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Database: PDB
Entry: 6PF8
LinkDB: 6PF8
Original site: 6PF8 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUN-19   6PF8              
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-CHLOROBENZOIC ACID            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE; 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM HOMINIS;                        
SOURCE   3 ORGANISM_TAXID: 237895;                                              
SOURCE   4 GENE: CHUDEA4_4460;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PA-414                                    
KEYWDS    INHIBITOR, TS, TS-DHFR, TRANSFERASE, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.CZYZYK,M.VALHONDO,W.L.JORGENSEN,K.S.ANDERSON                      
REVDAT   1   02-OCT-19 6PF8    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.    2.53 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) : 2.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 180529                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9027                            
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 47.8831 -  7.8589    0.99     5929   314  0.1525 0.1587        
REMARK   3     2  7.8589 -  6.2422    1.00     5883   310  0.1635 0.1887        
REMARK   3     3  6.2422 -  5.4544    1.00     5852   308  0.1749 0.1950        
REMARK   3     4  5.4544 -  4.9563    1.00     5822   306  0.1537 0.1601        
REMARK   3     5  4.9563 -  4.6014    1.00     5832   307  0.1408 0.1678        
REMARK   3     6  4.6014 -  4.3303    1.00     5811   306  0.1382 0.1481        
REMARK   3     7  4.3303 -  4.1135    1.00     5785   304  0.1552 0.1681        
REMARK   3     8  4.1135 -  3.9345    1.00     5766   304  0.1801 0.2124        
REMARK   3     9  3.9345 -  3.7831    0.99     5806   306  0.1950 0.2314        
REMARK   3    10  3.7831 -  3.6526    0.99     5732   301  0.2030 0.2239        
REMARK   3    11  3.6526 -  3.5385    1.00     5790   305  0.2085 0.2331        
REMARK   3    12  3.5385 -  3.4374    0.99     5777   304  0.2198 0.2256        
REMARK   3    13  3.4374 -  3.3469    0.99     5748   303  0.2308 0.2616        
REMARK   3    14  3.3469 -  3.2652    1.00     5752   302  0.2415 0.2993        
REMARK   3    15  3.2652 -  3.1910    0.99     5759   303  0.2440 0.2587        
REMARK   3    16  3.1910 -  3.1231    0.99     5767   304  0.2490 0.2825        
REMARK   3    17  3.1231 -  3.0607    1.00     5717   301  0.2417 0.2724        
REMARK   3    18  3.0607 -  3.0029    0.99     5795   303  0.2392 0.2735        
REMARK   3    19  3.0029 -  2.9493    1.00     5747   303  0.2477 0.2864        
REMARK   3    20  2.9493 -  2.8993    1.00     5760   303  0.2603 0.3008        
REMARK   3    21  2.8993 -  2.8526    1.00     5781   304  0.2478 0.2699        
REMARK   3    22  2.8526 -  2.8087    1.00     5757   303  0.2589 0.3077        
REMARK   3    23  2.8087 -  2.7674    1.00     5781   305  0.2817 0.3056        
REMARK   3    24  2.7674 -  2.7284    1.00     5748   301  0.2755 0.3174        
REMARK   3    25  2.7284 -  2.6915    1.00     5770   305  0.2737 0.2929        
REMARK   3    26  2.6915 -  2.6566    0.99     5708   300  0.2881 0.3404        
REMARK   3    27  2.6566 -  2.6234    1.00     5780   303  0.2852 0.3199        
REMARK   3    28  2.6234 -  2.5918    1.00     5767   304  0.2723 0.3195        
REMARK   3    29  2.5918 -  2.5616    1.00     5774   304  0.3009 0.3331        
REMARK   3    30  2.5616 -  2.5329    0.66     3806   201  0.3350 0.3821        
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)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.700           
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          21569                                  
REMARK   3   ANGLE     :  0.531          29295                                  
REMARK   3   CHIRALITY :  0.044           3118                                  
REMARK   3   PLANARITY :  0.003           3728                                  
REMARK   3   DIHEDRAL  :  9.882          12573                                  
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 6PF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000242255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-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   : 180633                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.530                              
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     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.60500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.750                              
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   (%): 74.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION 20 % PEG 6000, 0.2 M       
