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Database: PDB
Entry: 1DHI
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HEADER    OXIDOREDUCTASE                          29-OCT-93   1DHI              
TITLE     LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT  
TITLE    2 DIHYDROFOLATE REDUCTASE                                              
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: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.OATLEY,J.E.VILLAFRANCA,K.A.BROWN,J.KRAUT                          
REVDAT   4   07-FEB-24 1DHI    1       REMARK SEQADV LINK                       
REVDAT   3   29-NOV-17 1DHI    1       HELIX                                    
REVDAT   2   24-FEB-09 1DHI    1       VERSN                                    
REVDAT   1   31-JAN-94 1DHI    0                                                
JRNL        AUTH   K.A.BROWN,E.E.HOWELL,J.KRAUT                                 
JRNL        TITL   LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF  
JRNL        TITL 2 A MUTANT DIHYDROFOLATE REDUCTASE.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  90 11753 1993              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   8265622                                                      
JRNL        DOI    10.1073/PNAS.90.24.11753                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.DION,C.E.LINN,T.D.BRADRICK,S.GEORGHIOU,E.E.HOWELL          
REMARK   1  TITL   HOW DO MUTATION AT PHENYLALANINE-153 AND ISOLEUCINE-155      
REMARK   1  TITL 2 PARTIALLY SUPPRESS THE EFFECTS OF THE ASPARTATE-27-> SERINE  
REMARK   1  TITL 3 MUTATION IN ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE         
REMARK   1  REF    BIOCHEMISTRY                  V.  32  3479 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.R.APPLEMAN,E.E.HOWELL,J.KRAUT,R.L.BLAKELY                  
REMARK   1  TITL   ROLE OF ASPARTATE 27 OF DIHYDROFOLATE REDUCTASE FROM         
REMARK   1  TITL 2 ESCHERICHIA COLI IN INTERCONVERSION OF ACTIVE AND INACTIVE   
REMARK   1  TITL 3 ENZYME CONFORMERS AND THE BINDING OF NADPH                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 265  5579 1990              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.E.HOWELL,C.BOOTH,M.FARNUM,J.KRAUT,M.S.WARREN               
REMARK   1  TITL   A SECOND-SITE MUTATION AT PHENYLALANINE-137 THAT INCREASES   
REMARK   1  TITL 2 CATALYTIC EFFICIENCY IN THE MUTANT ASPARTATE-27-> SERINE     
REMARK   1  TITL 3 ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE                     
REMARK   1  REF    BIOCHEMISTRY                  V.  29  8561 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   S.M.DUNN,T.M.LANIGAN,E.E.HOWELL                              
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE FROM ESCHERICHIA COLI: PROBING THE   
REMARK   1  TITL 2 ROLE OF ASPARTATE-27 AND PHENYLALANINE-137 IN ENZYME         
REMARK   1  TITL 3 CONFORMATION AND THE BINDING OF NADPH                        
REMARK   1  REF    BIOCHEMISTRY                  V.  29  8569 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   E.E.HOWELL,J.E.VILLAFRANCA,M.S.WAREN,S.J.OATLEY,J.KRAUT      
REMARK   1  TITL   FUNCTIONAL ROLE OF ASPARTIC ACID-27 IN DIHYDROFOLATE         
REMARK   1  TITL 2 REDUCTASE REVEALED BY MUTAGENESIS                            
REMARK   1  REF    SCIENCE                       V. 231  1123 1986              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT         
REMARK   1  TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS     
REMARK   1  TITL 2 CASEI DIHYDROFOLATE REDUCTASE AT 1.7 ANGSTROMS RESOLUTION.   
REMARK   1  TITL 3 I. GENERAL FEATURES AND BINDING OF METHOTREXATE              
REMARK   1  REF    BIOCHEMISTRY                  V. 257 13650 1982              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   D.J.FILMAN,J.T.BOLIN,D.A.MATTHEWS,J.KRAUT                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS     
REMARK   1  TITL 2 CASEI DIHYDROFOLATE REDUCTASE AT 1.7 ANGSTROMS RESOLUTION.   
REMARK   1  TITL 3 II. ENVIRONMENT OF BOUND NADPH AND IMPLICATIONS FOR          
REMARK   1  TITL 4 CATALYSIS                                                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 257 13663 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
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  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
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  USING ALL DATA, NO SIGMA CUTOFF.                                    
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            : 2498                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 385                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.020 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.900 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DHI 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_1000172782.                                   
