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Entry: 2DHF
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HEADER    OXIDOREDUCTASE                          25-OCT-89   2DHF              
TITLE     CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE REDUCTASE       
TITLE    2 COMPLEXED WITH FOLATE AND 5-DEAZOFOLATE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
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                                                 
KEYWDS    OXIDO-REDUCTASE, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.DAVIES /II,J.KRAUT                                                
REVDAT   6   29-NOV-17 2DHF    1       KEYWDS HELIX                             
REVDAT   5   24-FEB-09 2DHF    1       VERSN                                    
REVDAT   4   01-APR-03 2DHF    1       JRNL                                     
REVDAT   3   15-JAN-95 2DHF    1       HET                                      
REVDAT   2   15-JAN-93 2DHF    2       CONECT                                   
REVDAT   1   15-JUL-90 2DHF    0                                                
JRNL        AUTH   J.F.DAVIES 2ND.,T.J.DELCAMP,N.J.PRENDERGAST,V.A.ASHFORD,     
JRNL        AUTH 2 J.H.FREISHEIM,J.KRAUT                                        
JRNL        TITL   CRYSTAL STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE        
JRNL        TITL 2 REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZAFOLATE.           
JRNL        REF    BIOCHEMISTRY                  V.  29  9467 1990              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   2248959                                                      
JRNL        DOI    10.1021/BI00492A021                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.J.PRENDERGAST,T.J.DELCAMP,P.L.SMITH,J.H.FREISHEIM          
REMARK   1  TITL   EXPRESSION AND SITE-DIRECTED MUTAGENESIS OF HUMAN            
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE                                      
REMARK   1  REF    BIOCHEMISTRY                  V.  27  3664 1988              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
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) : 0.194                           
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            : 2948                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
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) : 0.021 ; 0.018               
REMARK   3    ANGLE DISTANCE                  (A) : 0.035 ; 0.023               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.044 ; 0.035               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.015 ; 0.013               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.337 ; 0.200               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.222 ; 0.400               
REMARK   3    MULTIPLE TORSION                (A) : 0.290 ; 0.400               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.227 ; 0.400               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.300 ; 5.000               
REMARK   3    STAGGERED                 (DEGREES) : 25.900; 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) : 4.840 ; 2.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 6.410 ; 3.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 5.690 ; 2.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 7.680 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DHF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000177998.                                   
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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   (%): 46.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ASP B   186                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B  78    CG   CD   OE1  OE2                                  
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    HOH B   424     O    HOH B   434              1.96            
REMARK 500   OE1  GLU B   180     OH   TYR B   182              2.15            
REMARK 500   CE1  HIS B   130     OE1  GLU B   183              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   OD1  ASP A   141     NH1  ARG B    32     1554     2.08            
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    SER A  92   CB    SER A  92   OG     -0.089                       
REMARK 500    ARG B  70   CD    ARG B  70   NE     -0.117                       
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   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    PHE A  31   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLU A  62   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    LEU A  67   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    GLN A  84   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    SER A  90   N   -  CA  -  CB  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    LEU A 153   CB  -  CA  -  C   ANGL. DEV. =  12.4 DEGREES          
REMARK 500    GLU A 161   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    VAL A 181   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ALA B   9   CB  -  CA  -  C   ANGL. DEV. = -10.7 DEGREES          
REMARK 500    GLU B  30   CA  -  CB  -  CG  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ARG B  36   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B  36   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLU B  44   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG B  65   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  70   CD  -  NE  -  CZ  ANGL. DEV. =  24.7 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU B  93   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    LEU B  93   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ASP B  95   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP B  95   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    LEU B  97   CB  -  CA  -  C   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    MET B 111   CA  -  CB  -  CG  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ASP B 141   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    SER B 144   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ASP B 145   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 168   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TYR B 182   N   -  CA  -  CB  ANGL. DEV. =  11.9 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    GLU A  62      -29.83    -36.78                                   
REMARK 500    SER A  76      138.12   -172.61                                   
REMARK 500    GLU A  78      -60.50    -95.22                                   
REMARK 500    GLN A  84      168.72    -27.30                                   
REMARK 500    ASP A 110      -86.72   -104.65                                   
REMARK 500    HIS A 127      115.47    -33.66                                   
REMARK 500    TYR A 162      109.26   -164.06                                   
REMARK 500    GLU B  62       15.32    -39.65                                   
REMARK 500    LEU B  79      132.43    -28.73                                   
REMARK 500    LYS B  80      -71.71    -63.64                                   
REMARK 500    ASP B 110      -86.22    -98.08                                   
REMARK 500    HIS B 127      131.81    -30.99                                   
REMARK 500    MET B 139       45.46    -76.18                                   
REMARK 500    PRO B 149      150.39    -48.75                                   
REMARK 500    TYR B 162      118.01   -170.23                                   
REMARK 500    PRO B 163      138.07    -34.28                                   
REMARK 500    LYS B 173       29.57     48.92                                   
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  28         0.12    SIDE CHAIN                              
REMARK 500    ARG A  32         0.09    SIDE CHAIN                              
REMARK 500    ARG A  36         0.11    SIDE CHAIN                              
REMARK 500    ARG A  91         0.15    SIDE CHAIN                              
REMARK 500    ARG B  28         0.09    SIDE CHAIN                              
REMARK 500    ARG B  32         0.09    SIDE CHAIN                              
REMARK 500    ARG B  65         0.13    SIDE CHAIN                              
REMARK 500    ARG B  91         0.11    SIDE CHAIN                              
REMARK 500    ARG B 137         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 IN EACH CHAIN, RESIDUES ASP 21 - LEU 22 - PRO 23 -                   
REMARK 650 TRP 24 - PRO 25 - PRO 26 ARE IN LEFT-HANDED POLYPROLINE              
REMARK 650 HELIX CONFORMATION.                                                  
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700       THE FOLLOWING REMARKS APPLY TO EACH CHAIN.                     