REMARK 280  AMMONIUM SULFATE, 0.06 M LITHIUM SULFATE, 0.1 M TRIS DROP RATIO     
REMARK 280  2:1 ENZYME MIX/WELL SOLUTION, PH 8.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 295.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      107.38850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.76850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.38850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.76850            
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: 14130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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: 14190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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: 14280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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     -214.77700            
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     GLU C   179                                                      
REMARK 465     LYS C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     THR C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     CYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     GLN C   192                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     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     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  68    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     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     GLU A 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  95    CG   CD   OE1  OE2                                  
REMARK 470     MET B 102    CG   SD   CE                                        
REMARK 470     ASN B 103    CG   OD1  ND2                                       
REMARK 470     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 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     GLU C  95    CG   CD   OE1  OE2                                  
REMARK 470     MET C 102    CG   SD   CE                                        
REMARK 470     ASN C 103    CG   OD1  ND2                                       
REMARK 470     LYS C 124    CG   CD   CE   NZ                                   
REMARK 470     GLU C 149    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 178    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     GLU C 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 494    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     LYS D  68    CG   CD   CE   NZ                                   
REMARK 470     GLU D  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  95    CG   CD   OE1  OE2                                  
REMARK 470     MET D 102    CG   SD   CE                                        
REMARK 470     ASN D 103    CG   OD1  ND2                                       
REMARK 470     LYS D 124    CG   CD   CE   NZ                                   
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     GLU E   3    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  95    CG   CD   OE1  OE2                                  
REMARK 470     MET E 102    CG   SD   CE                                        
REMARK 470     ASN E 103    CG   OD1  ND2                                       
REMARK 470     LYS E 124    CG   CD   CE   NZ                                   
REMARK 470     GLU E 149    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 178    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 220    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     GLU E 352    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 370    CG   CD   CE   NZ                                   
REMARK 470     LYS E 516    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 103     -143.21   -151.92                                   
REMARK 500    ASP A 104       76.44     51.72                                   
REMARK 500    ASP A 140       47.56    -85.15                                   
REMARK 500    THR A 226       70.69     47.89                                   
REMARK 500    THR A 283        2.09    -69.79                                   
REMARK 500    ILE A 341     -160.66   -128.96                                   
REMARK 500    HIS A 348       58.24   -140.54                                   
REMARK 500    LYS A 354      -82.53   -114.20                                   
REMARK 500    ASN B 103     -143.13   -152.03                                   
REMARK 500    ASP B 104       76.03     52.01                                   
REMARK 500    ASP B 140       47.97    -85.42                                   
REMARK 500    THR B 226       70.22     48.14                                   
REMARK 500    THR B 283        2.48    -69.06                                   
