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Database: PDB
Entry: 4CZ1
LinkDB: 4CZ1
Original site: 4CZ1 
HEADER    HYDROLASE                               16-APR-14   4CZ1              
TITLE     CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BACILLUS ANTHRACIS   
TITLE    2 COMPLEXED WITH 2-AMINOACETOPHENONE.                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE FORMAMIDASE;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: KFA, KFASE, ARYLFORMAMIDASE, N-FORMYLKYNURENINE FORMAMIDASE,
COMPND   5 FKF;                                                                 
COMPND   6 EC: 3.5.1.9;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. AMES;                   
SOURCE   3 ORGANISM_TAXID: 198094;                                              
SOURCE   4 GENE: KYNB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    HYDROLASE, TRYPTOPHAN DEGRADATION PATHWAY VIA ANTHRANILATE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DIAZ-SAEZ,V.SRIKANNATHASAN,M.ZOLTNER,W.N.HUNTER                     
REVDAT   5   20-DEC-23 4CZ1    1       REMARK LINK                              
REVDAT   4   06-MAR-19 4CZ1    1       REMARK                                   
REVDAT   3   03-SEP-14 4CZ1    1       JRNL                                     
REVDAT   2   02-JUL-14 4CZ1    1       JRNL   REMARK HETATM CONECT              
REVDAT   2 2                   1       MASTER                                   
REVDAT   1   30-APR-14 4CZ1    0                                                
SPRSDE     30-APR-14 4CZ1      4COA                                             
JRNL        AUTH   L.DIAZ-SAEZ,V.SRIKANNATHASAN,M.ZOLTNER,W.N.HUNTER            
JRNL        TITL   STRUCTURE OF BACTERIAL KYNURENINE FORMAMIDASE REVEALS A      
JRNL        TITL 2 CROWDED BINUCLEAR-ZINC CATALYTIC SITE PRIMED TO GENERATE A   
JRNL        TITL 3 POTENT NUCLEOPHILE.                                          
JRNL        REF    BIOCHEM.J.                    V. 462   581 2014              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   24942958                                                     
JRNL        DOI    10.1042/BJ20140511                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1916                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2226                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6467                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 412                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.17000                                              
REMARK   3    B22 (A**2) : 5.74000                                              
REMARK   3    B33 (A**2) : -12.91000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 6.27000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.048         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.232         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6677 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6443 ; 0.009 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9098 ; 1.684 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14909 ; 1.343 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   821 ; 6.727 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   300 ;35.668 ;24.933       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1134 ;14.365 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;12.657 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1049 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7431 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1405 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1618 ; 0.238 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6205 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3221 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3373 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   163 ; 0.163 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     6 ; 0.132 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.205 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    45 ; 0.312 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    73 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.509 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     1 ; 0.145 ; 0.200       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3296 ; 2.008 ; 1.914       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3295 ; 2.006 ; 1.914       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4113 ; 3.090 ; 2.863       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3381 ; 2.495 ; 2.189       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4985 ; 3.963 ; 3.164       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     4    208       B     4    208   12607  0.07  0.05     
REMARK   3    2     A     4    208       C     4    208   12801  0.05  0.05     
REMARK   3    3     A     4    208       D     4    208   12447  0.09  0.05     
REMARK   3    4     B     4    209       C     4    209   12757  0.07  0.05     
REMARK   3    5     B     4    209       D     4    209   12810  0.06  0.05     
REMARK   3    6     C     4    209       D     4    209   12562  0.09  0.05     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.842                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.158                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4CZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060359.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38046                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4CO9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL PH 8.5, 140 MM MGCL2     
REMARK 280  AND 30 % (W/V) PEG 4000. 293 K. PROTEIN WAS PREVIOUSLY INCUBATED    
REMARK 280  WITH 5 % (V/V) 2-AMINOACETOPHENONE.                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.28050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.7 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.1 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D  2002     O    HOH D  2005              2.09            
REMARK 500   OD2  ASP A   130     O    HOH A  2078              2.14            
REMARK 500   O    GLU D   102     O    HOH D  2052              2.15            
REMARK 500   OE2  GLU A   105     O    HOH A  2083              2.15            
REMARK 500   OD1  ASP C    72     O    HOH C  2068              2.17            
