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Database: PDB
Entry: 6PFB
LinkDB: 6PFB
Original site: 6PFB 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUN-19   6PFB              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, FDUMP AND 3-(2-(4-((2-AMINO-4-OXO-4,7-DIHYDRO-3H-        
TITLE    3 PYRROLO[2,3-D]PYRIMIDIN-5-YL)METHYL)BENZAMIDO)PHENYL)PROPANOIC ACID. 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE; 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM HOMINIS;                        
SOURCE   3 ORGANISM_TAXID: 237895;                                              
SOURCE   4 GENE: CHUDEA4_4460;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PA-414                                    
KEYWDS    INHIBITOR, TS, TS-DHFR, TRANSFERASE, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.CZYZYK,M.VALHONDO,W.L.JORGENSEN,K.S.ANDERSON                      
REVDAT   1   02-OCT-19 6PFB    0                                                
JRNL        AUTH   D.J.CZYZYK,M.VALHONDO,L.DEIANA,J.TIRADO-RIVES,W.L.JORGENSEN, 
JRNL        AUTH 2 K.S.ANDERSON                                                 
JRNL        TITL   STRUCTURE ACTIVITY RELATIONSHIP TOWARDS DESIGN OF            
JRNL        TITL 2 CRYPTOSPORIDIUM SPECIFIC THYMIDYLATE SYNTHASE INHIBITORS.    
JRNL        REF    EUR.J.MED.CHEM.               V. 183 11673 2019              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   31536894                                                     
JRNL        DOI    10.1016/J.EJMECH.2019.111673                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472)                                 
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 97785                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2003                            
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 49.6579 -  7.4382    0.98     7055   150  0.1842 0.1844        
REMARK   3     2  7.4382 -  5.9070    0.99     6933   139  0.2231 0.2385        
REMARK   3     3  5.9070 -  5.1612    1.00     6976   144  0.2246 0.2861        
REMARK   3     4  5.1612 -  4.6897    0.98     6797   153  0.1921 0.2187        
REMARK   3     5  4.6897 -  4.3538    1.00     6931   143  0.1789 0.2320        
REMARK   3     6  4.3538 -  4.0973    1.00     6937   142  0.1976 0.2450        
REMARK   3     7  4.0973 -  3.8921    1.00     6918   138  0.2411 0.2678        
REMARK   3     8  3.8921 -  3.7228    0.98     6765   166  0.2595 0.3430        
REMARK   3     9  3.7228 -  3.5795    0.99     6861   130  0.2956 0.3504        
REMARK   3    10  3.5795 -  3.4560    0.99     6932   138  0.3350 0.3334        
REMARK   3    11  3.4560 -  3.3480    0.99     6826   164  0.3544 0.4012        
REMARK   3    12  3.3480 -  3.2523    0.99     6835   122  0.3712 0.4134        
REMARK   3    13  3.2523 -  3.1667    0.99     6867   152  0.4057 0.4563        
REMARK   3    14  3.1667 -  3.0894    0.89     6149   122  0.5055 0.5070        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.580            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          21058                                  
REMARK   3   ANGLE     :  0.483          28713                                  
REMARK   3   CHIRALITY :  0.042           3116                                  
REMARK   3   PLANARITY :  0.003           3667                                  
REMARK   3   DIHEDRAL  :  9.859          12139                                  
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 6PFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000242251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979300                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98232                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.089                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.39100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 3.07700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.740                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4Q0E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION 20 % PEG 6000, 0.2 M       
REMARK 280  AMMONIUM SULFATE, 0.06 M LITHIUM SULFATE, 0.1 M TRIS DROP RATIO     
REMARK 280  2:1 ENZYME MIX/WELL SOLUTION, PH 8.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 295.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      106.99700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.11900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.99700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.11900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      158.92522            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      662.73200            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A   179                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLN A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     CYS A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     GLN A   192                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B   179                                                      
REMARK 465     LYS B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     GLN B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     CYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     LYS C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     THR C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     CYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     GLN C   192                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     LYS D   180                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     THR D   182                                                      
REMARK 465     LEU D   183                                                      
REMARK 465     GLN D   184                                                      
REMARK 465     ASN D   185                                                      
REMARK 465     CYS D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     ARG D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     GLN D   192                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     GLU E   179                                                      
REMARK 465     LYS E   180                                                      
REMARK 465     LYS E   181                                                      
REMARK 465     THR E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     GLN E   184                                                      
REMARK 465     ASN E   185                                                      
REMARK 465     CYS E   186                                                      
REMARK 465     ASP E   187                                                      
REMARK 465     PRO E   188                                                      
REMARK 465     ALA E   189                                                      
REMARK 465     ARG E   190                                                      
REMARK 465     GLY E   191                                                      
REMARK 465     GLN E   192                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     ASN A   5    CG   OD1  ND2                                       
