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Entry: 1DLS
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HEADER    OXIDO-REDUCTASE                         25-JAN-95   1DLS              
TITLE     METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE                
TITLE    2 REDUCTASE WITH SUBSTITUTION OF LEUCINE 22: KINETICS,                 
TITLE    3 CRYSTALLOGRAPHY AND POTENTIAL AS SELECTABLE MARKERS                  
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: POTENTIAL                                                      
KEYWDS    OXIDO-REDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN                                 
REVDAT   2   24-FEB-09 1DLS    1       VERSN                                    
REVDAT   1   20-APR-95 1DLS    0                                                
JRNL        AUTH   W.S.LEWIS,V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,             
JRNL        AUTH 2 S.K.CHUNDURU,H.T.SPENCER,J.R.APPLEMAN,R.L.BLAKLEY            
JRNL        TITL   METHOTREXATE-RESISTANT VARIANTS OF HUMAN                     
JRNL        TITL 2 DIHYDROFOLATE REDUCTASE WITH SUBSTITUTIONS OF                
JRNL        TITL 3 LEUCINE 22. KINETICS, CRYSTALLOGRAPHY, AND                   
JRNL        TITL 4 POTENTIAL AS SELECTABLE MARKERS.                             
JRNL        REF    J.BIOL.CHEM.                  V. 270  5057 1995              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   7890613                                                      
JRNL        DOI    10.1074/JBC.270.10.5057                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.K.CHUNDURU,V.CODY,J.R.LUFT,W.PANGBORN,                     
REMARK   1  AUTH 2 J.R.APPLEMAN,R.L.BLAKLEY                                     
REMARK   1  TITL   METHOTREXATE-RESISTANT VARIANTS OF HUMAN                     
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE: EFFECTS OF PHE-31                   
REMARK   1  TITL 3 SUBSTITUTIONS                                                
REMARK   1  REF    J.BIOL.CHEM.                  V. 269  9547 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
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 ANGSTROMS             
REMARK   1  TITL 2 OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE                 
REMARK   1  TITL 3 TERNARY COMPLEX WITH NADPH AND                               
REMARK   1  TITL 4 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.    2.30 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) : 2.30                           
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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) : NULL                   
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            : 1506                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 111                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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) : 0.024 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.054 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.054 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.018 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.190 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.204 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.261 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.238 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.100 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 19.700; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 2.320 ; 1.750               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.310 ; 2.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 2.750 ; 1.750               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 4.270 ; 2.500               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DLS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11402                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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   (%): 53.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
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       43.74800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.25792            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.57767            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       43.74800            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       25.25792            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.57767            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       43.74800            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       25.25792            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.57767            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.51584            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.15533            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       50.51584            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.15533            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       50.51584            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.15533            
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   OD1  ASP A    94     O    HOH A   293              2.11            
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    LEU A   4   CB  -  CG  -  CD2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    CYS A   6   N   -  CA  -  CB  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    GLN A  12   CA  -  CB  -  CG  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LYS A  18   CB  -  CG  -  CD  ANGL. DEV. = -19.5 DEGREES          
REMARK 500    ASP A  21   CB  -  CG  -  OD2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    TYR A  22   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TRP A  24   CH2 -  CZ2 -  CE2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A  28   CD  -  NE  -  CZ  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG A  28   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    ASN A  29   CA  -  CB  -  CG  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    GLU A  30   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    PHE A  31   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR A  33   CB  -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TYR A  33   CB  -  CG  -  CD1 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG A  36   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG A  36   CD  -  NE  -  CZ  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    MET A  37   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    SER A  42   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    GLU A  44   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    GLU A  44   OE1 -  CD  -  OE2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    LYS A  54   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    PHE A  58   CB  -  CG  -  CD1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    SER A  59   CB  -  CA  -  C   ANGL. DEV. =  13.3 DEGREES          
REMARK 500    LYS A  63   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG A  65   CG  -  CD  -  NE  ANGL. DEV. =  21.7 DEGREES          
REMARK 500    ARG A  65   CD  -  NE  -  CZ  ANGL. DEV. =  29.3 DEGREES          
REMARK 500    ARG A  65   NH1 -  CZ  -  NH2 ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    GLU A  78   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLU A  78   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    GLU A  78   CG  -  CD  -  OE1 ANGL. DEV. =  15.4 DEGREES          
REMARK 500    LEU A  79   O   -  C   -  N   ANGL. DEV. =  11.0 DEGREES          
REMARK 500    GLU A  81   OE1 -  CD  -  OE2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    GLU A  81   CG  -  CD  -  OE1 ANGL. DEV. =  12.8 DEGREES          
REMARK 500    SER A  90   N   -  CA  -  CB  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ARG A  91   CD  -  NE  -  CZ  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A  91   O   -  C   -  N   ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A  94   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    GLU A 104   CA  -  CB  -  CG  ANGL. DEV. =  20.1 DEGREES          
REMARK 500    ASP A 110   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    MET A 111   CG  -  SD  -  CE  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    SER A 118   CB  -  CA  -  C   ANGL. DEV. = -11.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 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    GLU A 104      -74.52    -44.95                                   
REMARK 500    ASP A 110      -97.17    -92.98                                   
REMARK 500    ASN A 185      106.92   -162.07                                   
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 188                 
DBREF  1DLS A    1   186  UNP    P00374   DYR_HUMAN        1    186             
SEQADV 1DLS TYR A   22  UNP  P00374    LEU    22 CONFLICT                       
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 TYR 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 187      48                                                       
HET    MTX  A 188      33                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     MTX METHOTREXATE                                                     
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  MTX    C20 H22 N8 O5                                                
FORMUL   4  HOH   *111(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        -6.55                     
CISPEP   2 GLY A  116    GLY A  117          0         2.46                     
SITE     1 AC1 33 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 33 GLY A  20  ASP A  21  TRP A  24  GLY A  53                    
SITE     3 AC1 33 LYS A  54  LYS A  55  THR A  56  SER A  59                    
SITE     4 AC1 33 LEU A  75  SER A  76  ARG A  77  GLU A  78                    
SITE     5 AC1 33 ARG A  91  VAL A 115  GLY A 117  SER A 118                    
SITE     6 AC1 33 SER A 119  VAL A 120  TYR A 121  GLU A 123                    
SITE     7 AC1 33 THR A 146  MTX A 188  HOH A 206  HOH A 222                    
SITE     8 AC1 33 HOH A 261  HOH A 273  HOH A 285  HOH A 286                    
SITE     9 AC1 33 HOH A 287                                                     
SITE     1 AC2 16 ILE A   7  VAL A   8  ALA A   9  ARG A  28                    
SITE     2 AC2 16 GLU A  30  PHE A  31  PHE A  34  GLN A  35                    
SITE     3 AC2 16 SER A  59  ASN A  64  ARG A  70  VAL A 115                    
SITE     4 AC2 16 TYR A 121  THR A 136  NDP A 187  HOH A 191                    
CRYST1   87.496   87.496   76.733  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      0.011429  0.006599  0.000000        0.00000                         
SCALE2      0.000000  0.013197  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013032        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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