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Database: PDB
Entry: 4Q0E
LinkDB: 4Q0E
Original site: 4Q0E 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-APR-14   4Q0E              
TITLE     CRYSTAL STRUCTURE OF TS-DHFR FROM CRYPTOSPORIDIUM HOMINIS IN COMPLEX  
TITLE    2 WITH NADPH, FDUMP AND 2-AMINO-4-OXO-4,7-DIHYDRO-PYRROLO[2,3-         
TITLE    3 D]PYRIMIDINE-METHYL-PHENYL-L-GLUTAMIC ACID.                          
CAVEAT     4Q0E    THE CHIRAL CENTER ATOM CT1 OF LIGAND 2XB HAS GEOMETRY NOT    
CAVEAT   2 4Q0E    CORRESPONDING TO THE LIGAND DEFINITION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE; 
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: BIFUNCTIONAL THYMIDYLATE SYNTHASE-DIHYDROFOLATE REDUCTASE; 
COMPND   5 EC: 2.1.1.45, 1.5.1.3;                                               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM HOMINIS;                        
SOURCE   3 ORGANISM_TAXID: 237895;                                              
SOURCE   4 GENE: CHRO.40506, TS-DHFR;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: PA414;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    BIFUNCTIONAL ENZYME, TRANSFERASE, OXIDOREDUCTASE, TRANSFERASE-        
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.P.KUMAR,K.S.ANDERSON                                                
REVDAT   2   22-NOV-17 4Q0E    1       REMARK                                   
REVDAT   1   15-OCT-14 4Q0E    0                                                
JRNL        AUTH   V.P.KUMAR,J.A.CISNEROS,K.M.FREY,A.CASTELLANOS-GONZALEZ,      
JRNL        AUTH 2 Y.WANG,A.GANGJEE,A.C.WHITE,W.L.JORGENSEN,K.S.ANDERSON        
JRNL        TITL   STRUCTURAL STUDIES PROVIDE CLUES FOR ANALOG DESIGN OF        
JRNL        TITL 2 SPECIFIC INHIBITORS OF CRYPTOSPORIDIUM HOMINIS THYMIDYLATE   
JRNL        TITL 3 SYNTHASE-DIHYDROFOLATE REDUCTASE.                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  24  4158 2014              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   25127103                                                     
JRNL        DOI    10.1016/J.BMCL.2014.07.049                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 124074                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.620                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2015                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.0613 -  6.6936    0.99     9468   158  0.2074 0.2170        
REMARK   3     2  6.6936 -  5.3151    0.97     9126   150  0.2256 0.2458        
REMARK   3     3  5.3151 -  4.6439    0.93     8723   141  0.1963 0.2011        
REMARK   3     4  4.6439 -  4.2196    0.92     8660   142  0.1945 0.2185        
REMARK   3     5  4.2196 -  3.9173    0.93     8605   140  0.2323 0.2706        
REMARK   3     6  3.9173 -  3.6864    0.93     8671   139  0.2586 0.2675        
REMARK   3     7  3.6864 -  3.5019    0.93     8707   142  0.2788 0.2808        
REMARK   3     8  3.5019 -  3.3495    0.93     8674   157  0.3032 0.3167        
REMARK   3     9  3.3495 -  3.2205    0.94     8703   146  0.3261 0.3242        
REMARK   3    10  3.2205 -  3.1094    0.94     8724   131  0.3414 0.3307        
REMARK   3    11  3.1094 -  3.0122    0.94     8780   140  0.3602 0.3897        
REMARK   3    12  3.0122 -  2.9261    0.94     8780   145  0.3677 0.4247        
REMARK   3    13  2.9261 -  2.8491    0.94     8787   137  0.3696 0.3811        
REMARK   3    14  2.8491 -  2.7796    0.83     7651   147  0.3544 0.3641        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.11                          
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      :  0.004          21656                                  
REMARK   3   ANGLE     :  0.730          29375                                  
REMARK   3   CHIRALITY :  0.044           3110                                  
REMARK   3   PLANARITY :  0.004           3739                                  
REMARK   3   DIHEDRAL  : 14.580           8162                                  
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 : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 4095                                        
REMARK   3     RMSD               : 0.156                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 4099                                        
REMARK   3     RMSD               : 0.182                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 4099                                        
REMARK   3     RMSD               : 0.158                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 3:178 OR RESSEQ         
REMARK   3                          193:521 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 4099                                        
REMARK   3     RMSD               : 0.193                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Q0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085446.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY COOLED CRYSTAL       
REMARK 200                                   MONOCHROMATOR WITH HORIZONTAL      
REMARK 200                                   FOCUSING SAGITTAL BEND SECOND      
REMARK 200                                   MONO CRYSTAL WITH 4:1              
REMARK 200                                   MAGNIFICATION RATIO AND            
REMARK 200                                   VERTICALLY FOCUSING MIRROR.        
