GenomeNet

Database: PDB
Entry: 6PFF
LinkDB: 6PFF
Original site: 6PFF 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUN-19   6PFF              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, FDUMP AND 2-(4-((2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2, 
TITLE    3 3-D]PYRIMIDIN-5-YL)METHYL)BENZAMIDO)-4-CYANOBENZOIC ACID.            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE; 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM HOMINIS;                        
SOURCE   3 ORGANISM_TAXID: 237895;                                              
SOURCE   4 GENE: CHUDEA4_4460;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PA-414                                    
KEYWDS    INHIBITOR, TS, TS-DHFR, TRANSFERASE, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.CZYZYK,M.VALHONDO,W.L.JORGENSEN,K.S.ANDERSON                      
REVDAT   2   18-DEC-19 6PFF    1       REMARK                                   
REVDAT   1   02-OCT-19 6PFF    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.    2.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472: 000)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 108621                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5431                            
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 48.8237 -  9.2440    0.99     3609   189  0.1809 0.1962        
REMARK   3     2  9.2440 -  7.3453    1.00     3560   188  0.1528 0.1883        
REMARK   3     3  7.3453 -  6.4191    1.00     3526   185  0.1778 0.1777        
REMARK   3     4  6.4191 -  5.8333    1.00     3524   186  0.1952 0.2168        
REMARK   3     5  5.8333 -  5.4157    1.00     3550   187  0.1937 0.2284        
REMARK   3     6  5.4157 -  5.0968    1.00     3492   183  0.1786 0.1836        
REMARK   3     7  5.0968 -  4.8418    1.00     3507   185  0.1626 0.1852        
REMARK   3     8  4.8418 -  4.6312    1.00     3511   185  0.1581 0.2096        
REMARK   3     9  4.6312 -  4.4530    1.00     3500   183  0.1631 0.1933        
REMARK   3    10  4.4530 -  4.2995    1.00     3514   185  0.1674 0.2046        
REMARK   3    11  4.2995 -  4.1651    1.00     3488   184  0.1844 0.2297        
REMARK   3    12  4.1651 -  4.0461    1.00     3496   184  0.1970 0.2017        
REMARK   3    13  4.0461 -  3.9396    1.00     3487   183  0.2096 0.2580        
REMARK   3    14  3.9396 -  3.8436    1.00     3521   186  0.2149 0.2526        
REMARK   3    15  3.8436 -  3.7562    1.00     3490   184  0.2167 0.2400        
REMARK   3    16  3.7562 -  3.6763    1.00     3481   183  0.2290 0.2799        
REMARK   3    17  3.6763 -  3.6028    1.00     3497   184  0.2425 0.2770        
REMARK   3    18  3.6028 -  3.5348    1.00     3470   183  0.2274 0.2652        
REMARK   3    19  3.5348 -  3.4717    1.00     3463   182  0.2446 0.2494        
REMARK   3    20  3.4717 -  3.4129    1.00     3550   187  0.2657 0.3091        
REMARK   3    21  3.4129 -  3.3578    1.00     3440   181  0.2732 0.3020        
REMARK   3    22  3.3578 -  3.3062    1.00     3498   185  0.2772 0.3194        
REMARK   3    23  3.3062 -  3.2576    1.00     3486   183  0.2673 0.2824        
REMARK   3    24  3.2576 -  3.2117    1.00     3446   182  0.2610 0.3110        
REMARK   3    25  3.2117 -  3.1683    1.00     3527   185  0.2892 0.3417        
REMARK   3    26  3.1683 -  3.1272    1.00     3459   183  0.3022 0.3133        
REMARK   3    27  3.1272 -  3.0881    1.00     3526   186  0.3184 0.3938        
REMARK   3    28  3.0881 -  3.0509    1.00     3420   178  0.3091 0.3817        
REMARK   3    29  3.0509 -  3.0154    0.99     3471   184  0.3464 0.3451        
REMARK   3    30  3.0154 -  2.9815    0.48     1681    88  0.4247 0.5458        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.270           
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          21429                                  
REMARK   3   ANGLE     :  0.534          29152                                  
REMARK   3   CHIRALITY :  0.044           3117                                  
REMARK   3   PLANARITY :  0.003           3717                                  
REMARK   3   DIHEDRAL  :  9.355          12424                                  
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 6PFF 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_1000242247.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979180                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108730                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.980                              
