2           
REMARK 280  -AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL,      
REMARK 280  16-17% W/V PEG 6000, 4MM DTT, PH 6.4, VAPOR DIFFUSION,              
REMARK 280  TEMPERATURE 292K                                                    
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       70.26100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.51050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.52600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.51050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.26100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.52600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 300 REMARK: THERE ARE TWO TETRAMERS IN THE ASYMMETRIC UNIT (CHAINS A, B, 
REMARK 300 C, & D AND CHAINS E, F, G & H)                                       
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: 5390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 5340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
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: 5400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     SER E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLN E     6                                                      
REMARK 465     SER F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLN F     6                                                      
REMARK 465     SER G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     ALA G     3                                                      
REMARK 465     ALA G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLN G     6                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     ALA H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLN H     6                                                      
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    ASN A  20       15.36   -150.35                                   
REMARK 500    ARG A  34       -7.73     59.05                                   
REMARK 500    THR A  44      -10.22   -140.52                                   
REMARK 500    VAL A 120      -71.84   -114.93                                   
REMARK 500    THR A 197       59.84   -145.06                                   
REMARK 500    THR A 227      -79.43   -108.53                                   
REMARK 500    SER A 260     -105.81    -98.67                                   
REMARK 500    LEU A 269     -146.72   -111.35                                   
REMARK 500    TYR A 379       45.06   -108.38                                   
REMARK 500    ASP A 388       58.05     38.96                                   
REMARK 500    LYS A 469     -125.36     50.58                                   
REMARK 500    LEU A 477      169.44     80.42                                   
REMARK 500    GLN A 497      106.65   -164.40                                   
REMARK 500    ASN B  20       19.26   -155.89                                   
REMARK 500    ASN B  26       19.14     59.13                                   
REMARK 500    VAL B 120      -72.87   -115.47                                   
REMARK 500    THR B 227      -79.09   -104.19                                   
REMARK 500    SER B 260      -96.78   -101.11                                   
REMARK 500    LEU B 269     -162.19   -117.27                                   
REMARK 500    TYR B 379       53.43    -92.49                                   
REMARK 500    LYS B 469     -135.21     63.52                                   
REMARK 500    LEU B 477      171.62     69.11                                   
REMARK 500    ASN C  20       24.60   -147.76                                   
REMARK 500    GLN C  21     -169.61   -120.98                                   
REMARK 500    VAL C 120      -71.31   -104.99                                   
REMARK 500    THR C 227      -82.07   -111.89                                   
REMARK 500    SER C 260      -98.40    -98.60                                   
REMARK 500    LEU C 269     -155.60   -109.95                                   
REMARK 500    TYR C 379       54.22   -118.25                                   
REMARK 500    LYS C 411      -62.09   -100.93                                   
REMARK 500    SER C 423      143.76   -175.35                                   
REMARK 500    LYS C 469     -140.89     62.87                                   
REMARK 500    LEU C 477      169.78     64.60                                   
REMARK 500    GLN C 497      114.04   -161.12                                   
REMARK 500    ASN D  20       18.83   -165.94                                   
REMARK 500    GLN D  21     -169.14   -118.66                                   
REMARK 500    SER D  33        0.21    -69.28                                   
REMARK 500    ARG D  34       19.36     56.13                                   
REMARK 500    THR D  44      -22.25   -142.62                                   
REMARK 500    CYS D  49     -179.44   -175.39                                   
REMARK 500    VAL D 120      -78.14   -114.88                                   
REMARK 500    THR D 197       51.16   -148.34                                   
REMARK 500    THR D 227      -69.79    -99.71                                   
REMARK 500    SER D 260     -115.61    -80.49                                   
REMARK 500    LEU D 269     -164.93   -119.74                                   
REMARK 500    SER D 337       -9.83    -59.19                                   
REMARK 500    PHE D 401       42.24     79.26                                   
REMARK 500    SER D 423      145.99   -170.93                                   
REMARK 500    LYS D 469     -133.40     61.68                                   
REMARK 500    LEU D 477      177.30     63.77                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      87 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THE STARTING MATERIAL IS 1-(4-ETHYLPHENYL)PROP-2-EN-1-ONE. IT BINDS  
REMARK 600 COVALENTLY TO CYS 302. I3E CORRESPONDS TO THE FINAL PRODUCT.         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E A 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 6911                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E B 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 6821                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6911                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6961                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E C 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E D 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E E 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 6821                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6911                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6951                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 6961                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E F 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E G 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 6801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 6811                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6911                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 6921                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3E H 8001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SZA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALDH3A1 - APO FORM                        
REMARK 900 RELATED ID: 3SZB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALDH3A1 MODIFIED WITH THE BETA-           
REMARK 900 ELIMINATION PRODUCT OF ALDI-1; 1-PHENYL-2-PROPEN-1-ONE               
DBREF  3SZ9 A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3SZ9 H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