REMARK 470     LYS A  43    CG   CD   CE   NZ                                   
REMARK 470     ASN A  47    CG   OD1  ND2                                       
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLN A  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  95    CG   CD   OE1  OE2                                  
REMARK 470     MET A 102    CG   SD   CE                                        
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     ASP A 140    CG   OD1  OD2                                       
REMARK 470     GLU A 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 152    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     GLN A 178    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     ARG A 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 312    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 332    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 352    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 354    CG   CD   CE   NZ                                   
REMARK 470     LYS A 474    CG   CD   CE   NZ                                   
REMARK 470     LYS A 488    CG   CD   CE   NZ                                   
REMARK 470     LYS A 490    CG   CD   CE   NZ                                   
REMARK 470     LYS A 492    CG   CD   CE   NZ                                   
REMARK 470     GLU A 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 500    CG   CD   CE   NZ                                   
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     ASN B   5    CG   OD1  ND2                                       
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     ASN B  69    CG   OD1  ND2                                       
REMARK 470     GLU B  95    CG   CD   OE1  OE2                                  
REMARK 470     MET B 102    CG   SD   CE                                        
REMARK 470     ASN B 103    CG   OD1  ND2                                       
REMARK 470     LYS B 124    CG   CD   CE   NZ                                   
REMARK 470     ASP B 140    CG   OD1  OD2                                       
REMARK 470     GLU B 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     LYS B 220    CG   CD   CE   NZ                                   
REMARK 470     LYS B 311    CG   CD   CE   NZ                                   
REMARK 470     LYS B 312    CG   CD   CE   NZ                                   
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     GLU B 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 354    CG   CD   CE   NZ                                   
REMARK 470     MET B 356    CG   SD   CE                                        
REMARK 470     GLU B 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 474    CG   CD   CE   NZ                                   
REMARK 470     LYS B 488    CG   CD   CE   NZ                                   
REMARK 470     LYS B 490    CG   CD   CE   NZ                                   
REMARK 470     LYS B 492    CG   CD   CE   NZ                                   
REMARK 470     GLU B 494    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 497    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 500    CG   CD   CE   NZ                                   
REMARK 470     GLU B 502    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     ASN C   5    CG   OD1  ND2                                       
REMARK 470     LYS C  34    CG   CD   CE   NZ                                   
REMARK 470     ASP C  45    CG   OD1  OD2                                       
REMARK 470     ASN C  47    CG   OD1  ND2                                       
REMARK 470     LYS C  48    CG   CD   CE   NZ                                   
REMARK 470     LYS C  57    CG   CD   CE   NZ                                   
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
REMARK 470     GLN C  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  95    CG   CD   OE1  OE2                                  
REMARK 470     MET C 102    CG   SD   CE                                        
REMARK 470     ASN C 103    CG   OD1  ND2                                       
REMARK 470     ASP C 105    CG   OD1  OD2                                       
REMARK 470     LYS C 124    CG   CD   CE   NZ                                   
REMARK 470     ASP C 140    CG   OD1  OD2                                       
REMARK 470     GLU C 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 166    CG   CD   CE   NZ                                   
REMARK 470     LYS C 177    CG   CD   CE   NZ                                   
REMARK 470     GLU C 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     LYS C 220    CG   CD   CE   NZ                                   
REMARK 470     LYS C 312    CG   CD   CE   NZ                                   
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     GLU C 323    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 325    CG   CD1  CD2                                       
REMARK 470     GLU C 326    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 332    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 354    CG   CD   CE   NZ                                   
REMARK 470     ASP C 359    CG   OD1  OD2                                       
REMARK 470     LYS C 370    CG   CD   CE   NZ                                   
REMARK 470     GLU C 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 474    CG   CD   CE   NZ                                   
REMARK 470     LYS C 488    CG   CD   CE   NZ                                   
REMARK 470     LYS C 490    CG   CD   CE   NZ                                   
REMARK 470     LYS C 492    CG   CD   CE   NZ                                   
REMARK 470     GLU C 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 500    CG   CD   CE   NZ                                   
REMARK 470     GLU C 502    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     ASP C 518    CG   OD1  OD2                                       
REMARK 470     GLU D   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS D   4    CG   CD   CE   NZ                                   
REMARK 470     ASN D   5    CG   OD1  ND2                                       
REMARK 470     LYS D  34    CG   CD   CE   NZ                                   
REMARK 470     LYS D  43    CG   CD   CE   NZ                                   
REMARK 470     ASP D  45    CG   OD1  OD2                                       
REMARK 470     LYS D  48    CG   CD   CE   NZ                                   
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     LYS D  68    CG   CD   CE   NZ                                   
REMARK 470     ARG D  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  95    CG   CD   OE1  OE2                                  
REMARK 470     MET D 102    CG   SD   CE                                        
REMARK 470     ARG D 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     GLU D 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 166    CG   CD   CE   NZ                                   
