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Database: PDB
Entry: 1RAD
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HEADER    TRANSFERASE                             14-AUG-92   1RAD              
TITLE     CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE  
TITLE    2 AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE 
TITLE    3 MECHANISM OF NEGATIVE COOPERATIVITY                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: ASPARTATE TRANSCARBAMYLASE, ATCASE;                         
COMPND   5 EC: 2.1.3.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: PYRB, B4245, JW4204;                                           
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   8 ORGANISM_TAXID: 83333;                                               
SOURCE   9 STRAIN: K12;                                                         
SOURCE  10 GENE: PYRI, B4244, JW4203                                            
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.P.KOSMAN,J.E.GOUAUX,W.N.LIPSCOMB                                    
REVDAT   7   14-FEB-24 1RAD    1       REMARK LINK                              
REVDAT   6   29-NOV-17 1RAD    1       HELIX                                    
REVDAT   5   02-JUL-14 1RAD    1       COMPND SOURCE DBREF  REMARK              
REVDAT   4   13-JUL-11 1RAD    1       VERSN                                    
REVDAT   3   24-FEB-09 1RAD    1       VERSN                                    
REVDAT   2   01-APR-03 1RAD    1       JRNL                                     
REVDAT   1   31-JAN-94 1RAD    0                                                
JRNL        AUTH   R.P.KOSMAN,J.E.GOUAUX,W.N.LIPSCOMB                           
JRNL        TITL   CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE           
JRNL        TITL 2 TRANSCARBAMOYLASE AT 2.5 A RESOLUTION: IMPLICATIONS FOR      
JRNL        TITL 3 ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY.  
JRNL        REF    PROTEINS                      V.  15   147 1993              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   8441751                                                      
JRNL        DOI    10.1002/PROT.340150206                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.C.STEVENS,J.E.GOUAUX,W.N.LIPSCOMB                          
REMARK   1  TITL   STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE   
REMARK   1  TITL 2 OF ASPARTATE CARBAMOYLTRANSFERASE: CRYSTAL STRUCTURES OF THE 
REMARK   1  TITL 3 UNLIGATED AND ATP-AND CTP-COMPLEXED ENZYMES AT 2.6 ANGSTROMS 
REMARK   1  TITL 4 RESOLUTION                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7691 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.H.KIM,Z.PAN,R.B.HONZATKO,H.-M.KE,W.N.LIPSCOMB              
REMARK   1  TITL   STRUCTURAL ASYMMETRY IN THE CTP-LIGANDED FORM OF ASPARTATE   
REMARK   1  TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI                   
REMARK   1  REF    J.MOL.BIOL.                   V. 196   853 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.K.SCHACHMAN,C.D.PAUZA,M.NAVRE,M.J.KARELS,L.WU,Y.R.YANG     
REMARK   1  TITL   LOCATION OF AMINO ACID ALTERATIONS IN MUTANTS OF ASPARTATE   
REMARK   1  TITL 2 TRANSCARBAMOYLASE: STRUCTURAL ASPECTS OF INTERALLELIC        
REMARK   1  TITL 3 COMPLEMENTATION                                              
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  81   115 1984              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   T.A.HOOVER,W.D.ROOF,K.F.FOLTERMANN,G.A.O'DONOVAN,            
REMARK   1  AUTH 2 D.A.BENCINI,J.R.WILD                                         
REMARK   1  TITL   NUCLEOTIDE SEQUENCE OF THE STRUCTURAL GENE (PYRB) THAT       
REMARK   1  TITL 2 ENCODES THE CATALYTIC POLYPEPTIDE OF ASPARTATE               
REMARK   1  TITL 3 TRANSCARBAMOYLASE OF ESCHERICHIA COLI                        
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  80  2462 1983              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   W.H.KONIGSBERG,L.HENDERSON                                   
REMARK   1  TITL   AMINO ACID SEQUENCE OF THE CATALYTIC SUBUNIT OF ASPARTATE    
REMARK   1  TITL 2 TRANSCARBAMOYLASE FROM ESCHERICHIA COLI                      
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  80  2467 1983              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
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   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 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 SET) : 0.189                           
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   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7222                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
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  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.726                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RAD 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_1000175966.                                   