SEQRES   1 A  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 A  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 A  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 A  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 A  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 A  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 A  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 A  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 A  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 A  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 A  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 A  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 A  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 A  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 A  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 A  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 A  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 A  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 A  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 A  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 A  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 A  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 A  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 A  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 A  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 A  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 A  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 A  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 A  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 A  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 A  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 A  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 A  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 A  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 A  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 A  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 A  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 A  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 A  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 B  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 B  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 B  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 B  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 B  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 B  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 B  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 B  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 B  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 B  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 B  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 B  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 B  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 B  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 B  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 B  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 B  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 B  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 B  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 B  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 B  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 B  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 B  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 B  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 B  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 B  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 B  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 B  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 B  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 B  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 B  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 B  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 B  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 B  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 B  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 B  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 B  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 B  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 B  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 C  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 C  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 C  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 C  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 C  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 C  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 C  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 C  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 C  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 C  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 C  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 C  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 C  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 C  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 C  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 C  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 C  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 C  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 C  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 C  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 C  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 C  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 C  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 C  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 C  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 C  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 C  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 C  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 C  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 C  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 C  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 C  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 C  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 C  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 C  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 C  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 C  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 C  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 C  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 D  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 D  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 D  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 D  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 D  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 D  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 D  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 D  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 D  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 D  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 D  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 D  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 D  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 D  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 D  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 D  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 D  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 D  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 D  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 D  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 D  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 D  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 D  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 D  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 D  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 D  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 D  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 D  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 D  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 D  