REMARK 470     GLN D 178    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     LYS D 220    CG   CD   CE   NZ                                   
REMARK 470     GLU D 222    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 312    CG   CD   CE   NZ                                   
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     GLU D 326    CG   CD   OE1  OE2                                  
REMARK 470     HIS D 332    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 474    CG   CD   CE   NZ                                   
REMARK 470     LYS D 488    CG   CD   CE   NZ                                   
REMARK 470     LYS D 490    CG   CD   CE   NZ                                   
REMARK 470     LYS D 492    CG   CD   CE   NZ                                   
REMARK 470     LYS D 500    CG   CD   CE   NZ                                   
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     ASN E   5    CG   OD1  ND2                                       
REMARK 470     LYS E  34    CG   CD   CE   NZ                                   
REMARK 470     LYS E  43    CG   CD   CE   NZ                                   
REMARK 470     ASP E  45    CG   OD1  OD2                                       
REMARK 470     LYS E  48    CG   CD   CE   NZ                                   
REMARK 470     LYS E  49    CG   CD   CE   NZ                                   
REMARK 470     LYS E  57    CG   CD   CE   NZ                                   
REMARK 470     LYS E  68    CG   CD   CE   NZ                                   
REMARK 470     GLN E  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  95    CG   CD   OE1  OE2                                  
REMARK 470     MET E 102    CG   SD   CE                                        
REMARK 470     ASP E 105    CG   OD1  OD2                                       
REMARK 470     LYS E 124    CG   CD   CE   NZ                                   
REMARK 470     ASN E 126    CG   OD1  ND2                                       
REMARK 470     ASP E 140    CG   OD1  OD2                                       
REMARK 470     GLU E 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 152    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 166    CG   CD   CE   NZ                                   
REMARK 470     GLN E 178    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 194    CG   CD   CE   NZ                                   
REMARK 470     LYS E 211    CG   CD   CE   NZ                                   
REMARK 470     LYS E 217    CG   CD   CE   NZ                                   
REMARK 470     LYS E 220    CG   CD   CE   NZ                                   
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 300    CG   CD   CE   NZ                                   
REMARK 470     GLU E 310    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 311    CG   CD   CE   NZ                                   
REMARK 470     LYS E 312    CG   CD   CE   NZ                                   
REMARK 470     LYS E 322    CG   CD   CE   NZ                                   
REMARK 470     GLU E 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 352    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 354    CG   CD   CE   NZ                                   
REMARK 470     LYS E 370    CG   CD   CE   NZ                                   
REMARK 470     GLU E 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 474    CG   CD   CE   NZ                                   
REMARK 470     GLU E 475    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 488    CG   CD   CE   NZ                                   
REMARK 470     LYS E 490    CG   CD   CE   NZ                                   
REMARK 470     LYS E 492    CG   CD   CE   NZ                                   
REMARK 470     GLU E 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 500    CG   CD   CE   NZ                                   
REMARK 470     GLU E 502    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 516    CG   CD   CE   NZ                                   
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    LEU A  15      -64.26   -103.79                                   
REMARK 500    SER A  46      -61.85    -99.21                                   
REMARK 500    GLN A  81       87.18    -68.30                                   
REMARK 500    ASN A 103     -149.49   -131.51                                   
REMARK 500    ASP A 104       72.61     39.68                                   
REMARK 500    CYS A 113       24.15   -140.81                                   
REMARK 500    ASP A 140       21.75    -77.51                                   
REMARK 500    ILE A 141     -167.89   -115.90                                   
REMARK 500    ASP A 144      -18.94   -147.90                                   
REMARK 500    PRO A 279       81.04    -66.22                                   
REMARK 500    LYS A 285       96.79    -67.69                                   
REMARK 500    ALA A 287       93.59    -69.83                                   
REMARK 500    TYR A 314       62.61   -117.50                                   
REMARK 500    PRO A 340       88.74    -68.89                                   
REMARK 500    ILE A 341     -167.51   -111.50                                   
REMARK 500    GLU A 352       91.10    -67.06                                   
REMARK 500    LYS A 354      -77.48    -98.31                                   
REMARK 500    ARG A 383       51.54   -108.23                                   
REMARK 500    VAL A 404      -85.52   -100.69                                   
REMARK 500    ASN A 495     -128.66    -89.74                                   
REMARK 500    ILE A 496      -31.14   -135.96                                   
REMARK 500    LEU B  15      -65.03   -104.29                                   
REMARK 500    GLN B  81       86.94    -69.14                                   
REMARK 500    ASN B 100       26.58    -79.92                                   
REMARK 500    CYS B 113       23.83   -140.55                                   
REMARK 500    ASP B 140       21.24    -76.57                                   
REMARK 500    ILE B 141     -168.77   -116.82                                   
REMARK 500    ASP B 144      -18.46   -146.91                                   
REMARK 500    PRO B 279       81.34    -66.18                                   
REMARK 500    LYS B 285       97.42    -67.54                                   
REMARK 500    TYR B 314       63.11   -117.53                                   
REMARK 500    ILE B 341     -168.21   -108.98                                   
REMARK 500    GLU B 352       92.02    -66.26                                   
REMARK 500    LYS B 354      -78.10    -98.45                                   
REMARK 500    ARG B 383       50.38   -107.86                                   
REMARK 500    VAL B 404      -86.10   -101.18                                   
REMARK 500    ASN B 495     -128.14    -90.29                                   
REMARK 500    ILE B 496      -30.71   -135.28                                   
