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Database: PDB
Entry: 6PF7
LinkDB: 6PF7
Original site: 6PF7 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUN-19   6PF7              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, FDUMP AND 2-(4-((2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2, 
TITLE    3 3-D]PYRIMIDIN-5-YL)METHYL)BENZAMIDO)BENZOIC 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 6PF7    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 132427                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.510                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 49.1029 -  6.7317    1.00     9544   143  0.1826 0.1959        
REMARK   3     2  6.7317 -  5.3453    1.00     9426   149  0.2062 0.2040        
REMARK   3     3  5.3453 -  4.6702    1.00     9397   142  0.1740 0.2121        
REMARK   3     4  4.6702 -  4.2435    1.00     9365   144  0.1661 0.2067        
REMARK   3     5  4.2435 -  3.9394    1.00     9326   143  0.1956 0.2354        
REMARK   3     6  3.9394 -  3.7073    1.00     9324   143  0.2238 0.2408        
REMARK   3     7  3.7073 -  3.5217    1.00     9320   145  0.2484 0.2971        
REMARK   3     8  3.5217 -  3.3684    1.00     9292   148  0.2683 0.3401        
REMARK   3     9  3.3684 -  3.2388    1.00     9343   134  0.2770 0.2968        
REMARK   3    10  3.2388 -  3.1270    1.00     9259   152  0.2906 0.3444        
REMARK   3    11  3.1270 -  3.0292    1.00     9345   132  0.2999 0.3822        
REMARK   3    12  3.0292 -  2.9427    1.00     9303   154  0.3493 0.3766        
REMARK   3    13  2.9427 -  2.8652    0.99     9255   137  0.3781 0.3792        
REMARK   3    14  2.8652 -  2.7953    0.96     8928   134  0.3614 0.4222        
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)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.610           
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          21422                                  
REMARK   3   ANGLE     :  0.517          29149                                  
REMARK   3   CHIRALITY :  0.043           3123                                  
REMARK   3   PLANARITY :  0.003           3726                                  
REMARK   3   DIHEDRAL  :  9.648          12417                                  
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 6PF7 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_1000242256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-15                          
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-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979180                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132650                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 1.11600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.260                              
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   (%): 73.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION 18 % 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      107.38700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.89450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.38700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.89450            
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: 14610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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: 14720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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: 14230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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      196.81248            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      219.40803            
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     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     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     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   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     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     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 103    CG   OD1  ND2                                       
REMARK 470     ASP A 104    CG   OD1  OD2                                       
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     GLU B   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
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     GLU B 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 180    CG   CD   CE   NZ                                   
REMARK 470     LYS B 220    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 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 500    CG   CD   CE   NZ                                   