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124124                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.13200                            
REMARK 200  R SYM                      (I) : 0.13200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4KY8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG 6000, 60 MM AMMONIUM       
REMARK 280  SULFATE, 200 MM LITHIUM SULFATE, AND 100 MM TRIS PH 8.0. CHTS-      
REMARK 280  DHFR ENZYME (APPROXIMATELY 7 MG/ML) WITH 1 MM NADPH, 1 MM FDUMP     
REMARK 280  AND 0.5 MM INHIBITOR., VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      106.81450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.77000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.81450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.77000            
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: 11910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A   179                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLN A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     CYS A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     GLN A   192                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B   179                                                      
REMARK 465     LYS B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     THR B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     GLN B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     CYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLU C   179                                                      
REMARK 465     LYS C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     THR C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     GLN C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     CYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     GLN C   192                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLU D   179                                                      
REMARK 465     LYS D   180                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     THR D   182                                                      
REMARK 465     LEU D   183                                                      
REMARK 465     GLN D   184                                                      
REMARK 465     ASN D   185                                                      
REMARK 465     CYS D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     ARG D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     GLN D   192                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     GLU E   179                                                      
REMARK 465     LYS E   180                                                      
REMARK 465     LYS E   181                                                      
REMARK 465     THR E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     GLN E   184                                                      
REMARK 465     ASN E   185                                                      
REMARK 465     CYS E   186                                                      
REMARK 465     ASP E   187                                                      
REMARK 465     PRO E   188                                                      
REMARK 465     ALA E   189                                                      
REMARK 465     ARG E   190                                                      
REMARK 465     GLY E   191                                                      
REMARK 465     GLN E   192                                                      
REMARK 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     ASP A  82    CG   OD1  OD2                                       
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  99    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 194    CG   CD   CE   NZ                                   
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     ASP C  82    CG   OD1  OD2                                       
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 194    CG   CD   CE   NZ                                   
REMARK 470     LYS C 516    CG   CD   CE   NZ                                   
REMARK 470     ASP D  82    CG   OD1  OD2                                       
REMARK 470     GLU D  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     ASP E  82    CG   OD1  OD2                                       
REMARK 470     GLU E  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 194    CG   CD   CE   NZ                                   
REMARK 470     LYS E 516    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CZ   ARG B   254     OH   TYR D   409              1.93            
REMARK 500   NE   ARG B   254     OH   TYR D   409              1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 115   C   -  N   -  CA  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    GLY B 115   C   -  N   -  CA  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    GLY C 115   C   -  N   -  CA  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    GLY D 115   C   -  N   -  CA  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    GLY E 115   C   -  N   -  CA  ANGL. DEV. = -13.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 105        6.34    -55.90                                   
REMARK 500    ASN A 126       72.88     56.06                                   
REMARK 500    GLU A 139      -10.93   -151.62                                   
REMARK 500    ASP A 140       32.51    -88.69                                   
REMARK 500    HIS A 216       63.56   -118.50                                   
REMARK 500    THR A 226       74.52     51.32                                   
REMARK 500    PRO A 279       64.98    -64.05                                   
REMARK 500    ALA A 287       88.53    -68.07                                   
REMARK 500    SER A 321      151.82    -49.78                                   
REMARK 500    PRO A 340       59.49    -66.19                                   
REMARK 500    LYS A 354      -88.73   -106.13                                   
REMARK 500    TYR A 360       31.88    -90.30                                   
REMARK 500    ASN A 378       79.52   -152.92                                   
REMARK 500    HIS A 384       87.01    -68.43                                   
REMARK 500    ASP A 413       31.72    -96.18                                   
REMARK 500    LEU B  15      -69.44    -98.07                                   
REMARK 500    ASP B 104       80.91     55.99                                   
REMARK 500    ASN B 126       72.85     56.22                                   
REMARK 500    GLU B 139      -11.31   -151.61                                   
REMARK 500    ASP B 140       32.45    -88.67                                   
REMARK 500    HIS B 216       63.58   -118.45                                   
