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Database: PDB
Entry: 1EZZ
LinkDB: 1EZZ
Original site: 1EZZ 
HEADER    TRANSFERASE                             12-MAY-00   1EZZ              
TITLE     CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT 
TITLE    2 IN THE T-STATE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: ASPARTATE TRANSCARBAMOYLASE CATALYTIC CHAIN;                
COMPND   5 EC: 2.1.3.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;           
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 SYNONYM: ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN;               
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PEK412, A PLASMID WITH THE PYRBI GENES    
SOURCE   7 INSERTED INTO PUC119;                                                
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  10 ORGANISM_TAXID: 562;                                                 
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PEK412, A PLASMID WITH THE PYRBI GENES    
SOURCE  14 INSERTED INTO PUC119                                                 
KEYWDS    ASPARTATE TRANSCARBAMOYLASE, ASPARTATE CARBAMOYLTRANSFERASE, CIS-     
KEYWDS   2 PROLINE, CIS-AMINO ACID, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIN,B.STEC,E.R.KANTROWITZ                                           
REVDAT   4   07-FEB-24 1EZZ    1       REMARK                                   
REVDAT   3   03-NOV-21 1EZZ    1       REMARK SEQADV LINK                       
REVDAT   2   24-FEB-09 1EZZ    1       VERSN                                    
REVDAT   1   22-NOV-00 1EZZ    0                                                
JRNL        AUTH   L.JIN,B.STEC,E.R.KANTROWITZ                                  
JRNL        TITL   A CIS-PROLINE TO ALANINE MUTANT OF E. COLI ASPARTATE         
JRNL        TITL 2 TRANSCARBAMOYLASE: KINETIC STUDIES AND THREE-DIMENSIONAL     
JRNL        TITL 3 CRYSTAL STRUCTURES.                                          
JRNL        REF    BIOCHEMISTRY                  V.  39  8058 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10891088                                                     
JRNL        DOI    10.1021/BI000418+                                            
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-A        
REMARK   1  TITL 4 RESOLUTION                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  29  7691 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 29421                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2900                            
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            : 7228                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.10                          
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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.860                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.570                           
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 1EZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011075.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 295.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : UCSD MARK III                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS                               
REMARK 200  DATA SCALING SOFTWARE          : SDMS                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34422                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.2960                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.17                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42700                            
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: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME: 24 MG/ML; 1:1 ENZYME TO-BUFFER   
REMARK 280  RATIO, BUFFER: 20 MM HEPES, 14% (W/V) PEG 1450, PH 7.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
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   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        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  1.000000  0.000000  0.000000       64.93500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.49024            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       66.11333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       64.93500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       37.49024            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.11333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       64.93500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       37.49024            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.11333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       74.98048            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      132.22667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       74.98048            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      132.22667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       74.98048            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      132.22667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DODECAMER. THE ENTIRE MOLECULE  