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     GLU C   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS C   4    CG   CD   CE   NZ                                   
REMARK 470     LYS C  34    CG   CD   CE   NZ                                   
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     LYS C  49    CG   CD   CE   NZ                                   
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
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     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     GLU C 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 180    CG   CD   CE   NZ                                   
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     GLU C 222    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     GLU C 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 492    CG   CD   CE   NZ                                   
REMARK 470     LYS C 500    CG   CD   CE   NZ                                   
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     GLU D   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS D   4    CG   CD   CE   NZ                                   
REMARK 470     LYS D  34    CG   CD   CE   NZ                                   
REMARK 470     LYS D  48    CG   CD   CE   NZ                                   
REMARK 470     LYS D  68    CG   CD   CE   NZ                                   
REMARK 470     GLU D  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  95    CG   CD   OE1  OE2                                  
REMARK 470     MET D 102    CG   SD   CE                                        
REMARK 470     ASN D 103    CG   OD1  ND2                                       
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 180    CG   CD   CE   NZ                                   
REMARK 470     LYS D 217    CG   CD   CE   NZ                                   
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     GLU D 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 354    CG   CD   CE   NZ                                   
REMARK 470     LYS D 370    CG   CD   CE   NZ                                   
REMARK 470     GLU D 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 500    CG   CD   CE   NZ                                   
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     GLU E   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS E   4    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     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     GLU E  95    CG   CD   OE1  OE2                                  
REMARK 470     ASN E 100    CG   OD1  ND2                                       
REMARK 470     MET E 102    CG   SD   CE                                        
REMARK 470     ASN E 103    CG   OD1  ND2                                       
REMARK 470     LYS E 124    CG   CD   CE   NZ                                   
REMARK 470     GLU E 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 149    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 155    CG   CD1  CD2                                       
REMARK 470     GLU E 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 180    CG   CD   CE   NZ                                   
REMARK 470     LYS E 181    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 300    CG   CD   CE   NZ                                   
REMARK 470     LEU E 308    CG   CD1  CD2                                       
REMARK 470     ILE E 309    CG1  CG2  CD1                                       
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     ARG E 327    CG   CD   NE   CZ   NH1  NH2                        
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     LEU E 394    CG   CD1  CD2                                       
REMARK 470     LYS E 474    CG   CD   CE   NZ                                   
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     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    ASN A  47       38.06    -91.83                                   
REMARK 500    ASN A 103      -68.57    -93.53                                   
REMARK 500    CYS A 113       34.14   -158.90                                   
REMARK 500    ASP A 140       39.25    -90.73                                   
REMARK 500    GLU A 179     -143.42   -101.94                                   
REMARK 500    ALA A 287       86.21    -68.84                                   
REMARK 500    ILE A 341     -159.72   -132.77                                   
REMARK 500    LYS A 354      -87.45    -99.67                                   
