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Database: PDB
Entry: 3INL
LinkDB: 3INL
Original site: 3INL 
HEADER    OXIDOREDUCTASE                          12-AUG-09   3INL              
TITLE     HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE ASIAN VARIANT, ALDH2*2,    
TITLE    2 COMPLEXED WITH AGONIST ALDA-1                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL;                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;                               
COMPND   5 EC: 1.2.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT-7-7                                    
KEYWDS    OXIDOREDUCTASE, ALDH, E487K, ROSSMANN FOLD, ALDA-1, ACTIVATOR,        
KEYWDS   2 MITOCHONDRION, NAD, TRANSIT PEPTIDE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PEREZ-MILLER,T.D.HURLEY                                             
REVDAT   3   01-NOV-17 3INL    1       REMARK                                   
REVDAT   2   11-AUG-10 3INL    1       JRNL                                     
REVDAT   1   12-JAN-10 3INL    0                                                
JRNL        AUTH   S.PEREZ-MILLER,H.YOUNUS,R.VANAM,C.H.CHEN,D.MOCHLY-ROSEN,     
JRNL        AUTH 2 T.D.HURLEY                                                   
JRNL        TITL   ALDA-1 IS AN AGONIST AND CHEMICAL CHAPERONE FOR THE COMMON   
JRNL        TITL 2 HUMAN ALDEHYDE DEHYDROGENASE 2 VARIANT.                      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   159 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20062057                                                     
JRNL        DOI    10.1038/NSMB.1737                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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   1  PMID   18787169                                                     
REMARK   1  DOI    10.1126/SCIENCE.1158554                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.4_4                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.090                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 293169                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.136                           
REMARK   3   R VALUE            (WORKING SET) : 0.136                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.1170 -  4.4890    0.99    21545   142  0.1170 0.1440        
REMARK   3     2  4.4890 -  3.5640    0.99    21359   147  0.0890 0.1290        
REMARK   3     3  3.5640 -  3.1140    0.99    21353   135  0.1060 0.1340        
REMARK   3     4  3.1140 -  2.8290    0.99    21277   156  0.1290 0.1460        
REMARK   3     5  2.8290 -  2.6260    0.99    21272   148  0.1440 0.1880        
REMARK   3     6  2.6260 -  2.4720    0.99    21255   142  0.1470 0.1660        
REMARK   3     7  2.4720 -  2.3480    0.99    21181   152  0.1530 0.2180        
REMARK   3     8  2.3480 -  2.2460    0.99    21106   143  0.1530 0.2080        
REMARK   3     9  2.2460 -  2.1590    0.98    21069   133  0.1600 0.1770        
REMARK   3    10  2.1590 -  2.0850    0.97    20767   154  0.1690 0.1770        
REMARK   3    11  2.0850 -  2.0200    0.97    20776   108  0.1740 0.2160        
REMARK   3    12  2.0200 -  1.9620    0.95    20289   141  0.1810 0.2270        
REMARK   3    13  1.9620 -  1.9100    0.93    19979   136  0.1980 0.2180        
REMARK   3    14  1.9100 -  1.8640    0.84    17886   120  0.2200 0.2170        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 42.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.40900                                            
REMARK   3    B22 (A**2) : -16.87300                                            
REMARK   3    B33 (A**2) : -12.16600                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.60200                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.3780                                                   
REMARK   3   OPERATOR: L,-K,H                                                   
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          31433                                  
REMARK   3   ANGLE     :  0.906          42533                                  
REMARK   3   CHIRALITY :  0.055           4641                                  
REMARK   3   PLANARITY :  0.003           5570                                  
REMARK   3   DIHEDRAL  : 17.245          11252                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3INL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054634.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-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) : 1.07                               
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-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 299181                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
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, 8MM DTT, PH 6.4, VAPOR DIFFUSION,              
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       88.45000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24080 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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     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     GLN C     6                                                      
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 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       23.83   -150.13                                   