REMARK 300 REQUIRES TWO SYMMETRY PARTNERS GENERATED BY ROTATIONS AROUND THE     
REMARK 300 THREE-FOLD                                                           
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 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        0.00000            
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        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 338  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  60   CD    GLU A  60   OE2     0.069                       
REMARK 500    GLU A 147   CD    GLU A 147   OE2     0.079                       
REMARK 500    GLU C 147   CD    GLU C 147   OE2     0.072                       
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    PRO A   3   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO A  34   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ASP B   4   N   -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    PRO B  79   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LEU C 225   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    PRO C 281   C   -  N   -  CA  ANGL. DEV. =   9.1 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    ILE A  10      -67.11   -127.99                                   
REMARK 500    ALA A  32      -71.45    -79.56                                   
REMARK 500    LEU A  39       51.00   -109.95                                   
REMARK 500    HIS A  41       -7.59     76.59                                   
REMARK 500    SER A  52       54.73   -164.18                                   
REMARK 500    THR A  53      -68.24    -16.66                                   
REMARK 500    ARG A  56      -72.83    -82.66                                   
REMARK 500    LEU A  57      -55.15    -28.32                                   
REMARK 500    LEU A  66       25.02    -64.70                                   
REMARK 500    ASP A  75     -178.96     65.58                                   
REMARK 500    SER A  76      108.70   -176.32                                   
REMARK 500    ALA A  77       84.50   -162.13                                   
REMARK 500    THR A  79      -90.18   -155.26                                   
REMARK 500    SER A  80     -144.85   -115.10                                   
REMARK 500    ASN A 132      -88.25    -68.73                                   
REMARK 500    HIS A 134       78.14   -173.88                                   
REMARK 500    MET A 194      125.99    -30.86                                   
REMARK 500    GLN A 196      -69.45    -14.45                                   
REMARK 500    TYR A 197      -38.49    -39.14                                   
REMARK 500    ILE A 215      -49.22    -18.96                                   
REMARK 500    GLU A 216      -43.89    -29.50                                   
REMARK 500    LYS A 232      -18.65    -44.53                                   
REMARK 500    LYS A 244       81.22    -62.35                                   
REMARK 500    ALA A 245      -30.39   -151.02                                   
REMARK 500    PHE A 247       39.33    -83.57                                   
REMARK 500    VAL A 248     -152.59   -120.93                                   
REMARK 500    LEU A 249       89.41   -173.19                                   
REMARK 500    HIS A 255      -72.47     -2.04                                   
REMARK 500    ALA A 257      131.85    -29.30                                   
REMARK 500    LEU A 267      165.17     72.92                                   
REMARK 500    THR B   2       51.05     22.38                                   
REMARK 500    HIS B   3     -111.92   -106.56                                   
REMARK 500    LYS B   6     -149.55   -147.55                                   
REMARK 500    LEU B   7       82.56    174.23                                   
REMARK 500    GLN B   8      -80.70   -131.22                                   
REMARK 500    VAL B   9      113.55    -10.75                                   
REMARK 500    LYS B  13     -157.30    179.06                                   
REMARK 500    HIS B  20       90.12     95.85                                   
REMARK 500    LEU B  30      -28.39    -38.36                                   
REMARK 500    PHE B  33       70.30   -100.03                                   
REMARK 500    LYS B  34       90.82    -14.11                                   
REMARK 500    ASP B  39       49.93   -144.37                                   
REMARK 500    ARG B  41      115.86    -18.86                                   
REMARK 500    ASN B  47       39.27     79.80                                   
REMARK 500    GLU B  52       29.12   -157.40                                   
REMARK 500    MET B  53      -12.67     75.53                                   
REMARK 500    LYS B  56     -144.35   -143.51                                   
REMARK 500    ASN B  63       55.76     74.49                                   
REMARK 500    ALA B  75      -94.94    -24.05                                   