REMARK 500    ILE B 341     -161.04   -129.74                                   
REMARK 500    HIS B 348       57.75   -140.02                                   
REMARK 500    LYS B 354      -82.42   -113.33                                   
REMARK 500    ASN C 103     -143.36   -151.45                                   
REMARK 500    ASP C 104       75.33     51.21                                   
REMARK 500    ASP C 140       47.35    -84.60                                   
REMARK 500    THR C 226       71.09     48.18                                   
REMARK 500    THR C 283        2.59    -69.14                                   
REMARK 500    ILE C 341     -160.72   -128.98                                   
REMARK 500    HIS C 348       57.83   -140.96                                   
REMARK 500    LYS C 354      -82.83   -114.69                                   
REMARK 500    ASN D 103     -142.38   -152.04                                   
REMARK 500    ASP D 104       75.51     52.39                                   
REMARK 500    ASP D 140       47.28    -85.00                                   
REMARK 500    THR D 226       71.90     48.45                                   
REMARK 500    THR D 283        2.14    -69.51                                   
REMARK 500    ILE D 341     -160.62   -128.97                                   
REMARK 500    HIS D 348       57.38   -140.31                                   
REMARK 500    LYS D 354      -83.00   -112.61                                   
REMARK 500    ASN E 103     -143.22   -152.23                                   
REMARK 500    ASP E 104       76.01     52.26                                   
REMARK 500    ASP E 140       47.59    -84.87                                   
REMARK 500    THR E 226       71.13     47.99                                   
REMARK 500    THR E 283        1.78    -69.82                                   
REMARK 500    GLU E 335      -71.42    -45.32                                   
REMARK 500    HIS E 348       58.17   -141.00                                   
REMARK 500    LYS E 354      -83.38   -113.04                                   
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 OE7 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OE7 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OE7 C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OE7 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OE7 E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX E 604                 
DBREF1 6PF8 A    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF8 A     A0A0S4TER9                          1         521             
DBREF1 6PF8 B    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF8 B     A0A0S4TER9                          1         521             
DBREF1 6PF8 C    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF8 C     A0A0S4TER9                          1         521             
DBREF1 6PF8 D    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF8 D     A0A0S4TER9                          1         521             
DBREF1 6PF8 E    1   521  UNP                  A0A0S4TER9_CRYHO                 
DBREF2 6PF8 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    OE7  A 603      31                                                       
HET    MTX  A 604      33                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    OE7  B 603      31                                                       
HET    MTX  B 604      33                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    OE7  C 603      31                                                       
HET    MTX  C 604      33                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    OE7  D 603      31                                                       
HET    MTX  D 604      33                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    OE7  E 603      31                                                       
HET    MTX  E 604      33                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     UFP 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                        
HETNAM     OE7 2-({4-[(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-                
HETNAM   2 OE7  D]PYRIMIDIN-5-YL)METHYL]BENZENE-1-CARBONYL}AMINO)-4-            
HETNAM   3 OE7  CHLOROBENZOIC ACID                                              
HETNAM     MTX METHOTREXATE                                                     
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  OE7    5(C21 H16 CL N5 O4)                                          
FORMUL   9  MTX    5(C20 H22 N8 O5)                                             