REMARK 500    LEU C  15      -65.82   -104.59                                   
REMARK 500    SER C  46      -61.83    -99.61                                   
REMARK 500    GLN C  81       86.73    -67.32                                   
REMARK 500    ASP C 104       73.64     56.06                                   
REMARK 500    CYS C 113       23.93   -140.61                                   
REMARK 500    ASP C 140       21.42    -76.99                                   
REMARK 500    ILE C 141     -168.09   -116.68                                   
REMARK 500    ASP C 144      -18.12   -146.31                                   
REMARK 500    PRO C 279       81.35    -66.57                                   
REMARK 500    LYS C 285       97.77    -67.52                                   
REMARK 500    TYR C 314       63.34   -117.88                                   
REMARK 500    PRO C 340       58.58    -68.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     101 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG4 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG4 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG4 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX E 604                 
DBREF1 6PFB A    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFB A     A0A0S4TER9                          1         521             
DBREF1 6PFB B    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFB B     A0A0S4TER9                          1         521             
DBREF1 6PFB C    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFB C     A0A0S4TER9                          1         521             
DBREF1 6PFB D    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFB D     A0A0S4TER9                          1         521             
DBREF1 6PFB E    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFB E     A0A0S4TER9                          1         521             
SEQRES   1 A  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 A  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 A  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 A  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 A  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 A  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 A  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 A  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 A  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 A  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 A  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 A  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 A  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 A  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 A  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 A  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 A  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 A  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 A  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 A  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 A  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 A  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 A  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 A  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 A  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 A  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 A  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 A  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 A  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 A  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 A  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 A  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 A  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 A  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 A  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 A  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 A  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 A  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 A  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 A  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 A  521  VAL                                                          
SEQRES   1 B  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 B  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 B  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 B  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 B  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 B  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 B  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 B  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 B  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 B  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 B  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 B  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 B  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 B  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 B  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 B  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 B  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 B  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 B  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 B  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 B  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 B  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 B  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 B  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 B  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 B  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 B  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 B  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 B  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 B  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 B  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 B  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 B  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 B  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 B  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 B  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 B  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 B  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 B  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 B  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 B  521  VAL                                                          