REMARK 500    THR B 226       74.61     51.45                                   
REMARK 500    PRO B 279       65.14    -64.26                                   
REMARK 500    ALA B 287       88.52    -67.98                                   
REMARK 500    SER B 321      151.84    -49.75                                   
REMARK 500    LYS B 354      -88.76   -106.23                                   
REMARK 500    TYR B 360       31.87    -89.97                                   
REMARK 500    ASN B 378       79.51   -153.01                                   
REMARK 500    HIS B 384       81.40    -67.39                                   
REMARK 500    ASP B 413       31.72    -96.09                                   
REMARK 500    LEU C  15      -69.43    -98.00                                   
REMARK 500    ASP C 104       81.08     56.00                                   
REMARK 500    ASN C 126       72.80     56.13                                   
REMARK 500    ASP C 140       32.53    -88.83                                   
REMARK 500    HIS C 216       63.48   -118.46                                   
REMARK 500    THR C 226       74.51     51.47                                   
REMARK 500    PRO C 279       65.17    -64.05                                   
REMARK 500    ALA C 287       88.73    -68.15                                   
REMARK 500    SER C 321      151.68    -49.75                                   
REMARK 500    LYS C 354      -88.74   -106.11                                   
REMARK 500    TYR C 360       31.85    -90.12                                   
REMARK 500    ASN C 378       79.53   -152.97                                   
REMARK 500    HIS C 384       92.51    -65.97                                   
REMARK 500    ASP C 413       31.82    -96.25                                   
REMARK 500    LEU D  15      -69.72    -98.01                                   
REMARK 500    ASP D 104       80.96     55.97                                   
REMARK 500    ASN D 126       72.61     56.12                                   
REMARK 500    ASP D 140       32.55    -88.69                                   
REMARK 500    HIS D 216       63.50   -118.50                                   
REMARK 500    THR D 226       74.64     51.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      73 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB 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 2XB B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UFP E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2XB E 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QZF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HJ3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DL5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DL6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OIP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KY8   RELATED DB: PDB                                   
DBREF  4Q0E A    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4Q0E B    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4Q0E C    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4Q0E D    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
DBREF  4Q0E E    1   521  UNP    Q5CGA3   Q5CGA3_CRYHO     1    521             
SEQRES   1 A  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 A  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 A  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 A  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 A  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 A  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 A  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 A  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 A  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 A  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 A  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 A  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 A  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 A  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 A  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 A  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 A  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 A  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 A  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 A  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 A  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 A  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 A  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 A  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 A  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 A  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 A  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 A  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 A  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 A  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 A  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 A  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 A  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 A  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 A  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 A  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 A  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 A  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 A  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 A  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 A  521  VAL                                                          
SEQRES   1 B  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 B  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 B  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 B  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 B  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 B  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 B  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 B  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 B  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 B  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 B  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 B  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 B  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 B  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 B  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 B  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 B  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 B  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 B  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 B  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 B  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 B  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 B  