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -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        0.00000            
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        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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 35840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 105990 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000      122.13000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       61.06500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      105.76768            
REMARK 350   BIOMT3   3  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     GLN B   8    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN D   8    CB   CG   CD   OE1  NE2                             
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    HIS A  41   NE2   HIS A  41   CD2    -0.068                       
REMARK 500    GLU A  60   CD    GLU A  60   OE2     0.080                       
REMARK 500    HIS A 106   NE2   HIS A 106   CD2    -0.076                       
REMARK 500    GLU A 147   CD    GLU A 147   OE2     0.077                       
REMARK 500    HIS A 156   NE2   HIS A 156   CD2    -0.067                       
REMARK 500    HIS A 212   NE2   HIS A 212   CD2    -0.069                       
REMARK 500    HIS B  20   NE2   HIS B  20   CD2    -0.068                       
REMARK 500    HIS B 147   NE2   HIS B 147   CD2    -0.076                       
REMARK 500    HIS C   8   NE2   HIS C   8   CD2    -0.066                       
REMARK 500    HIS C  64   NE2   HIS C  64   CD2    -0.071                       
REMARK 500    HIS C 106   NE2   HIS C 106   CD2    -0.066                       
REMARK 500    HIS C 134   NE2   HIS C 134   CD2    -0.073                       
REMARK 500    GLU C 147   CD    GLU C 147   OE2     0.083                       
REMARK 500    HIS C 170   NE2   HIS C 170   CD2    -0.072                       
REMARK 500    HIS C 212   NE2   HIS C 212   CD2    -0.074                       
REMARK 500    HIS D 147   NE2   HIS D 147   CD2    -0.069                       
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    TYR A   5   CB  -  CG  -  CD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A  17   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    VAL A  43   CG1 -  CB  -  CG2 ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    SER A  80   N   -  CA  -  C   ANGL. DEV. =  20.8 DEGREES          
REMARK 500    LEU A  81   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    LYS A  83   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    MET A 159   CA  -  CB  -  CG  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 167   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    TRP A 209   CD1 -  CG  -  CD2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TRP A 209   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    TRP A 209   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    MET A 227   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG A 229   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 234   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 250   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 269   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 269   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TRP A 284   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TRP A 284   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG A 296   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    VAL A 303   CG1 -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    MET B   1   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ALA B  11   N   -  CA  -  C   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    LEU B  30   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLU B  52   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    GLU B  52   CA  -  C   -  N   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    MET B  53   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    LEU B  66   CA  -  CB  -  CG  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    GLN B  80   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    VAL B 106   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG B 128   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP B 133   N   -  CA  -  C   ANGL. DEV. =  18.8 DEGREES          
REMARK 500    PRO C  34   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG C  54   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ARG C  56   CB  -  CG  -  CD  ANGL. DEV. = -18.7 DEGREES          
REMARK 500    ARG C  56   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG C  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    SER C  80   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    THR C  97   N   -  CA  -  CB  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    TYR C  98   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG C 113   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    GLN C 174   CA  -  CB  -  CG  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ARG C 183   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG C 183   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    TRP C 209   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP C 209   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      75 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  79      106.19    -12.09                                   
REMARK 500    SER A  80      -44.29      0.63                                   
REMARK 500    LYS A  83      -71.70     45.94                                   