REMARK 500    ARG A  34       -0.22     70.25                                   
REMARK 500    VAL A 120      -72.07   -105.87                                   
REMARK 500    THR A 227      -75.61   -105.16                                   
REMARK 500    SER A 260      -81.91   -120.12                                   
REMARK 500    ASN A 261       20.17   -140.49                                   
REMARK 500    LEU A 269     -150.17   -104.25                                   
REMARK 500    TYR A 379       54.27   -105.25                                   
REMARK 500    LYS A 469     -134.95     54.88                                   
REMARK 500    LEU A 477      167.19     73.72                                   
REMARK 500    ASN B  20       27.67   -146.62                                   
REMARK 500    ASP B  55     -159.62   -138.63                                   
REMARK 500    VAL B 120      -71.31    -98.48                                   
REMARK 500    THR B 227      -82.02    -97.60                                   
REMARK 500    SER B 260      -95.73   -108.07                                   
REMARK 500    LEU B 269     -152.51   -116.90                                   
REMARK 500    GLN B 300       58.93    -96.81                                   
REMARK 500    LYS B 469     -128.99     57.22                                   
REMARK 500    LEU B 477      162.49     65.76                                   
REMARK 500    ASN C  20       27.34   -141.22                                   
REMARK 500    GLN C  21     -166.53   -124.14                                   
REMARK 500    ASP C  55     -162.99   -127.34                                   
REMARK 500    VAL C 120      -67.97    -95.95                                   
REMARK 500    THR C 227      -77.82   -103.10                                   
REMARK 500    SER C 260      -90.89   -117.97                                   
REMARK 500    LEU C 269     -166.31   -113.51                                   
REMARK 500    TYR C 379       53.61    -96.04                                   
REMARK 500    LYS C 469     -130.07     48.55                                   
REMARK 500    LEU C 477      167.39     81.13                                   
REMARK 500    ASN D  20       23.09   -148.68                                   
REMARK 500    GLN D  21     -169.96   -121.31                                   
REMARK 500    VAL D 120      -74.53   -101.53                                   
REMARK 500    THR D 227      -71.32   -110.79                                   
REMARK 500    SER D 260     -105.17   -116.47                                   
REMARK 500    LEU D 269     -165.15   -115.05                                   
REMARK 500    TYR D 379       50.67    -93.28                                   
REMARK 500    LYS D 469     -133.79     42.29                                   
REMARK 500    LEU D 477      161.89     73.92                                   
REMARK 500    ASN E  20       26.94   -152.59                                   
REMARK 500    GLN E  21     -166.61   -124.21                                   
REMARK 500    VAL E 120      -69.93   -102.98                                   
REMARK 500    THR E 197       58.96   -146.56                                   
REMARK 500    THR E 227      -72.54   -109.73                                   
REMARK 500    SER E 260     -107.81   -113.25                                   
REMARK 500    LEU E 269     -152.39   -109.32                                   
REMARK 500    LYS E 272       58.63   -147.26                                   
REMARK 500    GLN E 300       59.68    -93.91                                   
REMARK 500    TYR E 379       58.59   -103.65                                   
REMARK 500    LYS E 469     -130.96     50.92                                   
REMARK 500    LEU E 477      161.03     71.93                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  39   OG1                                                    
REMARK 620 2 VAL A  40   O   102.2                                              
REMARK 620 3 ASP A 109   O   142.0  97.9                                        
REMARK 620 4 ASP A 109   OD1  61.5 102.6  82.9                                  
REMARK 620 5 GLN A 196   O    76.9 163.8  92.0  91.2                            
REMARK 620 6 HOH A 501   O   131.6  88.7  80.3 160.9  80.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  39   OG1                                                    
REMARK 620 2 VAL B  40   O    99.6                                              
REMARK 620 3 ASP B 109   O   143.1  99.6                                        
REMARK 620 4 ASP B 109   OD1  58.7 106.5  85.7                                  
REMARK 620 5 GLN B 196   O    77.2 158.0  95.3  90.6                            
REMARK 620 6 HOH B3389   O   140.8  83.1  72.8 157.8  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  39   OG1                                                    
REMARK 620 2 VAL C  40   O   102.9                                              
REMARK 620 3 ASP C 109   O   143.9  93.6                                        
REMARK 620 4 ASP C 109   OD1  58.4 103.2  86.8                                  
REMARK 620 5 GLN C 196   O    76.5 160.2  98.1  93.4                            