FORMUL  26  HOH   *612(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 ALA A  393  MET A  397  5                                   5    
HELIX   17 AB8 LEU A  429  GLY A  450  1                                  22    
HELIX   18 AB9 HIS A  469  LEU A  477  1                                   9    
HELIX   19 AC1 ASN A  495  PHE A  499  5                                   5    
HELIX   20 AC2 LYS A  500  GLU A  502  5                                   3    
HELIX   21 AC3 ILE B   29  ASN B   42  1                                  14    
HELIX   22 AC4 ARG B   56  ILE B   62  1                                   7    
HELIX   23 AC5 ASN B   93  ILE B   98  1                                   6    
HELIX   24 AC6 ILE B   98  ASN B  103  1                                   6    
HELIX   25 AC7 GLY B  115  ASP B  125  1                                  11    
HELIX   26 AC8 LYS B  194  PHE B  207  1                                  14    
HELIX   27 AC9 LYS B  211  HIS B  216  1                                   6    
HELIX   28 AD1 LYS B  220  TYR B  224  5                                   5    
HELIX   29 AD2 GLU B  237  GLY B  251  1                                  15    
HELIX   30 AD3 ALA B  287  LYS B  300  1                                  14    
HELIX   31 AD4 GLY B  305  LYS B  311  1                                   7    
HELIX   32 AD5 SER B  317  GLY B  320  5                                   4    
HELIX   33 AD6 SER B  321  ILE B  328  1                                   8    
HELIX   34 AD7 GLY B  343  HIS B  348  1                                   6    
HELIX   35 AD8 ASP B  366  ASN B  378  1                                  13    
HELIX   36 AD9 ALA B  393  MET B  397  5                                   5    
HELIX   37 AE1 LEU B  429  GLY B  450  1                                  22    
HELIX   38 AE2 HIS B  469  LEU B  477  1                                   9    
HELIX   39 AE3 ASN B  495  PHE B  499  5                                   5    
HELIX   40 AE4 LYS B  500  GLU B  502  5                                   3    
HELIX   41 AE5 ILE C   29  ASN C   42  1                                  14    
HELIX   42 AE6 ARG C   56  ILE C   62  1                                   7    
HELIX   43 AE7 ASN C   93  ILE C   98  1                                   6    
HELIX   44 AE8 ILE C   98  ASN C  103  1                                   6    
HELIX   45 AE9 GLY C  115  ASP C  125  1                                  11    
HELIX   46 AF1 LYS C  194  PHE C  207  1                                  14    
HELIX   47 AF2 LYS C  211  HIS C  216  1                                   6    
HELIX   48 AF3 LYS C  220  TYR C  224  5                                   5    
HELIX   49 AF4 GLU C  237  GLY C  251  1                                  15    
HELIX   50 AF5 ALA C  287  LYS C  300  1                                  14    
HELIX   51 AF6 GLY C  305  LYS C  311  1                                   7    
HELIX   52 AF7 SER C  317  GLY C  320  5                                   4    
HELIX   53 AF8 SER C  321  ILE C  328  1                                   8    
HELIX   54 AF9 ASP C  366  ASN C  378  1                                  13    
HELIX   55 AG1 ALA C  393  MET C  397  5                                   5    
HELIX   56 AG2 LEU C  429  GLY C  450  1                                  22    
HELIX   57 AG3 HIS C  469  LEU C  477  1                                   9    
HELIX   58 AG4 ASN C  495  PHE C  499  5                                   5    
HELIX   59 AG5 LYS C  500  GLU C  502  5                                   3    
HELIX   60 AG6 ILE D   29  ASN D   42  1                                  14    
HELIX   61 AG7 ARG D   56  ILE D   62  1                                   7    
HELIX   62 AG8 ASN D   93  ILE D   98  1                                   6    
HELIX   63 AG9 ILE D   98  ASN D  103  1                                   6    
HELIX   64 AH1 GLY D  115  ASP D  125  1                                  11    
HELIX   65 AH2 LYS D  194  PHE D  207  1                                  14    
HELIX   66 AH3 LYS D  211  HIS D  216  1                                   6    
HELIX   67 AH4 LYS D  220  TYR D  224  5                                   5    
HELIX   68 AH5 GLU D  237  GLY D  251  1                                  15    
HELIX   69 AH6 ALA D  287  LYS D  300  1                                  14    
HELIX   70 AH7 GLY D  305  LYS D  311  1                                   7    
HELIX   71 AH8 SER D  317  GLY D  320  5                                   4    
HELIX   72 AH9 SER D  321  ILE D  328  1                                   8    
HELIX   73 AI1 GLY D  343  HIS D  348  1                                   6    
HELIX   74 AI2 ASP D  366  ASN D  378  1                                  13    