REMARK 500    LYS A  84      123.77    150.05                                   
REMARK 500    HIS A 134       63.67   -159.21                                   
REMARK 500    GLN A 231       94.95    -66.98                                   
REMARK 500    ARG A 234       40.13   -104.83                                   
REMARK 500    VAL A 243      106.84    -54.88                                   
REMARK 500    LYS A 244     -124.66     67.16                                   
REMARK 500    GLN A 246     -178.85     63.96                                   
REMARK 500    LEU A 267      153.59     64.97                                   
REMARK 500    VAL A 270      -61.30    -11.79                                   
REMARK 500    ASP A 271      -16.50   -153.11                                   
REMARK 500    THR B   2      135.35    175.81                                   
REMARK 500    HIS B   3       70.60     -4.48                                   
REMARK 500    ASP B   4      -71.48    -48.19                                   
REMARK 500    ASN B   5     -159.62     61.30                                   
REMARK 500    LYS B   6       -0.27   -152.84                                   
REMARK 500    ALA B  11      110.19      2.16                                   
REMARK 500    ARG B  14      127.17     58.10                                   
REMARK 500    GLN B  24       16.08     53.99                                   
REMARK 500    LYS B  34       44.47     38.56                                   
REMARK 500    GLU B  37       54.91    -92.96                                   
REMARK 500    ASN B  47       75.34     40.91                                   
REMARK 500    PRO B  49       60.62   -100.96                                   
REMARK 500    SER B  50     -155.61   -161.38                                   
REMARK 500    GLU B  52       91.54    -69.11                                   
REMARK 500    MET B  53      -34.01   -137.81                                   
REMARK 500    GLU B  68      -71.16     53.52                                   
REMARK 500    ASN B 105      -21.97     60.38                                   
REMARK 500    PRO B 120       41.08    -60.54                                   
REMARK 500    LYS B 129       77.18     65.45                                   
REMARK 500    ALA B 131      -17.47     41.84                                   
REMARK 500    ASP B 133       83.18    120.45                                   
REMARK 500    ILE B 134      121.17     -1.84                                   
REMARK 500    SER C  52       87.88   -155.20                                   
REMARK 500    ASP C  75     -138.04   -138.39                                   
REMARK 500    ALA C  77       61.09    178.88                                   
REMARK 500    ASN C  78       43.12      7.78                                   
REMARK 500    SER C  80       -4.72      9.61                                   
REMARK 500    LYS C  84     -100.88     70.31                                   
REMARK 500    TYR C  98        5.31   -153.18                                   
REMARK 500    ASN C 132      -90.26    -97.92                                   
REMARK 500    HIS C 134       63.37   -159.84                                   
REMARK 500    VAL C 243      -28.83    -19.98                                   
REMARK 500    ALA C 245       16.74    -67.79                                   
REMARK 500    GLN C 246       58.83    -99.19                                   
REMARK 500    HIS C 255      -56.80    -14.90                                   
REMARK 500    HIS C 265      117.24   -162.68                                   
REMARK 500    LEU C 267      160.09     73.42                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU D   48     PRO D   49                  145.16                    
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    PHE A  48         0.08    SIDE CHAIN                              
REMARK 500    TYR A  98         0.16    SIDE CHAIN                              
REMARK 500    PHE A 143         0.09    SIDE CHAIN                              
REMARK 500    TYR A 185         0.10    SIDE CHAIN                              
REMARK 500    TYR A 226         0.07    SIDE CHAIN                              
REMARK 500    TYR A 240         0.11    SIDE CHAIN                              
REMARK 500    ARG A 296         0.08    SIDE CHAIN                              
REMARK 500    TYR B  89         0.13    SIDE CHAIN                              
REMARK 500    TYR B 140         0.10    SIDE CHAIN                              
REMARK 500    TYR C   5         0.08    SIDE CHAIN                              
REMARK 500    TYR C  98         0.08    SIDE CHAIN                              
REMARK 500    PHE C 286         0.08    SIDE CHAIN                              
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                              ZN B 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 109   SG                                                     
REMARK 620 2 CYS B 114   SG  112.3                                              
REMARK 620 3 CYS B 138   SG  113.9 107.0                                        
REMARK 620 4 CYS B 141   SG  101.7 111.7 110.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 109   SG                                                     
REMARK 620 2 CYS D 114   SG  113.5                                              
REMARK 620 3 CYS D 138   SG  117.6 105.0                                        
