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Database: PDB
Entry: 4KY8
LinkDB: 4KY8
Original site: 4KY8 
HEADER    TRANSFERASE,OXIDOREDUCTASE/INHIBITOR    28-MAY-13   4KY8              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, METHOTREXATE, FDUMP AND 4-((2-AMINO-6-METHYL-4-OXO-4,7-  
TITLE    3 DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)THIO)-2-CHLOROPHENYL)-L-     
TITLE    4 GLUTAMIC ACID                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL THYMIDYLATE SYNTHASE-DIHYDROFOLATE REDUCTASE; 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 EC: 2.1.1.45, 1.5.1.3;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM HOMINIS;                        
SOURCE   3 ORGANISM_TAXID: 237895;                                              
SOURCE   4 GENE: CHRO.40506, TS-DHFR;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: PA414;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    BIFUNCTIONAL ENZYME, TRANSFERASE, OXIDOREDUCTASE, OXIDOREDUCTASE-     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.P.KUMAR,K.S.ANDERSON                                                
REVDAT   3   15-NOV-17 4KY8    1       REMARK                                   
REVDAT   2   18-SEP-13 4KY8    1       JRNL                                     
REVDAT   1   21-AUG-13 4KY8    0                                                
JRNL        AUTH   V.P.KUMAR,K.M.FREY,Y.WANG,H.K.JAIN,A.GANGJEE,K.S.ANDERSON    
JRNL        TITL   SUBSTITUTED PYRROLO[2,3-D]PYRIMIDINES AS CRYPTOSPORIDIUM     
JRNL        TITL 2 HOMINIS THYMIDYLATE SYNTHASE INHIBITORS.                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  5426 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23927969                                                     
JRNL        DOI    10.1016/J.BMCL.2013.07.037                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 71.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 70048                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1959                            
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 48.1258 -  7.4243    1.00     6989   209  0.2103 0.2531        
REMARK   3     2  7.4243 -  5.8963    1.00     6878   193  0.2358 0.2500        
REMARK   3     3  5.8963 -  5.1519    1.00     6851   198  0.2127 0.2477        
REMARK   3     4  5.1519 -  4.6813    1.00     6790   199  0.1912 0.2220        
REMARK   3     5  4.6813 -  4.3460    1.00     6828   184  0.1908 0.2404        
REMARK   3     6  4.3460 -  4.0899    1.00     6844   195  0.2114 0.2662        
REMARK   3     7  4.0899 -  3.8852    0.97     6633   185  0.2598 0.2946        
REMARK   3     8  3.8852 -  3.7161    0.85     5768   182  0.2798 0.2852        
REMARK   3     9  3.7161 -  3.5731    0.64     4331   127  0.2927 0.3414        
REMARK   3    10  3.5731 -  3.4499    0.53     3586   103  0.3032 0.2989        
REMARK   3    11  3.4499 -  3.3420    0.40     2694    70  0.3420 0.3566        
REMARK   3    12  3.3420 -  3.2465    0.28     1901    53  0.3496 0.3690        
REMARK   3    13  3.2465 -  3.1611    0.19     1260    39  0.3749 0.3879        
REMARK   3    14  3.1611 -  3.0840    0.11      736    22  0.3719 0.4148        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.40                          
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          21760                                  
REMARK   3   ANGLE     :  0.543          29505                                  
REMARK   3   CHIRALITY :  0.039           3115                                  
REMARK   3   PLANARITY :  0.002           3755                                  
REMARK   3   DIHEDRAL  : 12.125           8190                                  
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 4KY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000079944.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10                               
REMARK 200  MONOCHROMATOR                  : DOUBLE SILICON (111) CRYSTAL       
REMARK 200                                   MONOCHROMATOR WITH CRYOGENICALLY-  
REMARK 200                                   COOLED FIRST CRYSTAL AND           
REMARK 200                                   SAGITTALLY-BENT SECOND CRYSTAL     
REMARK 200                                   HORIZONTALLY FOCUSING AT 3.3:1     
REMARK 200                                   DEMAGNIFICATION                    
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70173                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 71.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.20700                            