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 D  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 D  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 D  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 D  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 D  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 D  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 D  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 D  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 D  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 E  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 E  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 E  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 E  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 E  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 E  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 E  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 E  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 E  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 E  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 E  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 E  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 E  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 E  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 E  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 E  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 E  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 E  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 E  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 E  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 E  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 E  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 E  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 E  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 E  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 E  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 E  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 E  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 E  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 E  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 E  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 E  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 E  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 E  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 E  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 E  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 E  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 E  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 E  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 F  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 F  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 F  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 F  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 F  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 F  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 F  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 F  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 F  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 F  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 F  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 F  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 F  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 F  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 F  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 F  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 F  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 F  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 F  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 F  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 F  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 F  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 F  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 F  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 F  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 F  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 F  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 F  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 F  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 F  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 F  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 F  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 F  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 F  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 F  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 F  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 F  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 F  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 F  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 G  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 G  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 G  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 G  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 G  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 G  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 G  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 G  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 G  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 G  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 G  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 G  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 G  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 G  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 G  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 G  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 G  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 G  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 G  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 G  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 G  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 G  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 G  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 G  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 G  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 G  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 G  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 G  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 G  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 G  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 G  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 G  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 G  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 G  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 G  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 G  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 G  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 G  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 G  500  VAL PRO GLN LYS ASN SER                                      
SEQRES   1 H  500  SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN          
SEQRES   2 H  500  GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN          
SEQRES   3 H  500  GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR          
SEQRES   4 H  500  VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA          
SEQRES   5 H  500  GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA          
SEQRES   6 H  500  ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG          
SEQRES   7 H  500  MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU          
SEQRES   8 H  500  ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA          
SEQRES   9 H  500  LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER          
SEQRES  10 H  500  TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG          
SEQRES  11 H  500  TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR          