REMARK 620 4 CYS D 141   SG  102.1 111.4 107.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE OF CHAIN B                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZND                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE OF CHAIN D                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP B 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP D 999                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AMINO ACID SEQUENCE OF ESCHERICHIA COLI ATCASE USED IN           
REMARK 999 THIS ENTRY REPRESENTS A DEPARTURE FROM THE SEQUENCE USED IN          
REMARK 999 PREVIOUS ATCASE STRUCTURES FROM THE SAME LABORATORY.  THE            
REMARK 999 NEW AMINO ACID ASSIGNMENTS FOR FIVE OF THE RESIDUES IN EACH          
REMARK 999 CATALYTIC-REGULATORY SUBUNIT ARE NOW IN ACCORD WITH THE              
REMARK 999 DNA-DETERMINED AMINO ACID SEQUENCE MOST RECENTLY DEFINED             
REMARK 999 FOR THIS ENZYME.  THE CHANGES ARE AS FOLLOWS:                        
REMARK 999                                                                      
REMARK 999        PREVIOUS                   PRESENT                            
REMARK 999        GLN A  60                  GLU A  60                          
REMARK 999        GLN A 147                  GLU A 147                          
REMARK 999        GLU A 149                  GLN A 149                          
REMARK 999        GLU A 196                  GLN A 196                          
REMARK 999        GLY B   8                  GLN B   8                          
REMARK 999        GLN C  60                  GLU C  60                          
REMARK 999        GLN C 147                  GLU C 147                          
REMARK 999        GLU C 149                  GLN C 149                          
REMARK 999        GLU C 196                  GLN C 196                          
REMARK 999        GLY D   8                  GLN D   8                          
REMARK 999                                                                      
REMARK 999 GLN 8 IS THE ONLY RESIDUE WHICH INVOLVED MORE THAN A SINGLE          
REMARK 999 ATOM CHANGE AND, AS A RESULT, IT IS THE ONLY RESIDUE IN              
REMARK 999 THIS LIST WHICH REQUIRED A REEXAMINATION OF THE                      
REMARK 999 CRYSTALLOGRAPHIC DATA IN ADDITION TO THE REEXAMINATION OF            
REMARK 999 THE CHEMICAL ENVIRONMENT THAT WAS PERFORMED FOR ALL OF               
REMARK 999 THESE RESIDUES.  OMIT MAPS BASED ON THE CTP-LIGATED ENZYME           
REMARK 999 DATA (SEE PAPER CITED ON *JRNL* RECORDS ABOVE) WERE                  
REMARK 999 CREATED, AND IN BOTH RESIDUES WITHIN THE ASYMMETRIC UNIT             
REMARK 999 (GLN B 8 AND GLN D 8) ELECTRON DENSITY CONSISTENT WITH THE           
REMARK 999 GLUTAMINE SIDE CHAINS WAS IDENTIFIED, ALTHOUGH IT WAS NOT            
REMARK 999 POSSIBLE TO POSITION THE SIDE CHAINS WITH CERTAINTY IN THIS          
REMARK 999 ELECTRON DENSITY.  CONSEQUENTLY, GLN 8 IS IDENTIFIED                 
REMARK 999 PROPERLY AS A GLUTAMINE BUT IT LACKS THE SIDE CHAIN ATOMS.           
REMARK 999 THERE IS STILL AN UNRESOLVED CONFLICT IN THE LITERATURE              
REMARK 999 REGARDING THE IDENTITY OF RESIDUE 220 OF THE CATALYTIC               
REMARK 999 CHAIN (SEE THE PAPERS CITED AS REFERENCES 3 - 5 ABOVE).              
REMARK 999 SINCE THERE WAS NO UNEQUIVOCAL CRYSTALLOGRAPHIC EVIDENCE             
REMARK 999 FOR A VALINE AT THIS POSITION (REFERENCES 4 AND 5), ALA              
REMARK 999 (REFERENCE 3) WAS LEFT IN THIS SITE.                                 
DBREF  1RAD A    1   310  UNP    P0A786   PYRB_ECOLI       2    311             
DBREF  1RAD B    1   153  UNP    P0A7F3   PYRI_ECOLI       1    153             
DBREF  1RAD C    1   310  UNP    P0A786   PYRB_ECOLI       2    311             
DBREF  1RAD D    1   153  UNP    P0A7F3   PYRI_ECOLI       1    153             
SEQRES   1 A  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 A  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 A  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 A  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 A  310  THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG          
SEQRES   6 A  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 A  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 A  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 A  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 A  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 A  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 A  310  THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 A  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 A  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 A  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 A  310  GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 A  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 A  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 A  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 A  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 A  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 A  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 A  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 A  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 B  153  MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS          