REMARK 200  R SYM                      (I) : 0.20700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 11.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QZF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% (W/V) PEG 6000, 60 MM AMMONIUM       
REMARK 280  SULFATE, 200 MM LITHIUM SULFATE AND 100 MM TRIS PH 8.0. CHTS-       
REMARK 280  DHFR ENZYME (~ 7 MG/ML) WITH 1 MM NADPH, 1 MM MTX, 1 MM FDUMP       
REMARK 280  AND 0.5 MM INHIBITOR., VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      107.08100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.83250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.08100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.83250            
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: 8340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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: 8380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A   179                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLN A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     CYS A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     GLN A   192                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B   179                                                      
REMARK 465     LYS B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     GLN B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     CYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLU C   179                                                      
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     GLU D   179                                                      
REMARK 465     LYS D   180                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     THR D   182                                                      
REMARK 465     LEU D   183                                                      
REMARK 465     GLN D   184                                                      
REMARK 465     ASN D   185                                                      
REMARK 465     CYS D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     ARG D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     GLN D   192                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     GLU E   179                                                      
REMARK 465     LYS E   180                                                      
REMARK 465     LYS E   181                                                      
REMARK 465     THR E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     GLN E   184                                                      
REMARK 465     ASN E   185                                                      
REMARK 465     CYS E   186                                                      
REMARK 465     ASP E   187                                                      
REMARK 465     PRO E   188                                                      
REMARK 465     ALA E   189                                                      
REMARK 465     ARG E   190                                                      
REMARK 465     GLY E   191                                                      
REMARK 465     GLN E   192                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   383     O3P  UFP B   602              2.05            
REMARK 500   NE   ARG E   257     O2P  UFP E   602              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG E   383     O3P  UFP E   602     2859     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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      -69.72    -98.28                                   
REMARK 500    GLN A  81       87.28    -66.38                                   
REMARK 500    ASP A 104       81.87     56.19                                   
REMARK 500    ASN A 126       73.38     56.20                                   
REMARK 500    ASP A 140       31.81    -88.77                                   
REMARK 500    ILE A 206      -70.03    -64.76                                   
REMARK 500    HIS A 216       63.23   -118.83                                   
REMARK 500    THR A 226       74.78     51.78                                   
REMARK 500    PRO A 279       65.74    -63.89                                   
REMARK 500    ALA A 287       90.25    -68.40                                   
REMARK 500    PRO A 340       62.56    -66.78                                   
REMARK 500    ILE A 341     -151.75    -89.05                                   