REMARK 500   O    LYS D   138     O    HOH D  2063              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2034     O    HOH D  2024     2656     2.04            
REMARK 500   ND2  ASN B    87     O    LYS C   166     1665     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP B  20   CB    TRP B  20   CG     -0.109                       
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    SER A   4       69.83     65.16                                   
REMARK 500    SER A  39      -44.26   -152.62                                   
REMARK 500    HIS A  50       51.14    -94.65                                   
REMARK 500    HIS A 114      -83.48   -135.91                                   
REMARK 500    ASP A 146       30.47    -91.20                                   
REMARK 500    ALA A 189       70.10   -155.67                                   
REMARK 500    SER B  39      -43.44   -153.71                                   
REMARK 500    HIS B  50       46.08    -92.51                                   
REMARK 500    HIS B 114      -85.61   -135.31                                   
REMARK 500    ALA B 189       69.37   -159.22                                   
REMARK 500    SER C  39      -44.59   -152.13                                   
REMARK 500    HIS C  50       55.82    -97.46                                   
REMARK 500    HIS C 114      -82.94   -134.63                                   
REMARK 500    ASP C 146       33.39    -90.78                                   
REMARK 500    ALA C 189       70.05   -158.51                                   
REMARK 500    SER D  39      -44.99   -154.92                                   
REMARK 500    HIS D  50       49.90    -91.51                                   
REMARK 500    HIS D 114      -84.63   -135.68                                   
REMARK 500    ASP D 146       33.64    -94.19                                   
REMARK 500    ALA D 189       67.29   -158.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2045        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH A2133        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH B2066        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B2067        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B2068        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH B2069        DISTANCE =  7.50 ANGSTROMS                       
REMARK 525    HOH C2015        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH C2116        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH C2117        DISTANCE =  9.70 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 ZINC ION (ZN): ZN2+ BINDING ACTIVE SITE RESIDUES                     
REMARK 600 2-AMINOACETOPHENONE (2AT): PLACE AT THE ACTIVE SITE                  
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 A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  50   ND1                                                    
REMARK 620 2 HIS A  54   NE2  95.0                                              
REMARK 620 3 ASP A  56   OD1 100.0 106.8                                        
REMARK 620 4 GLU A 173   OE1 171.2  77.4  86.5                                  
REMARK 620 5 HOH A2027   O   105.1  75.5 154.6  69.0                            
REMARK 620 6 HOH A2046   O    95.3 143.6 105.6  88.4  68.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD2                                                    
REMARK 620 2 HIS A 161   NE2  88.5                                              
REMARK 620 3 GLU A 173   OE2 107.0 101.2                                        
REMARK 620 4 GLU A 173   OE1  95.0 154.5  53.7                                  
REMARK 620 5 HOH A2046   O   107.8 113.6 130.7  89.3                            
REMARK 620 6 HOH A2103   O   167.0  78.6  75.2  96.4  78.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1210  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD1                                                    
REMARK 620 2 HOH A2054   O    89.3                                              
REMARK 620 3 HOH A2055   O    85.8 172.9                                        
REMARK 620 4 HOH A2132   O   104.4  75.1 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  50   ND1                                                    
REMARK 620 2 HIS B  54   NE2  95.2                                              
REMARK 620 3 ASP B  56   OD1  87.5 105.3                                        
REMARK 620 4 GLU B 173   OE1 176.8  83.4  90.1                                  
REMARK 620 5 HOH B2016   O   108.1  80.3 163.1  74.5                            
REMARK 620 6 HOH B2022   O    85.3 167.4  87.3  96.7  87.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  56   OD2                                                    
REMARK 620 2 HIS B 161   NE2  87.2                                              
REMARK 620 3 GLU B 173   OE1  95.9 161.5                                        
REMARK 620 4 GLU B 173   OE2 111.0 107.1  54.8                                  
REMARK 620 5 HOH B2022   O    87.0 108.3  90.0 140.8                            
REMARK 620 6 HOH B2053   O   164.5 101.9  79.4  78.5  78.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1210  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C  38   O                                                      
REMARK 620 2 HOH C2049   O    97.8                                              
REMARK 620 3 HOH C2050   O    83.3 119.7                                        
REMARK 620 4 HOH C2051   O    73.1 161.0  76.6                                  
REMARK 620 5 HOH C2052   O    87.4  87.6 152.1  75.5                            
REMARK 620 6 HOH C2115   O   153.9 107.8  79.8  83.7  98.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  50   ND1                                                    
REMARK 620 2 HIS C  54   NE2  97.4                                              
REMARK 620 3 ASP C  56   OD1  95.2 108.9                                        
REMARK 620 4 GLU C 173   OE1 176.2  79.6  87.9                                  
REMARK 620 5 HOH C2024   O   111.3  75.2 152.6  65.8                            
REMARK 620 6 HOH C2055   O    93.0 147.4 100.8  88.4  72.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  56   OD2                                                    
REMARK 620 2 HIS C 161   NE2  85.5                                              
REMARK 620 3 GLU C 173   OE2 109.6 103.9                                        
REMARK 620 4 GLU C 173   OE1  96.9 161.1  57.5                                  