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                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.65900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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      106.71200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.39700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.71200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.39700            
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: 14500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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: 14460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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     -213.42400            
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   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     GLN B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     CYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     LYS C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     THR C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     CYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     GLN C   192                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     LYS D   180                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     THR D   182                                                      
REMARK 465     LEU D   183                                                      
REMARK 465     GLN D   184                                                      
REMARK 465     ASN D   185                                                      
REMARK 465     CYS D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     ARG D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     GLN D   192                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     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  34    CG   CD   CE   NZ                                   
REMARK 470     GLU A  95    CG   CD   OE1  OE2                                  
REMARK 470     MET A 102    CG   SD   CE                                        
REMARK 470     ASN A 103    CG   OD1  ND2                                       
REMARK 470     LYS A 124    CG   CD   CE   NZ                                   
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
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     GLU A 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     GLU B  83    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 194    CG   CD   CE   NZ                                   
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     GLU C   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  34    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     ASN C 103    CG   OD1  ND2                                       
REMARK 470     LYS C 124    CG   CD   CE   NZ                                   
REMARK 470     GLU C 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 152    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 178    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     LYS C 217    CG   CD   CE   NZ                                   
REMARK 470     ARG C 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 311    CG   CD   CE   NZ                                   
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     GLU C 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 354    CG   CD   CE   NZ                                   
REMARK 470     LYS C 490    CG   CD   CE   NZ                                   
REMARK 470     GLU C 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 500    CG   CD   CE   NZ                                   
REMARK 470     GLU C 505    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     GLU D   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS D   4    CG   CD   CE   NZ                                   
REMARK 470     LYS D  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     MET D 102    CG   SD   CE                                        
REMARK 470     ASN D 103    CG   OD1  ND2                                       
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 166    CG   CD   CE   NZ                                   
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     GLU D 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     LYS E   4    CG   CD   CE   NZ                                   