REMARK 500    LYS A 354      -88.73   -106.47                                   
REMARK 500    TYR A 360       32.30    -90.30                                   
REMARK 500    ASN A 378       79.58   -152.63                                   
REMARK 500    HIS A 384       81.48    -68.95                                   
REMARK 500    ASP A 413       31.49    -95.66                                   
REMARK 500    LEU B  15      -69.63    -98.93                                   
REMARK 500    GLN B  81       87.15    -66.16                                   
REMARK 500    ASP B 104       82.26     56.78                                   
REMARK 500    ASN B 126       73.48     55.72                                   
REMARK 500    ASP B 140       31.96    -88.46                                   
REMARK 500    HIS B 216       63.95   -119.18                                   
REMARK 500    THR B 226       74.79     52.21                                   
REMARK 500    PRO B 279       65.22    -64.27                                   
REMARK 500    ALA B 287       89.82    -68.63                                   
REMARK 500    PRO B 340       62.37    -66.98                                   
REMARK 500    ILE B 341     -150.36    -87.22                                   
REMARK 500    LYS B 354      -88.41   -107.51                                   
REMARK 500    TYR B 360       33.11    -90.06                                   
REMARK 500    ASN B 378       79.28   -152.53                                   
REMARK 500    HIS B 384       82.95    -68.23                                   
REMARK 500    ASP B 413       31.55    -95.38                                   
REMARK 500    LEU C  15      -70.40    -98.21                                   
REMARK 500    GLN C  81       86.90    -66.72                                   
REMARK 500    ASP C 104       81.91     56.94                                   
REMARK 500    ASN C 126       73.77     56.12                                   
REMARK 500    ASP C 140       32.54    -88.05                                   
REMARK 500    HIS C 216       62.68   -119.53                                   
REMARK 500    THR C 226       74.63     51.98                                   
REMARK 500    PRO C 279       65.85    -64.00                                   
REMARK 500    ALA C 287       90.31    -68.58                                   
REMARK 500    PRO C 340       61.93    -67.40                                   
REMARK 500    ILE C 341     -149.14    -89.67                                   
REMARK 500    ASN C 350       19.92     59.88                                   
REMARK 500    LYS C 354      -88.81   -106.73                                   
REMARK 500    TYR C 360       32.14    -90.78                                   
REMARK 500    ASN C 378       79.15   -153.25                                   
REMARK 500    HIS C 384       82.44    -68.94                                   
REMARK 500    ASP C 413       31.38    -95.62                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 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 MTX A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UF 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 MTX B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UF 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: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UF C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UF D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UF E 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QZF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HJ3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DL5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DL6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OIP   RELATED DB: PDB                                   
DBREF  4KY8 A    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4KY8 B    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4KY8 C    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4KY8 D    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4KY8 E    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     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    MTX  A 603      33                                                       
HET    1UF  A 604      32                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    MTX  B 603      33                                                       
HET    1UF  B 604      32                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    MTX  C 603      33                                                       