HELIX   75 AI3 ALA D  393  MET D  397  5                                   5    
HELIX   76 AI4 LEU D  429  GLY D  450  1                                  22    
HELIX   77 AI5 HIS D  469  LEU D  477  1                                   9    
HELIX   78 AI6 ASN D  495  PHE D  499  5                                   5    
HELIX   79 AI7 LYS D  500  GLU D  502  5                                   3    
HELIX   80 AI8 ILE E   29  ASN E   42  1                                  14    
HELIX   81 AI9 ARG E   56  ILE E   62  1                                   7    
HELIX   82 AJ1 ASN E   93  ILE E   98  1                                   6    
HELIX   83 AJ2 ILE E   98  ASN E  103  1                                   6    
HELIX   84 AJ3 GLY E  115  ASP E  125  1                                  11    
HELIX   85 AJ4 LYS E  194  PHE E  207  1                                  14    
HELIX   86 AJ5 LYS E  211  HIS E  216  1                                   6    
HELIX   87 AJ6 LYS E  220  TYR E  224  5                                   5    
HELIX   88 AJ7 GLU E  237  GLY E  251  1                                  15    
HELIX   89 AJ8 ALA E  287  LYS E  300  1                                  14    
HELIX   90 AJ9 GLY E  305  LYS E  311  1                                   7    
HELIX   91 AK1 SER E  317  GLY E  320  5                                   4    
HELIX   92 AK2 SER E  321  ILE E  328  1                                   8    
HELIX   93 AK3 GLY E  343  HIS E  348  1                                   6    
HELIX   94 AK4 ASP E  366  ASN E  378  1                                  13    
HELIX   95 AK5 ALA E  393  MET E  397  5                                   5    
HELIX   96 AK6 LEU E  429  GLY E  450  1                                  22    
HELIX   97 AK7 HIS E  469  LEU E  477  1                                   9    
HELIX   98 AK8 ASN E  495  PHE E  499  5                                   5    
HELIX   99 AK9 LYS E  500  GLU E  502  5                                   3    
SHEET    1 AA1 8 VAL A  88  PHE A  91  0                                        
SHEET    2 AA1 8 ILE A  71  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3 AA1 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4 AA1 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5 AA1 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6 AA1 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7 AA1 8 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA1 8 PHE A 154  MET A 159 -1  N  VAL A 157   O  ILE A 174           
SHEET    1 AA2 8 VAL A  88  PHE A  91  0                                        
SHEET    2 AA2 8 ILE A  71  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3 AA2 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4 AA2 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5 AA2 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6 AA2 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7 AA2 8 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8 AA2 8 PHE A 163  THR A 165 -1  N  PHE A 163   O  TYR A 170           
SHEET    1 AA3 2 GLY A  18  GLY A  20  0                                        
SHEET    2 AA3 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
SHEET    1 AA4 6 ALA A 252  ARG A 254  0                                        
SHEET    2 AA4 6 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3 AA4 6 GLU A 452  TYR A 466 -1  O  ILE A 460   N  GLN A 268           
SHEET    4 AA4 6 CYS A 415  ASP A 426  1  N  LEU A 420   O  PHE A 459           
SHEET    5 AA4 6 HIS A 403  VAL A 410 -1  N  LEU A 405   O  TYR A 421           
SHEET    6 AA4 6 ILE A 385  THR A 387 -1  N  LEU A 386   O  SER A 406           
SHEET    1 AA5 2 GLN A 486  PHE A 489  0                                        
SHEET    2 AA5 2 ILE A 504  ILE A 507 -1  O  ILE A 507   N  GLN A 486           
SHEET    1 AA6 8 VAL B  88  PHE B  91  0                                        
SHEET    2 AA6 8 ILE B  71  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3 AA6 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4 AA6 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5 AA6 8 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6 AA6 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7 AA6 8 ILE B 168  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA6 8 PHE B 154  MET B 159 -1  N  VAL B 157   O  ILE B 174           
SHEET    1 AA7 8 VAL B  88  PHE B  91  0                                        
SHEET    2 AA7 8 ILE B  71  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3 AA7 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4 AA7 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5 AA7 8 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6 AA7 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7 AA7 8 ILE B 168  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8 AA7 8 PHE B 163  THR B 165 -1  N  PHE B 163   O  TYR B 170           
