GenomeNet

Database: PDB
Entry: 5HQY
LinkDB: 5HQY
Original site: 5HQY 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 22-JAN-16   5HQY              
TITLE     HUMAN DIHYDROFOLATE REDUCTASE COMPLEX WITH NADPH AND 5-METHYL-6-(2',  
TITLE    2 3',4'-TRIFLUOROPHENYLTHIO)THIENO[2,3-D]PYRIMIDINE-2,4-DIAMINE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DHFR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDS5                                      
KEYWDS    OXIDOREDUCTASE TERNARY COMPLEX WITH TRIFLUOROMETHYL INHIBITOR,        
KEYWDS   2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CODY                                                                
REVDAT   3   11-DEC-19 5HQY    1       REMARK                                   
REVDAT   2   20-SEP-17 5HQY    1       REMARK                                   
REVDAT   1   25-JAN-17 5HQY    0                                                
JRNL        AUTH   V.CODY,A.GANGJEE                                             
JRNL        TITL   HUMAN DIHYDROFOLATE REDUCTASE TERNARY COMPLEX WITH A SERIES  
JRNL        TITL 2 OF FLUORINE SUBSTITUTED                                      
JRNL        TITL 3 5-METHYL-6-PHENYTHIO)THIENO[2,3-D]PYRIMIDINE-2,4-DIAMINES    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34399                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1805                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.46                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2484                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.4220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1502                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.744         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1637 ; 0.029 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2227 ; 2.744 ; 2.051       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   185 ; 7.125 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    71 ;36.549 ;24.789       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   286 ;16.370 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;14.015 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   233 ; 0.201 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1228 ; 0.016 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5HQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217569.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.975                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 1.500                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : 0.02000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.30                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1U72                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM KP04, 60% AMSO4, 3%V/V ETOH, PH   
REMARK 280  6.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.25800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.97502            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.54900            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       43.25800            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       24.97502            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.54900            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       43.25800            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       24.97502            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.54900            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.95004            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.09800            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.95004            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.09800            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.95004            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.09800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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   O    TYR A   162     O    HOH A   301              1.16            
REMARK 500   CB   SER A    59     O    HOH A   304              1.47            
REMARK 500   O    ALA A    86     O    HOH A   302              1.57            
REMARK 500   C    ALA A    86     O    HOH A   302              1.67            
REMARK 500   ND2  ASN A     5     O    HOH A   303              1.74            
REMARK 500   C    TYR A   162     O    HOH A   301              1.75            
REMARK 500   CG   ASN A     5     O    HOH A   303              1.75            
REMARK 500   O    HOH A   328     O    HOH A   385              1.83            
REMARK 500   O    HOH A   311     O    HOH A   339              2.07            
REMARK 500   O    HOH A   355     O    HOH A   381              2.13            
REMARK 500   N    HIS A    87     O    HOH A   302              2.18            
REMARK 500   O2D  NDP A   201     FAE  63Y A   203              2.19            
REMARK 500   CB   SER A   167     O    HOH A   317              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   345     O    HOH A   386     8554     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  87   NE2   HIS A  87   CD2    -0.071                       
REMARK 500    HIS A 130   CG    HIS A 130   CD2     0.061                       
REMARK 500    SER A 167   CB    SER A 167   OG     -0.091                       
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    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL A 112   CA  -  CB  -  CG1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 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 110      -95.02    -76.92                                   
REMARK 500    MET A 139       34.58    -84.10                                   
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 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A      
REMARK 800  203                                                                 
DBREF  5HQY A    1   186  UNP    P00374   DYR_HUMAN        2    187             
SEQRES   1 A  186  VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN          
SEQRES   2 A  186  MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO          
SEQRES   3 A  186  LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR          
SEQRES   4 A  186  THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET          
SEQRES   5 A  186  GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG          
SEQRES   6 A  186  PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU          