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   (%): 52.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       24.64000            
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       49.28000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       36.96000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.60000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       12.32000            
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 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL   
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO          
REMARK 300 CHAIN *B*.                                                           
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 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     PRO A  66    CB   CG   CD                                        
REMARK 470     THR A  68    OG1  CG2                                            
REMARK 470     ASP A  70    OD1  OD2                                            
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     LYS A 106    CE   NZ                                             
REMARK 470     GLU A 129    CD   OE1  OE2                                       
REMARK 470     PRO A 130    O                                                   
REMARK 470     ASP A 131    CB   CG   OD1  OD2                                  
REMARK 470     ARG A 159    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B  87    OD2                                                 
REMARK 470     ASP B 127    OD2                                                 
REMARK 470     GLU B 129    CD   OE1  OE2                                       
REMARK 470     ASP B 131    CG   OD1  OD2                                       
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   680     O    HOH B   724              2.10            
REMARK 500   O    HOH A   412     O    HOH A   569              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   OD2  ASP B    70     O    HOH B   777     5564     1.88            
REMARK 500   CB   PRO A   130     O    HOH A   462     6655     1.91            
REMARK 500   O    HOH A   463     O    HOH B   723     3564     2.11            
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    GLU A  48   CD    GLU A  48   OE2     0.081                       
REMARK 500    GLU A  80   CD    GLU A  80   OE2     0.079                       
REMARK 500    GLU A  90   CD    GLU A  90   OE2     0.070                       
REMARK 500    GLU A 118   CD    GLU A 118   OE2     0.079                       
REMARK 500    GLU A 120   CD    GLU A 120   OE2     0.072                       
REMARK 500    GLU A 134   CD    GLU A 134   OE2     0.082                       
REMARK 500    GLU A 157   CD    GLU A 157   OE2     0.075                       
REMARK 500    GLU B  17   CD    GLU B  17   OE2     0.098                       
REMARK 500    GLU B  48   CD    GLU B  48   OE2     0.066                       
REMARK 500    GLU B  80   CD    GLU B  80   OE2     0.087                       
REMARK 500    GLU B  90   CD    GLU B  90   OE1    -0.066                       
REMARK 500    GLU B 101   CD    GLU B 101   OE2     0.079                       
REMARK 500    GLU B 118   CD    GLU B 118   OE2     0.086                       
REMARK 500    GLU B 120   CD    GLU B 120   OE2     0.080                       
REMARK 500    GLU B 139   CD    GLU B 139   OE1     0.067                       
REMARK 500    GLU B 157   CD    GLU B 157   OE2     0.084                       
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    ASP A  11   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  12   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    GLN A  65   CB  -  CA  -  C   ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ASP A  79   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A  87   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A  98   CG  -  CD  -  NE  ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ARG A  98   CD  -  NE  -  CZ  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A  98   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    GLU A 101   CG  -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    TYR A 111   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP A 142   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP A 144   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B  12   CG  -  CD  -  NE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG B  12   CD  -  NE  -  CZ  ANGL. DEV. =  19.3 DEGREES          
REMARK 500    ARG B  12   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B  33   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP B  37   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP B  37   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B  52   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP B  79   CB  -  CG  -  OD1 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ASP B  87   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 116   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 122   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B 127   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP B 142   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP B 142   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP B 144   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP B 144   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 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  17      -58.80   -146.66                                   
REMARK 500    PRO A 130       11.97    -54.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 620  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 483   O                                                      