REMARK 500    LEU B  76      -55.13    -22.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     127 RAMACHANDRAN OUTLIERS.                        
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    TYR A 226         0.06    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 313  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 109   SG                                                     
REMARK 620 2 CYS B 114   SG  116.6                                              
REMARK 620 3 CYS B 138   SG  120.8 109.6                                        
REMARK 620 4 CYS B 141   SG  105.6 109.8  90.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 314  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 109   SG                                                     
REMARK 620 2 CYS D 114   SG  127.8                                              
REMARK 620 3 CYS D 138   SG  118.5 107.7                                        
REMARK 620 4 CYS D 141   SG   97.8 104.4  91.3                                  
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 ZN B 313                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 314                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6AT1   RELATED DB: PDB                                   
REMARK 900 6AT1 IS WILD-TYPE STRUCTURE OF ASPARTATE TRANSCARBAMOYLASE T STATE   
REMARK 900 WITH NO MUTATION AT POSITION 268                                     
REMARK 900 RELATED ID: 1D09   RELATED DB: PDB                                   
REMARK 900 1D09 IS WILD-TYPE STRUCTURE OF ASPARTATE TRANSCARBAMOYLASE R STATE   
REMARK 900 WITH NO MUTATION AT POSITION 268 IN THE PRESENCE OF N-               
REMARK 900 PHOSPHONACETYL-L-ASPARTATE                                           
REMARK 900 RELATED ID: 1F1B   RELATED DB: PDB                                   
REMARK 900 1F1B IS ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE R-STATE IN   
REMARK 900 THE PRESENCE OF N-PHOSPHONACETYL-L-ASPARTATE                         
DBREF  1EZZ A    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  1EZZ C    1   310  UNP    P0A786   PYRB_ECOLI       1    310             
DBREF  1EZZ B    1   153  UNP    P0A7F3   PYRI_ECOLI       1    153             
DBREF  1EZZ D    1   153  UNP    P0A7F3   PYRI_ECOLI       1    153             
SEQADV 1EZZ ALA A  268  UNP  P0A786    PRO   268 ENGINEERED MUTATION            
SEQADV 1EZZ ALA C  268  UNP  P0A786    PRO   268 ENGINEERED MUTATION            
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 ALA 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 ALA 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 313       1                                                       
HET     ZN  D 314       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *247(H2 O)                                                    
HELIX    1   1 SER A   16  ASN A   33  1                                  18    
HELIX    2   2 SER A   52  LEU A   66  1                                  15    
HELIX    3   3 THR A   87  VAL A   99  1                                  13    
HELIX    4   4 GLY A  110  GLU A  117  1                                   8    
HELIX    5   5 HIS A  134  GLY A  150  1                                  17    
HELIX    6   6 GLY A  166  ALA A  177  1                                  12    
HELIX    7   7 GLN A  196  GLU A  204  1                                   9    
HELIX    8   8 SER A  214  VAL A  218  5                                   5    
HELIX    9   9 SER A  238  LYS A  244  1                                   7    
HELIX   10  10 ARG A  250  HIS A  255  1                                   6    
HELIX   11  11 ALA A  274  LYS A  279  1                                   6    
HELIX   12  12 TRP A  284  ASN A  305  1                                  22    
HELIX   13  13 ILE B   25  PHE B   33  1                                   9    
HELIX   14  14 SER B   67  GLN B   73  1                                   7    
HELIX   15  15 ILE B  115  GLU B  119  5                                   5    
HELIX   16  16 HIS B  147  LEU B  151  1                                   5    
HELIX   17  17 SER C   16  LYS C   31  1                                  16    
HELIX   18  18 SER C   52  LEU C   66  1                                  15    
HELIX   19  19 THR C   79  LYS C   83  5                                   5    
HELIX   20  20 THR C   87  VAL C   99  1                                  13    
HELIX   21  21 GLY C  110  GLU C  117  1                                   8    
HELIX   22  22 HIS C  134  GLY C  150  1                                  17    
HELIX   23  23 GLY C  166  ALA C  177  1                                  12    
HELIX   24  24 PRO C  195  LYS C  205  1                                  11    
HELIX   25  25 SER C  214  MET C  219  1                                   6    
HELIX   26  26 GLN C  231  LEU C  235  5                                   5    
HELIX   27  27 ASP C  236  VAL C  243  1                                   8    
HELIX   28  28 ARG C  250  ALA C  257  5                                   8    
HELIX   29  29 ALA C  274  LYS C  279  5                                   6    
