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Database: PDB
Entry: 1HFQ
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Original site: 1HFQ 
HEADER    OXIDOREDUCTASE                          04-NOV-97   1HFQ              
TITLE     COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE        
TITLE    2 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DHFR;                                                       
COMPND   5 EC: 1.5.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: COMPLEXED WITH NADPH AND FURO[2,3D]FUROPYRIMIDINE     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: POTENTIAL;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM107, F31S MUTANT                         
KEYWDS    OXIDOREDUCTASE, ONE-CARBON METABOLISM                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,R.L.BLAKLEY,A.GANGJEE           
REVDAT   3   11-DEC-13 1HFQ    1       HET    HETATM HETNAM REMARK              
REVDAT   3 2                   1       VERSN                                    
REVDAT   2   24-FEB-09 1HFQ    1       VERSN                                    
REVDAT   1   28-JAN-98 1HFQ    0                                                
JRNL        AUTH   V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,R.L.BLAKLEY,A.GANGJEE  
JRNL        TITL   COMPARISON OF TERNARY CRYSTAL COMPLEXES OF F31 VARIANTS OF   
JRNL        TITL 2 HUMAN DIHYDROFOLATE REDUCTASE WITH NADPH AND A CLASSICAL     
JRNL        TITL 3 ANTITUMOR FUROPYRIMIDINE.                                    
JRNL        REF    ANTI-CANCER DRUG DES.         V.  13   307 1998              
JRNL        REFN                   ISSN 0266-9536                               
JRNL        PMID   9627670                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,A.GANGJEE,R.DEVRAJ,    
REMARK   1  AUTH 2 S.F.QUEENER,R.L.BLAKLEY                                      
REMARK   1  TITL   COMPARISON OF TERNARY COMPLEXES OF PNEUMOCYSTIS CARINII AND  
REMARK   1  TITL 2 WILD-TYPE HUMAN DIHYDROFOLATE REDUCTASE WITH A NOVEL         
REMARK   1  TITL 3 CLASSICAL ANTITUMOR FURO[2,3-D]PYRIMIDINE ANTIFOLATE         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  53   638 1997              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.S.LEWIS,V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,             
REMARK   1  AUTH 2 S.K.CHUNDURU,H.T.SPENCER,J.R.APPLEMAN,R.L.BLAKLEY            
REMARK   1  TITL   METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE       
REMARK   1  TITL 2 REDUCTASE WITH SUBSTITUTIONS OF LEUCINE 22. KINETICS,        
REMARK   1  TITL 3 CRYSTALLOGRAPHY, AND POTENTIAL AS SELECTABLE MARKERS         
REMARK   1  REF    J.BIOL.CHEM.                  V. 270  5057 1995              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   S.K.CHUNDURU,V.CODY,J.R.LUFT,W.PANGBORN,J.R.APPLEMAN,        
REMARK   1  AUTH 2 R.L.BLAKLEY                                                  
REMARK   1  TITL   METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE       
REMARK   1  TITL 2 REDUCTASE. EFFECTS OF PHE31 SUBSTITUTIONS                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 269  9547 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   V.CODY,J.R.LUFT,E.CISZAK,T.I.KALMAN,J.H.FREISHEIM            
REMARK   1  TITL   CRYSTAL STRUCTURE DETERMINATION AT 2.3 A OF RECOMBINANT      
REMARK   1  TITL 2 HUMAN DIHYDROFOLATE REDUCTASE TERNARY COMPLEX WITH NADPH AND 
REMARK   1  TITL 3 METHOTREXATE-GAMMA-TETRAZOLE                                 
REMARK   1  REF    ANTI-CANCER DRUG DES.         V.   7   483 1992              
REMARK   1  REFN                   ISSN 0266-9536                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1750                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1497                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.42                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.025 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.058 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.062 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.021 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.218 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.197 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.277 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : 0.224 ; 0.500               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.600 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 18.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 21.600; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.539 ; 1.500               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.003 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.609 ; 1.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.399 ; 1.500               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-93                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS II                          
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13350                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 78.0                               