REMARK 700 IN THE *HELIX*, *SHEET* AND *TURN* RECORDS BELOW, AN *A*             
REMARK 700 OR *B* HAS BEEN APPENDED TO THE NAMES USED IN THIS REMARK            
REMARK 700 TO DISTINGUISH CHAINS.                                               
REMARK 700 RESIDUE GLN 102 PARTICIPATES IN BOTH HELIX E AND EP.                 
REMARK 700 RESIDUES LYS 108 AND VAL 109 PARTICIPATE IN BOTH HELIX               
REMARK 700 EP AND STRAND E.                                                     
REMARK 700 RESIDUE GLU 172 IS IN TIGHT-TURN 8 AND BETA STRAND G.                
REMARK 700 RESIDUE ILE 175 IS IN TIGHT-TURN 8 AND BETA STRAND H.                
REMARK 700 RESIDUES ASP 110 - MET 111 FORM A BETA-BULGE IN STRAND E.            
REMARK 700 RESIDUES VAL 115 - GLY 116 FORM A BETA-BULGE IN STRAND E.            
REMARK 700 TIGHT TURN 7 DISRUPTS STRAND G.  THIS IS REPRESENTED ON THE          
REMARK 700 SHEET RECORDS BELOW BY PRESENTING THE SHEET TWICE WITH               
REMARK 700 STRAND 8 DIFFERENT.                                                  
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DZF A 187                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DZF B 187                 
DBREF  2DHF A    1   186  UNP    P00374   DYR_HUMAN        1    186             
DBREF  2DHF B    1   186  UNP    P00374   DYR_HUMAN        1    186             
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                                              
SEQRES   1 B  186  VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN          
SEQRES   2 B  186  MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO          
SEQRES   3 B  186  LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR          
SEQRES   4 B  186  THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET          
SEQRES   5 B  186  GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG          
SEQRES   6 B  186  PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU          
SEQRES   7 B  186  LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG          
SEQRES   8 B  186  SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU          
SEQRES   9 B  186  LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY          
SEQRES  10 B  186  SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS          
SEQRES  11 B  186  LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU          
SEQRES  12 B  186  SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR          
SEQRES  13 B  186  LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL          
SEQRES  14 B  186  GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR          
SEQRES  15 B  186  GLU LYS ASN ASP                                              
HET    DZF  A 187      32                                                       
HET    DZF  B 187      32                                                       
HETNAM     DZF 5-DEAZAFOLIC ACID                                                
FORMUL   3  DZF    2(C20 H20 N6 O6)                                             
FORMUL   5  HOH   *111(H2 O)                                                    
HELIX    1  BA LEU A   27  THR A   40  1                                  14    
HELIX    2  CA GLY A   53  SER A   59  1                                   7    
HELIX    3  EA SER A   92  GLN A  102  1                                  11    
HELIX    4 EPA GLN A  102  VAL A  109  1NOT PRESENT IN BACTERIAL           8    
HELIX    5  FA GLY A  117  HIS A  127  1                                  11    
HELIX    6  BB LEU B   27  THR B   40  1                                  14    
HELIX    7  CB GLY B   53  SER B   59  1                                   7    
HELIX    8  EB SER B   92  GLN B  102  1                                  11    
HELIX    9 EPB GLN B  102  VAL B  109  1NOT PRESENT IN BACTERIAL           8    
HELIX   10  FB GLY B  117  HIS B  127  1                                  11    
SHEET    1 S1A 8 PHE A  88  SER A  90  0                                        
SHEET    2 S1A 8 ILE A  71  SER A  76  1  N  VAL A  74   O  PHE A  88           