REMARK 470     LYS E  34    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     GLU E  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  95    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  99    CG   CD   OE1  OE2                                  
REMARK 470     MET E 102    CG   SD   CE                                        
REMARK 470     ASN E 103    CG   OD1  ND2                                       
REMARK 470     ASP E 105    CG   OD1  OD2                                       
REMARK 470     LYS E 124    CG   CD   CE   NZ                                   
REMARK 470     GLU E 142    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 152    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 217    CG   CD   CE   NZ                                   
REMARK 470     PHE E 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 220    CG   CD   CE   NZ                                   
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 300    CG   CD   CE   NZ                                   
REMARK 470     ILE E 309    CG1  CG2  CD1                                       
REMARK 470     LYS E 311    CG   CD   CE   NZ                                   
REMARK 470     LYS E 312    CG   CD   CE   NZ                                   
REMARK 470     LYS E 322    CG   CD   CE   NZ                                   
REMARK 470     LEU E 325    CG   CD1  CD2                                       
REMARK 470     GLU E 326    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E 328    CG1  CG2  CD1                                       
REMARK 470     LYS E 354    CG   CD   CE   NZ                                   
REMARK 470     LYS E 370    CG   CD   CE   NZ                                   
REMARK 470     LYS E 380    CG   CD   CE   NZ                                   
REMARK 470     LYS E 474    CG   CD   CE   NZ                                   
REMARK 470     LYS E 488    CG   CD   CE   NZ                                   
REMARK 470     LYS E 492    CG   CD   CE   NZ                                   
REMARK 470     LYS E 500    CG   CD   CE   NZ                                   
REMARK 470     GLU E 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      -60.64    -98.66                                   
REMARK 500    GLN A  81       76.71    -67.84                                   
REMARK 500    ASN A 103     -161.51   -106.32                                   
REMARK 500    ASP A 104       74.95     54.22                                   
REMARK 500    ASP A 140       40.41    -93.42                                   
REMARK 500    THR A 226       72.23     48.06                                   
REMARK 500    ILE A 341     -157.27   -135.59                                   
REMARK 500    LYS A 354      -84.87   -115.82                                   
REMARK 500    ASP A 413       31.52    -99.26                                   
REMARK 500    GLN B  81       77.99    -67.68                                   
REMARK 500    ASN B 103     -161.62   -106.25                                   
REMARK 500    ASP B 104       74.40     53.98                                   
REMARK 500    ASP B 140       39.88    -93.36                                   
REMARK 500    ILE B 206      -70.59    -67.41                                   
REMARK 500    THR B 226       71.49     48.07                                   
REMARK 500    ILE B 341     -157.37   -135.35                                   
REMARK 500    LYS B 354      -84.53   -113.90                                   
REMARK 500    ASP B 413       31.42    -99.74                                   
REMARK 500    LEU C  15      -61.58    -98.79                                   
REMARK 500    GLN C  81       77.59    -67.28                                   
REMARK 500    ASN C 103     -162.24   -106.52                                   
REMARK 500    ASP C 104       73.83     53.72                                   
REMARK 500    ASP C 140       40.50    -92.61                                   
REMARK 500    ILE C 206      -71.14    -67.26                                   
REMARK 500    THR C 226       71.62     48.12                                   
REMARK 500    ILE C 341     -156.88   -136.20                                   
REMARK 500    LYS C 354      -85.35   -116.21                                   
REMARK 500    ASP C 413       30.90    -99.69                                   
REMARK 500    LEU D  15      -60.94    -98.45                                   
REMARK 500    GLN D  81       77.93    -67.21                                   
