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Database: PDB
Entry: 7DFR
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HEADER    OXIDOREDUCTASE                          21-OCT-88   7DFR              
TITLE     CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE   
TITLE    2 NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE 
TITLE    3 BINDING AND A MODEL FOR THE TRANSITION STATE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    OXIDO-REDUCTASE, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BYSTROFF,S.J.OATLEY,J.KRAUT                                         
REVDAT   6   29-NOV-17 7DFR    1       KEYWDS HELIX                             
REVDAT   5   24-FEB-09 7DFR    1       VERSN                                    
REVDAT   4   01-APR-03 7DFR    1       JRNL                                     
REVDAT   3   15-JUL-92 7DFR    2       CONECT                                   
REVDAT   2   15-OCT-90 7DFR    1       JRNL                                     
REVDAT   1   15-JUL-90 7DFR    0                                                
JRNL        AUTH   C.BYSTROFF,S.J.OATLEY,J.KRAUT                                
JRNL        TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE         
JRNL        TITL 2 REDUCTASE: THE NADP+ HOLOENZYME AND THE FOLATE.NADP+ TERNARY 
JRNL        TITL 3 COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION    
JRNL        TITL 4 STATE.                                                       
JRNL        REF    BIOCHEMISTRY                  V.  29  3263 1990              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   2185835                                                      
JRNL        DOI    10.1021/BI00465A018                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.BYSTROFF,J.KRAUT                                           
REMARK   1  TITL   CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI             
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL       
REMARK   1  TITL 3 CHANGES AND COOPERATIVITY IN BINDING                         
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
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 REFINED AT 1.7 ANGSTROMS       
REMARK   1  TITL 3 RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE  
REMARK   1  REF    J.BIOL.CHEM.                  V. 257 13650 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.M.PERRY,J.J.ONUFFER,N.A.TOUCHETTE,C.S.HERNDON,             
REMARK   1  AUTH 2 M.S.GITTELMAN,C.R.MATTHEWS,J.-T.CHEN,R.J.MAYER,K.TAIRA,      
REMARK   1  AUTH 3 S.J.BENKOVIC,E.E.HOWELL,J.KRAUT                              
REMARK   1  TITL   EFFECT OF SINGLE AMINO ACID REPLACEMENTS ON THE FOLDING AND  
REMARK   1  TITL 2 STABILITY OF DIHYDROFOLATE REDUCTASE FROM ESCHERICHIA COLI   
REMARK   1  REF    BIOCHEMISTRY                  V.  26  2674 1987              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
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 REFINED AT 1.7 ANGSTROMS       
REMARK   1  TITL 3 RESOLUTION. II. ENVIRONMENT OF BOUND NADPH AND IMPLICATIONS  
REMARK   1  TITL 4 FOR CATALYSIS                                                
REMARK   1  REF    J.BIOL.CHEM.                  V. 257 13663 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   K.W.VOLZ,D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,C.HANSCH,          
REMARK   1  AUTH 2 B.T.KAUFMAN,J.KRAUT                                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF AVIAN DIHYDROFOLATE REDUCTASE           
REMARK   1  TITL 2 CONTAINING PHENYLTRIAZINE AND NADPH                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 257  2528 1982              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   D.A.MATTHEWS                                                 
REMARK   1  TITL   INTERPRETATION OF NUCLEAR MAGNETIC RESONANCE SPECTRA FOR     
REMARK   1  TITL 2 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE BASED ON THE     
REMARK   1  TITL 3 X-RAY STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX     
REMARK   1  REF    BIOCHEMISTRY                  V.  18  1602 1979              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,N.-H.XUONG,J.KRAUT          
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI.            