REMARK 500    LEU B  15      -60.07   -101.16                                   
REMARK 500    ASN B  47       37.63    -91.99                                   
REMARK 500    ASN B 103      -66.86    -94.49                                   
REMARK 500    CYS B 113       34.18   -159.35                                   
REMARK 500    ASP B 140       39.77    -90.50                                   
REMARK 500    GLU B 179     -143.46   -103.89                                   
REMARK 500    ALA B 287       85.70    -67.95                                   
REMARK 500    ILE B 341     -158.43   -135.56                                   
REMARK 500    LYS B 354      -86.67   -101.10                                   
REMARK 500    LEU C  15      -60.17   -101.14                                   
REMARK 500    ASN C  47       38.63    -92.20                                   
REMARK 500    ASN C 103      -67.47    -96.38                                   
REMARK 500    CYS C 113       35.17   -159.32                                   
REMARK 500    ASP C 140       39.10    -89.18                                   
REMARK 500    GLU C 179     -143.39   -101.81                                   
REMARK 500    ALA C 287       86.84    -68.67                                   
REMARK 500    ILE C 341     -158.40   -134.56                                   
REMARK 500    LYS C 354      -87.30    -99.09                                   
REMARK 500    LEU D  15      -60.56   -101.65                                   
REMARK 500    ASN D  47       38.22    -91.97                                   
REMARK 500    ASN D 103      -67.17    -91.13                                   
REMARK 500    CYS D 113       34.50   -158.81                                   
REMARK 500    ASP D 140       40.08    -90.61                                   
REMARK 500    GLU D 179     -143.60   -103.53                                   
REMARK 500    ALA D 287       86.16    -68.45                                   
REMARK 500    ILE D 341     -158.72   -136.19                                   
REMARK 500    LYS D 354      -87.60   -101.02                                   
REMARK 500    LEU E  15      -60.68   -101.50                                   
REMARK 500    ASN E  47       37.73    -92.43                                   
REMARK 500    ASN E 103      -67.02    -92.76                                   
REMARK 500    CYS E 113       34.19   -159.32                                   
REMARK 500    ASP E 140       39.02    -90.51                                   
REMARK 500    GLU E 179     -145.40   -103.32                                   
REMARK 500    LYS E 194      -48.25   -154.76                                   
REMARK 500    ALA E 287       85.85    -69.67                                   
REMARK 500    ILE E 341     -159.28   -135.44                                   
REMARK 500    LYS E 354      -87.14   -100.31                                   
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 OG7 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 SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG7 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG7 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG7 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG7 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX E 604                 
DBREF1 6PF7 A    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF7 A     A0A0S4TER9                          1         521             
DBREF1 6PF7 B    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF7 B     A0A0S4TER9                          1         521             
DBREF1 6PF7 C    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF7 C     A0A0S4TER9                          1         521             
DBREF1 6PF7 D    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF7 D     A0A0S4TER9                          1         521             
DBREF1 6PF7 E    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF7 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    OG7  A 603      30                                                       
HET    MTX  A 604      33                                                       
HET    SO4  A 605       5                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    OG7  B 603      30                                                       
HET    MTX  B 604      33                                                       
HET    SO4  B 605       5                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    OG7  C 603      30                                                       
HET    MTX  C 604      33                                                       