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 B  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 B  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 B  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 B  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 B  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 B  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 B  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 B  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 B  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 B  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 B  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 B  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 B  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 B  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 B  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 B  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 B  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 B  521  VAL                                                          
SEQRES   1 C  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 C  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 C  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 C  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 C  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 C  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 C  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 C  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 C  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 C  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 C  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 C  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 C  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 C  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 C  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 C  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 C  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 C  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 C  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 C  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 C  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 C  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 C  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 C  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 C  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 C  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 C  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 C  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 C  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 C  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 C  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 C  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 C  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 C  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 C  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 C  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 C  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 C  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 C  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 C  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 C  521  VAL                                                          
SEQRES   1 D  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 D  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 D  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 D  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 D  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 D  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 D  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 D  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 D  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 D  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 D  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 D  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 D  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 D  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 D  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 D  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 D  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 D  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 D  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 D  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 D  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 D  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 D  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 D  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 D  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 D  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 D  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 D  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 D  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 D  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 D  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 D  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 D  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 D  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 D  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 D  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 D  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 D  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 D  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 D  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 D  521  VAL                                                          
SEQRES   1 E  521  MET SER GLU LYS ASN VAL SER ILE VAL VAL ALA ALA SER          
SEQRES   2 E  521  VAL LEU SER SER GLY ILE GLY ILE ASN GLY GLN LEU PRO          
SEQRES   3 E  521  TRP SER ILE SER GLU ASP LEU LYS PHE PHE SER LYS ILE          
SEQRES   4 E  521  THR ASN ASN LYS CYS ASP SER ASN LYS LYS ASN ALA LEU          
SEQRES   5 E  521  ILE MET GLY ARG LYS THR TRP ASP SER ILE GLY ARG ARG          
SEQRES   6 E  521  PRO LEU LYS ASN ARG ILE ILE VAL VAL ILE SER SER SER          
SEQRES   7 E  521  LEU PRO GLN ASP GLU ALA ASP PRO ASN VAL VAL VAL PHE          
SEQRES   8 E  521  ARG ASN LEU GLU ASP SER ILE GLU ASN LEU MET ASN ASP          
SEQRES   9 E  521  ASP SER ILE GLU ASN ILE PHE VAL CYS GLY GLY GLU SER          
SEQRES  10 E  521  ILE TYR ARG ASP ALA LEU LYS ASP ASN PHE VAL ASP ARG          
SEQRES  11 E  521  ILE TYR LEU THR ARG VAL ALA LEU GLU ASP ILE GLU PHE          
SEQRES  12 E  521  ASP THR TYR PHE PRO GLU ILE PRO GLU THR PHE LEU PRO          
SEQRES  13 E  521  VAL TYR MET SER GLN THR PHE CYS THR LYS ASN ILE SER          
SEQRES  14 E  521  TYR ASP PHE MET ILE PHE GLU LYS GLN GLU LYS LYS THR          
SEQRES  15 E  521  LEU GLN ASN CYS ASP PRO ALA ARG GLY GLN LEU LYS SER          