SEQRES   1 C  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 C  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 C  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 C  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 C  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 C  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 C  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 C  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 C  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 C  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 C  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 C  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 C  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 C  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 C  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 C  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 C  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 C  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 C  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 C  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 C  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 C  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 C  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 C  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 C  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 C  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 C  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 C  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 C  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 C  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 C  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 C  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 C  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 C  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 C  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 C  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 C  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 C  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 C  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 C  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 C  521  VAL                                                          
SEQRES   1 D  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 D  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 D  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 D  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 D  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 D  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 D  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 D  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 D  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 D  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 D  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 D  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 D  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 D  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 D  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 D  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 D  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 D  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 D  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 D  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 D  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 D  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 D  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 D  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 D  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 D  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 D  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 D  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 D  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 D  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 D  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 D  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 D  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 D  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 D  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 D  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 D  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 D  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 D  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 D  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 D  521  VAL                                                          
SEQRES   1 E  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 E  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 E  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 E  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 E  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 E  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 E  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 E  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 E  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 E  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 E  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 E  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 E  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 E  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 E  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 E  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 E  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 E  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 E  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 E  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 E  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 E  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 E  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 E  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 E  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 E  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 E  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 E  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 E  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 E  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 E  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 E  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 E  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 E  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 E  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 E  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 E  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 E  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 E  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 E  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 E  521  VAL                                                          
HET    NDP  A 601      48                                                       
HET    UFP  A 602      21                                                       
HET    OG4  A 603      32                                                       
HET    MTX  A 604      33                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    OG4  B 603      32                                                       
HET    MTX  B 604      33                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    OG4  C 603      32                                                       
HET    MTX  C 604      33                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    OG4  D 603      32                                                       