REMARK 200  DATA REDUNDANCY                : 3.090                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       43.56000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.14938            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.67133            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       43.56000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       25.14938            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.67133            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       43.56000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       25.14938            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.67133            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.29876            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.34267            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       50.29876            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.34267            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       50.29876            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.34267            
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 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   OG   SER A    42     OD2  ASP A   110              2.07            
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    ALA A   9   C     ALA A   9   O       0.161                       
REMARK 500    ILE A  16   CB    ILE A  16   CG1     0.173                       
REMARK 500    SER A  31   CA    SER A  31   CB      0.117                       
REMARK 500    PHE A  34   N     PHE A  34   CA      0.138                       
REMARK 500    SER A  59   CB    SER A  59   OG     -0.079                       
REMARK 500    ARG A  91   CZ    ARG A  91   NH1     0.097                       
REMARK 500    ARG A  91   CZ    ARG A  91   NH2     0.089                       
REMARK 500    SER A 119   CB    SER A 119   OG      0.196                       
REMARK 500    TYR A 121   CD1   TYR A 121   CE1     0.103                       
REMARK 500    PHE A 134   CG    PHE A 134   CD2     0.101                       
REMARK 500    THR A 136   C     THR A 136   O       0.117                       
REMARK 500    GLU A 172   CD    GLU A 172   OE2     0.084                       
REMARK 500    GLU A 183   CD    GLU A 183   OE2    -0.088                       
REMARK 500    ASN A 185   CG    ASN A 185   OD1     0.133                       
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    CYS A   6   N   -  CA  -  CB  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ALA A   9   N   -  CA  -  CB  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    VAL A  10   CG1 -  CB  -  CG2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    VAL A  10   CA  -  CB  -  CG2 ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ALA A   9   CA  -  C   -  N   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ALA A   9   O   -  C   -  N   ANGL. DEV. = -11.0 DEGREES          
REMARK 500    VAL A  10   C   -  N   -  CA  ANGL. DEV. =  17.6 DEGREES          
REMARK 500    ILE A  16   CA  -  C   -  N   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ASN A  19   OD1 -  CG  -  ND2 ANGL. DEV. = -20.6 DEGREES          
REMARK 500    ASN A  19   CB  -  CG  -  ND2 ANGL. DEV. =  18.2 DEGREES          
REMARK 500    LYS A  18   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ASP A  21   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU A  22   CB  -  CG  -  CD1 ANGL. DEV. =  15.9 DEGREES          
REMARK 500    LEU A  22   CB  -  CG  -  CD2 ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO A  25   CB  -  CA  -  C   ANGL. DEV. =  15.9 DEGREES          
REMARK 500    PRO A  26   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    LEU A  27   CA  -  C   -  O   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ARG A  28   N   -  CA  -  CB  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    SER A  31   CB  -  CA  -  C   ANGL. DEV. = -11.8 DEGREES          
REMARK 500    SER A  31   N   -  CA  -  CB  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ARG A  32   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  32   O   -  C   -  N   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    PHE A  34   CB  -  CG  -  CD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    TYR A  33   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A  36   CG  -  CD  -  NE  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    GLU A  44   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    GLU A  44   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    GLU A  44   OE1 -  CD  -  OE2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    GLU A  44   CG  -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    GLU A  44   CA  -  C   -  O   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    GLU A  44   O   -  C   -  N   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    LEU A  49   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    GLY A  53   CA  -  C   -  O   ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS A  54   CD  -  CE  -  NZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    GLY A  53   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    THR A  56   CA  -  CB  -  OG1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    PHE A  58   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    PHE A  58   CA  -  C   -  O   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PHE A  58   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A  65   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A  65   NH1 -  CZ  -  NH2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    VAL A  74   CA  -  CB  -  CG2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A  77   CG  -  CD  -  NE  ANGL. DEV. = -22.4 DEGREES          
REMARK 500    ARG A  77   CD  -  NE  -  CZ  ANGL. DEV. = -11.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     134 ANGLE DEVIATIONS.                             