REMARK 620 6 HOH C 501   O   137.3  89.0  73.8 157.8  79.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL D  40   O                                                      
REMARK 620 2 ASP D 109   O   100.1                                              
REMARK 620 3 ASP D 109   OD1 108.8  82.9                                        
REMARK 620 4 GLN D 196   O   157.9  95.9  88.1                                  
REMARK 620 5 HOH D 501   O    80.4  74.7 157.1  89.4                            
REMARK 620 6 THR D  39   OG1 105.8 144.0  65.4  67.7 133.7                      
REMARK 620 7 HOH D2497   O    80.1 146.9 128.8  78.1  72.7  63.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E  39   OG1                                                    
REMARK 620 2 VAL E  40   O   103.5                                              
REMARK 620 3 ASP E 109   O   140.8  97.7                                        
REMARK 620 4 ASP E 109   OD1  56.8 101.7  86.9                                  
REMARK 620 5 GLN E 196   O    76.4 162.0  93.1  93.2                            
REMARK 620 6 HOH E 503   O   135.8  84.3  78.4 164.8  83.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL F  40   O                                                      
REMARK 620 2 ASP F 109   O    96.1                                              
REMARK 620 3 ASP F 109   OD1 104.4  84.6                                        
REMARK 620 4 GLN F 196   O   163.0  93.7  90.3                                  
REMARK 620 5 HOH F 502   O    85.3  78.2 161.1  83.1                            
REMARK 620 6 THR F  39   OG1 103.0 142.7  59.9  76.8 134.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA G 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL G  40   O                                                      
REMARK 620 2 ASP G 109   O   103.7                                              
REMARK 620 3 ASP G 109   OD1 100.3  86.6                                        
REMARK 620 4 GLN G 196   O   163.1  89.1  91.3                                  
REMARK 620 5 HOH G 503   O    89.6  75.4 161.2  83.0                            
REMARK 620 6 THR G  39   OG1  96.2 140.7  56.3  80.0 139.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA H 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR H  39   OG1                                                    
REMARK 620 2 VAL H  40   O   106.5                                              
REMARK 620 3 ASP H 109   O   140.2 101.5                                        
REMARK 620 4 ASP H 109   OD1  62.7 104.5  83.4                                  
REMARK 620 5 GLN H 196   O    80.2 155.1  86.2  99.9                            
REMARK 620 6 HOH H 501   O   134.9  83.5  75.4 158.5  75.5                      
REMARK 620 N                    1     2     3     4     5                       
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 EDO A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB E 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB F 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB G 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BXB H 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3INJ   RELATED DB: PDB                                   
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH AGONIST    
REMARK 900 ALDA-1                                                               
DBREF  3INL A    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL B    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL C    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL D    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL E    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL F    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL G    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
DBREF  3INL H    1   500  UNP    P05091   ALDH2_HUMAN     18    517             
SEQADV 3INL SER A  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS A  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER B  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS B  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER C  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS C  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER D  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS D  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER E  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS E  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER F  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS F  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER G  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS G  487  UNP  P05091    GLU   504 ENGINEERED                     
SEQADV 3INL SER H  302  UNP  P05091    CYS   319 ENGINEERED                     
SEQADV 3INL LYS H  487  UNP  P05091    GLU   504 ENGINEERED                     
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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS 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 SER 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 LYS VAL LYS THR VAL THR VAL LYS          
SEQRES  39 H  500  VAL PRO GLN LYS ASN SER                                      
HET     NA  A 601       1                                                       
HET    EDO  A 701       4                                                       