HET    MTX  D 604      33                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    OG4  E 603      32                                                       
HET    MTX  E 604      33                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     UFP 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                        
HETNAM     OG4 3-[2-({4-[(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-             
HETNAM   2 OG4  D]PYRIMIDIN-5-YL)METHYL]BENZENE-1-CARBONYL}AMINO)               
HETNAM   3 OG4  PHENYL]PROPANOIC ACID                                           
HETNAM     MTX METHOTREXATE                                                     
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  OG4    5(C23 H21 N5 O4)                                             
FORMUL   9  MTX    5(C20 H22 N8 O5)                                             
HELIX    1 AA1 ILE A   29  ASN A   41  1                                  13    
HELIX    2 AA2 ARG A   56  ILE A   62  1                                   7    
HELIX    3 AA3 ASN A   93  ILE A   98  1                                   6    
HELIX    4 AA4 GLY A  115  ASP A  125  1                                  11    
HELIX    5 AA5 LYS A  194  PHE A  207  1                                  14    
HELIX    6 AA6 LYS A  211  HIS A  216  1                                   6    
HELIX    7 AA7 GLU A  237  GLY A  251  1                                  15    
HELIX    8 AA8 ALA A  287  LYS A  300  1                                  14    
HELIX    9 AA9 ASN A  304  GLU A  310  1                                   7    
HELIX   10 AB1 SER A  317  GLY A  320  5                                   4    
HELIX   11 AB2 SER A  321  ILE A  328  1                                   8    
HELIX   12 AB3 GLY A  343  HIS A  348  1                                   6    
HELIX   13 AB4 ASP A  366  ASN A  378  1                                  13    
HELIX   14 AB5 ASN A  390  LEU A  394  5                                   5    
HELIX   15 AB6 GLY A  430  GLY A  450  1                                  21    
HELIX   16 AB7 HIS A  469  LEU A  477  1                                   9    
HELIX   17 AB8 LYS A  500  GLU A  502  5                                   3    
HELIX   18 AB9 ILE B   29  ASN B   41  1                                  13    
HELIX   19 AC1 ARG B   56  ILE B   62  1                                   7    
HELIX   20 AC2 ASN B   93  ILE B   98  1                                   6    
HELIX   21 AC3 GLY B  115  ASP B  125  1                                  11    
HELIX   22 AC4 ILE B  196  PHE B  207  1                                  12    
HELIX   23 AC5 LYS B  211  HIS B  216  1                                   6    
HELIX   24 AC6 GLU B  237  GLY B  251  1                                  15    
HELIX   25 AC7 ALA B  287  LYS B  300  1                                  14    
HELIX   26 AC8 ASN B  304  GLU B  310  1                                   7    
HELIX   27 AC9 SER B  317  GLY B  320  5                                   4    
HELIX   28 AD1 SER B  321  ILE B  328  1                                   8    
HELIX   29 AD2 ASP B  366  ASN B  378  1                                  13    
HELIX   30 AD3 ASN B  390  LEU B  394  5                                   5    
HELIX   31 AD4 GLY B  430  GLY B  450  1                                  21    
HELIX   32 AD5 HIS B  469  LEU B  477  1                                   9    
HELIX   33 AD6 LYS B  500  GLU B  502  5                                   3    
HELIX   34 AD7 ILE C   29  ASN C   41  1                                  13    
HELIX   35 AD8 ARG C   56  ILE C   62  1                                   7    
HELIX   36 AD9 ASN C   93  ILE C   98  1                                   6    
HELIX   37 AE1 GLY C  115  ASP C  125  1                                  11    
HELIX   38 AE2 ILE C  196  PHE C  207  1                                  12    
HELIX   39 AE3 LYS C  211  HIS C  216  1                                   6    
HELIX   40 AE4 GLU C  237  GLY C  251  1                                  15    
HELIX   41 AE5 ALA C  287  LYS C  300  1                                  14    
HELIX   42 AE6 ASN C  304  GLU C  310  1                                   7    
HELIX   43 AE7 SER C  317  GLY C  320  5                                   4    
HELIX   44 AE8 SER C  321  ILE C  328  1                                   8    
HELIX   45 AE9 GLY C  343  HIS C  348  1                                   6    
HELIX   46 AF1 ASP C  366  ASN C  378  1                                  13    
HELIX   47 AF2 ASN C  390  LEU C  394  5                                   5    
HELIX   48 AF3 GLY C  430  GLY C  450  1                                  21    
HELIX   49 AF4 HIS C  469  LEU C  477  1                                   9    
HELIX   50 AF5 LYS C  500  GLU C  502  5                                   3    
HELIX   51 AF6 ILE D   29  ASN D   41  1                                  13    
HELIX   52 AF7 ARG D   56  ILE D   62  1                                   7    
HELIX   53 AF8 ASN D   93  ILE D   98  1                                   6    
HELIX   54 AF9 GLY D  115  ASP D  125  1                                  11    
HELIX   55 AG1 ILE D  196  PHE D  207  1                                  12    
HELIX   56 AG2 LYS D  211  HIS D  216  1                                   6    
HELIX   57 AG3 GLU D  237  GLY D  251  1                                  15    
HELIX   58 AG4 ALA D  287  LYS D  300  1                                  14    
HELIX   59 AG5 ASN D  304  GLU D  310  1                                   7    
HELIX   60 AG6 SER D  317  GLY D  320  5                                   4    
HELIX   61 AG7 SER D  321  ILE D  328  1                                   8    
HELIX   62 AG8 GLY D  343  HIS D  348  1                                   6    
HELIX   63 AG9 ASP D  366  ASN D  378  1                                  13    
HELIX   64 AH1 ASN D  390  LEU D  394  5                                   5    
HELIX   65 AH2 GLY D  430  GLY D  450  1                                  21    
HELIX   66 AH3 HIS D  469  LEU D  477  1                                   9    
HELIX   67 AH4 LYS D  500  GLU D  502  5                                   3    
HELIX   68 AH5 ILE E   29  ASN E   41  1                                  13    
HELIX   69 AH6 ARG E   56  ILE E   62  1                                   7    
HELIX   70 AH7 ASN E   93  ILE E   98  1                                   6    
HELIX   71 AH8 GLY E  115  ASP E  125  1                                  11    
HELIX   72 AH9 ILE E  196  PHE E  207  1                                  12    
HELIX   73 AI1 LYS E  211  HIS E  216  1                                   6    
HELIX   74 AI2 GLU E  237  GLY E  251  1                                  15    
HELIX   75 AI3 ALA E  287  LYS E  300  1                                  14    
HELIX   76 AI4 ASN E  304  GLU E  310  1                                   7    
HELIX   77 AI5 SER E  317  GLY E  320  5                                   4    
HELIX   78 AI6 SER E  321  ILE E  328  1                                   8    
HELIX   79 AI7 GLY E  343  HIS E  348  1                                   6    