HET    SO4  C 605       5                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    OG7  D 603      30                                                       
HET    MTX  D 604      33                                                       
HET    SO4  D 605       5                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    OG7  E 603      30                                                       
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     OG7 2-({4-[(2-AMINO-4-OXO-4,7-DIHYDRO-1H-PYRROLO[2,3-                
HETNAM   2 OG7  D]PYRIMIDIN-5-YL)METHYL]BENZENE-1-CARBONYL}AMINO)               
HETNAM   3 OG7  BENZOIC ACID                                                    
HETNAM     MTX METHOTREXATE                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  OG7    5(C21 H17 N5 O4)                                             
FORMUL   9  MTX    5(C20 H22 N8 O5)                                             
FORMUL  10  SO4    4(O4 S 2-)                                                   
FORMUL  30  HOH   *139(H2 O)                                                    
HELIX    1 AA1 ILE A   29  ASN A   42  1                                  14    
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 GLU A   99  LEU A  101  5                                   3    
HELIX    5 AA5 GLY A  114  ASP A  125  1                                  12    
HELIX    6 AA6 LYS A  194  PHE A  207  1                                  14    
HELIX    7 AA7 LYS A  211  HIS A  216  1                                   6    
HELIX    8 AA8 LYS A  220  TYR A  224  5                                   5    
HELIX    9 AA9 GLU A  237  GLY A  251  1                                  15    
HELIX   10 AB1 ALA A  287  LYS A  300  1                                  14    
HELIX   11 AB2 GLY A  305  GLU A  310  1                                   6    
HELIX   12 AB3 SER A  317  GLY A  320  5                                   4    
HELIX   13 AB4 SER A  321  ILE A  328  1                                   8    
HELIX   14 AB5 GLY A  343  HIS A  348  1                                   6    
HELIX   15 AB6 ASP A  366  ASN A  378  1                                  13    
HELIX   16 AB7 ALA A  393  MET A  397  5                                   5    
HELIX   17 AB8 LEU A  429  GLY A  450  1                                  22    
HELIX   18 AB9 HIS A  469  LEU A  477  1                                   9    
HELIX   19 AC1 ASN A  495  PHE A  499  5                                   5    
HELIX   20 AC2 LYS A  500  GLU A  502  5                                   3    
HELIX   21 AC3 ILE B   29  ASN B   42  1                                  14    
HELIX   22 AC4 ARG B   56  ILE B   62  1                                   7    
HELIX   23 AC5 ASN B   93  ILE B   98  1                                   6    
HELIX   24 AC6 ILE B   98  ASN B  103  1                                   6    
HELIX   25 AC7 GLY B  114  ASP B  125  1                                  12    
HELIX   26 AC8 LYS B  194  PHE B  207  1                                  14    
HELIX   27 AC9 LYS B  211  HIS B  216  1                                   6    
HELIX   28 AD1 LYS B  220  TYR B  224  5                                   5    
HELIX   29 AD2 GLU B  237  GLY B  251  1                                  15    
HELIX   30 AD3 ALA B  287  LYS B  300  1                                  14    
HELIX   31 AD4 GLY B  305  GLU B  310  1                                   6    
HELIX   32 AD5 SER B  317  GLY B  320  5                                   4    
HELIX   33 AD6 SER B  321  ILE B  328  1                                   8    
HELIX   34 AD7 ASP B  366  ASN B  378  1                                  13    
HELIX   35 AD8 ALA B  393  MET B  397  5                                   5    
HELIX   36 AD9 LEU B  429  GLY B  450  1                                  22    
HELIX   37 AE1 HIS B  469  SER B  478  1                                  10    
HELIX   38 AE2 ASN B  495  PHE B  499  5                                   5    
HELIX   39 AE3 LYS B  500  GLU B  502  5                                   3    
HELIX   40 AE4 ILE C   29  ASN C   42  1                                  14    
HELIX   41 AE5 ARG C   56  ILE C   62  1                                   7    
HELIX   42 AE6 GLU C   95  LEU C  101  5                                   7    
HELIX   43 AE7 GLY C  114  ASP C  125  1                                  12    
HELIX   44 AE8 LYS C  194  PHE C  207  1                                  14    
HELIX   45 AE9 LYS C  211  HIS C  216  1                                   6    
HELIX   46 AF1 LYS C  220  TYR C  224  5                                   5    