SEQRES  12 H  500  ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS          
SEQRES  13 H  500  GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN          
SEQRES  14 H  500  PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA          
SEQRES  15 H  500  LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU          
SEQRES  16 H  500  GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE          
SEQRES  17 H  500  LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL          
SEQRES  18 H  500  PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER          
SEQRES  19 H  500  HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR          
SEQRES  20 H  500  GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER          
SEQRES  21 H  500  ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 H  500  PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA          
SEQRES  23 H  500  VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY          
SEQRES  24 H  500  GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU          
SEQRES  25 H  500  ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG          
SEQRES  26 H  500  ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS          
SEQRES  27 H  500  THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS          
SEQRES  28 H  500  LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY          
SEQRES  29 H  500  ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG          
SEQRES  30 H  500  GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN          
SEQRES  31 H  500  ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO          
SEQRES  32 H  500  VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL          
SEQRES  33 H  500  VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA          
SEQRES  34 H  500  ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU          
SEQRES  35 H  500  SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS          
SEQRES  36 H  500  TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR          
SEQRES  37 H  500  LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY          
SEQRES  38 H  500  LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS          
SEQRES  39 H  500  VAL PRO GLN LYS ASN SER                                      
HET     NA  A 601       1                                                       
HET    GAI  A6801       4                                                       
HET    GAI  A6811       4                                                       
HET    EDO  A6901       4                                                       
HET    EDO  A6921       4                                                       
HET    I3E  A8001      12                                                       
HET     NA  B 601       1                                                       
HET    GAI  B6801       4                                                       
HET    GAI  B6811       4                                                       
HET    EDO  B6911       4                                                       
HET    I3E  B8001      12                                                       
HET    EDO  C6901       4                                                       
HET     NA  C 601       1                                                       
HET    GAI  C6801       4                                                       
HET    GAI  C6811       4                                                       
HET    GAI  C6821       4                                                       
HET    EDO  C 501       4                                                       
HET    EDO  C6911       4                                                       
HET    EDO  C6921       4                                                       
HET    EDO  C6961       4                                                       
HET    I3E  C8001      12                                                       
HET    GAI  C 502       4                                                       
HET     NA  D 601       1                                                       
HET    GAI  D6801       4                                                       
HET    EDO  D6901       4                                                       
HET    I3E  D8001      12                                                       
HET     NA  E 601       1                                                       
HET    GAI  E6801       4                                                       
HET    EDO  E6901       4                                                       
HET    EDO  E6921       4                                                       
HET    I3E  E8001      12                                                       
HET    GAI  E6811       4                                                       
HET    GAI  F6811       4                                                       
HET     NA  F 601       1                                                       
HET    GAI  F6801       4                                                       
HET    GAI  F6821       4                                                       
HET    EDO  F6901       4                                                       
HET    EDO  F6911       4                                                       
HET    EDO  F6921       4                                                       
HET    EDO  F6951       4                                                       
HET    EDO  F6961       4                                                       
HET    I3E  F8001      12                                                       
HET    EDO  F 501       4                                                       
HET     NA  G 601       1                                                       
HET    GAI  G6801       4                                                       
HET    GAI  G6811       4                                                       
HET    EDO  G6921       4                                                       
HET    I3E  G8001      12                                                       
HET     NA  H 601       1                                                       
HET    GAI  H6801       4                                                       
HET    GAI  H6811       4                                                       
HET    EDO  H6901       4                                                       
HET    EDO  H6911       4                                                       
HET    EDO  H6921       4                                                       
HET    I3E  H8001      12                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     GAI GUANIDINE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     I3E 1-(4-ETHYLPHENYL)PROPAN-1-ONE                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     I3E 1-(4-ETHYLPHENYL)PROP-2-EN-1-ONE, BOUND FORM                     
FORMUL   9   NA    8(NA 1+)                                                     
FORMUL  10  GAI    18(C H5 N3)                                                  
FORMUL  12  EDO    21(C2 H6 O2)                                                 
FORMUL  14  I3E    8(C11 H14 O)                                                 
FORMUL  64  HOH   *2594(H2 O)                                                   
HELIX    1   1 ASP A   55  PHE A   70  1                                  16    
HELIX    2   2 SER A   74  MET A   79  1                                   6    
HELIX    3   3 ASP A   80  ASP A   98  1                                  19    
HELIX    4   4 ASP A   98  GLY A  111  1                                  14    
HELIX    5   5 PRO A  113  VAL A  120  1                                   8    
HELIX    6   6 VAL A  120  ALA A  136  1                                  17    
HELIX    7   7 PHE A  170  THR A  185  1                                  16    
HELIX    8   8 PRO A  198  GLY A  212  1                                  15    