HET    EDO  A 702       4                                                       
HET    EDO  A 703       4                                                       
HET    EDO  A 704       4                                                       
HET    EDO  A 705       4                                                       
HET    EDO  A 706       4                                                       
HET    BXB  A1001      21                                                       
HET     NA  B 601       1                                                       
HET    EDO  B 701       4                                                       
HET    EDO  B 702       4                                                       
HET    EDO  B 703       4                                                       
HET    EDO  B 704       4                                                       
HET    BXB  B1001      21                                                       
HET     NA  C 601       1                                                       
HET    EDO  C 701       4                                                       
HET    EDO  C 702       4                                                       
HET    EDO  C 703       4                                                       
HET    BXB  C1001      21                                                       
HET     NA  D 601       1                                                       
HET    EDO  D 701       4                                                       
HET    EDO  D 702       4                                                       
HET    BXB  D1001      21                                                       
HET     NA  E 601       1                                                       
HET    EDO  E 701       4                                                       
HET    EDO  E 702       4                                                       
HET    EDO  E 703       4                                                       
HET    EDO  E 704       4                                                       
HET    BXB  E1001      21                                                       
HET    EDO  E 501       4                                                       
HET     NA  F 601       1                                                       
HET    EDO  F 701       4                                                       
HET    EDO  F 703       4                                                       
HET    BXB  F1001      21                                                       
HET    EDO  F 501       4                                                       
HET    EDO  G 702       4                                                       
HET     NA  G 601       1                                                       
HET    EDO  G 701       4                                                       
HET    EDO  G 501       4                                                       
HET    EDO  G 704       4                                                       
HET    EDO  G 705       4                                                       
HET    BXB  G1001      21                                                       
HET     NA  H 601       1                                                       
HET    EDO  H 701       4                                                       
HET    EDO  H 703       4                                                       
HET    EDO  H 704       4                                                       
HET    BXB  H1001      21                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     BXB N-(1,3-BENZODIOXOL-5-YLMETHYL)-2,6-DICHLOROBENZAMIDE             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   9   NA    8(NA 1+)                                                     
FORMUL  10  EDO    31(C2 H6 O2)                                                 
FORMUL  16  BXB    8(C15 H11 CL2 N O3)                                          
FORMUL  56  HOH   *3408(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  GLY A  258  1                                  13    
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  ARG A  329  1                                  18    
HELIX   14  14 ASP A  346  GLU A  363  1                                  18    
HELIX   15  15 MET A  393  GLU A  398  1                                   6    
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  259  1                                  14    
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 ILE B  314  ARG B  329  1                                  16    
HELIX   33  33 ASP B  346  GLY B  364  1                                  19    
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 GLU B  479  ALA B  484  1                                   6    
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  GLY C  134  1                                  15    
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  ALA C  257  1                                  12    
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 GLU C  312  ARG C  329  1                                  18    
HELIX   52  52 ASP C  346  GLU C  363  1                                  18    
HELIX   53  53 MET C  393  LYS C  397  5                                   5    