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    SER A  76      144.02   -173.80                                   
REMARK 500    GLU A 104      -70.73    -53.21                                   
REMARK 500    ASP A 110      -95.63    -90.85                                   
REMARK 500    ASN A 185      101.83   -164.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  65         0.08    SIDE CHAIN                              
REMARK 500    TYR A 156         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  10        24.2      L          L   OUTSIDE RANGE           
REMARK 500    PRO A  25        48.0      L          L   OUTSIDE RANGE           
REMARK 500    ARG A  28        23.0      L          L   OUTSIDE RANGE           
REMARK 500    SER A  31        24.0      L          L   OUTSIDE RANGE           
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 187                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOT A 188                 
DBREF  1HFQ A    1   186  UNP    P00374   DYR_HUMAN        1    186             
SEQADV 1HFQ SER A   31  UNP  P00374    PHE    31 ENGINEERED                     
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 SER 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 187      48                                                       
HET    MOT  A 188      32                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     MOT N-[4-[(2,4-DIAMINOFURO[2,3D]PYRIMIDIN-5-YL)                      
HETNAM   2 MOT  METHYL]METHYLAMINO]-BENZOYL]-L-GLUTAMATE                        
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  MOT    C20 H22 N6 O6                                                
FORMUL   4  HOH   *51(H2 O)                                                     
HELIX    1   1 ARG A   28  THR A   39  1                                  12    
HELIX    2   2 LYS A   54  SER A   59  1                                   6    
HELIX    3   3 GLU A   62  ASN A   64  5                                   3    
HELIX    4   4 LEU A   93  GLU A  101  1                                   9    
HELIX    5   5 PRO A  103  ALA A  106  1                                   4    
HELIX    6   6 SER A  118  ALA A  124  1                                   7    
SHEET    1   A 8 GLN A 170  GLU A 172  0                                        
SHEET    2   A 8 ILE A 175  ASN A 185 -1  N  TYR A 177   O  GLN A 170           
SHEET    3   A 8 HIS A 130  ILE A 138 -1  N  ARG A 137   O  LYS A 178           
SHEET    4   A 8 LEU A   4  VAL A  10  1  N  CYS A   6   O  LYS A 132           
SHEET    5   A 8 VAL A 112  ILE A 114  1  N  VAL A 112   O  ASN A   5           
SHEET    6   A 8 LEU A  49  GLY A  53  1  N  LEU A  49   O  TRP A 113           
SHEET    7   A 8 ILE A  71  LEU A  75  1  N  ILE A  71   O  VAL A  50           
SHEET    8   A 8 PHE A  88  SER A  90  1  N  PHE A  88   O  VAL A  74           
CISPEP   1 ARG A   65    PRO A   66          0        -4.34                     
CISPEP   2 GLY A  116    GLY A  117          0         0.03                     
SITE     1 AC1 28 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 28 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 28 LYS A  54  LYS A  55  THR A  56  SER A  59                    
SITE     4 AC1 28 LEU A  75  SER A  76  ARG A  77  GLU A  78                    
SITE     5 AC1 28 ARG A  91  SER A  92  VAL A 115  GLY A 117                    
SITE     6 AC1 28 SER A 118  SER A 119  VAL A 120  TYR A 121                    
SITE     7 AC1 28 THR A 146  MOT A 188  HOH A 195  HOH A 219                    
SITE     1 AC2 17 ILE A   7  VAL A   8  ALA A   9  GLU A  30                    
SITE     2 AC2 17 SER A  31  PHE A  34  GLN A  35  ILE A  60                    
SITE     3 AC2 17 ASN A  64  LEU A  67  ARG A  70  VAL A 115                    
SITE     4 AC2 17 TYR A 121  THR A 136  NDP A 187  HOH A 193                    
SITE     5 AC2 17 HOH A 203                                                     
CRYST1   87.120   87.120   77.014  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      0.011478  0.006627  0.000000        0.00000                         
SCALE2      0.000000  0.013254  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012985        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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