HELIX   47 AF2 GLU C  237  GLY C  251  1                                  15    
HELIX   48 AF3 ALA C  287  LYS C  300  1                                  14    
HELIX   49 AF4 GLY C  305  GLU C  310  1                                   6    
HELIX   50 AF5 SER C  317  GLY C  320  5                                   4    
HELIX   51 AF6 SER C  321  ILE C  328  1                                   8    
HELIX   52 AF7 ASP C  366  ASN C  378  1                                  13    
HELIX   53 AF8 ALA C  393  MET C  397  5                                   5    
HELIX   54 AF9 LEU C  429  GLY C  450  1                                  22    
HELIX   55 AG1 HIS C  469  SER C  478  1                                  10    
HELIX   56 AG2 ASN C  495  PHE C  499  5                                   5    
HELIX   57 AG3 LYS C  500  GLU C  502  5                                   3    
HELIX   58 AG4 ILE D   29  ASN D   42  1                                  14    
HELIX   59 AG5 ARG D   56  ILE D   62  1                                   7    
HELIX   60 AG6 ASN D   93  ILE D   98  1                                   6    
HELIX   61 AG7 GLU D   99  LEU D  101  5                                   3    
HELIX   62 AG8 GLY D  114  ASP D  125  1                                  12    
HELIX   63 AG9 LYS D  194  PHE D  207  1                                  14    
HELIX   64 AH1 LYS D  211  HIS D  216  1                                   6    
HELIX   65 AH2 LYS D  220  TYR D  224  5                                   5    
HELIX   66 AH3 GLU D  237  GLY D  251  1                                  15    
HELIX   67 AH4 ALA D  287  LYS D  300  1                                  14    
HELIX   68 AH5 GLY D  305  GLU D  310  1                                   6    
HELIX   69 AH6 SER D  317  GLY D  320  5                                   4    
HELIX   70 AH7 SER D  321  ILE D  328  1                                   8    
HELIX   71 AH8 ASP D  366  ASN D  378  1                                  13    
HELIX   72 AH9 ALA D  393  MET D  397  5                                   5    
HELIX   73 AI1 LEU D  429  GLY D  450  1                                  22    
HELIX   74 AI2 HIS D  469  SER D  478  1                                  10    
HELIX   75 AI3 ASN D  495  PHE D  499  5                                   5    
HELIX   76 AI4 LYS D  500  GLU D  502  5                                   3    
HELIX   77 AI5 ILE E   29  ASN E   42  1                                  14    
HELIX   78 AI6 ARG E   56  ILE E   62  1                                   7    
HELIX   79 AI7 GLU E   95  SER E   97  5                                   3    
HELIX   80 AI8 ILE E   98  ASN E  103  1                                   6    
HELIX   81 AI9 GLY E  114  ASP E  125  1                                  12    
HELIX   82 AJ1 SER E  195  PHE E  207  1                                  13    
HELIX   83 AJ2 LYS E  211  HIS E  216  1                                   6    
HELIX   84 AJ3 LYS E  220  TYR E  224  5                                   5    
HELIX   85 AJ4 GLU E  237  GLY E  251  1                                  15    
HELIX   86 AJ5 ALA E  287  LYS E  300  1                                  14    
HELIX   87 AJ6 GLY E  305  GLU E  310  1                                   6    
HELIX   88 AJ7 SER E  317  GLY E  320  5                                   4    
HELIX   89 AJ8 SER E  321  ILE E  328  1                                   8    
HELIX   90 AJ9 ASP E  366  ASN E  378  1                                  13    
HELIX   91 AK1 ALA E  393  MET E  397  5                                   5    
HELIX   92 AK2 LEU E  429  GLY E  450  1                                  22    
HELIX   93 AK3 HIS E  469  SER E  478  1                                  10    
HELIX   94 AK4 ASN E  495  PHE E  499  5                                   5    
HELIX   95 AK5 LYS E  500  GLU E  502  5                                   3    
SHEET    1 AA1 8 VAL A  88  PHE A  91  0                                        
SHEET    2 AA1 8 ILE A  71  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3 AA1 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4 AA1 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5 AA1 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6 AA1 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7 AA1 8 MET A 173  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA1 8 PHE A 154  MET A 159 -1  N  LEU A 155   O  GLU A 176           
SHEET    1 AA2 2 GLY A  18  GLY A  20  0                                        
SHEET    2 AA2 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
SHEET    1 AA3 2 PHE A 163  THR A 165  0                                        
SHEET    2 AA3 2 ILE A 168  TYR A 170 -1  O  TYR A 170   N  PHE A 163           
