GenomeNet

Database: PDB
Entry: 6PFI
LinkDB: 6PFI
Original site: 6PFI 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUN-19   6PFI              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, FDUMP AND 3-(4-((2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2, 
TITLE    3 3-D]PYRIMIDIN-5-YL)METHYL)BENZAMIDO)-4-(CARBOXYMETHYL)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,K.S.ANDERSON,W.L.JORGENSEN,M.VALHONDO                      
REVDAT   1   02-OCT-19 6PFI    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.    2.89 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) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 119210                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.680                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 48.5955 -  6.9592    0.99     8636   148  0.1846 0.2054        
REMARK   3     2  6.9592 -  5.5262    0.98     8404   142  0.2075 0.2535        
REMARK   3     3  5.5262 -  4.8284    1.00     8555   147  0.1779 0.1958        
REMARK   3     4  4.8284 -  4.3872    0.97     8292   141  0.1680 0.2087        
REMARK   3     5  4.3872 -  4.0730    0.99     8470   145  0.1779 0.2325        
REMARK   3     6  4.0730 -  3.8329    1.00     8464   144  0.2038 0.2476        
REMARK   3     7  3.8329 -  3.6410    1.00     8482   144  0.2143 0.2732        
REMARK   3     8  3.6410 -  3.4826    0.97     8255   141  0.2450 0.2664        
REMARK   3     9  3.4826 -  3.3486    0.99     8391   143  0.2529 0.3364        
REMARK   3    10  3.3486 -  3.2330    0.99     8451   144  0.2558 0.2971        
REMARK   3    11  3.2330 -  3.1320    0.99     8367   143  0.2849 0.3333        
REMARK   3    12  3.1320 -  3.0424    0.99     8400   143  0.3075 0.3544        
REMARK   3    13  3.0424 -  2.9624    0.99     8410   143  0.3308 0.3666        
REMARK   3    14  2.9624 -  2.8901    0.90     7635   130  0.3641 0.3772        
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) : 28.870           
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          21458                                  
REMARK   3   ANGLE     :  0.505          29178                                  
REMARK   3   CHIRALITY :  0.043           3119                                  
REMARK   3   PLANARITY :  0.003           3721                                  
REMARK   3   DIHEDRAL  :  9.383          12468                                  
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 6PFI 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_1000242218.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979200                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 119315                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.25500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.1800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 1.32400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4Q0E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION 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      106.69000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.37050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.69000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.37050            
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: 14140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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: 14160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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: 14240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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     -213.38000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLN A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     CYS A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     GLN A   192                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     GLN B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     CYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     LYS C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     THR C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     CYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     GLN C   192                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     LYS D   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     LYS E   180                                                      
REMARK 465     LYS E   181                                                      
REMARK 465     THR E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     GLN E   184                                                      
REMARK 465     ASN E   185                                                      
REMARK 465     CYS E   186                                                      
REMARK 465     ASP E   187                                                      
REMARK 465     PRO E   188                                                      
REMARK 465     ALA E   189                                                      
REMARK 465     ARG E   190                                                      
REMARK 465     GLY E   191                                                      
REMARK 465     GLN E   192                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  95    CG   CD   OE1  OE2                                  
REMARK 470     MET A 102    CG   SD   CE                                        