SEQRES   2 B  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 B  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 B  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 B  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 B  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 B  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 B  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 B  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 B  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 B  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 B  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
SEQRES   1 C  310  ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN          
SEQRES   2 C  310  ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR          
SEQRES   3 C  310  ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU          
SEQRES   4 C  310  LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER          
SEQRES   5 C  310  THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG          
SEQRES   6 C  310  LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN          
SEQRES   7 C  310  THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR          
SEQRES   8 C  310  ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET          
SEQRES   9 C  310  ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU          
SEQRES  10 C  310  PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY          
SEQRES  11 C  310  SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE          
SEQRES  12 C  310  THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS          
SEQRES  13 C  310  VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL          
SEQRES  14 C  310  HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN          
SEQRES  15 C  310  ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO          
SEQRES  16 C  310  GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA          
SEQRES  17 C  310  TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU          
SEQRES  18 C  310  VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG          
SEQRES  19 C  310  LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE          
SEQRES  20 C  310  VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN          
SEQRES  21 C  310  MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE          
SEQRES  22 C  310  ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE          
SEQRES  23 C  310  GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU          
SEQRES  24 C  310  LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU                  
SEQRES   1 D  153  MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS          
SEQRES   2 D  153  ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY          
SEQRES   3 D  153  PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP          
SEQRES   4 D  153  GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU          
SEQRES   5 D  153  MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE          
SEQRES   6 D  153  LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA          
SEQRES   7 D  153  PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL          
SEQRES   8 D  153  VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP          
SEQRES   9 D  153  ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS          
SEQRES  10 D  153  ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG          
SEQRES  11 D  153  ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS          
SEQRES  12 D  153  GLU PHE SER HIS ASN VAL VAL LEU ALA ASN                      
HET     ZN  B 154       1                                                       
HET    CTP  B 999      29                                                       
HET     ZN  D 154       1                                                       
HET    CTP  D 999      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CTP CYTIDINE-5'-TRIPHOSPHATE                                         
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  CTP    2(C9 H16 N3 O14 P3)                                          
FORMUL   9  HOH   *93(H2 O)                                                     
HELIX    1 H1A ARG A   17  ALA A   32  1                                  16    
HELIX    2 H2A THR A   53  LEU A   66  1                                  14    
HELIX    3 H3A ALA A   89  VAL A   99  1                                  11    
HELIX    4 H4A ALA A  111  SER A  119  1                                   9    
HELIX    5 H5A PRO A  135  GLN A  149  1                                  15    
HELIX    6 H6A ARG A  167  PHE A  179  1                                  13    
HELIX    7 H7A GLN A  196  LYS A  205  1                                  10    
HELIX    8 H8A ILE A  215  ALA A  220  1                                   6    
HELIX    9 H9A ALA A  251  ASN A  256  1                                   6    
HELIX   10 H0A THR A  275  LYS A  279  1                                   5    
HELIX   11 HEA TYR A  285  LEU A  304  1                                  20    
HELIX   12 H1B ILE B   25  PHE B   33  1                                   9    
HELIX   13 H2B ASP B   69  TYR B   77  5ENDS TYPE 1                        9    
HELIX   14 H3B HIS B  147  VAL B  150  1                                   4    
HELIX   15 H1C ARG C   17  ALA C   32  1                                  16    
HELIX   16 H2C THR C   53  LEU C   66  1                                  14    
HELIX   17 H3C ALA C   89  VAL C   99  1                                  11    
HELIX   18 H4C ALA C  111  SER C  119  1                                   9    
HELIX   19 H5C PRO C  135  GLN C  149  1                                  15    
HELIX   20 H6C ARG C  167  PHE C  179  1                                  13    
HELIX   21 H7C GLN C  196  LYS C  205  1                                  10    