SHEET    1 AA4 6 ALA A 252  ARG A 254  0                                        
SHEET    2 AA4 6 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3 AA4 6 GLU A 452  TYR A 466 -1  O  ILE A 460   N  GLN A 268           
SHEET    4 AA4 6 CYS A 415  ASP A 426  1  N  ARG A 423   O  ASP A 462           
SHEET    5 AA4 6 HIS A 403  VAL A 410 -1  N  GLN A 407   O  ASN A 419           
SHEET    6 AA4 6 ILE A 385  THR A 387 -1  N  LEU A 386   O  SER A 406           
SHEET    1 AA5 2 GLN A 486  PHE A 489  0                                        
SHEET    2 AA5 2 ILE A 504  ILE A 507 -1  O  ILE A 507   N  GLN A 486           
SHEET    1 AA6 8 VAL B  88  PHE B  91  0                                        
SHEET    2 AA6 8 ILE B  71  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3 AA6 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4 AA6 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5 AA6 8 ASN B   5  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6 AA6 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7 AA6 8 MET B 173  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA6 8 PHE B 154  MET B 159 -1  N  LEU B 155   O  GLU B 176           
SHEET    1 AA7 2 GLY B  18  GLY B  20  0                                        
SHEET    2 AA7 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
SHEET    1 AA8 2 PHE B 163  THR B 165  0                                        
SHEET    2 AA8 2 ILE B 168  TYR B 170 -1  O  TYR B 170   N  PHE B 163           
SHEET    1 AA9 6 ALA B 252  ARG B 254  0                                        
SHEET    2 AA9 6 THR B 262  ASP B 273 -1  O  THR B 262   N  ARG B 254           
SHEET    3 AA9 6 GLU B 452  TYR B 466 -1  O  ILE B 460   N  GLN B 268           
SHEET    4 AA9 6 CYS B 415  ASP B 426  1  N  LEU B 420   O  PHE B 459           
SHEET    5 AA9 6 HIS B 403  VAL B 410 -1  N  GLN B 407   O  ASN B 419           
SHEET    6 AA9 6 ILE B 385  THR B 387 -1  N  LEU B 386   O  SER B 406           
SHEET    1 AB1 2 GLN B 486  PHE B 489  0                                        
SHEET    2 AB1 2 ILE B 504  ILE B 507 -1  O  ILE B 507   N  GLN B 486           
SHEET    1 AB2 8 VAL C  88  PHE C  91  0                                        
SHEET    2 AB2 8 ILE C  71  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3 AB2 8 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4 AB2 8 ILE C 107  VAL C 112  1  O  PHE C 111   N  ILE C  53           
SHEET    5 AB2 8 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6 AB2 8 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7 AB2 8 MET C 173  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8 AB2 8 PHE C 154  MET C 159 -1  N  VAL C 157   O  ILE C 174           
SHEET    1 AB3 2 GLY C  18  GLY C  20  0                                        
SHEET    2 AB3 2 THR C 145  TYR C 146 -1  O  THR C 145   N  ILE C  19           
SHEET    1 AB4 2 PHE C 163  THR C 165  0                                        
SHEET    2 AB4 2 ILE C 168  TYR C 170 -1  O  TYR C 170   N  PHE C 163           
SHEET    1 AB5 6 ALA C 252  ARG C 254  0                                        
SHEET    2 AB5 6 THR C 262  ASP C 273 -1  O  SER C 264   N  ALA C 252           
SHEET    3 AB5 6 GLU C 452  TYR C 466 -1  O  ILE C 460   N  GLN C 268           
SHEET    4 AB5 6 CYS C 415  ASP C 426  1  N  LEU C 420   O  PHE C 459           
SHEET    5 AB5 6 HIS C 403  VAL C 410 -1  N  GLN C 407   O  ASN C 419           
SHEET    6 AB5 6 ILE C 385  THR C 387 -1  N  LEU C 386   O  SER C 406           
SHEET    1 AB6 2 GLN C 486  PHE C 489  0                                        
SHEET    2 AB6 2 ILE C 504  ILE C 507 -1  O  ILE C 507   N  GLN C 486           
SHEET    1 AB7 8 VAL D  88  PHE D  91  0                                        
SHEET    2 AB7 8 ILE D  71  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3 AB7 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4 AB7 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5 AB7 8 ASN D   5  SER D  13  1  N  SER D   7   O  ILE D 110           
SHEET    6 AB7 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB7 8 MET D 173  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB7 8 PHE D 154  MET D 159 -1  N  VAL D 157   O  ILE D 174           
SHEET    1 AB8 2 GLY D  18  GLY D  20  0                                        
SHEET    2 AB8 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
SHEET    1 AB9 2 PHE D 163  THR D 165  0                                        
SHEET    2 AB9 2 ILE D 168  TYR D 170 -1  O  TYR D 170   N  PHE D 163           
SHEET    1 AC1 6 ALA D 252  ARG D 254  0                                        
SHEET    2 AC1 6 THR D 262  ASP D 273 -1  O  THR D 262   N  ARG D 254           