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 GLU C  479  ALA C  484  5                                   6    
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 SER D  246  SER D  259  1                                  14    
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  SER D  328  1                                  17    
HELIX   70  70 ASP D  346  GLU D  363  1                                  18    
HELIX   71  71 MET D  393  GLU D  398  1                                   6    
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 GLU D  479  ALA D  484  1                                   6    
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  ALA E  136  1                                  17    
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  259  1                                  14    
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 ILE E  314  SER E  328  1                                  15    
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  GLN F   71  1                                  17    
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  259  1                                  14    
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 ILE F  314  ARG F  329  1                                  16    
HELIX  108 108 ASP F  346  GLU F  363  1                                  18    
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 GLU F  479  ALA F  484  1                                   6    
HELIX  113 113 ASP G   55  PHE G   70  1                                  16    
HELIX  114 114 SER G   74  MET G   79  1                                   6    
HELIX  115 115 ASP G   80  ASP G   98  1                                  19    
HELIX  116 116 ASP G   98  GLY G  111  1                                  14    
HELIX  117 117 PRO G  113  VAL G  120  1                                   8    
HELIX  118 118 VAL G  120  ALA G  136  1                                  17    
HELIX  119 119 PHE G  170  THR G  185  1                                  16    
HELIX  120 120 PRO G  198  GLY G  212  1                                  15    
HELIX  121 121 THR G  227  SER G  234  1                                   8    
HELIX  122 122 SER G  246  SER G  259  1                                  14    
HELIX  123 123 ASP G  282  PHE G  296  1                                  15    
HELIX  124 124 ASN G  297  GLN G  300  5                                   4    
HELIX  125 125 GLU G  312  ARG G  329  1                                  18    
HELIX  126 126 ASP G  346  GLY G  364  1                                  19    
HELIX  127 127 THR G  412  ASN G  422  1                                  11    
HELIX  128 128 ASP G  435  LEU G  446  1                                  12    
HELIX  129 129 GLU G  479  ALA G  484  1                                   6    
HELIX  130 130 ASP H   55  PHE H   70  1                                  16    
HELIX  131 131 SER H   74  MET H   79  1                                   6    
HELIX  132 132 ASP H   80  ASP H   98  1                                  19    
HELIX  133 133 ASP H   98  GLY H  111  1                                  14    
HELIX  134 134 PRO H  113  VAL H  120  1                                   8    
HELIX  135 135 VAL H  120  GLY H  134  1                                  15    
HELIX  136 136 PHE H  170  THR H  185  1                                  16    
HELIX  137 137 PRO H  198  GLY H  212  1                                  15    
HELIX  138 138 THR H  227  SER H  234  1                                   8    
HELIX  139 139 SER H  246  SER H  260  1                                  15    
HELIX  140 140 ASP H  282  PHE H  296  1                                  15    
HELIX  141 141 ASN H  297  GLN H  300  5                                   4    
HELIX  142 142 GLU H  312  ARG H  329  1                                  18    
HELIX  143 143 ASP H  346  GLU H  363  1                                  18    
HELIX  144 144 MET H  393  LYS H  397  5                                   5    
HELIX  145 145 THR H  412  ASN H  422  1                                  11    
HELIX  146 146 ASP H  435  LEU H  446  1                                  12    
HELIX  147 147 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  VAL A  51   N  PHE A  37           
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  THR B 384           
SHEET    4   C20 ARG B 307  GLN B 311  1  N  THR B 308   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  PHE B 432   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  GLU A 157   O  LYS A 487           
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  LYS 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  VAL C 431   O  TRP C 452           
SHEET   16   C20 PRO C 274  ILE C 277  1  N  ILE C 276   O  ALA C 430           
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  THR C 308           
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  LEU C 368   O  VAL C 385           
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  ARG A 264   N  VAL A 241           
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  GLY A 387 -1  O  VAL A 385   N  LEU A 368           
SHEET    3   E20 VAL A 404  PHE A 410  1  O  MET A 405   N  PHE A 386           
SHEET    4   E20 ARG A 307  GLN A 311  1  N  VAL A 310   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  PHE A 432   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  LYS 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  GLY C 141   N  THR B 143           