REMARK   1  TITL 2 STEREOCHEMISTRY OF NADPH BINDING                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 254  4144 1979              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   M.POE,K.HOOGSTEEN,D.A.MATTHEWS                               
REMARK   1  TITL   PROTON MAGNETIC RESONANCE STUDIES ON ESCHERICHIA COLI        
REMARK   1  TITL 2 DIHYDROFOLATE REDUCTASE. ASSIGNMENT OF HISTIDINE C-2 PROTONS 
REMARK   1  TITL 3 IN BINARY COMPLEXES WITH FOLATES ON THE BASIS OF THE CRYSTAL 
REMARK   1  TITL 4 STRUCTURE WITH METHOTREXATE AND ON CHEMICAL MODIFICATIONS    
REMARK   1  REF    J.BIOL.CHEM.                  V. 254  8143 1979              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,D.J.FILMAN,S.T.FREER,       
REMARK   1  AUTH 2 R.HAMLIN,W.G.J.HOL,R.L.KISLIUK,E.J.PASTORE,L.T.PLANTE,       
REMARK   1  AUTH 3 N.-H.XUONG,J.KRAUT                                           
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI. X-RAY      
REMARK   1  TITL 2 STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX           
REMARK   1  REF    J.BIOL.CHEM.                  V. 253  6946 1978              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 10                                                         
REMARK   1  AUTH   C.D.BENNETT,J.A.RODKEY,J.M.SONDEY,R.HIRSCHMANN               
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE. THE AMINO ACID SEQUENCE OF THE      
REMARK   1  TITL 2 ENZYME FROM A METHOTREXATE-RESISTANT MUTANT OF ESCHERICHIA   
REMARK   1  TITL 3 COLI                                                         
REMARK   1  REF    BIOCHEMISTRY                  V.  17  1328 1978              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 11                                                         
REMARK   1  AUTH   D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,S.T.FREER,R.HAMLIN,N.XUONG, 
REMARK   1  AUTH 2 J.KRAUT,M.POE,M.WILLIAMS,K.HOOGSTEEN                         
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE. X-RAY STRUCTURE OF THE BINARY       
REMARK   1  TITL 2 COMPLEX WITH METHOTREXATE                                    
REMARK   1  REF    SCIENCE                       V. 197   452 1977              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 12                                                         
REMARK   1  AUTH   M.POE,N.J.GREENFIELD,J.M.HIRSHFIELD,M.N.WILLIAMS,K.HOOGSTEEN 
REMARK   1  TITL   DIHYDROFOLATE REDUCTASE. PURIFICATION AND CHARACTERIZATION   
REMARK   1  TITL 2 OF THE ENZYME FROM AN AMETHOPTERIN-RESISTANT MUTANT OF       
REMARK   1  TITL 3 ESCHERICHIA COLI                                             
REMARK   1  REF    BIOCHEMISTRY                  V.  11  1023 1972              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
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) : 0.245                           
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            : 1229                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 55                                      
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) : 0.022 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.034 ; 0.025               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.039 ; 0.035               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.022 ; 0.018               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.232 ; 0.180               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.217 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.266 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.273 ; 0.300               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.400 ; 5.000               
REMARK   3    STAGGERED                 (DEGREES) : 23.600; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 2.595 ; 2.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.847 ; 3.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 2.649 ; 2.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.966 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7DFR 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_1000179892.                                   
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   (%): 62.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.35000            
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       35.17500            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.17500            
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       70.35000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 401  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 402  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 403  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 RESIDUES 16 - 19 FORM A TYPE I BETA TURN.  THIS PART OF              
REMARK 400 THE STRUCTURE IS DENOTED AS THE MET 20 LOOP.                         