REMARK 470     ASP A 105    CG   OD1  OD2                                       
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 193    CG   CD1  CD2                                       
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
REMARK 470     LYS A 312    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 500    CG   CD   CE   NZ                                   
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     LYS B  48    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
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 322    CG   CD   CE   NZ                                   
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     LYS C  48    CG   CD   CE   NZ                                   
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     MET C 102    CG   SD   CE                                        
REMARK 470     GLN C 178    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 179    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 193    CG   CD1  CD2                                       
REMARK 470     LYS C 217    CG   CD   CE   NZ                                   
REMARK 470     LYS C 220    CG   CD   CE   NZ                                   
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     GLU C 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 500    CG   CD   CE   NZ                                   
REMARK 470     GLU C 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     ASP D  45    CG   OD1  OD2                                       
REMARK 470     LYS D  48    CG   CD   CE   NZ                                   
REMARK 470     LYS D  49    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     ASP D 105    CG   OD1  OD2                                       
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 180    CG   CD   CE   NZ                                   
REMARK 470     LEU D 193    CG   CD1  CD2                                       
REMARK 470     LYS D 220    CG   CD   CE   NZ                                   
REMARK 470     ARG D 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 255    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     LYS D 516    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  68    CG   CD   CE   NZ                                   
REMARK 470     GLN E  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  95    CG   CD   OE1  OE2                                  
REMARK 470     MET E 102    CG   SD   CE                                        
REMARK 470     LYS E 124    CG   CD   CE   NZ                                   
REMARK 470     GLU E 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 220    CG   CD   CE   NZ                                   
REMARK 470     ARG E 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 255    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 300    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     LYS E 492    CG   CD   CE   NZ                                   
REMARK 470     GLU E 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 500    CG   CD   CE   NZ                                   
REMARK 470     GLU E 502    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 516    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  15      -61.20   -105.70                                   
REMARK 500    ASP A 104       79.48     54.25                                   
REMARK 500    CYS A 113       27.43   -158.47                                   
REMARK 500    ASP A 140       42.42    -95.28                                   
REMARK 500    GLU A 334     -174.96    -69.96                                   
REMARK 500    ILE A 341     -153.37   -124.32                                   
REMARK 500    HIS A 348       58.42   -140.73                                   
REMARK 500    LYS A 354      -81.58   -115.60                                   
REMARK 500    ASN A 378       80.67   -150.14                                   
REMARK 500    ARG A 382       33.34    -99.52                                   
REMARK 500    ASP A 413       30.05    -91.73                                   
REMARK 500    LEU A 429      -55.59   -122.77                                   
REMARK 500    ASP B 104       79.06     54.16                                   
REMARK 500    CYS B 113       26.33   -158.02                                   
REMARK 500    ASP B 140       42.57    -95.54                                   
REMARK 500    GLU B 334     -175.51    -67.77                                   
REMARK 500    ILE B 341     -153.87   -123.62                                   
REMARK 500    HIS B 348       58.42   -140.66                                   
REMARK 500    LYS B 354      -81.20   -114.19                                   
REMARK 500    ARG B 382       33.57    -99.50                                   
REMARK 500    ASP B 413       30.27    -91.61                                   
REMARK 500    LEU B 429      -55.88   -122.91                                   
REMARK 500    LEU C  15      -61.82   -105.53                                   
REMARK 500    ASP C 104       78.51     53.65                                   
REMARK 500    CYS C 113       28.01   -158.07                                   
REMARK 500    ASN C 126       60.77     60.52                                   
REMARK 500    ASP C 140       42.44    -94.22                                   