SHEET    1 AA8 2 GLY B  18  GLY B  20  0                                        
SHEET    2 AA8 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
SHEET    1 AA9 6 ALA B 252  ARG B 254  0                                        
SHEET    2 AA9 6 THR B 262  ASP B 273 -1  O  SER B 264   N  ALA B 252           
SHEET    3 AA9 6 GLU B 452  TYR B 466 -1  O  ILE B 460   N  GLN B 268           
SHEET    4 AA9 6 CYS B 415  ASP B 426  1  N  LEU B 420   O  PHE B 459           
SHEET    5 AA9 6 HIS B 403  VAL B 410 -1  N  LEU B 405   O  TYR B 421           
SHEET    6 AA9 6 ILE B 385  THR B 387 -1  N  LEU B 386   O  SER B 406           
SHEET    1 AB1 2 GLN B 486  PHE B 489  0                                        
SHEET    2 AB1 2 ILE B 504  ILE B 507 -1  O  ILE B 507   N  GLN B 486           
SHEET    1 AB2 8 VAL C  88  PHE C  91  0                                        
SHEET    2 AB2 8 ILE C  71  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3 AB2 8 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4 AB2 8 ILE C 107  VAL C 112  1  O  PHE C 111   N  ILE C  53           
SHEET    5 AB2 8 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6 AB2 8 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7 AB2 8 ILE C 168  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8 AB2 8 PHE C 154  MET C 159 -1  N  VAL C 157   O  ILE C 174           
SHEET    1 AB3 8 VAL C  88  PHE C  91  0                                        
SHEET    2 AB3 8 ILE C  71  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3 AB3 8 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4 AB3 8 ILE C 107  VAL C 112  1  O  PHE C 111   N  ILE C  53           
SHEET    5 AB3 8 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6 AB3 8 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7 AB3 8 ILE C 168  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8 AB3 8 PHE C 163  THR C 165 -1  N  PHE C 163   O  TYR C 170           
SHEET    1 AB4 2 GLY C  18  GLY C  20  0                                        
SHEET    2 AB4 2 THR C 145  TYR C 146 -1  O  THR C 145   N  ILE C  19           
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  LEU C 405   O  TYR C 421           
SHEET    6 AB5 6 ILE C 385  THR C 387 -1  N  LEU C 386   O  SER C 406           
SHEET    1 AB6 2 GLN C 486  PHE C 489  0                                        
SHEET    2 AB6 2 ILE C 504  ILE C 507 -1  O  ILE C 507   N  GLN C 486           
SHEET    1 AB7 8 VAL D  88  PHE D  91  0                                        
SHEET    2 AB7 8 ILE D  71  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3 AB7 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4 AB7 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5 AB7 8 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6 AB7 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB7 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB7 8 PHE D 154  MET D 159 -1  N  VAL D 157   O  ILE D 174           
SHEET    1 AB8 8 VAL D  88  PHE D  91  0                                        
SHEET    2 AB8 8 ILE D  71  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3 AB8 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4 AB8 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5 AB8 8 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6 AB8 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7 AB8 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8 AB8 8 PHE D 163  THR D 165 -1  N  PHE D 163   O  TYR D 170           
SHEET    1 AB9 2 GLY D  18  GLY D  20  0                                        
SHEET    2 AB9 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
SHEET    1 AC1 6 ALA D 252  ARG D 254  0                                        
SHEET    2 AC1 6 THR D 262  ASP D 273 -1  O  SER D 264   N  ALA D 252           
SHEET    3 AC1 6 GLU D 452  TYR D 466 -1  O  ILE D 460   N  GLN D 268           
SHEET    4 AC1 6 CYS D 415  ASP D 426  1  N  LEU D 420   O  PHE D 459           
SHEET    5 AC1 6 HIS D 403  VAL D 410 -1  N  LEU D 405   O  TYR D 421           
SHEET    6 AC1 6 ILE D 385  THR D 387 -1  N  LEU D 386   O  SER D 406           
SHEET    1 AC2 2 GLN D 486  PHE D 489  0                                        
SHEET    2 AC2 2 ILE D 504  ILE D 507 -1  O  ILE D 507   N  GLN D 486           
SHEET    1 AC3 8 VAL E  88  PHE E  91  0                                        
SHEET    2 AC3 8 ILE E  71  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3 AC3 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4 AC3 8 ILE E 107  VAL E 112  1  O  PHE E 111   N  ILE E  53           