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 A  17    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  44    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  52    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     ASP A 116    OD1  OD2                                            
REMARK 470     GLU A 120    OE1  OE2                                            
REMARK 470     GLU A 129    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A 131    CB   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   OG   SER A   148     O    HOH A   239              2.03            
REMARK 500   O    GLN A    65     O    HOH A   310              2.09            
REMARK 500   ND1  HIS A    45     O5B  NAP A   164              2.11            
REMARK 500   O    ARG A   158     O    HOH A   212              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   305     O    HOH A   305     4556     1.45            
REMARK 500   O    HOH A   311     O    HOH A   311     4556     1.89            
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    THR A 113   N     THR A 113   CA     -0.127                       
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. =   8.4 DEGREES          
REMARK 500    ARG A  12   CD  -  NE  -  CZ  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    ARG A  33   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    MET A  42   CG  -  SD  -  CE  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASN A  59   CA  -  CB  -  CG  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    LEU A  62   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ASP A  87   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    THR A 113   C   -  N   -  CA  ANGL. DEV. =  18.0 DEGREES          
REMARK 500    GLU A 118   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    PRO A 130   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    TYR A 151   O   -  C   -  N   ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  11       20.93     93.01                                   
REMARK 500    GLU A  17     -129.76     33.79                                   
REMARK 500    PRO A  21       22.23    -60.93                                   
REMARK 500    LEU A  36      133.47    -27.11                                   
REMARK 500    ARG A  52      148.94   -179.00                                   
REMARK 500    ALA A  84       -8.05    -53.03                                   
REMARK 500    TYR A 128      175.35    -56.33                                   
REMARK 500    PRO A 130      -54.49    -26.91                                   
REMARK 500    PHE A 137      142.91    178.18                                   
REMARK 500    ASP A 144     -168.25   -167.04                                   
REMARK 500    SER A 148      -14.64    -45.73                                   
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  12         0.20    SIDE CHAIN                              
REMARK 500    ARG A  33         0.10    SIDE CHAIN                              
REMARK 500    ARG A 159         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS A 114         10.08                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL A 161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 164                 
DBREF  7DFR A    1   159  UNP    P0ABQ4   DYR_ECOLI        1    159             
SEQADV 7DFR ASP A   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  ASP 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                                                  
HET    FOL  A 161      32                                                       
HET    NAP  A 164      48                                                       
HETNAM     FOL FOLIC ACID                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   2  FOL    C19 H19 N7 O6                                                
FORMUL   3  NAP    C21 H28 N7 O17 P3                                            
FORMUL   4  HOH   *55(H2 O)                                                     
HELIX    1  HB LEU A   24  THR A   35  1                                  12    
HELIX    2  HC GLY A   43  ILE A   50  1                                   8    
HELIX    3  HE SER A   77  GLY A   86  1                                  10    
HELIX    4  HF GLY A   96  LEU A  104  1                                   9    
SHEET    1  S1 8 THR A  73  VAL A  75  0                                        
SHEET    2  S1 8 LYS A  58  SER A  63  1  O  ASN A  59   N  THR A  73           
SHEET    3  S1 8 PRO A  39  GLY A  43  1  N  VAL A  40   O  LYS A  58           
SHEET    4  S1 8 ILE A  91  GLY A  95  1  N  MET A  92   O  PRO A  39           
SHEET    5  S1 8 MET A   1  LEU A   8  1  O  MET A   1   N  ILE A  91           
SHEET    6  S1 8 GLN A 108  ASP A 116  1  O  LYS A 109   N  LEU A   4           
SHEET    7  S1 8 SER A 150  ARG A 159 -1  N  ARG A 158   O  GLN A 108           
SHEET    8  S1 8 ASP A 132  HIS A 141 -1  N  GLU A 134   O  GLU A 157           
SSBOND   1 CYS A  152    CYS A  152                          1555   4556  2.56  
CISPEP   1 GLY A   95    GLY A   96          0        -2.73                     
SITE     1 AC1 15 ILE A   5  ALA A   7  MET A  20  ASP A  27                    
SITE     2 AC1 15 LEU A  28  PHE A  31  LYS A  32  THR A  46                    
SITE     3 AC1 15 ILE A  50  ARG A  57  ILE A  94  THR A 113                    
SITE     4 AC1 15 NAP A 164  HOH A 206  HOH A 301                               
SITE     1 AC2 27 ALA A   6  ALA A   7  ILE A  14  MET A  16                    
SITE     2 AC2 27 ASN A  18  ALA A  19  MET A  20  TRP A  22                    
SITE     3 AC2 27 GLY A  43  ARG A  44  HIS A  45  THR A  46                    
SITE     4 AC2 27 SER A  49  LEU A  62  SER A  63  SER A  64                    
SITE     5 AC2 27 LYS A  76  ILE A  94  GLY A  96  GLY A  97                    
SITE     6 AC2 27 ARG A  98  VAL A  99  TYR A 100  GLN A 102                    
SITE     7 AC2 27 FOL A 161  HOH A 225  HOH A 237                               
CRYST1   62.207   62.207  105.525  90.00  90.00 120.00 P 32 2 1      6          
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      0.016075  0.009281  0.000000        0.00000                         
SCALE2      0.000000  0.018562  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009476        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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