SEQRES  16 E  521  ILE ASP ASP THR VAL ASP LEU LEU GLY GLU ILE PHE GLY          
SEQRES  17 E  521  ILE ARG LYS MET GLY ASN ARG HIS LYS PHE PRO LYS GLU          
SEQRES  18 E  521  GLU ILE TYR ASN THR PRO SER ILE ARG PHE GLY ARG GLU          
SEQRES  19 E  521  HIS TYR GLU PHE GLN TYR LEU ASP LEU LEU SER ARG VAL          
SEQRES  20 E  521  LEU GLU ASN GLY ALA TYR ARG GLU ASN ARG THR GLY ILE          
SEQRES  21 E  521  SER THR TYR SER ILE PHE GLY GLN MET MET ARG PHE ASP          
SEQRES  22 E  521  MET ARG GLU SER PHE PRO LEU LEU THR THR LYS LYS VAL          
SEQRES  23 E  521  ALA ILE ARG SER ILE PHE GLU GLU LEU ILE TRP PHE ILE          
SEQRES  24 E  521  LYS GLY ASP THR ASN GLY ASN HIS LEU ILE GLU LYS LYS          
SEQRES  25 E  521  VAL TYR ILE TRP SER GLY ASN GLY SER LYS GLU TYR LEU          
SEQRES  26 E  521  GLU ARG ILE GLY LEU GLY HIS ARG GLU GLU ASN ASP LEU          
SEQRES  27 E  521  GLY PRO ILE TYR GLY PHE GLN TRP ARG HIS TYR ASN GLY          
SEQRES  28 E  521  GLU TYR LYS THR MET HIS ASP ASP TYR THR GLY VAL GLY          
SEQRES  29 E  521  VAL ASP GLN LEU ALA LYS LEU ILE GLU THR LEU LYS ASN          
SEQRES  30 E  521  ASN PRO LYS ASP ARG ARG HIS ILE LEU THR ALA TRP ASN          
SEQRES  31 E  521  PRO SER ALA LEU SER GLN MET ALA LEU PRO PRO CYS HIS          
SEQRES  32 E  521  VAL LEU SER GLN TYR TYR VAL THR ASN ASP ASN CYS LEU          
SEQRES  33 E  521  SER CYS ASN LEU TYR GLN ARG SER CYS ASP LEU GLY LEU          
SEQRES  34 E  521  GLY SER PRO PHE ASN ILE ALA SER TYR ALA ILE LEU THR          
SEQRES  35 E  521  MET MET LEU ALA GLN VAL CYS GLY TYR GLU PRO GLY GLU          
SEQRES  36 E  521  LEU ALA ILE PHE ILE GLY ASP ALA HIS ILE TYR GLU ASN          
SEQRES  37 E  521  HIS LEU THR GLN LEU LYS GLU GLN LEU SER ARG THR PRO          
SEQRES  38 E  521  ARG PRO PHE PRO GLN LEU LYS PHE LYS ARG LYS VAL GLU          
SEQRES  39 E  521  ASN ILE GLU ASP PHE LYS TRP GLU ASP ILE GLU LEU ILE          
SEQRES  40 E  521  GLY TYR TYR PRO TYR PRO THR ILE LYS MET ASP MET ALA          
SEQRES  41 E  521  VAL                                                          
HET    NDP  A 601      48                                                       
HET    UFP  A 602      21                                                       
HET    2XB  A 603      30                                                       
HET    2XB  A 604      30                                                       
HET    NDP  B 601      48                                                       
HET    UFP  B 602      21                                                       
HET    2XB  B 603      30                                                       
HET    2XB  B 604      30                                                       
HET    NDP  C 601      48                                                       
HET    UFP  C 602      21                                                       
HET    2XB  C 603      30                                                       
HET    2XB  C 604      30                                                       
HET    NDP  D 601      48                                                       
HET    UFP  D 602      21                                                       
HET    2XB  D 603      30                                                       
HET    2XB  D 604      30                                                       
HET    NDP  E 601      48                                                       
HET    UFP  E 602      21                                                       
HET    2XB  E 603      30                                                       
HET    2XB  E 604      30                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     UFP 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                        
HETNAM     2XB N-{4-[(2-AMINO-4-HYDROXY-7H-PYRROLO[2,3-D]PYRIMIDIN-5-           
HETNAM   2 2XB  YL)METHYL]BENZOYL}-L-GLUTAMIC ACID                              
FORMUL   6  NDP    5(C21 H30 N7 O17 P3)                                         
FORMUL   7  UFP    5(C9 H12 F N2 O8 P)                                          
FORMUL   8  2XB    10(C19 H19 N5 O6)                                            
FORMUL  26  HOH   *18(H2 O)                                                     
HELIX    1   1 ILE A   29  ASN A   42  1                                  14    
HELIX    2   2 ARG A   56  ILE A   62  1                                   7    
HELIX    3   3 ASN A   93  ILE A   98  1                                   6    
HELIX    4   4 GLY A  115  ASP A  125  1                                  11    
HELIX    5   5 LYS A  194  PHE A  207  1                                  14    
HELIX    6   6 LYS A  211  HIS A  216  1                                   6    
HELIX    7   7 LYS A  220  TYR A  224  5                                   5    
HELIX    8   8 GLU A  237  GLY A  251  1                                  15    
HELIX    9   9 ALA A  287  LYS A  300  1                                  14    
HELIX   10  10 ASN A  304  GLU A  310  1                                   7    
HELIX   11  11 SER A  321  ILE A  328  1                                   8    
HELIX   12  12 GLY A  343  HIS A  348  1                                   6    
HELIX   13  13 ASP A  366  ASN A  378  1                                  13    
HELIX   14  14 LEU A  429  CYS A  449  1                                  21    
HELIX   15  15 HIS A  469  LEU A  477  1                                   9    
HELIX   16  16 ASN A  495  PHE A  499  5                                   5    
HELIX   17  17 LYS A  500  GLU A  502  5                                   3    
HELIX   18  18 ILE B   29  ASN B   42  1                                  14    
HELIX   19  19 ARG B   56  ILE B   62  1                                   7    
HELIX   20  20 ASN B   93  ILE B   98  1                                   6    
HELIX   21  21 GLY B  115  ASP B  125  1                                  11    
HELIX   22  22 LYS B  194  PHE B  207  1                                  14    
HELIX   23  23 LYS B  211  ARG B  215  5                                   5    
HELIX   24  24 LYS B  220  TYR B  224  5                                   5    
HELIX   25  25 GLU B  237  GLY B  251  1                                  15    
HELIX   26  26 ALA B  287  LYS B  300  1                                  14    
HELIX   27  27 ASN B  304  GLU B  310  1                                   7    
HELIX   28  28 SER B  321  ILE B  328  1                                   8    
HELIX   29  29 GLY B  343  HIS B  348  1                                   6    
HELIX   30  30 ASP B  366  ASN B  378  1                                  13    
HELIX   31  31 LEU B  429  CYS B  449  1                                  21    
HELIX   32  32 HIS B  469  LEU B  477  1                                   9    
HELIX   33  33 ASN B  495  PHE B  499  5                                   5    