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  LYS 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  VAL D 431   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  ARG D 307   N  ASN D 275           
SHEET   18   E20 VAL D 404  PHE D 410  1  O  LEU D 408   N  THR D 308           
SHEET   19   E20 THR D 384  GLY D 387  1  N  PHE D 386   O  MET D 405           
SHEET   20   E20 LYS D 366  CYS D 369 -1  N  LEU D 368   O  VAL D 385           
SHEET    1   F 2 ILE B  22  ILE B  24  0                                        
SHEET    2   F 2 GLU B  27  HIS B  29 -1  O  HIS B  29   N  ILE B  22           
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  PRO B 222  0                                        
SHEET    2   H 6 VAL B 188  VAL B 193  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  VAL C  51   N  PHE C  37           
SHEET    1   K 6 VAL C 218  PRO C 222  0                                        
SHEET    2   K 6 VAL C 188  VAL C 193  1  N  MET C 191   O  ASN C 219           
SHEET    3   K 6 VAL C 161  ILE C 165  1  N  GLN C 164   O  LYS C 192           
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  HIS D  29   N  ILE D  22           
SHEET    1   N 2 THR D  36  VAL D  40  0                                        
SHEET    2   N 2 VAL D  47  ALA D  52 -1  O  VAL D  51   N  PHE D  37           
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  VAL E  51   N  PHE E  37           
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  VAL F 431           
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  LYS 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 491   N  TYR H 153           
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  ALA G 429   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  GLN G 406   N  THR G 308           
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  ILE E 220  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  GLN E 164   O  LYS E 192           
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  VAL E 385   N  LEU E 368           
SHEET    3   T20 VAL E 404  PHE E 410  1  O  MET E 405   N  THR E 384           
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  ILE E 277   O  PHE E 309           
SHEET    6   T20 ALA E 428  PHE E 432  1  O  PHE E 432   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  TYR F 153   O  VAL F 491           
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  GLY G 141   N  THR F 143           
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  LYS G 487   N  GLU G 157           
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  VAL H 431   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  GLN H 406   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 TYR F 425  GLY F 426  0                                        
SHEET    2   X 2 TYR F 468  LYS F 469 -1  N  TYR F 468   O  GLY F 426           
SHEET    1   Y 2 ILE G  22  ILE G  24  0                                        
SHEET    2   Y 2 GLU G  27  HIS G  29 -1  O  HIS G  29   N  ILE G  22           
SHEET    1   Z 2 THR G  36  VAL G  40  0                                        
SHEET    2   Z 2 VAL G  47  ALA G  52 -1  O  ILE G  48   N  THR G  39           
SHEET    1  AA 6 VAL G 218  PRO G 222  0                                        
SHEET    2  AA 6 VAL G 188  VAL G 193  1  N  MET G 191   O  VAL G 221           
SHEET    3  AA 6 VAL G 161  ILE G 165  1  N  CYS G 162   O  VAL G 188           
SHEET    4  AA 6 LYS G 240  THR G 244  1  O  LYS G 240   N  GLY G 163           
SHEET    5  AA 6 ARG G 264  GLU G 268  1  O  ARG G 264   N  VAL G 241           
SHEET    6  AA 6 GLY G 472  SER G 473 -1  O  SER G 473   N  LEU G 267           
SHEET    1  AB 2 TYR G 425  GLY G 426  0                                        
SHEET    2  AB 2 TYR G 468  LYS G 469 -1  N  TYR G 468   O  GLY G 426           
SHEET    1  AC 2 ILE H  22  ILE H  24  0                                        
SHEET    2  AC 2 GLU H  27  HIS H  29 -1  O  HIS H  29   N  ILE H  22           
SHEET    1  AD 2 THR H  36  VAL H  40  0                                        
SHEET    2  AD 2 VAL H  47  ALA H  52 -1  O  ILE H  48   N  THR H  39           
SHEET    1  AE 6 VAL H 218  ILE H 220  0                                        
SHEET    2  AE 6 VAL H 188  LYS H 192  1  N  MET H 191   O  ASN H 219           
SHEET    3  AE 6 VAL H 161  ILE H 165  1  N  GLN H 164   O  LYS H 192           
SHEET    4  AE 6 LYS H 240  THR H 244  1  O  LYS H 240   N  GLY H 163           
SHEET    5  AE 6 ARG H 264  GLU H 268  1  O  ARG H 264   N  VAL H 241           
SHEET    6  AE 6 GLY H 472  SER H 473 -1  O  SER H 473   N  LEU H 267           
SHEET    1  AF 2 TYR H 425  GLY H 426  0                                        
SHEET    2  AF 2 TYR H 468  LYS H 469 -1  N  TYR H 468   O  GLY H 426           
LINK         OG1 THR A  39                NA    NA A 601     1555   1555  2.98  
LINK         O   VAL A  40                NA    NA A 601     1555   1555  2.41  
LINK         O   ASP A 109                NA    NA A 601     1555   1555  2.47  
LINK         OD1 ASP A 109                NA    NA A 601     1555   1555  2.41  
LINK         O   GLN A 196                NA    NA A 601     1555   1555  2.37  