HELIX   30  30 TRP C  284  ASN C  305  1                                  22    
HELIX   31  31 ILE D   25  PHE D   33  1                                   9    
HELIX   32  32 SER D   67  LEU D   74  1                                   8    
HELIX   33  33 HIS D  147  LEU D  151  1                                   5    
SHEET    1   A 4 SER A  69  SER A  74  0                                        
SHEET    2   A 4 VAL A  43  PHE A  48  1  N  ILE A  44   O  SER A  69           
SHEET    3   A 4 ALA A 101  HIS A 106  1  O  ALA A 101   N  ALA A  45           
SHEET    4   A 4 VAL A 124  ASP A 129  1  N  LEU A 125   O  ILE A 102           
SHEET    1   B 5 ALA A 208  HIS A 212  0                                        
SHEET    2   B 5 ASN A 182  ILE A 187  1  O  ASN A 182   N  ALA A 208           
SHEET    3   B 5 LEU A 155  VAL A 160  1  O  LEU A 155   N  ARG A 183           
SHEET    4   B 5 ILE A 224  MET A 227  1  N  ILE A 224   O  HIS A 156           
SHEET    5   B 5 VAL A 263  LEU A 264  1  O  LEU A 264   N  MET A 227           
SHEET    1   C10 GLU D  90  VAL D  92  0                                        
SHEET    2   C10 VAL D  83  ASP D  87 -1  O  ARG D  85   N  VAL D  92           
SHEET    3   C10 GLY D  15  ILE D  18 -1  O  GLY D  15   N  ILE D  86           
SHEET    4   C10 MET D  53  ILE D  61 -1  O  ILE D  59   N  ILE D  18           
SHEET    5   C10 ILE D  42  SER D  50 -1  N  THR D  43   O  LYS D  60           
SHEET    6   C10 ILE B  42  LEU B  46 -1  O  ILE B  42   N  LEU D  46           
SHEET    7   C10 ARG B  55  ILE B  61 -1  O  LEU B  58   N  GLY B  45           
SHEET    8   C10 VAL B  17  ILE B  21 -1  N  ILE B  18   O  ILE B  59           
SHEET    9   C10 VAL B  83  ASP B  87 -1  N  ASN B  84   O  VAL B  17           
SHEET   10   C10 GLU B  90  SER B  95 -1  O  GLU B  90   N  ASP B  87           
SHEET    1   D 8 GLU D  90  VAL D  92  0                                        
SHEET    2   D 8 VAL D  83  ASP D  87 -1  O  ARG D  85   N  VAL D  92           
SHEET    3   D 8 GLY D  15  ILE D  18 -1  O  GLY D  15   N  ILE D  86           
SHEET    4   D 8 MET D  53  ILE D  61 -1  O  ILE D  59   N  ILE D  18           
SHEET    5   D 8 ILE D  42  SER D  50 -1  N  THR D  43   O  LYS D  60           
SHEET    6   D 8 ILE B  42  LEU B  46 -1  O  ILE B  42   N  LEU D  46           
SHEET    7   D 8 ARG B  55  ILE B  61 -1  O  LEU B  58   N  GLY B  45           
SHEET    8   D 8 LEU B  48  PRO B  49 -1  O  LEU B  48   N  LYS B  56           
SHEET    1   E 3 ARG B 128  ARG B 130  0                                        
SHEET    2   E 3 ASP B 133  LYS B 137 -1  O  ASP B 133   N  ARG B 130           
SHEET    3   E 3 GLU B 144  SER B 146 -1  N  PHE B 145   O  LEU B 136           
SHEET    1   F 2 LYS C  42  ILE C  44  0                                        
SHEET    2   F 2 ALA C  68  VAL C  70  1  O  SER C  69   N  ILE C  44           
SHEET    1   G 3 CYS C  47  PHE C  48  0                                        
SHEET    2   G 3 ILE C 102  HIS C 106  1  O  VAL C 103   N  CYS C  47           
SHEET    3   G 3 VAL C 124  ASP C 129  1  N  LEU C 125   O  ILE C 102           
SHEET    1   H 5 TRP C 209  HIS C 212  0                                        
SHEET    2   H 5 ARG C 183  ILE C 187  1  O  PHE C 184   N  SER C 210           
SHEET    3   H 5 HIS C 156  VAL C 160  1  N  VAL C 157   O  ARG C 183           
SHEET    4   H 5 ILE C 224  MET C 227  1  O  ILE C 224   N  ALA C 158           
SHEET    5   H 5 LYS C 262  LEU C 264  1  O  LYS C 262   N  LEU C 225           
SHEET    1   I 2 ALA D 135  LYS D 137  0                                        
SHEET    2   I 2 GLU D 144  SER D 146 -1  O  PHE D 145   N  LEU D 136           
LINK         SG  CYS B 109                ZN    ZN B 313     1555   1555  2.33  
LINK         SG  CYS B 114                ZN    ZN B 313     1555   1555  2.31  
LINK         SG  CYS B 138                ZN    ZN B 313     1555   1555  2.36  
LINK         SG  CYS B 141                ZN    ZN B 313     1555   1555  2.36  
LINK         SG  CYS D 109                ZN    ZN D 314     1555   1555  2.35  
LINK         SG  CYS D 114                ZN    ZN D 314     1555   1555  2.29  
LINK         SG  CYS D 138                ZN    ZN D 314     1555   1555  2.35  
LINK         SG  CYS D 141                ZN    ZN D 314     1555   1555  2.26  
CISPEP   1 LEU A  267    ALA A  268          0        -1.43                     
CISPEP   2 LEU C  267    ALA C  268          0        -0.28                     
SITE     1 AC1  4 CYS B 109  CYS B 114  CYS B 138  CYS B 141                    
SITE     1 AC2  5 CYS D 109  CYS D 114  SER D 116  CYS D 138                    
SITE     2 AC2  5 CYS D 141                                                     
CRYST1  129.870  129.870  198.340  90.00  90.00 120.00 H 3          18          
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      0.007700  0.004445  0.000000        0.00000                         
SCALE2      0.000000  0.008891  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005042        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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