HELIX    9   9 THR A  227  HIS A  235  1                                   9    
HELIX   10  10 SER A  246  SER A  260  1                                  15    
HELIX   11  11 ASP A  282  PHE A  296  1                                  15    
HELIX   12  12 ASN A  297  GLN A  300  5                                   4    
HELIX   13  13 GLU A  312  SER A  328  1                                  17    
HELIX   14  14 ASP A  346  GLN A  362  1                                  17    
HELIX   15  15 MET A  393  LYS A  397  5                                   5    
HELIX   16  16 THR A  412  ASN A  422  1                                  11    
HELIX   17  17 ASP A  435  LEU A  446  1                                  12    
HELIX   18  18 TYR A  468  MET A  470  5                                   3    
HELIX   19  19 GLY A  478  ALA A  484  5                                   7    
HELIX   20  20 ASP B   55  PHE B   70  1                                  16    
HELIX   21  21 SER B   74  MET B   79  1                                   6    
HELIX   22  22 ASP B   80  ASP B   98  1                                  19    
HELIX   23  23 ASP B   98  GLY B  111  1                                  14    
HELIX   24  24 PRO B  113  VAL B  120  1                                   8    
HELIX   25  25 VAL B  120  ALA B  136  1                                  17    
HELIX   26  26 PHE B  170  THR B  185  1                                  16    
HELIX   27  27 PRO B  198  GLY B  212  1                                  15    
HELIX   28  28 THR B  227  HIS B  235  1                                   9    
HELIX   29  29 SER B  246  SER B  260  1                                  15    
HELIX   30  30 ASP B  282  PHE B  296  1                                  15    
HELIX   31  31 ASN B  297  GLN B  300  5                                   4    
HELIX   32  32 GLU B  312  SER B  328  1                                  17    
HELIX   33  33 ASP B  346  GLU B  363  1                                  18    
HELIX   34  34 MET B  393  GLU B  398  1                                   6    
HELIX   35  35 THR B  412  ASN B  422  1                                  11    
HELIX   36  36 ASP B  435  LEU B  446  1                                  12    
HELIX   37  37 TYR B  468  MET B  470  5                                   3    
HELIX   38  38 GLY B  478  ALA B  484  5                                   7    
HELIX   39  39 ASP C   55  PHE C   70  1                                  16    
HELIX   40  40 SER C   74  MET C   79  1                                   6    
HELIX   41  41 ASP C   80  ASP C   98  1                                  19    
HELIX   42  42 ASP C   98  GLY C  111  1                                  14    
HELIX   43  43 PRO C  113  VAL C  120  1                                   8    
HELIX   44  44 VAL C  120  ALA C  136  1                                  17    
HELIX   45  45 PHE C  170  THR C  185  1                                  16    
HELIX   46  46 PRO C  198  GLY C  212  1                                  15    
HELIX   47  47 THR C  227  HIS C  235  1                                   9    
HELIX   48  48 SER C  246  SER C  260  1                                  15    
HELIX   49  49 ASP C  282  PHE C  296  1                                  15    
HELIX   50  50 ASN C  297  GLN C  300  5                                   4    
HELIX   51  51 ILE C  314  ARG C  329  1                                  16    
HELIX   52  52 ASP C  346  GLY C  364  1                                  19    
HELIX   53  53 MET C  393  GLU C  398  1                                   6    
HELIX   54  54 THR C  412  ASN C  422  1                                  11    
HELIX   55  55 ASP C  435  LEU C  446  1                                  12    
HELIX   56  56 GLY C  478  ALA C  484  5                                   7    
HELIX   57  57 ASP D   55  PHE D   70  1                                  16    
HELIX   58  58 SER D   74  MET D   79  1                                   6    
HELIX   59  59 ASP D   80  ASP D   98  1                                  19    
HELIX   60  60 ASP D   98  GLY D  111  1                                  14    
HELIX   61  61 PRO D  113  VAL D  120  1                                   8    
HELIX   62  62 VAL D  120  GLY D  134  1                                  15    
HELIX   63  63 PHE D  170  THR D  185  1                                  16    
HELIX   64  64 PRO D  198  GLY D  212  1                                  15    
HELIX   65  65 THR D  227  HIS D  235  1                                   9    
HELIX   66  66 GLU D  248  SER D  260  1                                  13    
HELIX   67  67 ASP D  282  PHE D  296  1                                  15    
HELIX   68  68 ASN D  297  GLN D  300  5                                   4    
HELIX   69  69 GLU D  312  ARG D  329  1                                  18    
HELIX   70  70 ASP D  346  GLY D  364  1                                  19    
HELIX   71  71 MET D  393  LYS D  397  5                                   5    
HELIX   72  72 THR D  412  ASN D  422  1                                  11    
HELIX   73  73 ASP D  435  LEU D  446  1                                  12    
HELIX   74  74 TYR D  468  MET D  470  5                                   3    
HELIX   75  75 GLY D  478  ALA D  484  5                                   7    
HELIX   76  76 ASP E   55  PHE E   70  1                                  16    
HELIX   77  77 SER E   74  MET E   79  1                                   6    
HELIX   78  78 ASP E   80  ASP E   98  1                                  19    
HELIX   79  79 ASP E   98  GLY E  111  1                                  14    
HELIX   80  80 PRO E  113  VAL E  120  1                                   8    
HELIX   81  81 VAL E  120  GLY E  134  1                                  15    
HELIX   82  82 PHE E  170  THR E  185  1                                  16    
HELIX   83  83 PRO E  198  GLY E  212  1                                  15    
HELIX   84  84 THR E  227  HIS E  235  1                                   9    
HELIX   85  85 SER E  246  SER E  260  1                                  15    
HELIX   86  86 ASP E  282  PHE E  296  1                                  15    
HELIX   87  87 ASN E  297  GLN E  300  5                                   4    
HELIX   88  88 GLU E  312  ARG E  329  1                                  18    
HELIX   89  89 ASP E  346  GLU E  363  1                                  18    
HELIX   90  90 MET E  393  LYS E  397  5                                   5    
HELIX   91  91 THR E  412  ASN E  422  1                                  11    
HELIX   92  92 ASP E  435  LEU E  446  1                                  12    
HELIX   93  93 TYR E  468  MET E  470  5                                   3    
HELIX   94  94 GLY E  478  ALA E  484  5                                   7    
HELIX   95  95 ASP F   55  PHE F   70  1                                  16    
HELIX   96  96 SER F   74  MET F   79  1                                   6    
HELIX   97  97 ASP F   80  ASP F   98  1                                  19    
HELIX   98  98 ASP F   98  GLY F  111  1                                  14    
HELIX   99  99 PRO F  113  VAL F  120  1                                   8    
HELIX  100 100 VAL F  120  ALA F  136  1                                  17    
HELIX  101 101 PHE F  170  THR F  185  1                                  16    
HELIX  102 102 PRO F  198  GLY F  212  1                                  15    
HELIX  103 103 THR F  227  HIS F  235  1                                   9    
HELIX  104 104 SER F  246  SER F  260  1                                  15    
HELIX  105 105 ASP F  282  PHE F  296  1                                  15    
HELIX  106 106 ASN F  297  GLN F  300  5                                   4    
HELIX  107 107 GLU F  312  ARG F  329  1                                  18    
HELIX  108 108 ASP F  346  GLY F  364  1                                  19    
HELIX  109 109 MET F  393  GLU F  398  1                                   6    