LINK         OG1 THR B  39                NA    NA B 601     1555   1555  2.98  
LINK         O   VAL B  40                NA    NA B 601     1555   1555  2.45  
LINK         O   ASP B 109                NA    NA B 601     1555   1555  2.43  
LINK         OD1 ASP B 109                NA    NA B 601     1555   1555  2.41  
LINK         O   GLN B 196                NA    NA B 601     1555   1555  2.36  
LINK         OG1 THR C  39                NA    NA C 601     1555   1555  3.00  
LINK         O   VAL C  40                NA    NA C 601     1555   1555  2.41  
LINK         O   ASP C 109                NA    NA C 601     1555   1555  2.46  
LINK         OD1 ASP C 109                NA    NA C 601     1555   1555  2.36  
LINK         O   GLN C 196                NA    NA C 601     1555   1555  2.38  
LINK         O   VAL D  40                NA    NA D 601     1555   1555  2.43  
LINK         O   ASP D 109                NA    NA D 601     1555   1555  2.45  
LINK         OD1 ASP D 109                NA    NA D 601     1555   1555  2.41  
LINK         O   GLN D 196                NA    NA D 601     1555   1555  2.35  
LINK         OG1 THR E  39                NA    NA E 601     1555   1555  2.98  
LINK         O   VAL E  40                NA    NA E 601     1555   1555  2.41  
LINK         O   ASP E 109                NA    NA E 601     1555   1555  2.42  
LINK         OD1 ASP E 109                NA    NA E 601     1555   1555  2.38  
LINK         O   GLN E 196                NA    NA E 601     1555   1555  2.36  
LINK         O   VAL F  40                NA    NA F 601     1555   1555  2.42  
LINK         O   ASP F 109                NA    NA F 601     1555   1555  2.47  
LINK         OD1 ASP F 109                NA    NA F 601     1555   1555  2.39  
LINK         O   GLN F 196                NA    NA F 601     1555   1555  2.34  
LINK         O   VAL G  40                NA    NA G 601     1555   1555  2.38  
LINK         O   ASP G 109                NA    NA G 601     1555   1555  2.42  
LINK         OD1 ASP G 109                NA    NA G 601     1555   1555  2.40  
LINK         O   GLN G 196                NA    NA G 601     1555   1555  2.34  
LINK         OG1 THR H  39                NA    NA H 601     1555   1555  3.00  
LINK         O   VAL H  40                NA    NA H 601     1555   1555  2.44  
LINK         O   ASP H 109                NA    NA H 601     1555   1555  2.45  
LINK         OD1 ASP H 109                NA    NA H 601     1555   1555  2.36  
LINK         O   GLN H 196                NA    NA H 601     1555   1555  2.36  
LINK        NA    NA A 601                 O   HOH A 501     1555   1555  2.73  
LINK        NA    NA B 601                 O   HOH B3389     1555   1555  2.56  
LINK        NA    NA C 601                 O   HOH C 501     1555   1555  2.66  
LINK        NA    NA D 601                 O   HOH D 501     1555   1555  2.81  
LINK        NA    NA E 601                 O   HOH E 503     1555   1555  2.55  
LINK        NA    NA F 601                 O   HOH F 502     1555   1555  2.74  
LINK        NA    NA G 601                 O   HOH G 503     1555   1555  2.56  
LINK        NA    NA H 601                 O   HOH H 501     1555   1555  2.77  
LINK         OG1 THR D  39                NA    NA D 601     1555   1555  3.00  
LINK         OG1 THR G  39                NA    NA G 601     1555   1555  3.02  
LINK         OG1 THR F  39                NA    NA F 601     1555   1555  3.02  
LINK        NA    NA D 601                 O   HOH D2497     1555   1555  3.13  
SITE     1 AC1  5 THR A  39  VAL A  40  ASP A 109  GLN A 196                    
SITE     2 AC1  5 HOH A 501                                                     
SITE     1 AC2  6 ASN A 169  CYS A 301  SER A 302  CYS A 303                    
SITE     2 AC2  6 PHE A 465  BXB A1001                                          
SITE     1 AC3  3 ASN A 440  PHE C 151  ASN D 440                               
SITE     1 AC4  4 LEU A 367  CYS A 369  GLY A 370  HOH A1692                    
SITE     1 AC5  4 TYR A 153  ARG A 155  SER B 443  PHE D 151                    
SITE     1 AC6  7 ASN A  41  THR A  44  GLU A  46  LEU A 108                    
SITE     2 AC6  7 HOH A1733  HOH A3047  GLU D  46                               
SITE     1 AC7  7 PHE A  18  ASP A  98  TYR A 101  TYR A 203                    
SITE     2 AC7  7 HOH A 572  HOH A1125  HOH A2611                               
SITE     1 AC8  8 MET A 124  LEU A 173  PHE A 292  PHE A 296                    
SITE     2 AC8  8 ASP A 457  VAL A 458  PHE A 459  EDO A 701                    
SITE     1 AC9  5 THR B  39  VAL B  40  ASP B 109  GLN B 196                    
SITE     2 AC9  5 HOH B3389                                                     
SITE     1 BC1  6 ASN B 169  PHE B 170  CYS B 301  SER B 302                    
SITE     2 BC1  6 CYS B 303  BXB B1001                                          
SITE     1 BC2  4 LYS B 327  CYS B 369  GLY B 370  HOH B2081                    
SITE     1 BC3  4 SER A 443  TYR B 153  ARG B 155  PHE C 151                    
SITE     1 BC4  5 ASN B  41  THR B  44  GLU B  46  LEU B 108                    
SITE     2 BC4  5 HOH B2322                                                     
SITE     1 BC5  9 MET B 124  PHE B 170  LEU B 173  PHE B 292                    
SITE     2 BC5  9 PHE B 296  ASP B 457  VAL B 458  PHE B 459                    