REMARK 500    ASN D 103     -161.47   -106.50                                   
REMARK 500    ASP D 104       73.75     54.31                                   
REMARK 500    ASP D 140       40.03    -92.66                                   
REMARK 500    ILE D 206      -71.53    -66.51                                   
REMARK 500    THR D 226       72.20     48.04                                   
REMARK 500    ILE D 341     -156.70   -135.69                                   
REMARK 500    LYS D 354      -85.63   -113.91                                   
REMARK 500    ASP D 413       30.52    -99.57                                   
REMARK 500    LEU E  15      -61.20    -98.60                                   
REMARK 500    GLN E  81       78.10    -67.34                                   
REMARK 500    ASN E 103     -161.79   -106.46                                   
REMARK 500    ASP E 104       74.70     54.44                                   
REMARK 500    ASP E 140       40.82    -93.14                                   
REMARK 500    ILE E 206      -71.47    -67.35                                   
REMARK 500    THR E 226       72.91     48.61                                   
REMARK 500    ILE E 341     -157.24   -136.00                                   
REMARK 500    LYS E 354      -85.81   -114.66                                   
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 OG1 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG1 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG1 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG1 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OG1 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX E 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 605                 
DBREF1 6PFF A    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFF A     A0A0S4TER9                          1         521             
DBREF1 6PFF B    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFF B     A0A0S4TER9                          1         521             
DBREF1 6PFF C    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFF C     A0A0S4TER9                          1         521             
DBREF1 6PFF D    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFF D     A0A0S4TER9                          1         521             
DBREF1 6PFF E    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PFF 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    OG1  A 603      32                                                       
HET    MTX  A 604      33                                                       
HET    SO4  A 605       5                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    OG1  B 603      32                                                       
HET    MTX  B 604      33                                                       
HET    SO4  B 605       5                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    OG1  C 603      32                                                       
HET    MTX  C 604      33                                                       
HET    SO4  C 605       5                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    OG1  D 603      32                                                       
HET    MTX  D 604      33                                                       
HET    SO4  D 605       5                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    OG1  E 603      32                                                       
HET    MTX  E 604      33                                                       
HET    SO4  E 605       5                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     UFP 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                        
HETNAM     OG1 2-({4-[(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-                
HETNAM   2 OG1  D]PYRIMIDIN-5-YL)METHYL]BENZENE-1-CARBONYL}AMINO)-4-            
HETNAM   3 OG1  CYANOBENZOIC ACID                                               
HETNAM     MTX METHOTREXATE                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  OG1    5(C22 H16 N6 O4)                                             
FORMUL   9  MTX    5(C20 H22 N8 O5)                                             
FORMUL  10  SO4    5(O4 S 2-)                                                   
FORMUL  31  HOH   *14(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 ILE A   98  ASN A  103  1                                   6    