REMARK 500    LYS C 194      -53.74   -141.01                                   
REMARK 500    GLU C 334     -174.85    -68.86                                   
REMARK 500    ILE C 341     -153.68   -124.31                                   
REMARK 500    HIS C 348       58.59   -140.69                                   
REMARK 500    LYS C 354      -80.94   -116.04                                   
REMARK 500    ASN C 378       80.79   -150.14                                   
REMARK 500    ASP C 413       30.19    -90.85                                   
REMARK 500    LEU C 429      -55.47   -122.91                                   
REMARK 500    LEU D  15      -60.79   -105.98                                   
REMARK 500    ASP D 104       78.53     55.73                                   
REMARK 500    CYS D 113       27.64   -157.97                                   
REMARK 500    ASP D 140       42.33    -95.60                                   
REMARK 500    GLU D 179     -120.36   -124.17                                   
REMARK 500    GLU D 334     -175.60    -68.69                                   
REMARK 500    ILE D 341     -153.71   -123.69                                   
REMARK 500    HIS D 348       58.31   -140.78                                   
REMARK 500    LYS D 354      -81.08   -114.30                                   
REMARK 500    ASN D 378       82.05   -150.73                                   
REMARK 500    ARG D 382       33.83    -99.45                                   
REMARK 500    LEU D 429      -55.30   -122.44                                   
REMARK 500    LEU E  15      -61.32   -105.73                                   
REMARK 500    ASP E 104       79.29     56.40                                   
REMARK 500    CYS E 113       27.04   -157.73                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEP A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEP B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEP C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEP D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEP E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX E 604                 
DBREF1 6PFI A    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFI A     A0A0S4TER9                          1         521             
DBREF1 6PFI B    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFI B     A0A0S4TER9                          1         521             
DBREF1 6PFI C    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFI C     A0A0S4TER9                          1         521             
DBREF1 6PFI D    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFI D     A0A0S4TER9                          1         521             
DBREF1 6PFI E    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFI 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    OEP  A 603      34                                                       
HET    MTX  A 604      33                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    OEP  B 603      34                                                       
HET    MTX  B 604      33                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    OEP  C 603      34                                                       
HET    MTX  C 604      33                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    OEP  D 603      34                                                       
HET    MTX  D 604      33                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    OEP  E 603      34                                                       
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     OEP 3-({4-[(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-                
HETNAM   2 OEP  D]PYRIMIDIN-5-YL)METHYL]BENZENE-1-CARBONYL}AMINO)-4-            
HETNAM   3 OEP  (CARBOXYMETHYL)BENZOIC ACID                                     
HETNAM     MTX METHOTREXATE                                                     
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  OEP    5(C23 H19 N5 O6)                                             
FORMUL   9  MTX    5(C20 H22 N8 O5)                                             
FORMUL  26  HOH   *26(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 GLY A  114  ASP A  125  1                                  12    
HELIX    5 AA5 SER A  195  PHE A  207  1                                  13    
HELIX    6 AA6 LYS A  211  HIS A  216  1                                   6    
HELIX    7 AA7 LYS A  220  TYR A  224  5                                   5    
HELIX    8 AA8 GLU A  237  GLY A  251  1                                  15    
HELIX    9 AA9 ALA A  287  LYS A  300  1                                  14    
HELIX   10 AB1 GLY A  305  GLU A  310  1                                   6    
HELIX   11 AB2 SER A  317  GLY A  320  5                                   4    
HELIX   12 AB3 SER A  321  ILE A  328  1                                   8    
HELIX   13 AB4 GLY A  343  HIS A  348  1                                   6    
HELIX   14 AB5 ASP A  366  ASN A  378  1                                  13    
HELIX   15 AB6 ALA A  393  MET A  397  5                                   5    
HELIX   16 AB7 LEU A  429  GLY A  450  1                                  22    
HELIX   17 AB8 HIS A  469  LEU A  477  1                                   9    