HELIX   80 AI8 ASP E  366  ASN E  378  1                                  13    
HELIX   81 AI9 ASN E  390  LEU E  394  5                                   5    
HELIX   82 AJ1 GLY E  430  GLY E  450  1                                  21    
HELIX   83 AJ2 HIS E  469  LEU E  477  1                                   9    
HELIX   84 AJ3 LYS E  500  GLU E  502  5                                   3    
SHEET    1 AA1 9 VAL A  88  PHE A  91  0                                        
SHEET    2 AA1 9 ARG A  70  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3 AA1 9 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4 AA1 9 ILE A 107  VAL A 112  1  O  PHE A 111   N  ALA A  51           
SHEET    5 AA1 9 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6 AA1 9 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7 AA1 9 MET A 173  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA1 9 PHE A 154  MET A 159 -1  N  VAL A 157   O  ILE A 174           
SHEET    9 AA1 9 GLY A 232  ARG A 233  1  O  GLY A 232   N  MET A 159           
SHEET    1 AA2 2 PHE A 163  CYS A 164  0                                        
SHEET    2 AA2 2 SER A 169  TYR A 170 -1  O  TYR A 170   N  PHE A 163           
SHEET    1 AA3 5 ALA A 252  ARG A 254  0                                        
SHEET    2 AA3 5 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3 AA3 5 GLU A 452  TYR A 466 -1  O  ILE A 460   N  GLN A 268           
SHEET    4 AA3 5 CYS A 415  ASP A 426  1  N  LEU A 420   O  PHE A 459           
SHEET    5 AA3 5 HIS A 403  VAL A 410 -1  N  TYR A 409   O  SER A 417           
SHEET    1 AA4 2 GLN A 486  PHE A 489  0                                        
SHEET    2 AA4 2 ILE A 504  ILE A 507 -1  O  ILE A 507   N  GLN A 486           
SHEET    1 AA5 9 VAL B  88  PHE B  91  0                                        
SHEET    2 AA5 9 ARG B  70  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3 AA5 9 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4 AA5 9 ILE B 107  VAL B 112  1  O  PHE B 111   N  ALA B  51           
SHEET    5 AA5 9 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6 AA5 9 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7 AA5 9 MET B 173  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA5 9 PHE B 154  MET B 159 -1  N  VAL B 157   O  ILE B 174           
SHEET    9 AA5 9 GLY B 232  ARG B 233  1  O  GLY B 232   N  MET B 159           
SHEET    1 AA6 2 PHE B 163  CYS B 164  0                                        
SHEET    2 AA6 2 SER B 169  TYR B 170 -1  O  TYR B 170   N  PHE B 163           
SHEET    1 AA7 6 ALA B 252  ARG B 254  0                                        
SHEET    2 AA7 6 THR B 262  ASP B 273 -1  O  THR B 262   N  ARG B 254           
SHEET    3 AA7 6 GLU B 452  TYR B 466 -1  O  ILE B 460   N  GLN B 268           
SHEET    4 AA7 6 CYS B 415  ASP B 426  1  N  LEU B 420   O  PHE B 459           
SHEET    5 AA7 6 HIS B 403  VAL B 410 -1  N  GLN B 407   O  ASN B 419           
SHEET    6 AA7 6 ILE B 385  LEU B 386 -1  N  LEU B 386   O  SER B 406           
SHEET    1 AA8 2 GLN B 486  PHE B 489  0                                        
SHEET    2 AA8 2 ILE B 504  ILE B 507 -1  O  ILE B 507   N  GLN B 486           
SHEET    1 AA9 9 VAL C  88  PHE C  91  0                                        
SHEET    2 AA9 9 ARG C  70  ILE C  75  1  N  ILE C  72   O  VAL C  89           
SHEET    3 AA9 9 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4 AA9 9 ILE C 107  VAL C 112  1  O  PHE C 111   N  ALA C  51           
SHEET    5 AA9 9 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6 AA9 9 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7 AA9 9 MET C 173  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8 AA9 9 PHE C 154  MET C 159 -1  N  VAL C 157   O  ILE C 174           
SHEET    9 AA9 9 GLY C 232  ARG C 233  1  O  GLY C 232   N  MET C 159           
SHEET    1 AB1 2 PHE C 163  CYS C 164  0                                        
SHEET    2 AB1 2 SER C 169  TYR C 170 -1  O  TYR C 170   N  PHE C 163           
SHEET    1 AB2 6 ALA C 252  ARG C 254  0                                        
SHEET    2 AB2 6 THR C 262  ASP C 273 -1  O  THR C 262   N  ARG C 254           
SHEET    3 AB2 6 GLU C 452  TYR C 466 -1  O  ILE C 460   N  GLN C 268           
SHEET    4 AB2 6 CYS C 415  ASP C 426  1  N  LEU C 420   O  PHE C 459           
SHEET    5 AB2 6 HIS C 403  VAL C 410 -1  N  TYR C 409   O  SER C 417           
SHEET    6 AB2 6 ILE C 385  LEU C 386 -1  N  LEU C 386   O  SER C 406           
SHEET    1 AB3 2 GLN C 486  PHE C 489  0                                        
SHEET    2 AB3 2 ILE C 504  ILE C 507 -1  O  ILE C 507   N  GLN C 486           
SHEET    1 AB4 9 VAL D  88  PHE D  91  0                                        
SHEET    2 AB4 9 ILE D  71  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3 AB4 9 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4 AB4 9 ILE D 107  VAL D 112  1  O  PHE D 111   N  ALA D  51           
SHEET    5 AB4 9 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6 AB4 9 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB4 9 MET D 173  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB4 9 PHE D 154  MET D 159 -1  N  VAL D 157   O  ILE D 174           
SHEET    9 AB4 9 GLY D 232  ARG D 233  1  O  GLY D 232   N  MET D 159           
SHEET    1 AB5 2 PHE D 163  CYS D 164  0                                        
SHEET    2 AB5 2 SER D 169  TYR D 170 -1  O  TYR D 170   N  PHE D 163           
SHEET    1 AB6 5 ALA D 252  ARG D 254  0                                        
SHEET    2 AB6 5 THR D 262  ASP D 273 -1  O  THR D 262   N  ARG D 254           
SHEET    3 AB6 5 GLU D 452  TYR D 466 -1  O  ILE D 460   N  GLN D 268           
SHEET    4 AB6 5 CYS D 415  ASP D 426  1  N  LEU D 420   O  PHE D 459           
SHEET    5 AB6 5 HIS D 403  VAL D 410 -1  N  GLN D 407   O  ASN D 419           
SHEET    1 AB7 2 GLN D 486  PHE D 489  0                                        
SHEET    2 AB7 2 ILE D 504  ILE D 507 -1  O  ILE D 507   N  GLN D 486           
SHEET    1 AB8 9 VAL E  88  PHE E  91  0                                        
SHEET    2 AB8 9 ARG E  70  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3 AB8 9 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4 AB8 9 ILE E 107  VAL E 112  1  O  PHE E 111   N  ALA E  51           
SHEET    5 AB8 9 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6 AB8 9 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7 AB8 9 MET E 173  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8 AB8 9 PHE E 154  MET E 159 -1  N  VAL E 157   O  ILE E 174           
SHEET    9 AB8 9 GLY E 232  ARG E 233  1  O  GLY E 232   N  MET E 159           
SHEET    1 AB9 2 PHE E 163  CYS E 164  0                                        
SHEET    2 AB9 2 SER E 169  TYR E 170 -1  O  TYR E 170   N  PHE E 163           
SHEET    1 AC1 6 ALA E 252  ARG E 254  0                                        
SHEET    2 AC1 6 THR E 262  ASP E 273 -1  O  THR E 262   N  ARG E 254           
SHEET    3 AC1 6 GLU E 452  TYR E 466 -1  O  ILE E 460   N  GLN E 268           
SHEET    4 AC1 6 CYS E 415  ASP E 426  1  N  LEU E 420   O  PHE E 459           
SHEET    5 AC1 6 HIS E 403  VAL E 410 -1  N  TYR E 409   O  SER E 417           