HELIX    5 AA5 GLY A  115  ASP A  125  1                                  11    
HELIX    6 AA6 LYS A  194  PHE A  207  1                                  14    
HELIX    7 AA7 LYS A  211  HIS A  216  1                                   6    
HELIX    8 AA8 LYS A  220  TYR A  224  5                                   5    
HELIX    9 AA9 GLU A  237  GLY A  251  1                                  15    
HELIX   10 AB1 ALA A  287  LYS A  300  1                                  14    
HELIX   11 AB2 GLY A  305  LYS A  311  1                                   7    
HELIX   12 AB3 SER A  317  GLY A  320  5                                   4    
HELIX   13 AB4 SER A  321  ILE A  328  1                                   8    
HELIX   14 AB5 GLY A  343  HIS A  348  1                                   6    
HELIX   15 AB6 ASP A  366  ASN A  378  1                                  13    
HELIX   16 AB7 LEU A  429  GLY A  450  1                                  22    
HELIX   17 AB8 HIS A  469  SER A  478  1                                  10    
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 GLU B   95  SER B   97  5                                   3    
HELIX   23 AC5 ILE B   98  ASN B  103  1                                   6    
HELIX   24 AC6 GLY B  115  ASP B  125  1                                  11    
HELIX   25 AC7 LYS B  194  PHE B  207  1                                  14    
HELIX   26 AC8 LYS B  211  HIS B  216  5                                   6    
HELIX   27 AC9 LYS B  220  TYR B  224  5                                   5    
HELIX   28 AD1 GLU B  237  GLY B  251  1                                  15    
HELIX   29 AD2 ALA B  287  LYS B  300  1                                  14    
HELIX   30 AD3 GLY B  305  LYS B  311  1                                   7    
HELIX   31 AD4 SER B  317  GLY B  320  5                                   4    
HELIX   32 AD5 SER B  321  ILE B  328  1                                   8    
HELIX   33 AD6 GLY B  343  HIS B  348  1                                   6    
HELIX   34 AD7 ASP B  366  ASN B  378  1                                  13    
HELIX   35 AD8 LEU B  429  GLY B  450  1                                  22    
HELIX   36 AD9 HIS B  469  SER B  478  1                                  10    
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 GLU C   95  SER C   97  5                                   3    
HELIX   42 AE6 ILE C   98  ASN C  103  1                                   6    
HELIX   43 AE7 GLY C  115  ASP C  125  1                                  11    
HELIX   44 AE8 LYS C  194  PHE C  207  1                                  14    
HELIX   45 AE9 LYS C  211  HIS C  216  5                                   6    
HELIX   46 AF1 LYS C  220  TYR C  224  5                                   5    
HELIX   47 AF2 GLU C  237  GLY C  251  1                                  15    
HELIX   48 AF3 ALA C  287  LYS C  300  1                                  14    
HELIX   49 AF4 GLY C  305  LYS C  311  1                                   7    
HELIX   50 AF5 SER C  317  GLY C  320  5                                   4    
HELIX   51 AF6 SER C  321  ILE C  328  1                                   8    
HELIX   52 AF7 ASP C  366  ASN C  378  1                                  13    
HELIX   53 AF8 LEU C  429  GLY C  450  1                                  22    
HELIX   54 AF9 HIS C  469  SER C  478  1                                  10    
HELIX   55 AG1 ASN C  495  PHE C  499  5                                   5    
HELIX   56 AG2 LYS C  500  GLU C  502  5                                   3    
HELIX   57 AG3 ILE D   29  ASN D   42  1                                  14    
HELIX   58 AG4 ARG D   56  ILE D   62  1                                   7    
HELIX   59 AG5 GLU D   95  SER D   97  5                                   3    
HELIX   60 AG6 ILE D   98  ASN D  103  1                                   6    
HELIX   61 AG7 GLY D  115  ASP D  125  1                                  11    
HELIX   62 AG8 LYS D  194  PHE D  207  1                                  14    
HELIX   63 AG9 LYS D  211  HIS D  216  5                                   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  LYS D  311  1                                   7    
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 GLU E   95  SER E   97  5                                   3    
HELIX   80 AI8 ILE E   98  ASN E  103  1                                   6    
HELIX   81 AI9 GLY E  115  ASP E  125  1                                  11    