HELIX   18 AB9 ASN A  495  PHE A  499  5                                   5    
HELIX   19 AC1 LYS A  500  GLU A  502  5                                   3    
HELIX   20 AC2 ILE B   29  ASN B   42  1                                  14    
HELIX   21 AC3 ARG B   56  ILE B   62  1                                   7    
HELIX   22 AC4 ASN B   93  ILE B   98  1                                   6    
HELIX   23 AC5 GLY B  114  ASP B  125  1                                  12    
HELIX   24 AC6 LYS B  194  PHE B  207  1                                  14    
HELIX   25 AC7 LYS B  211  HIS B  216  1                                   6    
HELIX   26 AC8 LYS B  220  TYR B  224  5                                   5    
HELIX   27 AC9 GLU B  237  GLY B  251  1                                  15    
HELIX   28 AD1 ALA B  287  LYS B  300  1                                  14    
HELIX   29 AD2 GLY B  305  GLU B  310  1                                   6    
HELIX   30 AD3 SER B  317  GLY B  320  5                                   4    
HELIX   31 AD4 SER B  321  ILE B  328  1                                   8    
HELIX   32 AD5 GLY B  343  HIS B  348  1                                   6    
HELIX   33 AD6 ASP B  366  ASN B  378  1                                  13    
HELIX   34 AD7 ALA B  393  MET B  397  5                                   5    
HELIX   35 AD8 LEU B  429  GLY B  450  1                                  22    
HELIX   36 AD9 HIS B  469  LEU B  477  1                                   9    
HELIX   37 AE1 ASN B  495  PHE B  499  5                                   5    
HELIX   38 AE2 LYS B  500  GLU B  502  5                                   3    
HELIX   39 AE3 ILE C   29  ASN C   42  1                                  14    
HELIX   40 AE4 ARG C   56  ILE C   62  1                                   7    
HELIX   41 AE5 ASN C   93  ILE C   98  1                                   6    
HELIX   42 AE6 GLY C  114  ASP C  125  1                                  12    
HELIX   43 AE7 LYS C  194  PHE C  207  1                                  14    
HELIX   44 AE8 LYS C  211  HIS C  216  1                                   6    
HELIX   45 AE9 LYS C  220  TYR C  224  5                                   5    
HELIX   46 AF1 GLU C  237  GLY C  251  1                                  15    
HELIX   47 AF2 ALA C  287  LYS C  300  1                                  14    
HELIX   48 AF3 GLY C  305  GLU C  310  1                                   6    
HELIX   49 AF4 SER C  317  GLY C  320  5                                   4    
HELIX   50 AF5 SER C  321  ILE C  328  1                                   8    
HELIX   51 AF6 GLY C  343  HIS C  348  1                                   6    
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  LEU C  477  1                                   9    
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 GLY D  114  ASP D  125  1                                  12    
HELIX   62 AG8 LYS D  194  PHE D  207  1                                  14    
HELIX   63 AG9 LYS D  211  HIS D  216  1                                   6    
HELIX   64 AH1 LYS D  220  TYR D  224  5                                   5    
HELIX   65 AH2 GLU D  237  GLY D  251  1                                  15    
HELIX   66 AH3 ALA D  287  LYS D  300  1                                  14    
HELIX   67 AH4 GLY D  305  GLU D  310  1                                   6    
HELIX   68 AH5 SER D  317  GLY D  320  5                                   4    
HELIX   69 AH6 SER D  321  ILE D  328  1                                   8    
HELIX   70 AH7 GLY D  343  HIS D  348  1                                   6    
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 ASN E   93  ILE E   98  1                                   6    
HELIX   80 AI8 GLY E  114  ASP E  125  1                                  12    
HELIX   81 AI9 LYS E  194  PHE E  207  1                                  14    
HELIX   82 AJ1 LYS E  211  HIS E  216  1                                   6    
HELIX   83 AJ2 LYS E  220  TYR E  224  5                                   5    
HELIX   84 AJ3 GLU E  237  GLY E  251  1                                  15    
HELIX   85 AJ4 ALA E  287  LYS E  300  1                                  14    
HELIX   86 AJ5 GLY E  305  GLU E  310  1                                   6    
HELIX   87 AJ6 SER E  317  GLY E  320  5                                   4    
HELIX   88 AJ7 SER E  321  ILE E  328  1                                   8    
HELIX   89 AJ8 ASP E  366  ASN E  378  1                                  13    
HELIX   90 AJ9 ALA E  393  MET E  397  5                                   5    
HELIX   91 AK1 LEU E  429  GLY E  450  1                                  22    
HELIX   92 AK2 HIS E  469  LEU E  477  1                                   9    
HELIX   93 AK3 ASN E  495  PHE E  499  5                                   5    
HELIX   94 AK4 LYS E  500  GLU E  502  5                                   3    
SHEET    1 AA1 8 VAL A  88  PHE A  91  0                                        
SHEET    2 AA1 8 ARG A  70  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 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA1 8 PHE A 154  MET A 159 -1  N  VAL A 157   O  ILE A 174           
SHEET    1 AA2 8 VAL A  88  PHE A  91  0                                        