SHEET    3 S1A 8 GLN A  47  GLY A  53  1  O  GLY A  53   N  LEU A  73           
SHEET    4 S1A 8 LYS A 108  GLY A 116  1  O  TRP A 113   N  ILE A  51           
SHEET    5 S1A 8 LEU A   4  VAL A  10  1  O  ASN A   5   N  ILE A 114           
SHEET    6 S1A 8 HIS A 130  MET A 139  1  N  PHE A 134   O  CYS A   6           
SHEET    7 S1A 8 ILE A 175  ASN A 185 -1  N  TYR A 182   O  LEU A 133           
SHEET    8 S1A 8 LYS A 157  LEU A 159 -1  O  LYS A 157   N  GLU A 183           
SHEET    1 S2A 8 PHE A  88  SER A  90  0                                        
SHEET    2 S2A 8 ILE A  71  SER A  76  1  N  VAL A  74   O  PHE A  88           
SHEET    3 S2A 8 GLN A  47  GLY A  53  1  O  GLY A  53   N  LEU A  73           
SHEET    4 S2A 8 LYS A 108  GLY A 116  1  O  TRP A 113   N  ILE A  51           
SHEET    5 S2A 8 LEU A   4  VAL A  10  1  O  ASN A   5   N  ILE A 114           
SHEET    6 S2A 8 HIS A 130  MET A 139  1  N  PHE A 134   O  CYS A   6           
SHEET    7 S2A 8 ILE A 175  ASN A 185 -1  N  TYR A 182   O  LEU A 133           
SHEET    8 S2A 8 ASP A 168  GLU A 172 -1  O  GLN A 170   N  TYR A 177           
SHEET    1 S1B 8 PHE B  88  SER B  90  0                                        
SHEET    2 S1B 8 ILE B  71  SER B  76  1  N  VAL B  74   O  PHE B  88           
SHEET    3 S1B 8 GLN B  47  GLY B  53  1  O  GLY B  53   N  LEU B  73           
SHEET    4 S1B 8 LYS B 108  GLY B 116  1  O  TRP B 113   N  ILE B  51           
SHEET    5 S1B 8 LEU B   4  VAL B  10  1  O  ASN B   5   N  ILE B 114           
SHEET    6 S1B 8 HIS B 130  MET B 139  1  N  PHE B 134   O  CYS B   6           
SHEET    7 S1B 8 ILE B 175  ASN B 185 -1  N  TYR B 182   O  LEU B 133           
SHEET    8 S1B 8 LYS B 157  LEU B 159 -1  O  LYS B 157   N  GLU B 183           
SHEET    1 S2B 8 PHE B  88  SER B  90  0                                        
SHEET    2 S2B 8 ILE B  71  SER B  76  1  N  VAL B  74   O  PHE B  88           
SHEET    3 S2B 8 GLN B  47  GLY B  53  1  O  GLY B  53   N  LEU B  73           
SHEET    4 S2B 8 LYS B 108  GLY B 116  1  O  TRP B 113   N  ILE B  51           
SHEET    5 S2B 8 LEU B   4  VAL B  10  1  O  ASN B   5   N  ILE B 114           
SHEET    6 S2B 8 HIS B 130  MET B 139  1  N  PHE B 134   O  CYS B   6           
SHEET    7 S2B 8 ILE B 175  ASN B 185 -1  N  TYR B 182   O  LEU B 133           
SHEET    8 S2B 8 ASP B 168  GLU B 172 -1  O  GLN B 170   N  TYR B 177           
CISPEP   1 ARG A   65    PRO A   66          0         1.51                     
CISPEP   2 GLY A  116    GLY A  117          0         1.81                     
CISPEP   3 ARG B   65    PRO B   66          0        -2.99                     
CISPEP   4 GLY B  116    GLY B  117          0         9.18                     
SITE     1 AC1 17 ILE A   7  VAL A   8  ALA A   9  LEU A  22                    
SITE     2 AC1 17 GLU A  30  PHE A  31  PHE A  34  GLN A  35                    
SITE     3 AC1 17 THR A  56  ILE A  60  PRO A  61  LEU A  67                    
SITE     4 AC1 17 ARG A  70  VAL A 115  TYR A 121  THR A 136                    
SITE     5 AC1 17 HOH A 403                                                     
SITE     1 AC2 14 ILE B   7  VAL B   8  GLU B  30  PHE B  31                    
SITE     2 AC2 14 PHE B  34  GLN B  35  ASN B  64  ARG B  70                    
SITE     3 AC2 14 VAL B 115  TYR B 121  THR B 136  HOH B 401                    
SITE     4 AC2 14 HOH B 410  HOH B 431                                          
CRYST1   36.100   38.500   76.800  93.90  91.40 111.50 P 1           2          
ORIGX1      0.027701  0.010912  0.001585        0.00000                         
ORIGX2      0.000000  0.027917  0.002318        0.00000                         
ORIGX3      0.000000  0.000000  0.013070        0.00000                         
SCALE1      0.027701  0.010912  0.001585        0.00000                         
SCALE2      0.000000  0.027917  0.002318        0.00000                         
SCALE3      0.000000  0.000000  0.013070        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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