SHEET    3 AC1 6 GLU D 452  TYR D 466 -1  O  ILE D 460   N  GLN D 268           
SHEET    4 AC1 6 CYS D 415  ASP D 426  1  N  LEU D 420   O  PHE D 459           
SHEET    5 AC1 6 HIS D 403  VAL D 410 -1  N  GLN D 407   O  ASN D 419           
SHEET    6 AC1 6 ILE D 385  THR D 387 -1  N  LEU D 386   O  SER D 406           
SHEET    1 AC2 2 GLN D 486  PHE D 489  0                                        
SHEET    2 AC2 2 ILE D 504  ILE D 507 -1  O  ILE D 507   N  GLN D 486           
SHEET    1 AC3 8 VAL E  88  PHE E  91  0                                        
SHEET    2 AC3 8 ARG E  70  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3 AC3 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4 AC3 8 ILE E 107  VAL E 112  1  O  PHE E 111   N  ILE E  53           
SHEET    5 AC3 8 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6 AC3 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7 AC3 8 MET E 173  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8 AC3 8 PHE E 154  MET E 159 -1  N  VAL E 157   O  ILE E 174           
SHEET    1 AC4 2 GLY E  18  GLY E  20  0                                        
SHEET    2 AC4 2 THR E 145  TYR E 146 -1  O  THR E 145   N  ILE E  19           
SHEET    1 AC5 2 PHE E 163  THR E 165  0                                        
SHEET    2 AC5 2 ILE E 168  TYR E 170 -1  O  TYR E 170   N  PHE E 163           
SHEET    1 AC6 6 ALA E 252  ARG E 254  0                                        
SHEET    2 AC6 6 THR E 262  ASP E 273 -1  O  THR E 262   N  ARG E 254           
SHEET    3 AC6 6 GLU E 452  TYR E 466 -1  O  ILE E 460   N  GLN E 268           
SHEET    4 AC6 6 CYS E 415  ASP E 426  1  N  LEU E 420   O  PHE E 459           
SHEET    5 AC6 6 HIS E 403  VAL E 410 -1  N  GLN E 407   O  ASN E 419           
SHEET    6 AC6 6 ILE E 385  THR E 387 -1  N  LEU E 386   O  SER E 406           
SHEET    1 AC7 2 GLN E 486  PHE E 489  0                                        
SHEET    2 AC7 2 ILE E 504  ILE E 507 -1  O  ILE E 507   N  GLN E 486           
SITE     1 AC1 24 VAL A  10  ALA A  11  ILE A  19  GLY A  20                    
SITE     2 AC1 24 GLY A  23  GLN A  24  LEU A  25  GLY A  55                    
SITE     3 AC1 24 ARG A  56  LYS A  57  THR A  58  ILE A  75                    
SITE     4 AC1 24 SER A  76  SER A  77  SER A  78  ARG A  92                    
SITE     5 AC1 24 CYS A 113  GLY A 114  GLY A 115  GLU A 116                    
SITE     6 AC1 24 SER A 117  THR A 145  MTX A 604  HOH A 740                    
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 OG7 A 603  ARG B 382  ARG B 383                               
SITE     1 AC3  9 ILE A 315  ASN A 319  LEU A 399  ASP A 426                    
SITE     2 AC3  9 LEU A 429  GLY A 430  PHE A 433  ALA A 520                    
SITE     3 AC3  9 UFP A 602                                                     
SITE     1 AC4 15 VAL A   9  VAL A  10  ALA A  11  ASP A  32                    
SITE     2 AC4 15 PHE A  36  SER A  37  THR A  58  ILE A  62                    
SITE     3 AC4 15 LEU A  67  ARG A  70  CYS A 113  TYR A 119                    
SITE     4 AC4 15 THR A 134  NDP A 601  HOH A 702                               
SITE     1 AC5  5 HIS A 216  ARG A 246  GLN A 268  HOH A 728                    
SITE     2 AC5  5 ARG B 271                                                     
SITE     1 AC6 24 VAL B  10  ALA B  11  ILE B  19  GLY B  20                    
SITE     2 AC6 24 GLY B  23  GLN B  24  LEU B  25  GLY B  55                    
SITE     3 AC6 24 ARG B  56  LYS B  57  THR B  58  ILE B  75                    
SITE     4 AC6 24 SER B  76  SER B  77  SER B  78  ARG B  92                    
SITE     5 AC6 24 CYS B 113  GLY B 114  GLY B 115  GLU B 116                    
SITE     6 AC6 24 SER B 117  ASP B 121  THR B 145  MTX B 604                    
SITE     1 AC7 13 ARG A 382  ARG A 383  ARG B 257  CYS B 402                    
SITE     2 AC7 13 HIS B 403  ARG B 423  SER B 424  CYS B 425                    
SITE     3 AC7 13 ASP B 426  ASN B 434  HIS B 464  TYR B 466                    
SITE     4 AC7 13 OG7 B 603                                                     
SITE     1 AC8 11 ALA B 287  ILE B 315  ASN B 319  LEU B 399                    
SITE     2 AC8 11 ASP B 426  LEU B 429  GLY B 430  PHE B 433                    
SITE     3 AC8 11 TYR B 466  ALA B 520  UFP B 602                               
SITE     1 AC9 15 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC9 15 ASP B  32  LEU B  33  PHE B  36  SER B  37                    
SITE     3 AC9 15 THR B  58  ILE B  62  ARG B  70  CYS B 113                    
SITE     4 AC9 15 TYR B 119  THR B 134  NDP B 601                               