HELIX   82 AJ1 LYS E  194  PHE E  207  1                                  14    
HELIX   83 AJ2 LYS E  211  HIS E  216  1                                   6    
HELIX   84 AJ3 LYS E  220  TYR E  224  5                                   5    
HELIX   85 AJ4 GLU E  237  GLY E  251  1                                  15    
HELIX   86 AJ5 ALA E  287  LYS E  300  1                                  14    
HELIX   87 AJ6 GLY E  305  LYS E  311  1                                   7    
HELIX   88 AJ7 SER E  317  GLY E  320  5                                   4    
HELIX   89 AJ8 SER E  321  ILE E  328  1                                   8    
HELIX   90 AJ9 ASP E  366  ASN E  378  1                                  13    
HELIX   91 AK1 LEU E  429  GLY E  450  1                                  22    
HELIX   92 AK2 HIS E  469  SER E  478  1                                  10    
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  PHE A  91           
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 ASN A   5  SER A  13  1  N  VAL A   9   O  VAL A 112           
SHEET    6 AA1 8 ARG A 130  VAL A 136  1  O  ARG A 130   N  ILE A   8           
SHEET    7 AA1 8 MET A 173  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA1 8 PHE A 154  MET A 159 -1  N  VAL A 157   O  ILE A 174           
SHEET    1 AA2 2 GLY A  18  GLY A  20  0                                        
SHEET    2 AA2 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
SHEET    1 AA3 2 PHE A 163  THR A 165  0                                        
SHEET    2 AA3 2 ILE A 168  TYR A 170 -1  O  TYR A 170   N  PHE A 163           
SHEET    1 AA4 6 ALA A 252  ARG A 254  0                                        
SHEET    2 AA4 6 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3 AA4 6 GLU A 452  TYR A 466 -1  O  ILE A 460   N  GLN A 268           
SHEET    4 AA4 6 CYS A 415  ASP A 426  1  N  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  GLU A 505   N  LYS A 488           
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  PHE B  91           
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  ALA B  51           
SHEET    5 AA6 8 VAL B   6  SER B  13  1  N  SER B   7   O  ILE B 110           
SHEET    6 AA6 8 ARG B 130  VAL B 136  1  O  ARG B 130   N  ILE B   8           
SHEET    7 AA6 8 MET B 173  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA6 8 PHE B 154  MET B 159 -1  N  LEU B 155   O  GLU B 176           
SHEET    1 AA7 2 GLY B  18  GLY B  20  0                                        
SHEET    2 AA7 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
SHEET    1 AA8 2 PHE B 163  THR B 165  0                                        
SHEET    2 AA8 2 ILE B 168  TYR B 170 -1  O  TYR B 170   N  PHE B 163           
SHEET    1 AA9 6 ALA B 252  ARG B 254  0                                        
SHEET    2 AA9 6 THR B 262  ASP B 273 -1  O  THR B 262   N  ARG B 254           
SHEET    3 AA9 6 GLU B 452  TYR B 466 -1  O  ILE B 460   N  GLN B 268           
SHEET    4 AA9 6 CYS B 415  ASP B 426  1  N  LEU B 420   O  PHE B 459           
SHEET    5 AA9 6 HIS B 403  VAL B 410 -1  N  GLN B 407   O  ASN B 419           
SHEET    6 AA9 6 ILE B 385  THR B 387 -1  N  LEU B 386   O  SER B 406           
SHEET    1 AB1 2 GLN B 486  PHE B 489  0                                        
SHEET    2 AB1 2 ILE B 504  ILE B 507 -1  O  GLU B 505   N  LYS B 488           
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  PHE C  91           
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  ALA C  51           
SHEET    5 AB2 8 ASN C   5  SER C  13  1  N  VAL C   9   O  VAL C 112           
SHEET    6 AB2 8 ARG C 130  VAL C 136  1  O  ARG C 130   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  GLN C 407   O  ASN C 419           
SHEET    6 AB5 6 ILE C 385  THR C 387 -1  N  LEU C 386   O  SER C 406           
SHEET    1 AB6 2 GLN C 486  PHE C 489  0                                        
SHEET    2 AB6 2 ILE C 504  ILE C 507 -1  O  GLU C 505   N  LYS C 488           
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  PHE D  91           
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  ALA D  51           
SHEET    5 AB7 8 ASN D   5  SER D  13  1  N  SER D   7   O  ILE D 110           
SHEET    6 AB7 8 ARG D 130  VAL D 136  1  O  ARG D 130   N  ILE D   8           
SHEET    7 AB7 8 MET D 173  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB7 8 PHE D 154  MET D 159 -1  N  VAL D 157   O  ILE D 174           
SHEET    1 AB8 2 GLY D  18  GLY D  20  0                                        