HELIX   34  34 LYS B  500  GLU B  502  5                                   3    
HELIX   35  35 ILE C   29  ASN C   42  1                                  14    
HELIX   36  36 ARG C   56  ILE C   62  1                                   7    
HELIX   37  37 ASN C   93  ILE C   98  1                                   6    
HELIX   38  38 GLY C  115  ASP C  125  1                                  11    
HELIX   39  39 LYS C  194  PHE C  207  1                                  14    
HELIX   40  40 LYS C  211  ARG C  215  5                                   5    
HELIX   41  41 LYS C  220  TYR C  224  5                                   5    
HELIX   42  42 GLU C  237  GLY C  251  1                                  15    
HELIX   43  43 ALA C  287  LYS C  300  1                                  14    
HELIX   44  44 ASN C  304  GLU C  310  1                                   7    
HELIX   45  45 SER C  321  ILE C  328  1                                   8    
HELIX   46  46 GLY C  343  HIS C  348  1                                   6    
HELIX   47  47 ASP C  366  ASN C  378  1                                  13    
HELIX   48  48 LEU C  429  CYS C  449  1                                  21    
HELIX   49  49 HIS C  469  LEU C  477  1                                   9    
HELIX   50  50 ASN C  495  PHE C  499  5                                   5    
HELIX   51  51 LYS C  500  GLU C  502  5                                   3    
HELIX   52  52 ILE D   29  ASN D   42  1                                  14    
HELIX   53  53 ARG D   56  ILE D   62  1                                   7    
HELIX   54  54 ASN D   93  ILE D   98  1                                   6    
HELIX   55  55 GLY D  115  ASP D  125  1                                  11    
HELIX   56  56 LYS D  194  PHE D  207  1                                  14    
HELIX   57  57 LYS D  211  ARG D  215  5                                   5    
HELIX   58  58 LYS D  220  TYR D  224  5                                   5    
HELIX   59  59 GLU D  237  GLY D  251  1                                  15    
HELIX   60  60 ALA D  287  LYS D  300  1                                  14    
HELIX   61  61 ASN D  304  GLU D  310  1                                   7    
HELIX   62  62 SER D  321  ILE D  328  1                                   8    
HELIX   63  63 GLY D  343  HIS D  348  1                                   6    
HELIX   64  64 ASP D  366  ASN D  378  1                                  13    
HELIX   65  65 LEU D  429  CYS D  449  1                                  21    
HELIX   66  66 HIS D  469  LEU D  477  1                                   9    
HELIX   67  67 ASN D  495  PHE D  499  5                                   5    
HELIX   68  68 LYS D  500  GLU D  502  5                                   3    
HELIX   69  69 ILE E   29  ASN E   42  1                                  14    
HELIX   70  70 ARG E   56  ILE E   62  1                                   7    
HELIX   71  71 ASN E   93  ILE E   98  1                                   6    
HELIX   72  72 GLY E  115  ASP E  125  1                                  11    
HELIX   73  73 LYS E  194  PHE E  207  1                                  14    
HELIX   74  74 LYS E  211  ARG E  215  5                                   5    
HELIX   75  75 LYS E  220  TYR E  224  5                                   5    
HELIX   76  76 GLU E  237  GLY E  251  1                                  15    
HELIX   77  77 ALA E  287  LYS E  300  1                                  14    
HELIX   78  78 ASN E  304  GLU E  310  1                                   7    
HELIX   79  79 SER E  321  ILE E  328  1                                   8    
HELIX   80  80 GLY E  343  HIS E  348  1                                   6    
HELIX   81  81 ASP E  366  ASN E  378  1                                  13    
HELIX   82  82 LEU E  429  CYS E  449  1                                  21    
HELIX   83  83 HIS E  469  LEU E  477  1                                   9    
HELIX   84  84 ASN E  495  PHE E  499  5                                   5    
HELIX   85  85 LYS E  500  GLU E  502  5                                   3    
SHEET    1   A 8 VAL A  88  PHE A  91  0                                        
SHEET    2   A 8 ARG A  70  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3   A 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4   A 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5   A 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6   A 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7   A 8 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8   A 8 PHE A 154  MET A 159 -1  N  LEU A 155   O  GLU A 176           
SHEET    1   B 8 VAL A  88  PHE A  91  0                                        
SHEET    2   B 8 ARG A  70  ILE A  75  1  N  VAL A  74   O  VAL A  89           
SHEET    3   B 8 LYS A  49  GLY A  55  1  N  LEU A  52   O  VAL A  73           
SHEET    4   B 8 ILE A 107  VAL A 112  1  O  PHE A 111   N  ILE A  53           
SHEET    5   B 8 VAL A   6  SER A  13  1  N  SER A   7   O  VAL A 112           
SHEET    6   B 8 ARG A 130  VAL A 136  1  O  TYR A 132   N  ILE A   8           
SHEET    7   B 8 ILE A 168  LYS A 177 -1  O  MET A 173   N  LEU A 133           
SHEET    8   B 8 PHE A 163  THR A 165 -1  N  PHE A 163   O  TYR A 170           
SHEET    1   C 2 GLY A  18  GLY A  20  0                                        
SHEET    2   C 2 THR A 145  TYR A 146 -1  O  THR A 145   N  ILE A  19           
SHEET    1   D 6 ALA A 252  ARG A 254  0                                        
SHEET    2   D 6 THR A 262  ASP A 273 -1  O  THR A 262   N  ARG A 254           
SHEET    3   D 6 GLU A 452  TYR A 466 -1  O  ILE A 458   N  MET A 270           
SHEET    4   D 6 CYS A 415  ASP A 426  1  N  GLN A 422   O  GLY A 461           
SHEET    5   D 6 HIS A 403  VAL A 410 -1  N  LEU A 405   O  TYR A 421           
SHEET    6   D 6 ILE A 385  THR A 387 -1  N  LEU A 386   O  SER A 406           
SHEET    1   E 2 GLN A 486  PHE A 489  0                                        
SHEET    2   E 2 ILE A 504  ILE A 507 -1  O  GLU A 505   N  LYS A 488           
SHEET    1   F 8 VAL B  88  PHE B  91  0                                        
SHEET    2   F 8 ARG B  70  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3   F 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4   F 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5   F 8 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6   F 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7   F 8 ILE B 168  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8   F 8 PHE B 154  MET B 159 -1  N  LEU B 155   O  GLU B 176           
SHEET    1   G 8 VAL B  88  PHE B  91  0                                        
SHEET    2   G 8 ARG B  70  ILE B  75  1  N  VAL B  74   O  VAL B  89           
SHEET    3   G 8 LYS B  49  GLY B  55  1  N  LEU B  52   O  VAL B  73           