HET    1UF  C 604      32                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    MTX  D 603      33                                                       
HET    1UF  D 604      32                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    MTX  E 603      33                                                       
HET    1UF  E 604      32                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     UFP 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                        
HETNAM     MTX METHOTREXATE                                                     
HETNAM     1UF N-{4-[(2-AMINO-6-METHYL-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,          
HETNAM   2 1UF  3-D]PYRIMIDIN-5-YL)SULFANYL]-2-CHLOROBENZOYL}-L-                
HETNAM   3 1UF  GLUTAMIC ACID                                                   
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  MTX    5(C20 H22 N8 O5)                                             
FORMUL   9  1UF    5(C19 H18 CL N5 O6 S)                                        
HELIX    1   1 ILE A   29  ASN A   42  1                                  14    
HELIX    2   2 ARG A   56  ILE A   62  1                                   7    
HELIX    3   3 ASN A   93  ILE A   98  1                                   6    
HELIX    4   4 GLY A  115  ASP A  125  1                                  11    
HELIX    5   5 LYS A  194  PHE A  207  1                                  14    
HELIX    6   6 LYS A  211  ARG A  215  5                                   5    
HELIX    7   7 LYS A  220  TYR A  224  5                                   5    
HELIX    8   8 GLU A  237  GLY A  251  1                                  15    
HELIX    9   9 ALA A  287  LYS A  300  1                                  14    
HELIX   10  10 ASN A  304  GLU A  310  1                                   7    
HELIX   11  11 SER A  321  ILE A  328  1                                   8    
HELIX   12  12 GLY A  343  HIS A  348  1                                   6    
HELIX   13  13 ASP A  366  ASN A  378  1                                  13    
HELIX   14  14 LEU A  429  CYS A  449  1                                  21    
HELIX   15  15 HIS A  469  LEU A  477  1                                   9    
HELIX   16  16 ASN A  495  PHE A  499  5                                   5    
HELIX   17  17 LYS A  500  GLU A  502  5                                   3    
HELIX   18  18 ILE B   29  ASN B   42  1                                  14    
HELIX   19  19 ARG B   56  ILE B   62  1                                   7    
HELIX   20  20 ASN B   93  ILE B   98  1                                   6    
HELIX   21  21 GLY B  115  ASP B  125  1                                  11    
HELIX   22  22 LYS B  194  PHE B  207  1                                  14    
HELIX   23  23 LYS B  211  HIS B  216  1                                   6    
HELIX   24  24 LYS B  220  TYR B  224  5                                   5    
HELIX   25  25 GLU B  237  GLY B  251  1                                  15    
HELIX   26  26 ALA B  287  LYS B  300  1                                  14    
HELIX   27  27 GLY B  305  LYS B  311  1                                   7    
HELIX   28  28 SER B  321  ILE B  328  1                                   8    
HELIX   29  29 GLY B  343  HIS B  348  1                                   6    
HELIX   30  30 ASP B  366  ASN B  378  1                                  13    
HELIX   31  31 LEU B  429  CYS B  449  1                                  21    
HELIX   32  32 HIS B  469  LEU B  477  1                                   9    
HELIX   33  33 ASN B  495  PHE B  499  5                                   5    
HELIX   34  34 LYS B  500  GLU B  502  5                                   3    
HELIX   35  35 ILE C   29  ASN C   42  1                                  14    
HELIX   36  36 ARG C   56  ILE C   62  1                                   7    
HELIX   37  37 ASN C   93  ILE C   98  1                                   6    
HELIX   38  38 GLY C  115  ASP C  125  1                                  11    
HELIX   39  39 LYS C  194  PHE C  207  1                                  14    
HELIX   40  40 LYS C  211  ARG C  215  5                                   5    
HELIX   41  41 LYS C  220  TYR C  224  5                                   5    
HELIX   42  42 GLU C  237  GLY C  251  1                                  15    
HELIX   43  43 ALA C  287  LYS C  300  1                                  14    
HELIX   44  44 GLY C  305  LYS C  311  1                                   7    