SHEET    5 AC3 8 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6 AC3 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7 AC3 8 ILE E 168  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8 AC3 8 PHE E 154  MET E 159 -1  N  VAL E 157   O  ILE E 174           
SHEET    1 AC4 8 VAL E  88  PHE E  91  0                                        
SHEET    2 AC4 8 ILE E  71  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3 AC4 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4 AC4 8 ILE E 107  VAL E 112  1  O  PHE E 111   N  ILE E  53           
SHEET    5 AC4 8 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6 AC4 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7 AC4 8 ILE E 168  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8 AC4 8 PHE E 163  THR E 165 -1  N  PHE E 163   O  TYR E 170           
SHEET    1 AC5 2 GLY E  18  GLY E  20  0                                        
SHEET    2 AC5 2 THR E 145  TYR E 146 -1  O  THR E 145   N  ILE E  19           
SHEET    1 AC6 6 ALA E 252  ARG E 254  0                                        
SHEET    2 AC6 6 THR E 262  ASP E 273 -1  O  THR E 262   N  ARG E 254           
SHEET    3 AC6 6 GLU E 452  TYR E 466 -1  O  ILE E 460   N  GLN E 268           
SHEET    4 AC6 6 CYS E 415  ASP E 426  1  N  LEU E 420   O  PHE E 459           
SHEET    5 AC6 6 HIS E 403  VAL E 410 -1  N  GLN E 407   O  ASN E 419           
SHEET    6 AC6 6 ILE E 385  THR E 387 -1  N  LEU E 386   O  SER E 406           
SHEET    1 AC7 2 GLN E 486  PHE E 489  0                                        
SHEET    2 AC7 2 ILE E 504  ILE E 507 -1  O  ILE E 507   N  GLN E 486           
SITE     1 AC1 24 VAL A  10  ALA A  11  ILE A  19  GLY A  23                    
SITE     2 AC1 24 GLN A  24  LEU A  25  GLY A  55  ARG A  56                    
SITE     3 AC1 24 LYS A  57  THR A  58  ILE A  75  SER A  76                    
SITE     4 AC1 24 SER A  77  SER A  78  ARG A  92  GLY A 114                    
SITE     5 AC1 24 GLY A 115  GLU A 116  SER A 117  THR A 145                    
SITE     6 AC1 24 MTX A 604  HOH A 709  HOH A 776  HOH A 787                    
SITE     1 AC2 14 ARG A 257  CYS A 402  HIS A 403  GLN A 422                    
SITE     2 AC2 14 ARG A 423  SER A 424  CYS A 425  ASP A 426                    
SITE     3 AC2 14 ASN A 434  HIS A 464  TYR A 466  OE7 A 603                    
SITE     4 AC2 14 ARG B 382  ARG B 383                                          
SITE     1 AC3 14 ALA A 287  SER A 290  ILE A 315  ASN A 319                    
SITE     2 AC3 14 ASP A 426  LEU A 429  GLY A 430  PHE A 433                    
SITE     3 AC3 14 TYR A 466  ILE A 515  ALA A 520  UFP A 602                    
SITE     4 AC3 14 HOH A 718  HOH A 790                                          
SITE     1 AC4 15 VAL A   9  VAL A  10  ALA A  11  ASP A  32                    
SITE     2 AC4 15 PHE A  36  SER A  37  SER A  61  ILE A  62                    
SITE     3 AC4 15 ARG A  70  CYS A 113  TYR A 119  THR A 134                    
SITE     4 AC4 15 NDP A 601  HOH A 788  HOH A 808                               
SITE     1 AC5 27 VAL B  10  ALA B  11  ILE B  19  GLY B  20                    
SITE     2 AC5 27 GLY B  23  GLN B  24  LEU B  25  GLY B  55                    
SITE     3 AC5 27 ARG B  56  LYS B  57  THR B  58  ILE B  75                    
SITE     4 AC5 27 SER B  76  SER B  77  SER B  78  ARG B  92                    
SITE     5 AC5 27 GLY B 114  GLY B 115  GLU B 116  SER B 117                    
SITE     6 AC5 27 THR B 145  MTX B 604  HOH B 701  HOH B 710                    
SITE     7 AC5 27 HOH B 765  HOH B 777  HOH B 845                               
SITE     1 AC6 15 ARG A 382  ARG A 383  ARG B 257  CYS B 402                    
SITE     2 AC6 15 HIS B 403  GLN B 422  ARG B 423  SER B 424                    
SITE     3 AC6 15 CYS B 425  ASP B 426  ASN B 434  HIS B 464                    
SITE     4 AC6 15 TYR B 466  OE7 B 603  HOH B 852                               
SITE     1 AC7 17 ALA B 287  SER B 290  ILE B 315  ASN B 319                    
SITE     2 AC7 17 LEU B 399  ASP B 426  LEU B 429  GLY B 430                    
SITE     3 AC7 17 PHE B 433  TYR B 466  ILE B 515  ALA B 520                    
SITE     4 AC7 17 UFP B 602  HOH B 703  HOH B 708  HOH B 755                    
SITE     5 AC7 17 HOH B 801                                                     
SITE     1 AC8 17 VAL B   9  VAL B  10  ALA B  11  LEU B  25                    
SITE     2 AC8 17 ASP B  32  LEU B  33  PHE B  36  SER B  37                    
SITE     3 AC8 17 ILE B  62  ARG B  70  CYS B 113  TYR B 119                    
SITE     4 AC8 17 THR B 134  NDP B 601  HOH B 701  HOH B 789                    
SITE     5 AC8 17 HOH B 814                                                     
SITE     1 AC9 25 VAL C  10  ALA C  11  ILE C  19  GLY C  20                    