SHEET    4   G 8 ILE B 107  VAL B 112  1  O  PHE B 111   N  ILE B  53           
SHEET    5   G 8 VAL B   6  SER B  13  1  N  SER B   7   O  VAL B 112           
SHEET    6   G 8 ARG B 130  VAL B 136  1  O  TYR B 132   N  ILE B   8           
SHEET    7   G 8 ILE B 168  LYS B 177 -1  O  MET B 173   N  LEU B 133           
SHEET    8   G 8 PHE B 163  THR B 165 -1  N  PHE B 163   O  TYR B 170           
SHEET    1   H 2 GLY B  18  GLY B  20  0                                        
SHEET    2   H 2 THR B 145  TYR B 146 -1  O  THR B 145   N  ILE B  19           
SHEET    1   I 6 ALA B 252  ARG B 254  0                                        
SHEET    2   I 6 THR B 262  ASP B 273 -1  O  THR B 262   N  ARG B 254           
SHEET    3   I 6 GLU B 452  TYR B 466 -1  O  ALA B 463   N  ILE B 265           
SHEET    4   I 6 CYS B 415  ASP B 426  1  N  GLN B 422   O  GLY B 461           
SHEET    5   I 6 HIS B 403  VAL B 410 -1  N  GLN B 407   O  ASN B 419           
SHEET    6   I 6 ILE B 385  THR B 387 -1  N  LEU B 386   O  SER B 406           
SHEET    1   J 2 GLN B 486  PHE B 489  0                                        
SHEET    2   J 2 ILE B 504  ILE B 507 -1  O  GLU B 505   N  LYS B 488           
SHEET    1   K 8 VAL C  88  PHE C  91  0                                        
SHEET    2   K 8 ARG C  70  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3   K 8 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4   K 8 ILE C 107  VAL C 112  1  O  PHE C 111   N  ILE C  53           
SHEET    5   K 8 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6   K 8 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7   K 8 ILE C 168  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8   K 8 PHE C 154  MET C 159 -1  N  LEU C 155   O  GLU C 176           
SHEET    1   L 8 VAL C  88  PHE C  91  0                                        
SHEET    2   L 8 ARG C  70  ILE C  75  1  N  VAL C  74   O  VAL C  89           
SHEET    3   L 8 LYS C  49  GLY C  55  1  N  LEU C  52   O  VAL C  73           
SHEET    4   L 8 ILE C 107  VAL C 112  1  O  PHE C 111   N  ILE C  53           
SHEET    5   L 8 VAL C   6  SER C  13  1  N  SER C   7   O  VAL C 112           
SHEET    6   L 8 ARG C 130  VAL C 136  1  O  TYR C 132   N  ILE C   8           
SHEET    7   L 8 ILE C 168  LYS C 177 -1  O  MET C 173   N  LEU C 133           
SHEET    8   L 8 PHE C 163  THR C 165 -1  N  PHE C 163   O  TYR C 170           
SHEET    1   M 2 GLY C  18  GLY C  20  0                                        
SHEET    2   M 2 THR C 145  TYR C 146 -1  O  THR C 145   N  ILE C  19           
SHEET    1   N 6 ALA C 252  ARG C 254  0                                        
SHEET    2   N 6 THR C 262  ASP C 273 -1  O  THR C 262   N  ARG C 254           
SHEET    3   N 6 GLU C 452  TYR C 466 -1  O  ILE C 458   N  MET C 270           
SHEET    4   N 6 CYS C 415  ASP C 426  1  N  GLN C 422   O  GLY C 461           
SHEET    5   N 6 HIS C 403  VAL C 410 -1  N  TYR C 409   O  SER C 417           
SHEET    6   N 6 ILE C 385  THR C 387 -1  N  LEU C 386   O  SER C 406           
SHEET    1   O 2 GLN C 486  PHE C 489  0                                        
SHEET    2   O 2 ILE C 504  ILE C 507 -1  O  GLU C 505   N  LYS C 488           
SHEET    1   P 8 VAL D  88  PHE D  91  0                                        
SHEET    2   P 8 ARG D  70  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3   P 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4   P 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5   P 8 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6   P 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7   P 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8   P 8 PHE D 154  MET D 159 -1  N  LEU D 155   O  GLU D 176           
SHEET    1   Q 8 VAL D  88  PHE D  91  0                                        
SHEET    2   Q 8 ARG D  70  ILE D  75  1  N  VAL D  74   O  VAL D  89           
SHEET    3   Q 8 LYS D  49  GLY D  55  1  N  LEU D  52   O  VAL D  73           
SHEET    4   Q 8 ILE D 107  VAL D 112  1  O  PHE D 111   N  ILE D  53           
SHEET    5   Q 8 VAL D   6  SER D  13  1  N  SER D   7   O  VAL D 112           
SHEET    6   Q 8 ARG D 130  VAL D 136  1  O  TYR D 132   N  ILE D   8           
SHEET    7   Q 8 ILE D 168  LYS D 177 -1  O  MET D 173   N  LEU D 133           
SHEET    8   Q 8 PHE D 163  THR D 165 -1  N  PHE D 163   O  TYR D 170           
SHEET    1   R 2 GLY D  18  GLY D  20  0                                        
SHEET    2   R 2 THR D 145  TYR D 146 -1  O  THR D 145   N  ILE D  19           
SHEET    1   S 6 ALA D 252  ARG D 254  0                                        
SHEET    2   S 6 THR D 262  ASP D 273 -1  O  THR D 262   N  ARG D 254           
SHEET    3   S 6 GLU D 452  TYR D 466 -1  O  ILE D 458   N  MET D 270           
SHEET    4   S 6 CYS D 415  ASP D 426  1  N  GLN D 422   O  GLY D 461           
SHEET    5   S 6 HIS D 403  VAL D 410 -1  N  LEU D 405   O  TYR D 421           
SHEET    6   S 6 ILE D 385  THR D 387 -1  N  LEU D 386   O  SER D 406           
SHEET    1   T 2 GLN D 486  PHE D 489  0                                        
SHEET    2   T 2 ILE D 504  ILE D 507 -1  O  GLU D 505   N  LYS D 488           
SHEET    1   U 8 VAL E  88  PHE E  91  0                                        
SHEET    2   U 8 ARG E  70  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3   U 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4   U 8 ILE E 107  VAL E 112  1  O  PHE E 111   N  ILE E  53           
SHEET    5   U 8 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6   U 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7   U 8 ILE E 168  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8   U 8 PHE E 154  MET E 159 -1  N  LEU E 155   O  GLU E 176           
SHEET    1   V 8 VAL E  88  PHE E  91  0                                        
SHEET    2   V 8 ARG E  70  ILE E  75  1  N  VAL E  74   O  VAL E  89           
SHEET    3   V 8 LYS E  49  GLY E  55  1  N  LEU E  52   O  VAL E  73           
SHEET    4   V 8 ILE E 107  VAL E 112  1  O  PHE E 111   N  ILE E  53           
SHEET    5   V 8 VAL E   6  SER E  13  1  N  SER E   7   O  VAL E 112           
SHEET    6   V 8 ARG E 130  VAL E 136  1  O  TYR E 132   N  ILE E   8           
SHEET    7   V 8 ILE E 168  LYS E 177 -1  O  MET E 173   N  LEU E 133           
SHEET    8   V 8 PHE E 163  THR E 165 -1  N  PHE E 163   O  TYR E 170           
SHEET    1   W 2 GLY E  18  GLY E  20  0                                        
SHEET    2   W 2 THR E 145  TYR E 146 -1  O  THR E 145   N  ILE E  19           
SHEET    1   X 6 ALA E 252  ARG E 254  0                                        
SHEET    2   X 6 THR E 262  ASP E 273 -1  O  THR E 262   N  ARG E 254           
SHEET    3   X 6 GLU E 452  TYR E 466 -1  O  ILE E 458   N  MET E 270           
SHEET    4   X 6 CYS E 415  ASP E 426  1  N  GLN E 422   O  GLY E 461           
SHEET    5   X 6 HIS E 403  VAL E 410 -1  N  TYR E 409   O  SER E 417           