SHEET    6 AC1 6 ILE E 385  LEU E 386 -1  N  LEU E 386   O  SER E 406           
SHEET    1 AC2 2 GLN E 486  PHE E 489  0                                        
SHEET    2 AC2 2 ILE E 504  ILE E 507 -1  O  ILE E 507   N  GLN E 486           
SITE     1 AC1 22 VAL A  10  ALA A  11  ILE A  19  GLY A  20                    
SITE     2 AC1 22 GLY A  23  GLN A  24  GLY A  55  ARG A  56                    
SITE     3 AC1 22 LYS A  57  THR A  58  ILE A  75  SER A  76                    
SITE     4 AC1 22 SER A  77  SER A  78  ARG A  92  CYS A 113                    
SITE     5 AC1 22 GLY A 114  GLY A 115  GLU A 116  SER A 117                    
SITE     6 AC1 22 THR A 145  MTX A 604                                          
SITE     1 AC2 15 ARG A 257  LEU A 399  CYS A 402  HIS A 403                    
SITE     2 AC2 15 GLN A 422  ARG A 423  SER A 424  CYS A 425                    
SITE     3 AC2 15 ASP A 426  ASN A 434  HIS A 464  TYR A 466                    
SITE     4 AC2 15 OG4 A 603  ARG B 382  ARG B 383                               
SITE     1 AC3 10 ALA A 287  SER A 290  ILE A 315  ASN A 319                    
SITE     2 AC3 10 LEU A 399  ASP A 426  LEU A 429  PHE A 433                    
SITE     3 AC3 10 ALA A 520  UFP A 602                                          
SITE     1 AC4 14 VAL A   9  VAL A  10  ALA A  11  LEU A  25                    
SITE     2 AC4 14 ASP A  32  LYS A  34  PHE A  36  SER A  37                    
SITE     3 AC4 14 THR A  58  ARG A  70  CYS A 113  TYR A 119                    
SITE     4 AC4 14 THR A 134  NDP A 601                                          
SITE     1 AC5 24 VAL B  10  ALA B  11  ILE B  19  GLY B  20                    
SITE     2 AC5 24 GLY B  23  GLN B  24  LEU B  25  GLY B  55                    
SITE     3 AC5 24 ARG B  56  LYS B  57  THR B  58  ILE B  75                    
SITE     4 AC5 24 SER B  76  SER B  77  SER B  78  ARG B  92                    
SITE     5 AC5 24 CYS B 113  GLY B 114  GLY B 115  GLU B 116                    
SITE     6 AC5 24 SER B 117  ASP B 121  THR B 145  MTX B 604                    
SITE     1 AC6 15 ARG A 382  ARG A 383  ARG B 257  TYR B 342                    
SITE     2 AC6 15 CYS B 402  HIS B 403  GLN B 422  ARG B 423                    
SITE     3 AC6 15 SER B 424  CYS B 425  ASP B 426  ASN B 434                    
SITE     4 AC6 15 HIS B 464  TYR B 466  OG4 B 603                               
SITE     1 AC7 10 ALA B 287  SER B 290  ILE B 315  ASN B 319                    
SITE     2 AC7 10 ASP B 426  LEU B 429  GLY B 430  PHE B 433                    
SITE     3 AC7 10 ALA B 520  UFP B 602                                          
SITE     1 AC8 15 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC8 15 ASP B  32  LEU B  33  PHE B  36  SER B  37                    
SITE     3 AC8 15 THR B  58  ILE B  62  ARG B  70  CYS B 113                    
SITE     4 AC8 15 TYR B 119  THR B 134  NDP B 601                               
SITE     1 AC9 24 VAL C  10  ALA C  11  ILE C  19  GLY C  20                    
SITE     2 AC9 24 GLY C  23  GLN C  24  LEU C  25  GLY C  55                    
SITE     3 AC9 24 ARG C  56  LYS C  57  THR C  58  ILE C  75                    
SITE     4 AC9 24 SER C  76  SER C  77  SER C  78  ARG C  92                    
SITE     5 AC9 24 CYS C 113  GLY C 114  GLY C 115  GLU C 116                    
SITE     6 AC9 24 SER C 117  ILE C 118  THR C 145  MTX C 604                    
SITE     1 AD1 14 ARG C 257  TRP C 316  TYR C 342  CYS C 402                    
SITE     2 AD1 14 HIS C 403  GLN C 422  ARG C 423  SER C 424                    
SITE     3 AD1 14 ASP C 426  ASN C 434  HIS C 464  TYR C 466                    
SITE     4 AD1 14 OG4 C 603  ARG D 382                                          
SITE     1 AD2  8 SER C 290  ILE C 315  ASN C 319  ASP C 426                    
SITE     2 AD2  8 LEU C 429  PHE C 433  ALA C 520  UFP C 602                    
SITE     1 AD3 15 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 AD3 15 ASP C  32  LEU C  33  PHE C  36  SER C  37                    
SITE     3 AD3 15 THR C  58  ILE C  62  ARG C  70  CYS C 113                    
SITE     4 AD3 15 TYR C 119  THR C 134  NDP C 601                               
SITE     1 AD4 21 ALA D  11  ILE D  19  GLY D  20  GLY D  23                    
SITE     2 AD4 21 GLN D  24  GLY D  55  ARG D  56  LYS D  57                    
SITE     3 AD4 21 THR D  58  ILE D  75  SER D  76  SER D  77                    
SITE     4 AD4 21 SER D  78  ARG D  92  CYS D 113  GLY D 114                    
SITE     5 AD4 21 GLY D 115  GLU D 116  SER D 117  THR D 145                    
SITE     6 AD4 21 MTX D 604                                                     
SITE     1 AD5 14 ARG C 382  ARG C 383  ARG D 257  TYR D 342                    
SITE     2 AD5 14 CYS D 402  GLN D 422  ARG D 423  SER D 424                    
SITE     3 AD5 14 CYS D 425  ASP D 426  ASN D 434  HIS D 464                    
SITE     4 AD5 14 TYR D 466  OG4 D 603                                          
SITE     1 AD6 10 ALA D 287  SER D 290  ILE D 315  ASN D 319                    
SITE     2 AD6 10 ASP D 426  LEU D 429  PHE D 433  TYR D 466                    
SITE     3 AD6 10 ALA D 520  UFP D 602                                          
SITE     1 AD7 15 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 AD7 15 ASP D  32  LEU D  33  PHE D  36  SER D  37                    
SITE     3 AD7 15 THR D  58  ILE D  62  ARG D  70  CYS D 113                    
SITE     4 AD7 15 TYR D 119  THR D 134  NDP D 601                               
SITE     1 AD8 21 ALA E  11  ILE E  19  GLY E  23  GLN E  24                    
SITE     2 AD8 21 GLY E  55  ARG E  56  LYS E  57  THR E  58                    
SITE     3 AD8 21 ILE E  75  SER E  76  SER E  77  SER E  78                    
SITE     4 AD8 21 ARG E  92  CYS E 113  GLY E 114  GLY E 115                    
SITE     5 AD8 21 GLU E 116  SER E 117  ASP E 121  THR E 145                    
SITE     6 AD8 21 MTX E 604                                                     
SITE     1 AD9 12 ARG E 257  CYS E 402  HIS E 403  GLN E 422                    
SITE     2 AD9 12 ARG E 423  SER E 424  CYS E 425  ASP E 426                    
SITE     3 AD9 12 ASN E 434  HIS E 464  TYR E 466  OG4 E 603                    
SITE     1 AE1 11 ALA E 287  SER E 290  ILE E 315  ASN E 319                    
SITE     2 AE1 11 LEU E 399  ASP E 426  LEU E 429  PHE E 433                    
SITE     3 AE1 11 TYR E 466  ALA E 520  UFP E 602                               
SITE     1 AE2 15 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 AE2 15 ASP E  32  LEU E  33  PHE E  36  SER E  37                    
SITE     3 AE2 15 THR E  58  ILE E  62  ARG E  70  CYS E 113                    
SITE     4 AE2 15 TYR E 119  THR E 134  NDP E 601                               
CRYST1  213.994  116.238  221.672  90.00  94.75  90.00 C 1 2 1      20          
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      0.004673  0.000000  0.000389        0.00000                         
SCALE2      0.000000  0.008603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004527        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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