HELIX  110 110 THR F  412  ASN F  422  1                                  11    
HELIX  111 111 ASP F  435  LEU F  446  1                                  12    
HELIX  112 112 TYR F  468  MET F  470  5                                   3    
HELIX  113 113 GLY F  478  ALA F  484  5                                   7    
HELIX  114 114 ASP G   55  PHE G   70  1                                  16    
HELIX  115 115 SER G   74  MET G   79  1                                   6    
HELIX  116 116 ASP G   80  ASP G   98  1                                  19    
HELIX  117 117 ASP G   98  GLY G  111  1                                  14    
HELIX  118 118 PRO G  113  VAL G  120  1                                   8    
HELIX  119 119 VAL G  120  ALA G  136  1                                  17    
HELIX  120 120 PHE G  170  THR G  185  1                                  16    
HELIX  121 121 PRO G  198  GLY G  212  1                                  15    
HELIX  122 122 THR G  227  HIS G  235  1                                   9    
HELIX  123 123 SER G  246  SER G  260  1                                  15    
HELIX  124 124 ASP G  282  PHE G  296  1                                  15    
HELIX  125 125 ASN G  297  GLN G  300  5                                   4    
HELIX  126 126 GLU G  312  ARG G  329  1                                  18    
HELIX  127 127 ASP G  346  GLU G  363  1                                  18    
HELIX  128 128 MET G  393  GLU G  398  1                                   6    
HELIX  129 129 THR G  412  ASN G  422  1                                  11    
HELIX  130 130 ASP G  435  LEU G  446  1                                  12    
HELIX  131 131 TYR G  468  MET G  470  5                                   3    
HELIX  132 132 GLY G  478  ALA G  484  5                                   7    
HELIX  133 133 ASP H   55  PHE H   70  1                                  16    
HELIX  134 134 SER H   74  MET H   79  1                                   6    
HELIX  135 135 ASP H   80  ASP H   98  1                                  19    
HELIX  136 136 ASP H   98  GLY H  111  1                                  14    
HELIX  137 137 PRO H  113  VAL H  120  1                                   8    
HELIX  138 138 VAL H  120  ALA H  136  1                                  17    
HELIX  139 139 PHE H  170  THR H  185  1                                  16    
HELIX  140 140 PRO H  198  GLY H  212  1                                  15    
HELIX  141 141 THR H  227  HIS H  235  1                                   9    
HELIX  142 142 SER H  246  SER H  260  1                                  15    
HELIX  143 143 ASP H  282  PHE H  296  1                                  15    
HELIX  144 144 ASN H  297  GLN H  300  5                                   4    
HELIX  145 145 GLU H  312  SER H  328  1                                  17    
HELIX  146 146 ASP H  346  GLU H  363  1                                  18    
HELIX  147 147 MET H  393  GLU H  398  1                                   6    
HELIX  148 148 THR H  412  ASN H  422  1                                  11    
HELIX  149 149 ASP H  435  LEU H  446  1                                  12    
HELIX  150 150 GLY H  478  ALA H  484  5                                   7    
SHEET    1   A 2 ILE A  22  ILE A  24  0                                        
SHEET    2   A 2 GLU A  27  HIS A  29 -1  O  HIS A  29   N  ILE A  22           
SHEET    1   B 2 THR A  36  VAL A  40  0                                        
SHEET    2   B 2 VAL A  47  ALA A  52 -1  O  ILE A  48   N  THR A  39           
SHEET    1   C20 LYS B 366  CYS B 369  0                                        
SHEET    2   C20 THR B 384  GLY B 387 -1  O  VAL B 385   N  LEU B 368           
SHEET    3   C20 VAL B 404  PHE B 410  1  O  MET B 405   N  PHE B 386           
SHEET    4   C20 ARG B 307  GLN B 311  1  N  VAL B 310   O  LEU B 408           
SHEET    5   C20 PRO B 274  ILE B 277  1  N  ILE B 277   O  PHE B 309           
SHEET    6   C20 ALA B 428  PHE B 432  1  O  ALA B 430   N  ILE B 276           
SHEET    7   C20 THR B 450  VAL B 453  1  O  TRP B 452   N  ALA B 429           
SHEET    8   C20 THR A 486  LYS A 494  1  N  THR A 490   O  VAL B 451           
SHEET    9   C20 PHE A 150  PRO A 158 -1  N  TYR A 153   O  VAL A 491           
SHEET   10   C20 GLY A 141  ILE A 144 -1  N  ILE A 144   O  SER A 152           
SHEET   11   C20 GLY D 141  ILE D 144 -1  O  GLY D 141   N  THR A 143           
SHEET   12   C20 PHE D 150  PRO D 158 -1  O  SER D 152   N  ILE D 144           
SHEET   13   C20 THR D 486  LYS D 494 -1  O  GLU D 487   N  GLU D 157           
SHEET   14   C20 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490           
SHEET   15   C20 ALA C 428  PHE C 432  1  N  ALA C 429   O  TRP C 452           
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  PHE C 432           
SHEET   17   C20 ARG C 307  GLN C 311  1  O  PHE C 309   N  ILE C 277           
SHEET   18   C20 VAL C 404  PHE C 410  1  O  LEU C 408   N  VAL C 310           
SHEET   19   C20 THR C 384  GLY C 387  1  N  PHE C 386   O  MET C 405           
SHEET   20   C20 LYS C 366  CYS C 369 -1  N  LYS C 366   O  GLY C 387           
SHEET    1   D 6 VAL A 218  ILE A 220  0                                        
SHEET    2   D 6 VAL A 188  LYS A 192  1  N  MET A 191   O  ASN A 219           
SHEET    3   D 6 VAL A 161  ILE A 165  1  N  GLN A 164   O  LYS A 192           
SHEET    4   D 6 LYS A 240  THR A 244  1  O  LYS A 240   N  GLY A 163           
SHEET    5   D 6 ARG A 264  GLU A 268  1  O  GLU A 268   N  PHE A 243           
SHEET    6   D 6 GLY A 472  SER A 473 -1  O  SER A 473   N  LEU A 267           
SHEET    1   E20 LYS A 366  CYS A 369  0                                        
SHEET    2   E20 THR A 384  VAL A 389 -1  O  GLY A 387   N  LYS A 366           
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  THR A 384           
SHEET    4   E20 ARG A 307  GLN A 311  1  N  THR A 308   O  LEU A 408           
SHEET    5   E20 PRO A 274  ILE A 277  1  N  ILE A 277   O  PHE A 309           
SHEET    6   E20 ALA A 428  PHE A 432  1  O  ALA A 430   N  ILE A 276           
SHEET    7   E20 THR A 450  VAL A 453  1  O  TRP A 452   N  ALA A 429           
SHEET    8   E20 THR B 486  LYS B 494  1  O  THR B 490   N  VAL A 451           
SHEET    9   E20 PHE B 150  PRO B 158 -1  N  GLU B 157   O  GLU B 487           
SHEET   10   E20 GLY B 141  ILE B 144 -1  N  ILE B 144   O  SER B 152           
SHEET   11   E20 GLY C 141  ILE C 144 -1  O  THR C 143   N  GLY B 141           
SHEET   12   E20 PHE C 150  PRO C 158 -1  O  SER C 152   N  ILE C 144           
SHEET   13   E20 THR C 486  LYS C 494 -1  O  GLU C 487   N  GLU C 157           
SHEET   14   E20 THR D 450  VAL D 453  1  O  VAL D 451   N  THR C 490           
SHEET   15   E20 ALA D 428  PHE D 432  1  N  ALA D 429   O  TRP D 452           
SHEET   16   E20 PRO D 274  ILE D 277  1  N  ILE D 276   O  PHE D 432           
SHEET   17   E20 ARG D 307  GLN D 311  1  O  PHE D 309   N  ILE D 277           
SHEET   18   E20 VAL D 404  PHE D 410  1  O  GLN D 406   N  THR D 308           
SHEET   19   E20 THR D 384  GLY D 387  1  N  THR D 384   O  MET D 405           
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LYS D 366   O  GLY D 387           
SHEET    1   F 2 ILE B  22  ILE B  24  0                                        
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  GLU B  27   N  ILE B  24           
SHEET    1   G 2 THR B  36  VAL B  40  0                                        
SHEET    2   G 2 VAL B  47  ALA B  52 -1  O  ILE B  48   N  THR B  39           
SHEET    1   H 6 VAL B 218  ILE B 220  0                                        
SHEET    2   H 6 VAL B 188  LYS B 192  1  N  MET B 191   O  ASN B 219           
SHEET    3   H 6 VAL B 161  ILE B 165  1  N  GLN B 164   O  LYS B 192           
SHEET    4   H 6 LYS B 240  THR B 244  1  O  LYS B 240   N  GLY B 163           
SHEET    5   H 6 ARG B 264  GLU B 268  1  O  ARG B 264   N  VAL B 241           