REMARK 620 2 SER B 135   O    92.3                                              
REMARK 620 3 HOH B 658   O    87.0  91.3                                        
REMARK 620 4 HOH B 659   O    92.6 173.2  84.2                                  
REMARK 620 5 HOH B 661   O   177.7  89.7  91.9  85.3                            
REMARK 620 6 HOH B 673   O    89.9  95.9 172.2  88.8  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: APT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PTERIDINE OF THE     
REMARK 800  METHOTREXATE INHIBITOR IN CHAIN A                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ANM                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE N(10) METHYL OF      
REMARK 800  THE METHOTREXATE INHIBITOR IN CHAIN A                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AAB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF   
REMARK 800  THE METHOTREXATE INHIBITOR IN CHAIN A                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AGL                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE GLUTAMATE OF THE     
REMARK 800  METHOTREXATE INHIBITOR IN CHAIN A                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BPT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PTERIDINE OF THE     
REMARK 800  METHOTREXATE INHIBITOR IN CHAIN B                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BNM                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE N(10) METHYL OF      
REMARK 800  THE METHOTREXATE INHIBITOR IN CHAIN B                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BAB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF   
REMARK 800  THE METHOTREXATE INHIBITOR IN CHAIN B                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BGL                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE GLUTAMATE OF THE     
REMARK 800  METHOTREXATE INHIBITOR IN CHAIN B                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX B 361                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: DYRA_ECOLI                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        ASN     37            ASP    A     37                         
REMARK 999        ASN     37            ASP    B     37                         
DBREF  1DHI A    1   159  UNP    P0ABQ4   DYR_ECOLI        1    159             
DBREF  1DHI B    1   159  UNP    P0ABQ4   DYR_ECOLI        1    159             
SEQADV 1DHI SER A   27  UNP  P0ABQ4    ASP    27 CONFLICT                       
SEQADV 1DHI ASP A   37  UNP  P0ABQ4    ASN    37 CONFLICT                       
SEQADV 1DHI SER B   27  UNP  P0ABQ4    ASP    27 CONFLICT                       
SEQADV 1DHI ASP B   37  UNP  P0ABQ4    ASN    37 CONFLICT                       
SEQRES   1 A  159  MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL          
SEQRES   2 A  159  ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA          
SEQRES   3 A  159  SER LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO          
SEQRES   4 A  159  VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG          
SEQRES   5 A  159  PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN          
SEQRES   6 A  159  PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL          
SEQRES   7 A  159  ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE          
SEQRES   8 A  159  MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU          
SEQRES   9 A  159  PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA          
SEQRES  10 A  159  GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO          
SEQRES  11 A  159  ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA          
SEQRES  12 A  159  ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU          
SEQRES  13 A  159  GLU ARG ARG                                                  
SEQRES   1 B  159  MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL          
SEQRES   2 B  159  ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA          
SEQRES   3 B  159  SER LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO          
SEQRES   4 B  159  VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG          
SEQRES   5 B  159  PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN          
SEQRES   6 B  159  PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL          
SEQRES   7 B  159  ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE          
SEQRES   8 B  159  MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU          
SEQRES   9 B  159  PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA          
SEQRES  10 B  159  GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO          
SEQRES  11 B  159  ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA          
SEQRES  12 B  159  ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU          
SEQRES  13 B  159  GLU ARG ARG                                                  
HET     CL  A 401       1                                                       
HET    MTX  A 161      33                                                       
HET     CL  B 605       1                                                       
HET     CA  B 620       1                                                       
HET    MTX  B 361      33                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MTX METHOTREXATE                                                     
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  MTX    2(C20 H22 N8 O5)                                             