HELIX   45  45 SER C  321  ILE C  328  1                                   8    
HELIX   46  46 GLY C  343  HIS C  348  1                                   6    
HELIX   47  47 ASP C  366  ASN C  378  1                                  13    
HELIX   48  48 LEU C  429  CYS C  449  1                                  21    
HELIX   49  49 HIS C  469  LEU C  477  1                                   9    
HELIX   50  50 ASN C  495  PHE C  499  5                                   5    
HELIX   51  51 LYS C  500  GLU C  502  5                                   3    
HELIX   52  52 ILE D   29  ASN D   42  1                                  14    
HELIX   53  53 ARG D   56  ILE D   62  1                                   7    
HELIX   54  54 ASN D   93  ILE D   98  1                                   6    
HELIX   55  55 GLY D  115  ASP D  125  1                                  11    
HELIX   56  56 LYS D  194  PHE D  207  1                                  14    
HELIX   57  57 LYS D  211  ARG D  215  5                                   5    
HELIX   58  58 LYS D  220  TYR D  224  5                                   5    
HELIX   59  59 GLU D  237  GLY D  251  1                                  15    
HELIX   60  60 ALA D  287  LYS D  300  1                                  14    
HELIX   61  61 ASN D  304  GLU D  310  1                                   7    
HELIX   62  62 SER D  321  ILE D  328  1                                   8    
HELIX   63  63 GLY D  343  HIS D  348  1                                   6    
HELIX   64  64 ASP D  366  ASN D  378  1                                  13    
HELIX   65  65 LEU D  429  CYS D  449  1                                  21    
HELIX   66  66 HIS D  469  LEU D  477  1                                   9    
HELIX   67  67 ASN D  495  PHE D  499  5                                   5    
HELIX   68  68 LYS D  500  GLU D  502  5                                   3    
HELIX   69  69 ILE E   29  ASN E   42  1                                  14    
HELIX   70  70 ARG E   56  ILE E   62  1                                   7    
HELIX   71  71 ASN E   93  ILE E   98  1                                   6    
HELIX   72  72 GLY E  115  ASP E  125  1                                  11    
HELIX   73  73 LYS E  194  PHE E  207  1                                  14    
HELIX   74  74 LYS E  211  HIS E  216  1                                   6    
HELIX   75  75 LYS E  220  TYR E  224  5                                   5    
HELIX   76  76 GLU E  237  GLY E  251  1                                  15    
HELIX   77  77 ALA E  287  LYS E  300  1                                  14    
HELIX   78  78 GLY E  305  GLU E  310  1                                   6    
HELIX   79  79 SER E  321  ILE E  328  1                                   8    
HELIX   80  80 GLY E  343  HIS E  348  1                                   6    
HELIX   81  81 ASP E  366  ASN E  378  1                                  13    
HELIX   82  82 LEU E  429  CYS E  449  1                                  21    
HELIX   83  83 HIS E  469  LEU E  477  1                                   9    
HELIX   84  84 ASN E  495  PHE E  499  5                                   5    
HELIX   85  85 LYS E  500  GLU E  502  5                                   3    
SHEET    1   A 8 VAL A  88  PHE A  91  0                                        
SHEET    2   A 8 ARG A  70  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3   A 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4   A 8 ILE A 107  GLY A 114  1  O  PHE A 111   N  ILE A  53           
SHEET    5   A 8 VAL A   6  SER A  13  1  N  VAL A   9   O  VAL A 112           
SHEET    6   A 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7   A 8 MET A 173  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8   A 8 PHE A 154  MET A 159 -1  N  LEU A 155   O  GLU A 176           
SHEET    1   B 2 GLY A  18  GLY A  20  0                                        
SHEET    2   B 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
SHEET    1   C 2 PHE A 163  THR A 165  0                                        
SHEET    2   C 2 ILE A 168  TYR A 170 -1  O  TYR A 170   N  PHE A 163           
SHEET    1   D 6 ALA A 252  ARG A 254  0                                        
SHEET    2   D 6 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3   D 6 GLU A 452  TYR A 466 -1  O  ILE A 458   N  MET A 270           
SHEET    4   D 6 CYS A 415  ASP A 426  1  N  GLN A 422   O  GLY A 461           
SHEET    5   D 6 HIS A 403  VAL A 410 -1  N  LEU A 405   O  TYR A 421           