SHEET    6   H 6 GLY B 472  SER B 473 -1  O  SER B 473   N  LEU B 267           
SHEET    1   I 2 ILE C  22  ILE C  24  0                                        
SHEET    2   I 2 GLU C  27  HIS C  29 -1  O  HIS C  29   N  ILE C  22           
SHEET    1   J 2 THR C  36  VAL C  40  0                                        
SHEET    2   J 2 VAL C  47  ALA C  52 -1  O  ILE C  48   N  THR C  39           
SHEET    1   K 6 VAL C 218  ILE C 220  0                                        
SHEET    2   K 6 VAL C 188  LYS C 192  1  N  MET C 191   O  ASN C 219           
SHEET    3   K 6 VAL C 161  ILE C 165  1  N  CYS C 162   O  VAL C 188           
SHEET    4   K 6 LYS C 240  THR C 244  1  O  LYS C 240   N  GLY C 163           
SHEET    5   K 6 ARG C 264  GLU C 268  1  O  ARG C 264   N  VAL C 241           
SHEET    6   K 6 GLY C 472  SER C 473 -1  O  SER C 473   N  LEU C 267           
SHEET    1   L 2 TYR C 425  GLY C 426  0                                        
SHEET    2   L 2 TYR C 468  LYS C 469 -1  O  TYR C 468   N  GLY C 426           
SHEET    1   M 2 ILE D  22  ILE D  24  0                                        
SHEET    2   M 2 GLU D  27  HIS D  29 -1  O  GLU D  27   N  ILE D  24           
SHEET    1   N 2 THR D  36  VAL D  40  0                                        
SHEET    2   N 2 VAL D  47  ALA D  52 -1  O  ILE D  48   N  THR D  39           
SHEET    1   O 6 VAL D 218  ILE D 220  0                                        
SHEET    2   O 6 VAL D 188  LYS D 192  1  N  MET D 191   O  ASN D 219           
SHEET    3   O 6 VAL D 161  ILE D 165  1  N  CYS D 162   O  VAL D 188           
SHEET    4   O 6 LYS D 240  THR D 244  1  O  LYS D 240   N  GLY D 163           
SHEET    5   O 6 ARG D 264  GLU D 268  1  O  GLU D 268   N  PHE D 243           
SHEET    6   O 6 GLY D 472  SER D 473 -1  O  SER D 473   N  LEU D 267           
SHEET    1   P 2 ILE E  22  ILE E  24  0                                        
SHEET    2   P 2 GLU E  27  HIS E  29 -1  O  HIS E  29   N  ILE E  22           
SHEET    1   Q 2 THR E  36  VAL E  40  0                                        
SHEET    2   Q 2 VAL E  47  ALA E  52 -1  O  ILE E  48   N  THR E  39           
SHEET    1   R20 LYS F 366  CYS F 369  0                                        
SHEET    2   R20 THR F 384  GLY F 387 -1  O  VAL F 385   N  LEU F 368           
SHEET    3   R20 VAL F 404  PHE F 410  1  O  MET F 405   N  THR F 384           
SHEET    4   R20 ARG F 307  GLN F 311  1  N  VAL F 310   O  LEU F 408           
SHEET    5   R20 PRO F 274  ILE F 277  1  N  ILE F 277   O  PHE F 309           
SHEET    6   R20 ALA F 428  PHE F 432  1  O  ALA F 430   N  ILE F 276           
SHEET    7   R20 THR F 450  VAL F 453  1  O  TRP F 452   N  ALA F 429           
SHEET    8   R20 THR E 486  LYS E 494  1  N  THR E 490   O  VAL F 451           
SHEET    9   R20 PHE E 150  PRO E 158 -1  N  GLU E 157   O  GLU E 487           
SHEET   10   R20 GLY E 141  ILE E 144 -1  N  ILE E 144   O  SER E 152           
SHEET   11   R20 GLY H 141  ILE H 144 -1  O  GLY H 141   N  THR E 143           
SHEET   12   R20 PHE H 150  PRO H 158 -1  O  SER H 152   N  ILE H 144           
SHEET   13   R20 THR H 486  LYS H 494 -1  O  VAL H 493   N  PHE H 151           
SHEET   14   R20 THR G 450  VAL G 453  1  N  VAL G 451   O  THR H 490           
SHEET   15   R20 ALA G 428  PHE G 432  1  N  VAL G 431   O  TRP G 452           
SHEET   16   R20 PRO G 274  ILE G 277  1  N  ILE G 276   O  PHE G 432           
SHEET   17   R20 ARG G 307  GLN G 311  1  O  PHE G 309   N  ILE G 277           
SHEET   18   R20 VAL G 404  PHE G 410  1  O  LEU G 408   N  VAL G 310           
SHEET   19   R20 THR G 384  GLY G 387  1  N  PHE G 386   O  MET G 405           
SHEET   20   R20 LYS G 366  CYS G 369 -1  N  LEU G 368   O  VAL G 385           
SHEET    1   S 6 VAL E 218  VAL E 221  0                                        
SHEET    2   S 6 VAL E 188  LYS E 192  1  N  MET E 191   O  ASN E 219           
SHEET    3   S 6 VAL E 161  ILE E 165  1  N  CYS E 162   O  VAL E 188           
SHEET    4   S 6 LYS E 240  THR E 244  1  O  LYS E 240   N  GLY E 163           
SHEET    5   S 6 ARG E 264  GLU E 268  1  O  GLU E 268   N  PHE E 243           
SHEET    6   S 6 GLY E 472  SER E 473 -1  O  SER E 473   N  LEU E 267           
SHEET    1   T20 LYS E 366  CYS E 369  0                                        
SHEET    2   T20 THR E 384  GLY E 387 -1  O  GLY E 387   N  LYS E 366           
SHEET    3   T20 VAL E 404  PHE E 410  1  O  MET E 405   N  PHE E 386           
SHEET    4   T20 ARG E 307  GLN E 311  1  N  THR E 308   O  LEU E 408           
SHEET    5   T20 PRO E 274  ILE E 277  1  N  ASN E 275   O  ARG E 307           
SHEET    6   T20 ALA E 428  PHE E 432  1  O  ALA E 430   N  ILE E 276           
SHEET    7   T20 THR E 450  VAL E 453  1  O  TRP E 452   N  ALA E 429           
SHEET    8   T20 THR F 486  LYS F 494  1  O  THR F 490   N  VAL E 451           
SHEET    9   T20 PHE F 150  PRO F 158 -1  N  PHE F 151   O  VAL F 493           
SHEET   10   T20 GLY F 141  ILE F 144 -1  N  ILE F 144   O  SER F 152           
SHEET   11   T20 GLY G 141  ILE G 144 -1  O  THR G 143   N  GLY F 141           
SHEET   12   T20 PHE G 150  PRO G 158 -1  O  SER G 152   N  ILE G 144           
SHEET   13   T20 THR G 486  LYS G 494 -1  O  VAL G 491   N  TYR G 153           
SHEET   14   T20 THR H 450  VAL H 453  1  O  VAL H 451   N  THR G 490           
SHEET   15   T20 ALA H 428  PHE H 432  1  N  ALA H 429   O  TRP H 452           
SHEET   16   T20 PRO H 274  ILE H 277  1  N  ILE H 276   O  ALA H 430           
SHEET   17   T20 ARG H 307  GLN H 311  1  O  PHE H 309   N  ILE H 277           
SHEET   18   T20 VAL H 404  PHE H 410  1  O  LEU H 408   N  THR H 308           
SHEET   19   T20 THR H 384  GLY H 387  1  N  PHE H 386   O  MET H 405           
SHEET   20   T20 LYS H 366  CYS H 369 -1  N  LEU H 368   O  VAL H 385           
SHEET    1   U 2 ILE F  22  ILE F  24  0                                        
SHEET    2   U 2 GLU F  27  HIS F  29 -1  O  HIS F  29   N  ILE F  22           
SHEET    1   V 2 THR F  36  VAL F  40  0                                        
SHEET    2   V 2 VAL F  47  ALA F  52 -1  O  ILE F  48   N  THR F  39           
SHEET    1   W 6 VAL F 218  ILE F 220  0                                        
SHEET    2   W 6 VAL F 188  LYS F 192  1  N  MET F 191   O  ASN F 219           
SHEET    3   W 6 VAL F 161  ILE F 165  1  N  GLN F 164   O  LYS F 192           
SHEET    4   W 6 LYS F 240  THR F 244  1  O  LYS F 240   N  GLY F 163           
SHEET    5   W 6 ARG F 264  GLU F 268  1  O  ARG F 264   N  VAL F 241           
SHEET    6   W 6 GLY F 472  SER F 473 -1  O  SER F 473   N  LEU F 267           
SHEET    1   X 2 ILE G  22  ILE G  24  0                                        
SHEET    2   X 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22           
SHEET    1   Y 2 THR G  36  VAL G  40  0                                        
SHEET    2   Y 2 VAL G  47  ALA G  52 -1  O  ILE G  48   N  THR G  39           
SHEET    1   Z 6 VAL G 218  ILE G 220  0                                        
SHEET    2   Z 6 VAL G 188  LYS G 192  1  N  MET G 191   O  ASN G 219           
SHEET    3   Z 6 VAL G 161  ILE G 165  1  N  GLN G 164   O  LYS G 192           
SHEET    4   Z 6 LYS G 240  THR G 244  1  O  LYS G 240   N  GLY G 163           
SHEET    5   Z 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241           
SHEET    6   Z 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267           
SHEET    1  AA 2 ILE H  22  ILE H  24  0                                        
SHEET    2  AA 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22           
SHEET    1  AB 2 THR H  36  VAL H  40  0                                        
SHEET    2  AB 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39           
SHEET    1  AC 6 VAL H 218  ILE H 220  0                                        
SHEET    2  AC 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219           
SHEET    3  AC 6 VAL H 161  ILE H 165  1  N  CYS H 162   O  VAL H 188           
SHEET    4  AC 6 LYS H 240  THR H 244  1  O  LYS H 240   N  GLY H 163           