FORMUL   6   CA    CA 2+                                                        
FORMUL   8  HOH   *385(H2 O)                                                    
HELIX    1 HBA LEU A   24  THR A   35  1                                  12    
HELIX    2 HCA GLY A   43  ILE A   50  1                                   8    
HELIX    3 HEA SER A   77  GLY A   86  1                                  10    
HELIX    4 HFA GLY A   96  LEU A  104  1                                   9    
HELIX    5 HBB LEU B   24  THR B   35  1                                  12    
HELIX    6 HCB GLY B   43  ILE B   50  1                                   8    
HELIX    7 HEB SER B   77  GLY B   86  1                                  10    
HELIX    8 HFB GLY B   96  LEU B  104  1                                   9    
SHEET    1 S1A 8 THR A  73  VAL A  75  0                                        
SHEET    2 S1A 8 LYS A  58  SER A  63  1  O  ASN A  59   N  THR A  73           
SHEET    3 S1A 8 PRO A  39  GLY A  43  1  N  VAL A  40   O  LYS A  58           
SHEET    4 S1A 8 ILE A  91  GLY A  95  1  N  MET A  92   O  PRO A  39           
SHEET    5 S1A 8 MET A   1  LEU A   8  1  O  MET A   1   N  ILE A  91           
SHEET    6 S1A 8 GLN A 108  ASP A 116  1  O  LYS A 109   N  LEU A   4           
SHEET    7 S1A 8 SER A 150  ARG A 159 -1  N  ARG A 158   O  GLN A 108           
SHEET    8 S1A 8 ASP A 132  HIS A 141 -1  N  GLU A 134   O  GLU A 157           
SHEET    1 S1B 8 THR B  73  VAL B  75  0                                        
SHEET    2 S1B 8 LYS B  58  SER B  63  1  O  ASN B  59   N  THR B  73           
SHEET    3 S1B 8 PRO B  39  GLY B  43  1  N  VAL B  40   O  LYS B  58           
SHEET    4 S1B 8 PRO B  89  GLY B  95  1  N  MET B  92   O  PRO B  39           
SHEET    5 S1B 8 MET B   1  LEU B   8  1  O  MET B   1   N  ILE B  91           
SHEET    6 S1B 8 GLN B 108  ASP B 116  1  O  LYS B 109   N  LEU B   4           
SHEET    7 S1B 8 SER B 150  ARG B 159 -1  N  ARG B 158   O  GLN B 108           
SHEET    8 S1B 8 ASP B 132  HIS B 141 -1  N  GLU B 134   O  GLU B 157           
LINK         O   HOH A 483                CA    CA B 620     2665   1555  2.34  
LINK         O   SER B 135                CA    CA B 620     1555   1555  2.28  
LINK        CA    CA B 620                 O   HOH B 658     1555   1555  2.31  
LINK        CA    CA B 620                 O   HOH B 659     1555   2665  2.42  
LINK        CA    CA B 620                 O   HOH B 661     1555   2665  2.49  
LINK        CA    CA B 620                 O   HOH B 673     1555   1555  2.36  
CISPEP   1 GLY A   95    GLY A   96          0         2.83                     
CISPEP   2 GLY B   95    GLY B   96          0         2.85                     
SITE     1 APT 11 ILE A   5  ALA A   6  ALA A   7  TRP A  22                    
SITE     2 APT 11 SER A  27  LEU A  28  PHE A  31  ILE A  94                    
SITE     3 APT 11 THR A 113  HOH A 404  HOH A 410                               
SITE     1 ANM  1 SER A  49                                                     
SITE     1 AAB  5 LEU A  28  PHE A  31  ILE A  50  ARG A  52                    
SITE     2 AAB  5 LEU A  54                                                     
SITE     1 AGL  5 LEU A  28  PHE A  31  LYS A  32  LEU A  54                    
SITE     2 AGL  5 ARG A  57                                                     
SITE     1 BPT 11 ILE B   5  ALA B   6  ALA B   7  TRP B  22                    
SITE     2 BPT 11 SER B  27  LEU B  28  PHE B  31  ILE B  94                    
SITE     3 BPT 11 THR B 113  HOH B 627  HOH B 656                               
SITE     1 BNM  1 SER B  49                                                     
SITE     1 BAB  5 LEU B  28  PHE B  31  ILE B  50  ARG B  52                    
SITE     2 BAB  5 LEU B  54                                                     
SITE     1 BGL  5 LEU B  28  PHE B  31  LYS B  32  LEU B  54                    
SITE     2 BGL  5 ARG B  57                                                     
SITE     1 AC1  5 GLY A  43  HIS A  45  THR A  46  GLY A  96                    
SITE     2 AC1  5 HOH A 464                                                     
SITE     1 AC2  4 GLY B  43  HIS B  45  THR B  46  GLY B  96                    
SITE     1 AC3  6 HOH A 483  SER B 135  HOH B 658  HOH B 659                    
SITE     2 AC3  6 HOH B 661  HOH B 673                                          
SITE     1 AC4 13 ILE A   5  ALA A   6  PHE A  31  LYS A  32                    
SITE     2 AC4 13 SER A  49  ILE A  50  ARG A  52  ARG A  57                    
SITE     3 AC4 13 ILE A  94  TYR A 100  THR A 113  HOH A 496                    
SITE     4 AC4 13 HOH A 525                                                     
SITE     1 AC5 13 ILE B   5  ALA B   6  PHE B  31  LYS B  32                    
SITE     2 AC5 13 ILE B  50  ARG B  52  ARG B  57  ILE B  94                    
SITE     3 AC5 13 TYR B 100  THR B 113  HOH B 656  HOH B 696                    
SITE     4 AC5 13 HOH B 713                                                     
CRYST1   93.190   93.190   73.920  90.00  90.00 120.00 P 61         12          
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      0.010731  0.006195  0.000000        0.00000                         
SCALE2      0.000000  0.012391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013528        0.00000                         
MTRIX1   1 -0.924500 -0.374890  0.069060       59.67269    1                    
MTRIX2   1 -0.333130  0.706490 -0.624410       46.60130    1                    
MTRIX3   1  0.185290 -0.600270 -0.778030       96.32106    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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