SHEET    2 AB8 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
SHEET    1 AB9 2 PHE D 163  THR D 165  0                                        
SHEET    2 AB9 2 ILE D 168  TYR D 170 -1  O  TYR D 170   N  PHE D 163           
SHEET    1 AC1 6 ALA D 252  ARG D 254  0                                        
SHEET    2 AC1 6 THR D 262  ASP D 273 -1  O  THR D 262   N  ARG D 254           
SHEET    3 AC1 6 GLU D 452  TYR D 466 -1  O  ILE D 458   N  MET D 270           
SHEET    4 AC1 6 CYS D 415  ASP D 426  1  N  LEU D 420   O  PHE D 459           
SHEET    5 AC1 6 HIS D 403  VAL D 410 -1  N  GLN D 407   O  ASN D 419           
SHEET    6 AC1 6 ILE D 385  THR D 387 -1  N  LEU D 386   O  SER D 406           
SHEET    1 AC2 2 GLN D 486  PHE D 489  0                                        
SHEET    2 AC2 2 ILE D 504  ILE D 507 -1  O  GLU D 505   N  LYS D 488           
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  PHE E  91           
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  ALA E  51           
SHEET    5 AC3 8 ASN E   5  SER E  13  1  N  SER E   7   O  ILE E 110           
SHEET    6 AC3 8 ARG E 130  VAL E 136  1  O  ARG E 130   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  LEU E 155   O  GLU E 176           
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 458   N  MET E 270           
SHEET    4 AC6 6 CYS E 415  ASP E 426  1  N  LEU E 420   O  PHE E 459           
SHEET    5 AC6 6 HIS E 403  VAL E 410 -1  N  GLN E 407   O  ASN E 419           
SHEET    6 AC6 6 ILE E 385  THR E 387 -1  N  LEU E 386   O  SER E 406           
SHEET    1 AC7 2 GLN E 486  PHE E 489  0                                        
SHEET    2 AC7 2 ILE E 504  ILE E 507 -1  O  GLU E 505   N  LYS E 488           
SITE     1 AC1 23 VAL A  10  ALA A  11  ILE A  19  GLY A  23                    
SITE     2 AC1 23 GLN A  24  LEU A  25  GLY A  55  ARG A  56                    
SITE     3 AC1 23 LYS A  57  THR A  58  SER A  61  ILE A  75                    
SITE     4 AC1 23 SER A  76  SER A  77  SER A  78  ARG A  92                    
SITE     5 AC1 23 CYS A 113  GLY A 114  GLY A 115  GLU A 116                    
SITE     6 AC1 23 SER A 117  THR A 145  MTX A 604                               
SITE     1 AC2 15 ARG A 257  TYR A 342  CYS A 402  HIS A 403                    
SITE     2 AC2 15 GLN A 422  ARG A 423  SER A 424  CYS A 425                    
SITE     3 AC2 15 ASP A 426  ASN A 434  HIS A 464  TYR A 466                    
SITE     4 AC2 15 OG1 A 603  ARG B 382  ARG B 383                               
SITE     1 AC3 12 LYS A 284  ALA A 287  ILE A 315  ASN A 319                    
SITE     2 AC3 12 LEU A 399  LEU A 429  GLY A 430  PHE A 433                    
SITE     3 AC3 12 ILE A 515  MET A 517  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  LEU A  33  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  4 HIS A 216  ARG A 246  GLN A 268  ARG B 271                    
SITE     1 AC6 22 VAL B  10  ALA B  11  ILE B  19  GLY B  20                    
SITE     2 AC6 22 GLY B  23  GLN B  24  GLY B  55  ARG B  56                    
SITE     3 AC6 22 LYS B  57  THR B  58  ILE B  75  SER B  76                    
SITE     4 AC6 22 SER B  77  SER B  78  ARG B  92  CYS B 113                    
SITE     5 AC6 22 GLY B 114  GLY B 115  GLU B 116  SER B 117                    
SITE     6 AC6 22 THR B 145  MTX B 604                                          
SITE     1 AC7 15 ARG A 382  ARG A 383  ARG B 257  LEU B 399                    
SITE     2 AC7 15 CYS B 402  HIS B 403  GLN B 422  ARG B 423                    
SITE     3 AC7 15 SER B 424  CYS B 425  ASP B 426  ASN B 434                    
SITE     4 AC7 15 HIS B 464  TYR B 466  OG1 B 603                               
SITE     1 AC8 13 LYS B 284  ALA B 287  ILE B 315  ASN B 319                    
SITE     2 AC8 13 LEU B 399  LEU B 429  GLY B 430  PHE B 433                    
SITE     3 AC8 13 ILE B 515  MET B 517  MET B 519  ALA B 520                    
SITE     4 AC8 13 UFP B 602                                                     
SITE     1 AC9 16 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC9 16 ASP B  32  LEU B  33  LYS B  34  PHE B  36                    
SITE     3 AC9 16 SER B  37  THR B  58  ILE B  62  ARG B  70                    
SITE     4 AC9 16 CYS B 113  TYR B 119  THR B 134  NDP B 601                    
SITE     1 AD1  3 ARG A 271  HIS B 216  GLN B 268                               
SITE     1 AD2 23 VAL C  10  ALA C  11  ILE C  19  GLY C  23                    
SITE     2 AD2 23 GLN C  24  GLY C  55  ARG C  56  LYS C  57                    
