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Database: PDB
Entry: 4P68
LinkDB: 4P68
Original site: 4P68 
HEADER    OXIDOREDUCTASE                          22-MAR-14   4P68              
TITLE     ELECTROSTATICS OF ACTIVE SITE MICROENVIRONMENTS FOR E. COLI DHFR      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: FOLA, ECS0051, LF82_0721;                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ELECTROSTATICS, CATALYSIS, OXIDOREDUCTASE, DHFR                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.T.LIU,J.P.LAYFIELD,R.J.STEWART III,J.B.FRENCH,P.HANOIAN,J.B.ASBURY, 
AUTHOR   2 S.HAMMES-SCHIFFER,S.J.BENKOVIC                                       
REVDAT   6   27-DEC-23 4P68    1       REMARK LINK                              
REVDAT   5   25-DEC-19 4P68    1       REMARK                                   
REVDAT   4   20-SEP-17 4P68    1       SOURCE REMARK                            
REVDAT   3   01-OCT-14 4P68    1       JRNL                                     
REVDAT   2   06-AUG-14 4P68    1       AUTHOR                                   
REVDAT   1   16-JUL-14 4P68    0                                                
JRNL        AUTH   C.T.LIU,J.P.LAYFIELD,R.J.STEWART,J.B.FRENCH,P.HANOIAN,       
JRNL        AUTH 2 J.B.ASBURY,S.HAMMES-SCHIFFER,S.J.BENKOVIC                    
JRNL        TITL   PROBING THE ELECTROSTATICS OF ACTIVE SITE MICROENVIRONMENTS  
JRNL        TITL 2 ALONG THE CATALYTIC CYCLE FOR ESCHERICHIA COLI DIHYDROFOLATE 
JRNL        TITL 3 REDUCTASE.                                                   
JRNL        REF    J.AM.CHEM.SOC.                V. 136 10349 2014              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   24977791                                                     
JRNL        DOI    10.1021/JA5038947                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6821                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 320                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 426                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 12                           
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1234                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 91                                      
REMARK   3   SOLVENT ATOMS            : 39                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37000                                             
REMARK   3    B22 (A**2) : 0.78000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.510         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.268         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.191         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.664         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1361 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   877 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1856 ; 1.593 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2131 ; 1.107 ; 3.019       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   156 ; 5.790 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;37.282 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   194 ;17.329 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;10.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   199 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1480 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   270 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   807 ; 0.863 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   321 ; 0.148 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1288 ; 1.623 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   554 ; 2.210 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   568 ; 3.658 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4P68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200790.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6821                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM CALCIUM ACETATE, 34% PEG 400,      
REMARK 280  100 MM HEPES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       17.06600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.29300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.32500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.29300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.06600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.32500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     ASN A  23    CG   OD1  ND2                                       
REMARK 470     LEU A  28    CG   CD1  CD2                                       
REMARK 470     ARG A  33    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  52    CZ   NH1  NH2                                       
REMARK 470     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 118    CD   OE1  OE2                                       
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
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    XCN A  54   O   -  C   -  N   ANGL. DEV. = -15.1 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    ALA A   9     -153.41   -110.60                                   
REMARK 500    ASP A  69      119.24   -160.45                                   
REMARK 500    ASP A 144     -152.92   -143.53                                   
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    XCN A  54         26.29                                           
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 A 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 116   O                                                      
REMARK 620 2 ARG A 159   OXT  18.0                                              
REMARK 620 3 HOH A 306   O    21.6   4.2                                        