SITE     3 BC5  9 EDO B 701                                                     
SITE     1 BC6  5 THR C  39  VAL C  40  ASP C 109  GLN C 196                    
SITE     2 BC6  5 HOH C 501                                                     
SITE     1 BC7  4 ASN C 169  CYS C 301  SER C 302  BXB C1001                    
SITE     1 BC8  5 PHE B 151  TYR C 153  ARG C 155  HOH C1990                    
SITE     2 BC8  5 SER D 443                                                     
SITE     1 BC9  5 ASN C  41  THR C  44  ILE C  48  LEU C 108                    
SITE     2 BC9  5 HOH C2616                                                     
SITE     1 CC1 10 MET C 124  PHE C 170  LEU C 173  PHE C 292                    
SITE     2 CC1 10 PHE C 296  ASP C 457  VAL C 458  PHE C 459                    
SITE     3 CC1 10 EDO C 701  HOH D2063                                          
SITE     1 CC2  5 THR D  39  VAL D  40  ASP D 109  GLN D 196                    
SITE     2 CC2  5 HOH D 501                                                     
SITE     1 CC3  6 ASN D 169  PHE D 170  SER D 302  CYS D 303                    
SITE     2 CC3  6 PHE D 465  BXB D1001                                          
SITE     1 CC4  5 PHE A 151  ASN C 440  SER C 443  TYR D 153                    
SITE     2 CC4  5 ARG D 155                                                     
SITE     1 CC5  8 MET D 124  PHE D 170  LEU D 173  PHE D 296                    
SITE     2 CC5  8 ASP D 457  PHE D 459  EDO D 701  HOH D1940                    
SITE     1 CC6  5 THR E  39  VAL E  40  ASP E 109  GLN E 196                    
SITE     2 CC6  5 HOH E 503                                                     
SITE     1 CC7  6 ASN E 169  CYS E 301  SER E 302  PHE E 465                    
SITE     2 CC7  6 BXB E1001  HOH E2328                                          
SITE     1 CC8  6 ARG E 329  VAL E 330  VAL E 331  HOH E2473                    
SITE     2 CC8  6 HOH E2895  HOH E3046                                          
SITE     1 CC9  4 TYR E 153  ARG E 155  SER F 443  PHE H 151                    
SITE     1 DC1  5 PHE E  18  TYR E 101  TYR E 203  HOH E 538                    
SITE     2 DC1  5 HOH E1986                                                     
SITE     1 DC2 10 MET E 124  PHE E 170  LEU E 173  PHE E 292                    
SITE     2 DC2 10 PHE E 296  ASP E 457  VAL E 458  PHE E 459                    
SITE     3 DC2 10 EDO E 701  HOH E2027                                          
SITE     1 DC3  4 PHE E 151  SER G 443  TYR H 153  ARG H 155                    
SITE     1 DC4  5 THR F  39  VAL F  40  ASP F 109  GLN F 196                    
SITE     2 DC4  5 HOH F 502                                                     
SITE     1 DC5  6 ASN F 169  PHE F 170  SER F 302  CYS F 303                    
SITE     2 DC5  6 PHE F 465  BXB F1001                                          
SITE     1 DC6  4 ASN F  41  THR F  44  GLU F  46  HOH F1546                    
SITE     1 DC7  9 MET F 124  PHE F 170  LEU F 173  PHE F 292                    
SITE     2 DC7  9 PHE F 296  ASP F 457  PHE F 459  EDO F 701                    
SITE     3 DC7  9 HOH F1400                                                     
SITE     1 DC8  4 PHE F 151  TYR G 153  ARG G 155  SER H 443                    
SITE     1 DC9  5 ASN E 440  SER E 443  TYR F 153  ARG F 155                    
SITE     2 DC9  5 PHE G 151                                                     
SITE     1 EC1  5 THR G  39  VAL G  40  ASP G 109  GLN G 196                    
SITE     2 EC1  5 HOH G 503                                                     
SITE     1 EC2  5 ASN G 169  SER G 302  CYS G 303  PHE G 465                    
SITE     2 EC2  5 BXB G1001                                                     
SITE     1 EC3  4 ILE G 373  ALA G 375  ASP G 376  GLY G 378                    
SITE     1 EC4  4 ASN G  41  THR G  44  ILE G  48  LEU G 108                    
SITE     1 EC5  5 ASP G  98  TYR G 101  TYR G 203  HOH G 534                    
SITE     2 EC5  5 HOH G 951                                                     
SITE     1 EC6 10 MET G 124  PHE G 170  LEU G 173  PHE G 292                    
SITE     2 EC6 10 PHE G 296  ASP G 457  PHE G 459  HOH G 591                    
SITE     3 EC6 10 EDO G 701  HOH G 884                                          
SITE     1 EC7  5 THR H  39  VAL H  40  ASP H 109  GLN H 196                    
SITE     2 EC7  5 HOH H 501                                                     
SITE     1 EC8  5 ASN H 169  PHE H 170  SER H 302  CYS H 303                    
SITE     2 EC8  5 BXB H1001                                                     
SITE     1 EC9  4 ASN H  41  THR H  44  GLU H  46  VAL H  47                    
SITE     1 FC1  4 PHE H  18  TYR H 101  TYR H 203  HOH H1808                    
SITE     1 FC2 10 MET H 124  PHE H 170  LEU H 173  TRP H 177                    
SITE     2 FC2 10 PHE H 292  PHE H 296  ASP H 457  PHE H 459                    
SITE     3 FC2 10 EDO H 701  HOH H1597                                          
CRYST1  102.121  176.900  102.323  90.00  94.57  90.00 P 1 21 1     16          
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      0.009792  0.000000  0.000783        0.00000                         
SCALE2      0.000000  0.005653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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