SEQRES   7 A  186  LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG          
SEQRES   8 A  186  SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU          
SEQRES   9 A  186  LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY          
SEQRES  10 A  186  SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS          
SEQRES  11 A  186  LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU          
SEQRES  12 A  186  SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR          
SEQRES  13 A  186  LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL          
SEQRES  14 A  186  GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR          
SEQRES  15 A  186  GLU LYS ASN ASP                                              
HET    NDP  A 201      48                                                       
HET    63Y  A 202      22                                                       
HET    63Y  A 203      22                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     63Y 5-METHYL-6-[(2,3,4-TRIFLUOROPHENYL)SULFANYL]THIENO[2,3-          
HETNAM   2 63Y  D]PYRIMIDINE-2,4-DIAMINE                                        
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  63Y    2(C13 H9 F3 N4 S2)                                           
FORMUL   5  HOH   *93(H2 O)                                                     
HELIX    1 AA1 LEU A   27  THR A   40  1                                  14    
HELIX    2 AA2 LYS A   54  ILE A   60  1                                   7    
HELIX    3 AA3 PRO A   61  ARG A   65  5                                   5    
HELIX    4 AA4 SER A   92  GLU A  101  1                                  10    
HELIX    5 AA5 GLN A  102  ASN A  107  1                                   6    
HELIX    6 AA6 GLY A  117  ASN A  126  1                                  10    
SHEET    1 AA1 8 PHE A  88  SER A  90  0                                        
SHEET    2 AA1 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3 AA1 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4 AA1 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5 AA1 8 LEU A   4  SER A  11  1  N  ASN A   5   O  ILE A 114           
SHEET    6 AA1 8 HIS A 130  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7 AA1 8 ILE A 175  ASN A 185 -1  O  LYS A 178   N  ARG A 137           
SHEET    8 AA1 8 LYS A 157  LEU A 158 -1  N  LYS A 157   O  GLU A 183           
SHEET    1 AA2 8 PHE A  88  SER A  90  0                                        
SHEET    2 AA2 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3 AA2 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4 AA2 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5 AA2 8 LEU A   4  SER A  11  1  N  ASN A   5   O  ILE A 114           
SHEET    6 AA2 8 HIS A 130  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7 AA2 8 ILE A 175  ASN A 185 -1  O  LYS A 178   N  ARG A 137           
SHEET    8 AA2 8 GLN A 170  GLU A 172 -1  N  GLN A 170   O  TYR A 177           
SHEET    1 AA3 2 GLY A  15  GLY A  17  0                                        
SHEET    2 AA3 2 THR A 146  PHE A 147 -1  O  THR A 146   N  ILE A  16           
LINK         C4  63Y A 202                 N3  63Y A 203     1555   1555  1.20  
LINK         C4  63Y A 202                 C5  63Y A 203     1555   1555  1.63  
LINK         C4  63Y A 202                 SAL 63Y A 203     1555   1555  1.88  
LINK         C5  63Y A 202                 C4  63Y A 203     1555   1555  1.27  
LINK         C5  63Y A 202                 C6  63Y A 203     1555   1555  1.41  
LINK         C6  63Y A 202                 C5  63Y A 203     1555   1555  1.48  
LINK         N1  63Y A 202                 C6  63Y A 203     1555   1555  1.56  
LINK         N3  63Y A 202                 C2  63Y A 203     1555   1555  1.37  
LINK         N3  63Y A 202                 C4  63Y A 203     1555   1555  1.50  
LINK         FAF 63Y A 202                 CAG 63Y A 203     1555   1555  1.56  
LINK         CAS 63Y A 202                 CAH 63Y A 203     1555   1555  1.49  
LINK         CAS 63Y A 202                 SAK 63Y A 203     1555   1555  1.79  
LINK         CAQ 63Y A 202                 CAQ 63Y A 203     1555   1555  1.34  
LINK         CAT 63Y A 202                 CAT 63Y A 203     1555   1555  1.13  
LINK         CAT 63Y A 202                 SAL 63Y A 203     1555   1555  1.89  
LINK         CAT 63Y A 202                 CAP 63Y A 203     1555   1555  1.65  
LINK         SAL 63Y A 202                 C4  63Y A 203     1555   1555  1.74  
LINK         SAL 63Y A 202                 CAT 63Y A 203     1555   1555  1.91  
LINK         C2  63Y A 202                 N3  63Y A 203     1555   1555  1.33  
LINK         C2  63Y A 202                 N1  63Y A 203     1555   1555  1.55  
LINK         NAB 63Y A 202                 C2  63Y A 203     1555   1555  1.56  
LINK         CAP 63Y A 202                 C5  63Y A 203     1555   1555  1.35  
LINK         CAA 63Y A 202                 CAA 63Y A 203     1555   1555  1.26  
CISPEP   1 ARG A   65    PRO A   66          0        -8.94                     
CISPEP   2 GLY A  116    GLY A  117          0        12.34                     
SITE     1 AC1 31 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 31 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 31 LYS A  54  LYS A  55  THR A  56  SER A  59                    
SITE     4 AC1 31 LEU A  75  SER A  76  ARG A  77  GLU A  78                    
SITE     5 AC1 31 ARG A  91  SER A  92  VAL A 115  GLY A 117                    
SITE     6 AC1 31 SER A 118  SER A 119  TYR A 121  THR A 146                    
SITE     7 AC1 31 63Y A 202  63Y A 203  HOH A 306  HOH A 309                    
SITE     8 AC1 31 HOH A 319  HOH A 346  HOH A 356                               
SITE     1 AC2 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC2 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC2 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC2 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC2 18 NDP A 201  HOH A 391                                          
SITE     1 AC3 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC3 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC3 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC3 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC3 18 NDP A 201  HOH A 391                                          
SITE     1 AC4 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC4 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC4 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC4 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC4 18 NDP A 201  HOH A 391                                          