SHEET    2 AA2 8 ARG A  70  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3 AA2 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4 AA2 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5 AA2 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6 AA2 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7 AA2 8 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA2 8 PHE A 163  THR A 165 -1  N  PHE A 163   O  TYR A 170           
SHEET    1 AA3 2 GLY A  18  GLY A  20  0                                        
SHEET    2 AA3 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
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  LEU A 420   O  PHE A 459           
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 ARG B  70  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 VAL B   6  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 ILE B 168  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 8 VAL B  88  PHE B  91  0                                        
SHEET    2 AA7 8 ARG B  70  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3 AA7 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4 AA7 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5 AA7 8 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6 AA7 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7 AA7 8 ILE B 168  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA7 8 PHE B 163  THR B 165 -1  N  PHE B 163   O  TYR B 170           
SHEET    1 AA8 2 GLY B  18  GLY B  20  0                                        
SHEET    2 AA8 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
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  LEU B 405   O  TYR B 421           
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 ARG C  70  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  LEU C 155   O  GLU C 176           
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  THR C 262   N  ARG C 254           
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  TYR C 409   O  SER C 417           
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 ARG D  70  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 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6 AB7 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB7 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB7 8 PHE D 154  MET D 159 -1  N  LEU D 155   O  GLU D 176           
SHEET    1 AB8 8 VAL D  88  PHE D  91  0                                        
SHEET    2 AB8 8 ARG D  70  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3 AB8 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4 AB8 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5 AB8 8 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6 AB8 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB8 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB8 8 PHE D 163  THR D 165 -1  N  PHE D 163   O  TYR D 170           
SHEET    1 AB9 2 GLY D  18  GLY D  20  0                                        
SHEET    2 AB9 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
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  LEU D 405   O  TYR D 421           
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  TYR E 409   O  SER E 417           
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 22 VAL A  10  ALA A  11  ILE A  19  GLY A  23                    
SITE     2 AC1 22 GLN A  24  LEU A  25  GLY A  55  ARG A  56                    
SITE     3 AC1 22 LYS A  57  THR A  58  ILE A  75  SER A  76                    
SITE     4 AC1 22 SER A  77  ARG A  92  CYS A 113  GLY A 114                    
SITE     5 AC1 22 GLY A 115  GLU A 116  SER A 117  ASP A 121                    
SITE     6 AC1 22 THR A 145  MTX A 604                                          
SITE     1 AC2 14 ARG A 257  CYS A 402  HIS A 403  GLN A 422                    
SITE     2 AC2 14 ARG A 423  SER A 424  CYS A 425  ASP A 426                    
SITE     3 AC2 14 ASN A 434  HIS A 464  TYR A 466  OEP A 603                    
SITE     4 AC2 14 ARG B 382  ARG B 383                                          
SITE     1 AC3 14 LYS A 284  ALA A 287  SER A 290  ILE A 315                    
SITE     2 AC3 14 ASN A 319  LEU A 399  ASP A 426  LEU A 429                    
SITE     3 AC3 14 GLY A 430  PHE A 433  TYR A 466  ILE A 515                    
SITE     4 AC3 14 ALA A 520  UFP A 602                                          
SITE     1 AC4 15 VAL A   9  VAL A  10  ALA A  11  LEU A  25                    
SITE     2 AC4 15 ASP A  32  LYS A  34  PHE A  36  SER A  37                    
SITE     3 AC4 15 THR A  58  ILE A  62  ARG A  70  CYS A 113                    
SITE     4 AC4 15 TYR A 119  THR A 134  NDP A 601                               
SITE     1 AC5 24 VAL B  10  ALA B  11  ILE B  19  GLY B  20                    
SITE     2 AC5 24 GLY B  23  GLN B  24  LEU B  25  GLY B  55                    
SITE     3 AC5 24 ARG B  56  LYS B  57  THR B  58  ILE B  75                    
SITE     4 AC5 24 SER B  76  SER B  77  SER B  78  ARG B  92                    
SITE     5 AC5 24 CYS B 113  GLY B 114  GLY B 115  GLU B 116                    
SITE     6 AC5 24 SER B 117  ASP B 121  THR B 145  MTX B 604                    
SITE     1 AC6 14 ARG A 382  ARG A 383  ARG B 257  CYS B 402                    
SITE     2 AC6 14 HIS B 403  GLN B 422  ARG B 423  SER B 424                    
SITE     3 AC6 14 CYS B 425  ASP B 426  ASN B 434  HIS B 464                    
SITE     4 AC6 14 TYR B 466  OEP B 603                                          