SHEET    6   D 6 ILE A 385  THR A 387 -1  N  LEU A 386   O  SER A 406           
SHEET    1   E 2 GLN A 486  PHE A 489  0                                        
SHEET    2   E 2 ILE A 504  ILE A 507 -1  O  GLU A 505   N  LYS A 488           
SHEET    1   F 9 VAL B  88  PHE B  91  0                                        
SHEET    2   F 9 ARG B  70  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3   F 9 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4   F 9 ILE B 107  GLY B 114  1  O  PHE B 111   N  ILE B  53           
SHEET    5   F 9 VAL B   6  SER B  13  1  N  VAL B   9   O  VAL B 112           
SHEET    6   F 9 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7   F 9 MET B 173  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8   F 9 PHE B 154  MET B 159 -1  N  VAL B 157   O  ILE B 174           
SHEET    9   F 9 GLY B 232  ARG B 233  1  O  GLY B 232   N  MET B 159           
SHEET    1   G 2 GLY B  18  GLY B  20  0                                        
SHEET    2   G 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
SHEET    1   H 2 PHE B 163  THR B 165  0                                        
SHEET    2   H 2 ILE B 168  TYR B 170 -1  O  TYR B 170   N  PHE B 163           
SHEET    1   I 6 ALA B 252  ARG B 254  0                                        
SHEET    2   I 6 THR B 262  ASP B 273 -1  O  THR B 262   N  ARG B 254           
SHEET    3   I 6 GLU B 452  TYR B 466 -1  O  ILE B 458   N  MET B 270           
SHEET    4   I 6 CYS B 415  ASP B 426  1  N  GLN B 422   O  GLY B 461           
SHEET    5   I 6 HIS B 403  VAL B 410 -1  N  LEU B 405   O  TYR B 421           
SHEET    6   I 6 ILE B 385  THR B 387 -1  N  LEU B 386   O  SER B 406           
SHEET    1   J 2 GLN B 486  PHE B 489  0                                        
SHEET    2   J 2 ILE B 504  ILE B 507 -1  O  GLU B 505   N  LYS B 488           
SHEET    1   K 9 VAL C  88  PHE C  91  0                                        
SHEET    2   K 9 ARG C  70  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3   K 9 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4   K 9 ILE C 107  GLY C 114  1  O  PHE C 111   N  ILE C  53           
SHEET    5   K 9 VAL C   6  SER C  13  1  N  VAL C   9   O  VAL C 112           
SHEET    6   K 9 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7   K 9 MET C 173  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8   K 9 PHE C 154  MET C 159 -1  N  LEU C 155   O  GLU C 176           
SHEET    9   K 9 GLY C 232  ARG C 233  1  O  GLY C 232   N  MET C 159           
SHEET    1   L 2 GLY C  18  GLY C  20  0                                        
SHEET    2   L 2 THR C 145  TYR C 146 -1  O  THR C 145   N  ILE C  19           
SHEET    1   M 2 PHE C 163  THR C 165  0                                        
SHEET    2   M 2 ILE C 168  TYR C 170 -1  O  TYR C 170   N  PHE C 163           
SHEET    1   N 6 ALA C 252  ARG C 254  0                                        
SHEET    2   N 6 THR C 262  ASP C 273 -1  O  THR C 262   N  ARG C 254           
SHEET    3   N 6 GLU C 452  TYR C 466 -1  O  ILE C 458   N  MET C 270           
SHEET    4   N 6 CYS C 415  ASP C 426  1  N  GLN C 422   O  GLY C 461           
SHEET    5   N 6 HIS C 403  VAL C 410 -1  N  LEU C 405   O  TYR C 421           
SHEET    6   N 6 ILE C 385  THR C 387 -1  N  LEU C 386   O  SER C 406           
SHEET    1   O 2 GLN C 486  PHE C 489  0                                        
SHEET    2   O 2 ILE C 504  ILE C 507 -1  O  GLU C 505   N  LYS C 488           
SHEET    1   P 9 VAL D  88  PHE D  91  0                                        
SHEET    2   P 9 ARG D  70  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3   P 9 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4   P 9 ILE D 107  GLY D 114  1  O  PHE D 111   N  ILE D  53           
SHEET    5   P 9 VAL D   6  SER D  13  1  N  VAL D   9   O  VAL D 112           
SHEET    6   P 9 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7   P 9 MET D 173  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8   P 9 PHE D 154  MET D 159 -1  N  VAL D 157   O  ILE D 174           
SHEET    9   P 9 GLY D 232  ARG D 233  1  O  GLY D 232   N  MET D 159           
SHEET    1   Q 2 GLY D  18  GLY D  20  0                                        
SHEET    2   Q 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
SHEET    1   R 2 PHE D 163  THR D 165  0                                        
SHEET    2   R 2 ILE D 168  TYR D 170 -1  O  TYR D 170   N  PHE D 163           
SHEET    1   S 6 ALA D 252  ARG D 254  0                                        
SHEET    2   S 6 THR D 262  ASP D 273 -1  O  THR D 262   N  ARG D 254           