SITE     3 AD2 23 THR C  58  SER C  61  ILE C  75  SER C  76                    
SITE     4 AD2 23 SER C  77  SER C  78  ARG C  92  CYS C 113                    
SITE     5 AD2 23 GLY C 114  GLY C 115  GLU C 116  SER C 117                    
SITE     6 AD2 23 ILE C 118  THR C 145  MTX C 604                               
SITE     1 AD3 14 ARG C 257  CYS C 402  HIS C 403  GLN C 422                    
SITE     2 AD3 14 ARG C 423  SER C 424  CYS C 425  ASP C 426                    
SITE     3 AD3 14 ASN C 434  HIS C 464  TYR C 466  OG1 C 603                    
SITE     4 AD3 14 ARG D 382  ARG D 383                                          
SITE     1 AD4 13 LYS C 284  ALA C 287  SER C 290  ILE C 315                    
SITE     2 AD4 13 ASN C 319  LEU C 399  LEU C 429  GLY C 430                    
SITE     3 AD4 13 PHE C 433  ILE C 515  MET C 517  ALA C 520                    
SITE     4 AD4 13 UFP C 602                                                     
SITE     1 AD5 16 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 AD5 16 ASP C  32  LEU C  33  PHE C  36  SER C  37                    
SITE     3 AD5 16 THR C  58  ILE C  62  LEU C  67  ARG C  70                    
SITE     4 AD5 16 CYS C 113  TYR C 119  THR C 134  NDP C 601                    
SITE     1 AD6  4 HIS C 216  ARG C 246  GLN C 268  ARG D 271                    
SITE     1 AD7 22 ALA D  11  ILE D  19  GLY D  20  GLY D  23                    
SITE     2 AD7 22 GLN D  24  LEU D  25  GLY D  55  ARG D  56                    
SITE     3 AD7 22 LYS D  57  THR D  58  ILE D  75  SER D  76                    
SITE     4 AD7 22 SER D  77  SER D  78  ARG D  92  CYS D 113                    
SITE     5 AD7 22 GLY D 114  GLY D 115  GLU D 116  SER D 117                    
SITE     6 AD7 22 THR D 145  MTX D 604                                          
SITE     1 AD8 15 ARG C 382  ARG C 383  ARG D 257  LEU D 399                    
SITE     2 AD8 15 CYS D 402  HIS D 403  GLN D 422  ARG D 423                    
SITE     3 AD8 15 SER D 424  CYS D 425  ASP D 426  ASN D 434                    
SITE     4 AD8 15 HIS D 464  TYR D 466  OG1 D 603                               
SITE     1 AD9 12 LYS D 284  ALA D 287  ILE D 315  ASN D 319                    
SITE     2 AD9 12 LEU D 399  LEU D 429  PHE D 433  ILE D 515                    
SITE     3 AD9 12 MET D 517  MET D 519  ALA D 520  UFP D 602                    
SITE     1 AE1 15 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 AE1 15 ASP D  32  LEU D  33  PHE D  36  SER D  37                    
SITE     3 AE1 15 THR D  58  ILE D  62  ARG D  70  CYS D 113                    
SITE     4 AE1 15 TYR D 119  THR D 134  NDP D 601                               
SITE     1 AE2  2 HIS D 216  GLN D 268                                          
SITE     1 AE3 22 VAL E  10  ALA E  11  ILE E  19  GLY E  23                    
SITE     2 AE3 22 GLN E  24  GLY E  55  ARG E  56  LYS E  57                    
SITE     3 AE3 22 THR E  58  SER E  61  ILE E  75  SER E  76                    
SITE     4 AE3 22 SER E  77  SER E  78  ARG E  92  CYS E 113                    
SITE     5 AE3 22 GLY E 114  GLY E 115  GLU E 116  SER E 117                    
SITE     6 AE3 22 THR E 145  MTX E 604                                          
SITE     1 AE4 16 ARG E 257  ARG E 382  ARG E 383  LEU E 399                    
SITE     2 AE4 16 CYS E 402  HIS E 403  GLN E 422  ARG E 423                    
SITE     3 AE4 16 SER E 424  CYS E 425  ASP E 426  GLY E 430                    
SITE     4 AE4 16 ASN E 434  HIS E 464  TYR E 466  OG1 E 603                    
SITE     1 AE5 12 LYS E 284  ALA E 287  SER E 290  ILE E 315                    
SITE     2 AE5 12 ASN E 319  LEU E 399  LEU E 429  PHE E 433                    
SITE     3 AE5 12 ILE E 515  MET E 517  ALA E 520  UFP E 602                    
SITE     1 AE6 14 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 AE6 14 ASP E  32  LEU E  33  PHE E  36  SER E  37                    
SITE     3 AE6 14 THR E  58  ILE E  62  ARG E  70  CYS E 113                    
SITE     4 AE6 14 THR E 134  NDP E 601                                          
SITE     1 AE7  3 HIS E 216  GLN E 268  ARG E 271                               
CRYST1  213.424  116.794  221.760  90.00  95.69  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  0.000467        0.00000                         
SCALE2      0.000000  0.008562  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004532        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system