SITE     1 AC7 17 LYS B 284  ALA B 287  SER B 290  ILE B 315                    
SITE     2 AC7 17 ASN B 319  LEU B 399  ASP B 426  LEU B 429                    
SITE     3 AC7 17 GLY B 430  PRO B 432  PHE B 433  TYR B 466                    
SITE     4 AC7 17 ILE B 515  MET B 517  MET B 519  ALA B 520                    
SITE     5 AC7 17 UFP B 602                                                     
SITE     1 AC8 17 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC8 17 ASP B  32  LEU B  33  LYS B  34  PHE B  36                    
SITE     3 AC8 17 SER B  37  THR B  58  ILE B  62  LEU B  67                    
SITE     4 AC8 17 ARG B  70  CYS B 113  TYR B 119  THR B 134                    
SITE     5 AC8 17 NDP B 601                                                     
SITE     1 AC9 24 VAL C  10  ALA C  11  ILE C  19  GLY C  20                    
SITE     2 AC9 24 GLY C  23  GLN C  24  LEU C  25  GLY C  55                    
SITE     3 AC9 24 ARG C  56  LYS C  57  THR C  58  ILE C  75                    
SITE     4 AC9 24 SER C  76  SER C  77  ARG C  92  CYS C 113                    
SITE     5 AC9 24 GLY C 114  GLY C 115  GLU C 116  SER C 117                    
SITE     6 AC9 24 TYR C 119  ASP C 121  THR C 145  MTX C 604                    
SITE     1 AD1 14 ARG C 257  CYS C 402  HIS C 403  GLN C 422                    
SITE     2 AD1 14 ARG C 423  SER C 424  CYS C 425  ASP C 426                    
SITE     3 AD1 14 ASN C 434  HIS C 464  TYR C 466  OEP C 603                    
SITE     4 AD1 14 ARG D 382  ARG D 383                                          
SITE     1 AD2 16 LYS C 284  ALA C 287  SER C 290  ILE C 315                    
SITE     2 AD2 16 ASN C 319  LEU C 399  ASP C 426  LEU C 429                    
SITE     3 AD2 16 GLY C 430  PRO C 432  PHE C 433  TYR C 466                    
SITE     4 AD2 16 ILE C 515  MET C 517  ALA C 520  UFP C 602                    
SITE     1 AD3 15 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 AD3 15 ASP C  32  PHE C  36  SER C  37  THR C  58                    
SITE     3 AD3 15 ILE C  62  LEU C  67  ARG C  70  CYS C 113                    
SITE     4 AD3 15 TYR C 119  THR C 134  NDP C 601                               
SITE     1 AD4 21 VAL D  10  ALA D  11  ILE D  19  GLY D  20                    
SITE     2 AD4 21 GLY D  23  GLN D  24  GLY D  55  ARG D  56                    
SITE     3 AD4 21 LYS D  57  THR D  58  ILE D  75  SER D  76                    
SITE     4 AD4 21 SER D  77  ARG D  92  CYS D 113  GLY D 114                    
SITE     5 AD4 21 GLY D 115  GLU D 116  SER D 117  THR D 145                    
SITE     6 AD4 21 MTX D 604                                                     
SITE     1 AD5 14 ARG C 382  ARG C 383  ARG D 257  CYS D 402                    
SITE     2 AD5 14 HIS D 403  GLN D 422  ARG D 423  SER D 424                    
SITE     3 AD5 14 CYS D 425  ASP D 426  ASN D 434  HIS D 464                    
SITE     4 AD5 14 TYR D 466  OEP D 603                                          
SITE     1 AD6 14 LYS D 284  ALA D 287  SER D 290  ILE D 315                    
SITE     2 AD6 14 ASN D 319  LEU D 399  ASP D 426  LEU D 429                    
SITE     3 AD6 14 GLY D 430  TYR D 466  ILE D 515  MET D 517                    
SITE     4 AD6 14 ALA D 520  UFP D 602                                          
SITE     1 AD7 17 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 AD7 17 ASP D  32  LEU D  33  LYS D  34  PHE D  36                    
SITE     3 AD7 17 SER D  37  THR D  58  ILE D  62  LEU D  67                    
SITE     4 AD7 17 ARG D  70  CYS D 113  TYR D 119  THR D 134                    
SITE     5 AD7 17 NDP D 601                                                     
SITE     1 AD8 22 VAL E  10  ALA E  11  ILE E  19  GLY E  20                    
SITE     2 AD8 22 GLY E  23  GLN E  24  GLY E  55  ARG E  56                    
SITE     3 AD8 22 LYS E  57  THR E  58  SER E  61  ILE E  75                    
SITE     4 AD8 22 SER E  76  SER E  77  ARG E  92  CYS E 113                    
SITE     5 AD8 22 GLY E 114  GLY E 115  GLU E 116  SER E 117                    
SITE     6 AD8 22 THR E 145  MTX E 604                                          
SITE     1 AD9 14 ARG E 257  ARG E 382  ARG E 383  CYS E 402                    
SITE     2 AD9 14 HIS E 403  GLN E 422  ARG E 423  SER E 424                    
SITE     3 AD9 14 CYS E 425  ASP E 426  ASN E 434  HIS E 464                    
SITE     4 AD9 14 TYR E 466  OEP E 603                                          
SITE     1 AE1 14 LYS E 284  ALA E 287  SER E 290  ILE E 315                    
SITE     2 AE1 14 ASN E 319  LEU E 399  ASP E 426  LEU E 429                    
SITE     3 AE1 14 GLY E 430  TYR E 466  ILE E 515  MET E 519                    
SITE     4 AE1 14 ALA E 520  UFP E 602                                          
SITE     1 AE2 15 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 AE2 15 ASP E  32  LYS E  34  PHE E  36  SER E  37                    
SITE     3 AE2 15 THR E  58  ILE E  62  ARG E  70  CYS E 113                    
SITE     4 AE2 15 TYR E 119  THR E 134  NDP E 601                               
CRYST1  213.380  116.741  221.580  90.00  95.05  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      0.004686  0.000000  0.000414        0.00000                         
SCALE2      0.000000  0.008566  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system