SITE     2 AC9 25 GLY C  23  GLN C  24  LEU C  25  GLY C  55                    
SITE     3 AC9 25 ARG C  56  LYS C  57  THR C  58  ILE C  75                    
SITE     4 AC9 25 SER C  76  SER C  77  SER C  78  ARG C  92                    
SITE     5 AC9 25 CYS C 113  GLY C 114  GLY C 115  GLU C 116                    
SITE     6 AC9 25 SER C 117  THR C 145  MTX C 604  HOH C 731                    
SITE     7 AC9 25 HOH C 754                                                     
SITE     1 AD1 13 ARG C 257  CYS C 402  GLN C 422  ARG C 423                    
SITE     2 AD1 13 SER C 424  CYS C 425  ASP C 426  ASN C 434                    
SITE     3 AD1 13 HIS C 464  TYR C 466  OE7 C 603  ARG D 382                    
SITE     4 AD1 13 ARG D 383                                                     
SITE     1 AD2 13 LYS C 284  ALA C 287  ILE C 315  ASN C 319                    
SITE     2 AD2 13 ASP C 426  LEU C 429  GLY C 430  PHE C 433                    
SITE     3 AD2 13 ILE C 515  ALA C 520  UFP C 602  HOH C 709                    
SITE     4 AD2 13 HOH C 741                                                     
SITE     1 AD3 15 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 AD3 15 ASP C  32  PHE C  36  SER C  37  SER C  61                    
SITE     3 AD3 15 ILE C  62  ARG C  70  CYS C 113  TYR C 119                    
SITE     4 AD3 15 THR C 134  NDP C 601  HOH C 727                               
SITE     1 AD4 22 VAL D  10  ALA D  11  ILE D  19  GLY D  20                    
SITE     2 AD4 22 GLY D  23  GLN D  24  LEU D  25  GLY D  55                    
SITE     3 AD4 22 ARG D  56  LYS D  57  THR D  58  ILE D  75                    
SITE     4 AD4 22 SER D  76  SER D  77  SER D  78  ARG D  92                    
SITE     5 AD4 22 GLY D 114  GLY D 115  GLU D 116  SER D 117                    
SITE     6 AD4 22 THR D 145  MTX D 604                                          
SITE     1 AD5 14 ARG C 382  ARG C 383  ARG D 257  CYS D 402                    
SITE     2 AD5 14 HIS D 403  GLN D 422  ARG D 423  SER D 424                    
SITE     3 AD5 14 CYS D 425  ASP D 426  ASN D 434  HIS D 464                    
SITE     4 AD5 14 TYR D 466  OE7 D 603                                          
SITE     1 AD6 14 LYS D 284  ALA D 287  ILE D 315  ASN D 319                    
SITE     2 AD6 14 LEU D 399  ASP D 426  LEU D 429  GLY D 430                    
SITE     3 AD6 14 PHE D 433  TYR D 466  ILE D 515  ALA D 520                    
SITE     4 AD6 14 UFP D 602  HOH D 736                                          
SITE     1 AD7 16 VAL D   9  VAL D  10  ALA D  11  LEU D  25                    
SITE     2 AD7 16 ASP D  32  LEU D  33  PHE D  36  SER D  37                    
SITE     3 AD7 16 SER D  61  ILE D  62  ARG D  70  CYS D 113                    
SITE     4 AD7 16 TYR D 119  THR D 134  NDP D 601  HOH D 757                    
SITE     1 AD8 26 VAL E  10  ALA E  11  ILE E  19  GLY E  20                    
SITE     2 AD8 26 ILE E  21  GLY E  23  GLN E  24  LEU E  25                    
SITE     3 AD8 26 GLY E  55  ARG E  56  LYS E  57  THR E  58                    
SITE     4 AD8 26 ILE E  75  SER E  76  SER E  77  SER E  78                    
SITE     5 AD8 26 ARG E  92  CYS E 113  GLY E 114  GLY E 115                    
SITE     6 AD8 26 GLU E 116  SER E 117  ASP E 121  THR E 145                    
SITE     7 AD8 26 MTX E 604  HOH E 719                                          
SITE     1 AD9 13 ARG E 257  ARG E 382  ARG E 383  CYS E 402                    
SITE     2 AD9 13 GLN E 422  ARG E 423  SER E 424  CYS E 425                    
SITE     3 AD9 13 ASP E 426  ASN E 434  HIS E 464  TYR E 466                    
SITE     4 AD9 13 OE7 E 603                                                     
SITE     1 AE1 14 LYS E 284  ALA E 287  SER E 290  ILE E 315                    
SITE     2 AE1 14 ASN E 319  LEU E 399  ASP E 426  LEU E 429                    
SITE     3 AE1 14 GLY E 430  PHE E 433  TYR E 466  ILE E 515                    
SITE     4 AE1 14 ALA E 520  UFP E 602                                          
SITE     1 AE2 16 VAL E   9  VAL E  10  ALA E  11  LEU E  25                    
SITE     2 AE2 16 ASP E  32  LEU E  33  PHE E  36  SER E  37                    
SITE     3 AE2 16 SER E  61  ILE E  62  ARG E  70  CYS E 113                    
SITE     4 AE2 16 TYR E 119  THR E 134  NDP E 601  HOH E 702                    
CRYST1  214.777  117.537  222.817  90.00  95.65  90.00 C 1 2 1      20          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004656  0.000000  0.000460        0.00000                         
SCALE2      0.000000  0.008508  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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