REMARK 620 4 HOH A 324   O    25.6   7.6   5.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 205                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P66   RELATED DB: PDB                                   
REMARK 900 4P66 CONTAINS THE SAME PROTEIN WITH THE NITRILE PROBE INSTALLED AT   
REMARK 900 A DIFFERENT POSITION                                                 
DBREF  4P68 A    1   159  UNP    C3TR70   C3TR70_ECOLX     1    159             
SEQADV 4P68 XCN A   54  UNP  C3TR70    LEU    54 ENGINEERED MUTATION            
SEQADV 4P68 ALA A   85  UNP  C3TR70    CYS    85 ENGINEERED MUTATION            
SEQADV 4P68 SER A  152  UNP  C3TR70    CYS   152 ENGINEERED MUTATION            
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 ASN LYS PRO          
SEQRES   4 A  159  VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG          
SEQRES   5 A  159  PRO XCN 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 ALA 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 SER PHE GLU ILE LEU          
SEQRES  13 A  159  GLU ARG ARG                                                  
HET    XCN  A  54       8                                                       
HET    MTX  A 201      33                                                       
HET    NAP  A 202      48                                                       
HET    ACT  A 203       4                                                       
HET    ACT  A 204       4                                                       
HET     CA  A 205       1                                                       
HET     CA  A 206       1                                                       
HETNAM     XCN S-CYANO-L-CYSTEINE                                               
HETNAM     MTX METHOTREXATE                                                     
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     ACT ACETATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   1  XCN    C4 H6 N2 O2 S                                                
FORMUL   2  MTX    C20 H22 N8 O5                                                
FORMUL   3  NAP    C21 H28 N7 O17 P3                                            
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6   CA    2(CA 2+)                                                     
FORMUL   8  HOH   *39(H2 O)                                                     
HELIX    1 AA1 ALA A    9  ASP A   11  5                                   3    
HELIX    2 AA2 LEU A   24  LEU A   36  1                                  13    
HELIX    3 AA3 ARG A   44  GLY A   51  1                                   8    
HELIX    4 AA4 SER A   77  ALA A   85  1                                   9    
HELIX    5 AA5 GLY A   96  LEU A  104  1                                   9    
HELIX    6 AA6 PRO A  105  ALA A  107  5                                   3    
SHEET    1 AA1 8 THR A  73  VAL A  75  0                                        
SHEET    2 AA1 8 ASN A  59  LEU A  62  1  N  ASN A  59   O  THR A  73           
SHEET    3 AA1 8 VAL A  40  GLY A  43  1  N  MET A  42   O  LEU A  62           
SHEET    4 AA1 8 ILE A  91  GLY A  95  1  O  ILE A  94   N  ILE A  41           
SHEET    5 AA1 8 ILE A   2  LEU A   8  1  N  SER A   3   O  VAL A  93           
SHEET    6 AA1 8 LYS A 109  ILE A 115  1  O  ILE A 115   N  LEU A   8           
SHEET    7 AA1 8 TYR A 151  ARG A 158 -1  O  GLU A 154   N  LEU A 112           
SHEET    8 AA1 8 TRP A 133  HIS A 141 -1  N  HIS A 141   O  TYR A 151           
SHEET    1 AA2 2 VAL A  13  GLY A  15  0                                        
SHEET    2 AA2 2 THR A 123  HIS A 124 -1  O  THR A 123   N  ILE A  14           
LINK         C   PRO A  53                 N   XCN A  54     1555   1555  1.27  
LINK         C   XCN A  54                 N   PRO A  55     1555   1555  1.30  
LINK         O   ASP A 116                CA    CA A 205     1555   1655  2.45  
LINK         OXT ARG A 159                CA    CA A 205     1555   1555  2.73  
LINK        CA    CA A 205                 O   HOH A 306     1555   3454  2.17  
LINK        CA    CA A 205                 O   HOH A 324     1555   1455  2.07  
CISPEP   1 GLY A   95    GLY A   96          0        -0.61                     
SITE     1 AC1 13 ILE A   5  ALA A   6  ALA A   7  MET A  20                    
SITE     2 AC1 13 ASP A  27  PHE A  31  ILE A  50  XCN A  54                    
SITE     3 AC1 13 ARG A  57  ILE A  94  TYR A 100  NAP A 202                    
SITE     4 AC1 13 HOH A 328                                                     
SITE     1 AC2 28 ALA A   6  ALA A   7  ILE A  14  ASN A  18                    
SITE     2 AC2 28 ALA A  19  MET A  20  GLY A  43  ARG A  44                    
SITE     3 AC2 28 HIS A  45  THR A  46  LEU A  62  SER A  63                    
SITE     4 AC2 28 SER A  64  GLN A  65  LYS A  76  ILE A  94                    
SITE     5 AC2 28 GLY A  96  GLY A  97  ARG A  98  VAL A  99                    
SITE     6 AC2 28 TYR A 100  GLN A 102  ASP A 131  GLU A 139                    
SITE     7 AC2 28 MTX A 201  HOH A 303  HOH A 315  HOH A 333                    
SITE     1 AC3  2 ASP A  70  ASP A  87                                          
SITE     1 AC4  1 ASP A  70                                                     
SITE     1 AC5  5 ASP A 116  HIS A 149  ARG A 159  HOH A 306                    
SITE     2 AC5  5 HOH A 324                                                     
CRYST1   34.132   42.650   98.586  90.00  90.00  90.00 P 21 21 21    4          
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      0.029298  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.023447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010143        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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