REMARK 620 5 HOH C2055   O    97.7 119.1 130.4  79.2                            
REMARK 620 6 HOH C2092   O   161.7 101.0  85.6  82.4  64.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  50   ND1                                                    
REMARK 620 2 HIS D  54   NE2  93.5                                              
REMARK 620 3 ASP D  56   OD1  90.8 102.0                                        
REMARK 620 4 GLU D 173   OE1 172.7  79.3  90.8                                  
REMARK 620 5 HOH D2022   O   107.6  74.9 161.3  70.5                            
REMARK 620 6 HOH D2033   O    94.2 148.5 108.4  92.0  73.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  56   OD2                                                    
REMARK 620 2 HIS D 161   NE2  87.7                                              
REMARK 620 3 GLU D 173   OE2 110.2 105.6                                        
REMARK 620 4 GLU D 173   OE1  95.5 159.9  54.6                                  
REMARK 620 5 HOH D2033   O   102.4 115.3 127.9  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1210  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE D 209   O                                                      
REMARK 620 2 HOH D2090   O    98.9                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VNJ A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1210                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CO9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BACILLUS ANTHRACIS  
REMARK 900 RELATED ID: 4COB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE KYNURENINE FORMAMIDASE FROM PSEUDOMONAS AERUGINOSA 
REMARK 900 RELATED ID: 4COG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BURKHOLDERIA        
REMARK 900 CENOCEPACIA                                                          
DBREF  4CZ1 A    1   209  UNP    Q81PP9   KYNB_BACAN       1    209             
DBREF  4CZ1 B    1   209  UNP    Q81PP9   KYNB_BACAN       1    209             
DBREF  4CZ1 C    1   209  UNP    Q81PP9   KYNB_BACAN       1    209             
DBREF  4CZ1 D    1   209  UNP    Q81PP9   KYNB_BACAN       1    209             
SEQRES   1 A  209  MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU          
SEQRES   2 A  209  ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE          
SEQRES   3 A  209  SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER          
SEQRES   4 A  209  VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY          
SEQRES   5 A  209  THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY          
SEQRES   6 A  209  LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY          
SEQRES   7 A  209  PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE          
SEQRES   8 A  209  GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL          
SEQRES   9 A  209  GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA          
SEQRES  10 A  209  ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP          
SEQRES  11 A  209  ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE          
SEQRES  12 A  209  GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS          
SEQRES  13 A  209  GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE          
SEQRES  14 A  209  HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP          
SEQRES  15 A  209  GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER          
SEQRES  16 A  209  ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO          
SEQRES  17 A  209  ILE                                                          
SEQRES   1 B  209  MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU          
SEQRES   2 B  209  ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE          
SEQRES   3 B  209  SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER          
SEQRES   4 B  209  VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY          
SEQRES   5 B  209  THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY          
SEQRES   6 B  209  LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY          
SEQRES   7 B  209  PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE          
SEQRES   8 B  209  GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL          
SEQRES   9 B  209  GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA          
SEQRES  10 B  209  ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP          
SEQRES  11 B  209  ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE          
SEQRES  12 B  209  GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS          
SEQRES  13 B  209  GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE          
SEQRES  14 B  209  HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP          
SEQRES  15 B  209  GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER          
SEQRES  16 B  209  ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO          
SEQRES  17 B  209  ILE                                                          
SEQRES   1 C  209  MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU          
SEQRES   2 C  209  ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE          
SEQRES   3 C  209  SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER          
SEQRES   4 C  209  VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY          
SEQRES   5 C  209  THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY          
SEQRES   6 C  209  LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY          
SEQRES   7 C  209  PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE          
SEQRES   8 C  209  GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL          
SEQRES   9 C  209  GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA          
SEQRES  10 C  209  ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP          
SEQRES  11 C  209  ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE          
SEQRES  12 C  209  GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS          
SEQRES  13 C  209  GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE          
SEQRES  14 C  209  HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP          
SEQRES  15 C  209  GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER          
SEQRES  16 C  209  ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO          
SEQRES  17 C  209  ILE                                                          