SHEET    3   S 6 GLU D 452  TYR D 466 -1  O  ILE D 458   N  MET D 270           
SHEET    4   S 6 CYS D 415  ASP D 426  1  N  GLN D 422   O  GLY D 461           
SHEET    5   S 6 HIS D 403  VAL D 410 -1  N  LEU D 405   O  TYR D 421           
SHEET    6   S 6 ILE D 385  THR D 387 -1  N  LEU D 386   O  SER D 406           
SHEET    1   T 2 GLN D 486  PHE D 489  0                                        
SHEET    2   T 2 ILE D 504  ILE D 507 -1  O  GLU D 505   N  LYS D 488           
SHEET    1   U 8 VAL E  88  PHE E  91  0                                        
SHEET    2   U 8 ARG E  70  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3   U 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4   U 8 ILE E 107  GLY E 114  1  O  PHE E 111   N  ILE E  53           
SHEET    5   U 8 VAL E   6  SER E  13  1  N  VAL E   9   O  VAL E 112           
SHEET    6   U 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7   U 8 MET E 173  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8   U 8 PHE E 154  MET E 159 -1  N  VAL E 157   O  ILE E 174           
SHEET    1   V 2 GLY E  18  GLY E  20  0                                        
SHEET    2   V 2 THR E 145  TYR E 146 -1  O  THR E 145   N  ILE E  19           
SHEET    1   W 2 PHE E 163  THR E 165  0                                        
SHEET    2   W 2 ILE E 168  TYR E 170 -1  O  TYR E 170   N  PHE E 163           
SHEET    1   X 6 ALA E 252  ARG E 254  0                                        
SHEET    2   X 6 THR E 262  ASP E 273 -1  O  THR E 262   N  ARG E 254           
SHEET    3   X 6 GLU E 452  TYR E 466 -1  O  ILE E 458   N  MET E 270           
SHEET    4   X 6 CYS E 415  ASP E 426  1  N  GLN E 422   O  GLY E 461           
SHEET    5   X 6 HIS E 403  VAL E 410 -1  N  LEU E 405   O  TYR E 421           
SHEET    6   X 6 ILE E 385  THR E 387 -1  N  LEU E 386   O  SER E 406           
SHEET    1   Y 2 GLN E 486  PHE E 489  0                                        
SHEET    2   Y 2 ILE E 504  ILE E 507 -1  O  GLU E 505   N  LYS E 488           
SITE     1 AC1 21 ALA A  11  ILE A  19  GLY A  23  GLN A  24                    
SITE     2 AC1 21 LEU A  25  GLY A  55  ARG A  56  LYS A  57                    
SITE     3 AC1 21 THR A  58  ILE A  75  SER A  76  SER A  77                    
SITE     4 AC1 21 SER A  78  ARG A  92  CYS A 113  GLY A 114                    
SITE     5 AC1 21 GLY A 115  GLU A 116  SER A 117  THR A 145                    
SITE     6 AC1 21 MTX A 603                                                     
SITE     1 AC2 13 ARG A 257  CYS A 402  ARG A 423  SER A 424                    
SITE     2 AC2 13 CYS A 425  ASP A 426  GLY A 430  ASN A 434                    
SITE     3 AC2 13 HIS A 464  TYR A 466  1UF A 604  ARG B 382                    
SITE     4 AC2 13 ARG B 383                                                     
SITE     1 AC3 15 VAL A   9  VAL A  10  ALA A  11  LEU A  25                    
SITE     2 AC3 15 ASP A  32  LEU A  33  LYS A  34  PHE A  36                    
SITE     3 AC3 15 SER A  37  SER A  61  ILE A  62  ARG A  70                    
SITE     4 AC3 15 CYS A 113  THR A 134  NDP A 601                               
SITE     1 AC4 12 ALA A 287  ILE A 315  TRP A 316  ASN A 319                    
SITE     2 AC4 12 ASP A 426  LEU A 429  GLY A 430  PHE A 433                    
SITE     3 AC4 12 TYR A 466  MET A 519  ALA A 520  UFP A 602                    
SITE     1 AC5 21 ALA B  11  ILE B  19  GLY B  23  GLN B  24                    
SITE     2 AC5 21 LEU B  25  GLY B  55  ARG B  56  LYS B  57                    
SITE     3 AC5 21 THR B  58  ILE B  75  SER B  76  SER B  77                    
SITE     4 AC5 21 SER B  78  ARG B  92  CYS B 113  GLY B 114                    
SITE     5 AC5 21 GLY B 115  GLU B 116  SER B 117  THR B 145                    
SITE     6 AC5 21 MTX B 603                                                     
SITE     1 AC6 14 ARG A 382  ARG A 383  ARG B 257  CYS B 402                    
SITE     2 AC6 14 HIS B 403  ARG B 423  SER B 424  CYS B 425                    
SITE     3 AC6 14 ASP B 426  GLY B 430  ASN B 434  HIS B 464                    
SITE     4 AC6 14 TYR B 466  1UF B 604                                          
SITE     1 AC7 14 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC7 14 ASP B  32  LYS B  34  PHE B  36  SER B  37                    
SITE     3 AC7 14 SER B  61  ILE B  62  ARG B  70  CYS B 113                    
SITE     4 AC7 14 THR B 134  NDP B 601                                          
SITE     1 AC8 14 ALA B 287  ILE B 315  TRP B 316  ASN B 319                    
SITE     2 AC8 14 LEU B 399  ASP B 426  LEU B 429  GLY B 430                    