SITE     1 AD1  5 ARG A 271  HIS B 216  ARG B 246  GLN B 268                    
SITE     2 AD1  5 HOH B 714                                                     
SITE     1 AD2 23 ALA C  11  ILE C  19  GLY C  20  ILE C  21                    
SITE     2 AD2 23 GLY C  23  GLN C  24  GLY C  55  ARG C  56                    
SITE     3 AD2 23 LYS C  57  THR C  58  ILE C  75  SER C  76                    
SITE     4 AD2 23 SER C  77  SER C  78  ARG C  92  CYS C 113                    
SITE     5 AD2 23 GLY C 114  GLY C 115  GLU C 116  SER C 117                    
SITE     6 AD2 23 ASP C 121  THR C 145  MTX C 604                               
SITE     1 AD3 14 ARG C 257  CYS C 402  HIS C 403  GLN C 422                    
SITE     2 AD3 14 ARG C 423  SER C 424  CYS C 425  ASP C 426                    
SITE     3 AD3 14 ASN C 434  HIS C 464  TYR C 466  OG7 C 603                    
SITE     4 AD3 14 ARG D 382  ARG D 383                                          
SITE     1 AD4  8 ILE C 315  ASN C 319  LEU C 399  ASP C 426                    
SITE     2 AD4  8 LEU C 429  GLY C 430  ALA C 520  UFP C 602                    
SITE     1 AD5 15 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 AD5 15 ASP C  32  LEU C  33  PHE C  36  SER C  37                    
SITE     3 AD5 15 THR C  58  ILE C  62  LEU C  67  ARG C  70                    
SITE     4 AD5 15 CYS C 113  THR C 134  NDP C 601                               
SITE     1 AD6  4 HIS C 216  ARG C 246  GLN C 268  ARG D 271                    
SITE     1 AD7 25 ALA D  11  ILE D  19  GLY D  20  ILE D  21                    
SITE     2 AD7 25 GLY D  23  GLN D  24  LEU D  25  GLY D  55                    
SITE     3 AD7 25 ARG D  56  LYS D  57  THR D  58  ILE D  75                    
SITE     4 AD7 25 SER D  76  SER D  77  SER D  78  ARG D  92                    
SITE     5 AD7 25 CYS D 113  GLY D 114  GLY D 115  GLU D 116                    
SITE     6 AD7 25 SER D 117  ASP D 121  THR D 145  MTX D 604                    
SITE     7 AD7 25 HOH D 717                                                     
SITE     1 AD8 15 ARG C 382  ARG C 383  ARG D 257  LEU D 399                    
SITE     2 AD8 15 CYS D 402  HIS D 403  GLN D 422  ARG D 423                    
SITE     3 AD8 15 SER D 424  CYS D 425  ASP D 426  ASN D 434                    
SITE     4 AD8 15 HIS D 464  TYR D 466  OG7 D 603                               
SITE     1 AD9 11 ALA D 287  ILE D 315  ASN D 319  LEU D 399                    
SITE     2 AD9 11 ASP D 426  LEU D 429  GLY D 430  PHE D 433                    
SITE     3 AD9 11 MET D 519  ALA D 520  UFP D 602                               
SITE     1 AE1 14 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 AE1 14 ASP D  32  PHE D  36  SER D  37  THR D  58                    
SITE     3 AE1 14 ILE D  62  LEU D  67  ARG D  70  CYS D 113                    
SITE     4 AE1 14 THR D 134  NDP D 601                                          
SITE     1 AE2  3 HIS D 216  ARG D 246  GLN D 268                               
SITE     1 AE3 24 VAL E  10  ALA E  11  ILE E  19  GLY E  20                    
SITE     2 AE3 24 GLY E  23  GLN E  24  GLY E  55  ARG E  56                    
SITE     3 AE3 24 LYS E  57  THR E  58  ILE E  75  SER E  76                    
SITE     4 AE3 24 SER E  77  SER E  78  ARG E  92  CYS E 113                    
SITE     5 AE3 24 GLY E 114  GLY E 115  GLU E 116  SER E 117                    
SITE     6 AE3 24 ASP E 121  THR E 145  MTX E 604  HOH E 701                    
SITE     1 AE4 14 ARG E 257  ARG E 382  ARG E 383  CYS E 402                    
SITE     2 AE4 14 HIS E 403  GLN E 422  ARG E 423  SER E 424                    
SITE     3 AE4 14 CYS E 425  ASP E 426  ASN E 434  HIS E 464                    
SITE     4 AE4 14 TYR E 466  OG7 E 603                                          
SITE     1 AE5  9 ALA E 287  ILE E 315  ASP E 426  LEU E 429                    
SITE     2 AE5  9 GLY E 430  PHE E 433  MET E 519  ALA E 520                    
SITE     3 AE5  9 UFP E 602                                                     
SITE     1 AE6 15 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 AE6 15 ASP E  32  LEU E  33  PHE E  36  SER E  37                    
SITE     3 AE6 15 THR E  58  ILE E  62  LEU E  67  ARG E  70                    
SITE     4 AE6 15 CYS E 113  THR E 134  NDP E 601                               
CRYST1  214.774  115.789  220.142  90.00  94.68  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      0.004656  0.000000  0.000381        0.00000                         
SCALE2      0.000000  0.008636  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004558        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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