HELIX   22 H8C ILE C  215  ALA C  220  1                                   6    
HELIX   23 H9C ALA C  251  ASN C  256  1                                   6    
HELIX   24 H0C THR C  275  LYS C  279  1                                   5    
HELIX   25 HEC TYR C  285  LEU C  304  1                                  20    
HELIX   26 H1D ILE D   25  PHE D   33  1                                   9    
HELIX   27 H2D ASP D   69  TYR D   77  5ENDS TYPE 1                        9    
HELIX   28 H3D HIS D  147  VAL D  150  1                                   4    
SHEET    1 C1A 5 LYS A   7  ILE A   9  0                                        
SHEET    2 C1A 5 PRO A 123  ALA A 127  1                                        
SHEET    3 C1A 5 ALA A 101  HIS A 106  1                                        
SHEET    4 C1A 5 LYS A  42  PHE A  48  1                                        
SHEET    5 C1A 5 ALA A  68  SER A  74  1                                        
SHEET    1 C2A 6 ALA A 208  HIS A 212  0                                        
SHEET    2 C2A 6 ASN A 182  ALA A 188  1                                        
SHEET    3 C2A 6 LEU A 155  VAL A 160  1                                        
SHEET    4 C2A 6 ILE A 224  VAL A 230  1                                        
SHEET    5 C2A 6 LYS A 262  HIS A 265  1                                        
SHEET    6 C2A 6 PRO A 281  ALA A 283  1                                        
SHEET    1 R1B 5 ARG B  41  LEU B  46  0                                        
SHEET    2 R1B 5 ARG B  55  GLU B  62 -1                                        
SHEET    3 R1B 5 ARG B  14  ASP B  19 -1                                        
SHEET    4 R1B 5 THR B  82  ASP B  87 -1                                        
SHEET    5 R1B 5 GLY B  93  PRO B  97 -1                                        
SHEET    1 R2B 4 GLU B 101  ASP B 104  0                                        
SHEET    2 R2B 4 SER B 123  LYS B 129 -1                                        
SHEET    3 R2B 4 ILE B 134  CYS B 138 -1                                        
SHEET    4 R2B 4 LYS B 143  SER B 146 -1                                        
SHEET    1 C1C 5 LYS C   7  ILE C   9  0                                        
SHEET    2 C1C 5 PRO C 123  ALA C 127  1                                        
SHEET    3 C1C 5 ALA C 101  HIS C 106  1                                        
SHEET    4 C1C 5 LYS C  42  PHE C  48  1                                        
SHEET    5 C1C 5 ALA C  68  SER C  74  1                                        
SHEET    1 C2C 6 ALA C 208  HIS C 212  0                                        
SHEET    2 C2C 6 ASN C 182  ALA C 188  1                                        
SHEET    3 C2C 6 LEU C 155  VAL C 160  1                                        
SHEET    4 C2C 6 ILE C 224  VAL C 230  1                                        
SHEET    5 C2C 6 LYS C 262  HIS C 265  1                                        
SHEET    6 C2C 6 PRO C 281  ALA C 283  1                                        
SHEET    1 R1D 5 ARG D  41  LEU D  46  0                                        
SHEET    2 R1D 5 ARG D  55  GLU D  62 -1                                        
SHEET    3 R1D 5 ARG D  14  ASP D  19 -1                                        
SHEET    4 R1D 5 THR D  82  ASP D  87 -1                                        
SHEET    5 R1D 5 GLY D  93  PRO D  97 -1                                        
SHEET    1 R2D 4 GLU D 101  ASP D 104  0                                        
SHEET    2 R2D 4 SER D 123  LYS D 129 -1                                        
SHEET    3 R2D 4 ILE D 134  CYS D 138 -1                                        
SHEET    4 R2D 4 LYS D 143  SER D 146 -1                                        
LINK         SG  CYS B 109                ZN    ZN B 154     1555   1555  2.35  
LINK         SG  CYS B 114                ZN    ZN B 154     1555   1555  2.30  
LINK         SG  CYS B 138                ZN    ZN B 154     1555   1555  2.34  
LINK         SG  CYS B 141                ZN    ZN B 154     1555   1555  2.31  
LINK         SG  CYS D 109                ZN    ZN D 154     1555   1555  2.33  
LINK         SG  CYS D 114                ZN    ZN D 154     1555   1555  2.27  
LINK         SG  CYS D 138                ZN    ZN D 154     1555   1555  2.30  
LINK         SG  CYS D 141                ZN    ZN D 154     1555   1555  2.33  
CISPEP   1 LEU A  267    PRO A  268          0         3.83                     
CISPEP   2 LEU C  267    PRO C  268          0        -2.96                     
SITE     1 ZNB  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 ZND  4 CYS D 109  CYS D 114  CYS D 138  CYS D 141                    
SITE     1 AC1  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 AC2  4 CYS D 109  CYS D 114  CYS D 138  CYS D 141                    
SITE     1 AC3  7 VAL B   9  ALA B  11  ILE B  12  LYS B  60                    
SITE     2 AC3  7 TYR B  89  VAL B  91  LYS B  94                               
SITE     1 AC4 10 GLU D  10  ALA D  11  ILE D  12  ASP D  19                    
SITE     2 AC4 10 THR D  82  ASN D  84  TYR D  89  GLU D  90                    
SITE     3 AC4 10 VAL D  91  LYS D  94                                          
CRYST1  122.130  122.130  142.510  90.00  90.00 120.00 P 3 2 1      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      0.008188  0.004727  0.000000        0.00000                         
SCALE2      0.000000  0.009455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007017        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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