SITE     3 AC8 14 PHE B 433  TYR B 466  ILE B 515  MET B 519                    
SITE     4 AC8 14 ALA B 520  UFP B 602                                          
SITE     1 AC9 22 VAL C  10  ALA C  11  ILE C  19  GLY C  23                    
SITE     2 AC9 22 GLN C  24  LEU C  25  GLY C  55  ARG C  56                    
SITE     3 AC9 22 LYS C  57  THR C  58  ILE C  75  SER C  76                    
SITE     4 AC9 22 SER C  77  SER C  78  ARG C  92  CYS C 113                    
SITE     5 AC9 22 GLY C 114  GLY C 115  GLU C 116  SER C 117                    
SITE     6 AC9 22 THR C 145  MTX C 603                                          
SITE     1 BC1 13 ARG C 257  CYS C 402  ARG C 423  SER C 424                    
SITE     2 BC1 13 CYS C 425  ASP C 426  GLY C 430  ASN C 434                    
SITE     3 BC1 13 HIS C 464  TYR C 466  1UF C 604  ARG D 382                    
SITE     4 BC1 13 ARG D 383                                                     
SITE     1 BC2 14 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 BC2 14 ASP C  32  LEU C  33  LYS C  34  PHE C  36                    
SITE     3 BC2 14 SER C  37  ILE C  62  ARG C  70  CYS C 113                    
SITE     4 BC2 14 THR C 134  NDP C 601                                          
SITE     1 BC3 12 SER C 290  ILE C 315  TRP C 316  ASN C 319                    
SITE     2 BC3 12 ASP C 426  LEU C 429  GLY C 430  PHE C 433                    
SITE     3 BC3 12 TYR C 466  MET C 519  ALA C 520  UFP C 602                    
SITE     1 BC4 22 ALA D  11  ILE D  19  GLY D  23  GLN D  24                    
SITE     2 BC4 22 LEU D  25  GLY D  55  ARG D  56  LYS D  57                    
SITE     3 BC4 22 THR D  58  ILE D  75  SER D  76  SER D  77                    
SITE     4 BC4 22 SER D  78  ARG D  92  CYS D 113  GLY D 114                    
SITE     5 BC4 22 GLY D 115  GLU D 116  SER D 117  ILE D 118                    
SITE     6 BC4 22 THR D 145  MTX D 603                                          
SITE     1 BC5 14 ARG C 382  ARG C 383  ARG D 257  CYS D 402                    
SITE     2 BC5 14 HIS D 403  ARG D 423  SER D 424  CYS D 425                    
SITE     3 BC5 14 ASP D 426  GLY D 430  ASN D 434  HIS D 464                    
SITE     4 BC5 14 TYR D 466  1UF D 604                                          
SITE     1 BC6 14 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 BC6 14 ASP D  32  LYS D  34  PHE D  36  SER D  37                    
SITE     3 BC6 14 SER D  61  ILE D  62  ARG D  70  CYS D 113                    
SITE     4 BC6 14 THR D 134  NDP D 601                                          
SITE     1 BC7 13 ALA D 287  ILE D 315  TRP D 316  ASN D 319                    
SITE     2 BC7 13 ASP D 426  LEU D 429  GLY D 430  PHE D 433                    
SITE     3 BC7 13 TYR D 466  ILE D 515  MET D 519  ALA D 520                    
SITE     4 BC7 13 UFP D 602                                                     
SITE     1 BC8 21 ALA E  11  ILE E  19  GLY E  23  GLN E  24                    
SITE     2 BC8 21 LEU E  25  GLY E  55  ARG E  56  LYS E  57                    
SITE     3 BC8 21 THR E  58  ILE E  75  SER E  76  SER E  77                    
SITE     4 BC8 21 SER E  78  ARG E  92  CYS E 113  GLY E 114                    
SITE     5 BC8 21 GLY E 115  GLU E 116  SER E 117  THR E 145                    
SITE     6 BC8 21 MTX E 603                                                     
SITE     1 BC9 11 ARG E 257  CYS E 402  ARG E 423  SER E 424                    
SITE     2 BC9 11 CYS E 425  ASP E 426  GLY E 430  ASN E 434                    
SITE     3 BC9 11 HIS E 464  TYR E 466  1UF E 604                               
SITE     1 CC1 16 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 CC1 16 ASP E  32  LEU E  33  LYS E  34  PHE E  36                    
SITE     3 CC1 16 SER E  37  SER E  61  ILE E  62  LEU E  67                    
SITE     4 CC1 16 ARG E  70  CYS E 113  THR E 134  NDP E 601                    
SITE     1 CC2 13 ALA E 287  ILE E 315  TRP E 316  ASN E 319                    
SITE     2 CC2 13 ASP E 426  LEU E 429  GLY E 430  PHE E 433                    
SITE     3 CC2 13 TYR E 466  ILE E 515  MET E 519  ALA E 520                    
SITE     4 CC2 13 UFP E 602                                                     
CRYST1  214.162  115.665  218.767  90.00  94.36  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      0.004669  0.000000  0.000356        0.00000                         
SCALE2      0.000000  0.008646  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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