SITE     1 AC5 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC5 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC5 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC5 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC5 18 NDP A 201  HOH A 391                                          
SITE     1 AC6 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC6 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC6 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC6 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC6 18 NDP A 201  HOH A 391                                          
SITE     1 AC7 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC7 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC7 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC7 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC7 18 NDP A 201  HOH A 391                                          
SITE     1 AC8 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC8 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC8 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC8 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC8 18 NDP A 201  HOH A 391                                          
SITE     1 AC9 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AC9 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AC9 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AC9 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC9 18 NDP A 201  HOH A 391                                          
SITE     1 AD1 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD1 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD1 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD1 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD1 18 NDP A 201  HOH A 391                                          
SITE     1 AD2 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD2 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD2 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD2 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD2 18 NDP A 201  HOH A 391                                          
SITE     1 AD3 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD3 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD3 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD3 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD3 18 NDP A 201  HOH A 391                                          
SITE     1 AD4 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD4 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD4 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD4 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD4 18 NDP A 201  HOH A 391                                          
SITE     1 AD5 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD5 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD5 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD5 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD5 18 NDP A 201  HOH A 391                                          
SITE     1 AD6 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD6 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD6 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD6 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD6 18 NDP A 201  HOH A 391                                          
SITE     1 AD7 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD7 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD7 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD7 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD7 18 NDP A 201  HOH A 391                                          
SITE     1 AD8 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD8 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD8 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD8 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD8 18 NDP A 201  HOH A 391                                          
SITE     1 AD9 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AD9 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AD9 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AD9 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AD9 18 NDP A 201  HOH A 391                                          
SITE     1 AE1 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE1 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE1 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE1 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE1 18 NDP A 201  HOH A 391                                          
SITE     1 AE2 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE2 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE2 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE2 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE2 18 NDP A 201  HOH A 391                                          
SITE     1 AE3 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE3 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE3 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE3 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE3 18 NDP A 201  HOH A 391                                          
SITE     1 AE4 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE4 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE4 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE4 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE4 18 NDP A 201  HOH A 391                                          
SITE     1 AE5 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE5 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE5 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE5 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE5 18 NDP A 201  HOH A 391                                          
SITE     1 AE6 18 ILE A   7  VAL A   8  ALA A   9  GLY A  20                    
SITE     2 AE6 18 ASP A  21  LEU A  22  GLU A  30  PHE A  31                    
SITE     3 AE6 18 PHE A  34  SER A  59  PRO A  61  ASN A  64                    
SITE     4 AE6 18 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AE6 18 NDP A 201  HOH A 391                                          
CRYST1   86.516   86.516   76.647  90.00  90.00 120.00 H 3           9          
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      0.011559  0.006673  0.000000        0.00000                         
SCALE2      0.000000  0.013347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013047        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system