SHEET    5  AC 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241           
SHEET    6  AC 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267           
SHEET    1  AD 2 TYR H 425  GLY H 426  0                                        
SHEET    2  AD 2 TYR H 468  LYS H 469 -1  O  TYR H 468   N  GLY H 426           
LINK         SG ACYS A 302                 C11 I3E A8001     1555   1555  1.82  
LINK         SG ACYS B 302                 C11 I3E B8001     1555   1555  1.82  
LINK         SG ACYS C 302                 C11 I3E C8001     1555   1555  1.83  
LINK         SG ACYS D 302                 C11 I3E D8001     1555   1555  1.83  
LINK         SG ACYS E 302                 C11 I3E E8001     1555   1555  1.83  
LINK         SG ACYS F 302                 C11 I3E F8001     1555   1555  1.82  
LINK         SG ACYS G 302                 C11 I3E G8001     1555   1555  1.84  
LINK         SG ACYS H 302                 C11 I3E H8001     1555   1555  1.83  
SITE     1 AC1  4 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     1 AC2  6 PHE A  70  GLU A 157  PRO A 158  VAL A 159                    
SITE     2 AC2  6 HOH A1261  TYR B 468                                          
SITE     1 AC3  5 ILE A 146  ASP A 147  PHE A 150  PHE B 459                    
SITE     2 AC3  5 HOH B 659                                                     
SITE     1 AC4  4 TYR A 153  ARG A 155  SER B 443  PHE D 151                    
SITE     1 AC5  4 PHE A  18  TYR A 101  TYR A 203  HOH A1298                    
SITE     1 AC6  8 PHE A 170  LEU A 173  GLU A 268  PHE A 296                    
SITE     2 AC6  8 CYS A 301  CYS A 302  ASP A 457  PHE A 459                    
SITE     1 AC7  5 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC7  5 HOH B2061                                                     
SITE     1 AC8  4 TYR A 468  GLU B 157  PRO B 158  VAL B 159                    
SITE     1 AC9  4 PHE A 459  ILE B 146  ASP B 147  PHE B 150                    
SITE     1 BC1  3 ASN B  41  THR B  44  LEU B 108                               
SITE     1 BC2  8 PHE B 170  GLU B 268  PHE B 296  CYS B 301                    
SITE     2 BC2  8 CYS B 302  CYS B 303  ASP B 457  PHE B 459                    
SITE     1 BC3  4 SER A 443  TYR B 153  ARG B 155  PHE C 151                    
SITE     1 BC4  6 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 BC4  6 HOH C 783  HOH C1793                                          
SITE     1 BC5  4 GLU C 157  PRO C 158  VAL C 159  TYR D 468                    
SITE     1 BC6  5 ILE C 146  ASP C 147  PHE C 150  HOH C1214                    
SITE     2 BC6  5 PHE D 459                                                     
SITE     1 BC7  5 PHE C 350  ALA C 375  ASP C 376  GLY C 378                    
SITE     2 BC7  5 EDO C6961                                                     
SITE     1 BC8  5 PHE B 151  TYR C 153  ARG C 155  ASN D 440                    
SITE     2 BC8  5 SER D 443                                                     
SITE     1 BC9  5 ASN C  41  THR C  44  GLU C  46  LEU C 108                    
SITE     2 BC9  5 HOH C1539                                                     
SITE     1 CC1  3 PHE C  18  TYR C 203  HOH C 589                               
SITE     1 CC2  3 GLU C 347  GAI C6821  GLY F  45                               
SITE     1 CC3  7 PHE C 170  GLU C 268  PHE C 296  CYS C 301                    
SITE     2 CC3  7 CYS C 302  CYS C 303  PHE C 459                               
SITE     1 CC4  6 PHE C 459  HOH C1458  HOH C2049  ILE D 146                    
SITE     2 CC4  6 ASP D 147  PHE D 150                                          
SITE     1 CC5  4 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     1 CC6  4 TYR C 468  GLU D 157  PRO D 158  VAL D 159                    
SITE     1 CC7  4 PHE A 151  SER C 443  TYR D 153  ARG D 155                    
SITE     1 CC8  8 ASN D 169  PHE D 170  GLU D 268  PHE D 296                    
SITE     2 CC8  8 CYS D 301  CYS D 302  PHE D 459  PHE D 465                    
SITE     1 CC9  5 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     2 CC9  5 HOH E2549                                                     
SITE     1 DC1  6 PHE E  70  GLU E 157  PRO E 158  VAL E 159                    
SITE     2 DC1  6 HOH E1588  TYR F 468                                          
SITE     1 DC2  4 TYR E 153  ARG E 155  SER F 443  PHE H 151                    
SITE     1 DC3  4 PHE E  18  TYR E 101  TYR E 203  HOH E2283                    
SITE     1 DC4  6 PHE E 170  GLU E 268  PHE E 296  CYS E 301                    
SITE     2 DC4  6 CYS E 302  PHE E 459                                          
SITE     1 DC5  4 PHE E 459  ILE F 146  ASP F 147  PHE F 150                    
SITE     1 DC6  4 ASP E 147  PHE E 150  PHE F 459  HOH F1930                    
SITE     1 DC7  5 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     2 DC7  5 HOH F 591                                                     
SITE     1 DC8  7 TYR E 468  GLU F 157  PRO F 158  VAL F 159                    
SITE     2 DC8  7 HOH F 549  HOH F1128  HOH F2342                               
SITE     1 DC9  5 ALA F 375  ASP F 376  GLY F 378  HOH F2564                    
SITE     2 DC9  5 EDO F6961                                                     
SITE     1 EC1  4 SER E 443  TYR F 153  ARG F 155  PHE G 151                    
SITE     1 EC2  5 ASN F  41  THR F  44  GLU F  46  LEU F 108                    
SITE     2 EC2  5 HOH F2374                                                     
SITE     1 EC3  6 PHE F  18  TYR F 101  TYR F 203  HOH F 629                    
SITE     2 EC3  6 HOH F1304  HOH F2251                                          
SITE     1 EC4  5 ILE B 373  ALA F  68  SER F  74  HOH F 617                    
SITE     2 EC4  5 HOH F2184                                                     
SITE     1 EC5  3 GLY C  45  GLU F 347  GAI F6821                               
SITE     1 EC6  7 ASN F 169  PHE F 170  GLU F 268  PHE F 296                    
SITE     2 EC6  7 CYS F 301  CYS F 302  PHE F 459                               
SITE     1 EC7  4 PHE F 151  TYR G 153  ARG G 155  SER H 443                    
SITE     1 EC8  6 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     2 EC8  6 HOH G 528  HOH G1885                                          
SITE     1 EC9  6 PHE G  70  GLU G 157  PRO G 158  VAL G 159                    
SITE     2 EC9  6 HOH G1393  TYR H 468                                          
SITE     1 FC1  5 ILE G 146  ASP G 147  PHE G 150  VAL H 458                    
SITE     2 FC1  5 PHE H 459                                                     
SITE     1 FC2  3 ALA D   7  TYR G 101  TYR G 203                               
SITE     1 FC3  8 ASN G 169  PHE G 170  GLU G 268  PHE G 296                    
SITE     2 FC3  8 CYS G 301  CYS G 302  CYS G 303  PHE G 459                    
SITE     1 FC4  4 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     1 FC5  7 TYR G 468  PHE H  70  GLU H 157  PRO H 158                    
SITE     2 FC5  7 VAL H 159  HOH H1616  HOH H1711                               
SITE     1 FC6  6 PHE G 459  HOH G 504  ILE H 146  ASP H 147                    
SITE     2 FC6  6 PHE H 150  HOH H1679                                          
SITE     1 FC7  4 PHE E 151  SER G 443  TYR H 153  ARG H 155                    
SITE     1 FC8  7 LYS G 469  ASP H 239  ASN H 261  LYS H 263                    
SITE     2 FC8  7 ARG H 264  HOH H1647  HOH H2299                               
SITE     1 FC9  4 LYS E 361  PHE H  18  TYR H 101  TYR H 203                    
SITE     1 GC1  8 MET H 124  PHE H 170  GLU H 268  PHE H 296                    
SITE     2 GC1  8 CYS H 301  CYS H 302  CYS H 303  PHE H 459                    
CRYST1  140.522  151.052  177.021  90.00  90.00  90.00 P 21 21 21   32          
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      0.007116  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006620  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005649        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system