SHEET    6   X 6 ILE E 385  THR E 387 -1  N  LEU E 386   O  SER E 406           
SHEET    1   Y 2 GLN E 486  PHE E 489  0                                        
SHEET    2   Y 2 ILE E 504  ILE E 507 -1  O  GLU E 505   N  LYS E 488           
SITE     1 AC1 21 VAL A  10  ALA A  11  ILE A  19  GLY A  23                    
SITE     2 AC1 21 GLN A  24  LEU A  25  GLY A  55  ARG A  56                    
SITE     3 AC1 21 LYS A  57  THR A  58  ILE A  75  SER A  76                    
SITE     4 AC1 21 SER A  77  SER A  78  ARG A  92  GLY A 114                    
SITE     5 AC1 21 GLY A 115  GLU A 116  SER A 117  THR A 145                    
SITE     6 AC1 21 2XB A 604                                                     
SITE     1 AC2 16 ARG A 257  TYR A 342  CYS A 402  HIS A 403                    
SITE     2 AC2 16 ARG A 423  SER A 424  CYS A 425  ASP A 426                    
SITE     3 AC2 16 GLY A 430  ASN A 434  HIS A 464  TYR A 466                    
SITE     4 AC2 16 2XB A 603  HOH A 704  ARG C 382  ARG C 383                    
SITE     1 AC3 11 SER A 290  ILE A 315  ASN A 319  ASP A 426                    
SITE     2 AC3 11 LEU A 429  GLY A 430  PHE A 433  TYR A 466                    
SITE     3 AC3 11 MET A 519  ALA A 520  UFP A 602                               
SITE     1 AC4 11 VAL A   9  VAL A  10  ALA A  11  ASP A  32                    
SITE     2 AC4 11 LYS A  34  PHE A  36  SER A  37  ARG A  70                    
SITE     3 AC4 11 CYS A 113  THR A 134  NDP A 601                               
SITE     1 AC5 21 VAL B  10  ALA B  11  ILE B  19  GLY B  23                    
SITE     2 AC5 21 GLN B  24  LEU B  25  GLY B  55  ARG B  56                    
SITE     3 AC5 21 LYS B  57  THR B  58  ILE B  75  SER B  76                    
SITE     4 AC5 21 SER B  77  SER B  78  ARG B  92  GLY B 114                    
SITE     5 AC5 21 GLY B 115  GLU B 116  SER B 117  THR B 145                    
SITE     6 AC5 21 2XB B 604                                                     
SITE     1 AC6 15 ARG B 257  TYR B 342  CYS B 402  HIS B 403                    
SITE     2 AC6 15 ARG B 423  SER B 424  CYS B 425  ASP B 426                    
SITE     3 AC6 15 GLY B 430  ASN B 434  HIS B 464  TYR B 466                    
SITE     4 AC6 15 2XB B 603  ARG D 382  ARG D 383                               
SITE     1 AC7 11 SER B 290  ILE B 315  ASN B 319  ASP B 426                    
SITE     2 AC7 11 LEU B 429  GLY B 430  PHE B 433  TYR B 466                    
SITE     3 AC7 11 MET B 519  ALA B 520  UFP B 602                               
SITE     1 AC8 11 VAL B   9  VAL B  10  ALA B  11  ASP B  32                    
SITE     2 AC8 11 LYS B  34  PHE B  36  SER B  37  ARG B  70                    
SITE     3 AC8 11 CYS B 113  THR B 134  NDP B 601                               
SITE     1 AC9 21 VAL C  10  ALA C  11  ILE C  19  GLY C  23                    
SITE     2 AC9 21 GLN C  24  LEU C  25  GLY C  55  ARG C  56                    
SITE     3 AC9 21 LYS C  57  THR C  58  ILE C  75  SER C  76                    
SITE     4 AC9 21 SER C  77  SER C  78  ARG C  92  GLY C 114                    
SITE     5 AC9 21 GLY C 115  GLU C 116  SER C 117  THR C 145                    
SITE     6 AC9 21 2XB C 604                                                     
SITE     1 BC1 14 ARG A 382  ARG A 383  ARG C 257  TYR C 342                    
SITE     2 BC1 14 CYS C 402  HIS C 403  ARG C 423  SER C 424                    
SITE     3 BC1 14 CYS C 425  ASP C 426  ASN C 434  HIS C 464                    
SITE     4 BC1 14 TYR C 466  2XB C 603                                          
SITE     1 BC2 11 SER C 290  ILE C 315  ASN C 319  ASP C 426                    
SITE     2 BC2 11 LEU C 429  GLY C 430  PHE C 433  TYR C 466                    
SITE     3 BC2 11 MET C 519  ALA C 520  UFP C 602                               
SITE     1 BC3 12 VAL C   9  VAL C  10  ALA C  11  LEU C  25                    
SITE     2 BC3 12 ASP C  32  LYS C  34  PHE C  36  SER C  37                    
SITE     3 BC3 12 ARG C  70  CYS C 113  THR C 134  NDP C 601                    
SITE     1 BC4 21 VAL D  10  ALA D  11  ILE D  19  GLY D  23                    
SITE     2 BC4 21 GLN D  24  LEU D  25  GLY D  55  ARG D  56                    
SITE     3 BC4 21 LYS D  57  THR D  58  ILE D  75  SER D  76                    
SITE     4 BC4 21 SER D  77  SER D  78  ARG D  92  GLY D 114                    
SITE     5 BC4 21 GLY D 115  GLU D 116  SER D 117  THR D 145                    
SITE     6 BC4 21 2XB D 604                                                     
SITE     1 BC5 15 ARG B 382  ARG B 383  ARG D 257  TYR D 342                    
SITE     2 BC5 15 CYS D 402  HIS D 403  ARG D 423  SER D 424                    
SITE     3 BC5 15 CYS D 425  ASP D 426  GLY D 430  ASN D 434                    
SITE     4 BC5 15 HIS D 464  TYR D 466  2XB D 603                               
SITE     1 BC6 11 SER D 290  ILE D 315  ASN D 319  ASP D 426                    
SITE     2 BC6 11 LEU D 429  GLY D 430  PHE D 433  TYR D 466                    
SITE     3 BC6 11 MET D 519  ALA D 520  UFP D 602                               
SITE     1 BC7 11 VAL D   9  VAL D  10  ALA D  11  ASP D  32                    
SITE     2 BC7 11 LYS D  34  PHE D  36  SER D  37  ARG D  70                    
SITE     3 BC7 11 CYS D 113  THR D 134  NDP D 601                               
SITE     1 BC8 19 ALA E  11  ILE E  19  GLY E  23  GLN E  24                    
SITE     2 BC8 19 GLY E  55  ARG E  56  LYS E  57  THR E  58                    
SITE     3 BC8 19 ILE E  75  SER E  76  SER E  77  SER E  78                    
SITE     4 BC8 19 ARG E  92  GLY E 114  GLY E 115  GLU E 116                    
SITE     5 BC8 19 SER E 117  THR E 145  2XB E 604                               
SITE     1 BC9 13 ARG E 257  TYR E 342  CYS E 402  HIS E 403                    
SITE     2 BC9 13 ARG E 423  SER E 424  CYS E 425  ASP E 426                    
SITE     3 BC9 13 GLY E 430  ASN E 434  HIS E 464  TYR E 466                    
SITE     4 BC9 13 2XB E 603                                                     
SITE     1 CC1 11 SER E 290  ILE E 315  ASN E 319  ASP E 426                    
SITE     2 CC1 11 LEU E 429  GLY E 430  PHE E 433  TYR E 466                    
SITE     3 CC1 11 MET E 519  ALA E 520  UFP E 602                               
SITE     1 CC2 11 VAL E   9  VAL E  10  ALA E  11  ASP E  32                    
SITE     2 CC2 11 LYS E  34  PHE E  36  SER E  37  ARG E  70                    
SITE     3 CC2 11 CYS E 113  THR E 134  NDP E 601                               
CRYST1  213.629  115.540  217.973  90.00  94.56  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      0.004681  0.000000  0.000373        0.00000                         
SCALE2      0.000000  0.008655  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004602        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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