SEQRES   1 D  209  MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU          
SEQRES   2 D  209  ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE          
SEQRES   3 D  209  SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER          
SEQRES   4 D  209  VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY          
SEQRES   5 D  209  THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY          
SEQRES   6 D  209  LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY          
SEQRES   7 D  209  PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE          
SEQRES   8 D  209  GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL          
SEQRES   9 D  209  GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA          
SEQRES  10 D  209  ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP          
SEQRES  11 D  209  ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE          
SEQRES  12 D  209  GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS          
SEQRES  13 D  209  GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE          
SEQRES  14 D  209  HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP          
SEQRES  15 D  209  GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER          
SEQRES  16 D  209  ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO          
SEQRES  17 D  209  ILE                                                          
HET     ZN  A 401       1                                                       
HET     ZN  A 402       1                                                       
HET    VNJ  A 501      10                                                       
HET     MG  A1210       1                                                       
HET     ZN  B 401       1                                                       
HET     ZN  B 402       1                                                       
HET     ZN  C 401       1                                                       
HET     ZN  C 402       1                                                       
HET     MG  C1210       1                                                       
HET     ZN  D 401       1                                                       
HET     ZN  D 402       1                                                       
HET     MG  D1210       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     VNJ 2-AMINOACETOPHENONE                                              
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   7  VNJ    C8 H9 N O                                                    
FORMUL   8   MG    3(MG 2+)                                                     
FORMUL  17  HOH   *412(H2 O)                                                    
HELIX    1   1 SER A   33  GLY A   38  1                                   6    
HELIX    2   2 PRO A   58  PHE A   61  5                                   4    
HELIX    3   3 LYS A   67  LEU A   71  5                                   5    
HELIX    4   4 ASP A   72  VAL A   75  5                                   4    
HELIX    5   5 GLY A   92  GLU A   97  1                                   6    
HELIX    6   6 ASP A  130  LYS A  138  1                                   9    
HELIX    7   7 LEU A  158  HIS A  167  1                                  10    
HELIX    8   8 SER B   33  GLY B   38  1                                   6    
HELIX    9   9 PRO B   58  PHE B   61  5                                   4    
HELIX   10  10 LYS B   67  LEU B   71  5                                   5    
HELIX   11  11 ASP B   72  VAL B   75  5                                   4    
HELIX   12  12 GLY B   92  GLU B   97  1                                   6    
HELIX   13  13 ASP B  130  GLY B  139  1                                  10    
HELIX   14  14 LEU B  158  HIS B  167  1                                  10    
HELIX   15  15 SER C   33  GLY C   38  1                                   6    
HELIX   16  16 PRO C   58  PHE C   61  5                                   4    
HELIX   17  17 LYS C   67  LEU C   71  5                                   5    
HELIX   18  18 ASP C   72  VAL C   75  5                                   4    
HELIX   19  19 GLY C   92  GLU C   97  1                                   6    
HELIX   20  20 ASP C  130  GLY C  139  1                                  10    
HELIX   21  21 LEU C  158  HIS C  167  1                                  10    
HELIX   22  22 SER D   33  GLY D   38  1                                   6    
HELIX   23  23 PRO D   58  PHE D   61  5                                   4    
HELIX   24  24 LYS D   67  LEU D   71  5                                   5    
HELIX   25  25 ASP D   72  VAL D   75  5                                   4    
HELIX   26  26 GLY D   92  GLU D   97  1                                   6    
HELIX   27  27 ASP D  130  GLY D  139  1                                  10    
HELIX   28  28 LEU D  158  HIS D  167  1                                  10    
SHEET    1  AA 9 ILE A   7  ASP A   8  0                                        
SHEET    2  AA 9 VAL A 205  PRO A 208 -1  O  ILE A 206   N  ILE A   7           
SHEET    3  AA 9 GLY A 183  ILE A 188 -1  O  GLU A 186   N  ARG A 207           
SHEET    4  AA 9 VAL A  77  ASP A  84 -1  O  GLY A  78   N  LEU A 187           
SHEET    5  AA 9 ARG A 106  ARG A 110  1  O  ARG A 106   N  ARG A  81           
SHEET    6  AA 9 LEU A 142  VAL A 145  1  O  LEU A 142   N  LEU A 107           
SHEET    7  AA 9 HIS A 170  GLU A 173  1  O  HIS A 170   N  ILE A 143           
SHEET    8  AA 9 HIS A  54  ASP A  56 -1  O  HIS A  54   N  GLU A 173           
SHEET    9  AA 9 GLY A 199  PRO A 201 -1  O  SER A 200   N  ILE A  55           
SHEET    1  AB 4 SER A  27  TRP A  32  0                                        
SHEET    2  AB 4 VAL A  42  SER A  48 -1  O  VAL A  42   N  LEU A  31           
SHEET    3  AB 4 VAL B  42  MET B  47 -1  O  LEU B  45   N  MET A  47           
SHEET    4  AB 4 SER B  27  TRP B  32 -1  O  SER B  27   N  THR B  46           
SHEET    1  AC 2 SER A  90  ILE A  91  0                                        
SHEET    2  AC 2 HIS A 126  LEU A 127  1  O  HIS A 126   N  ILE A  91           
SHEET    1  BA 9 ILE B   7  ASP B   8  0                                        
SHEET    2  BA 9 VAL B 205  PRO B 208 -1  O  ILE B 206   N  ILE B   7           
SHEET    3  BA 9 GLY B 183  ILE B 188 -1  O  GLU B 186   N  ARG B 207           
SHEET    4  BA 9 VAL B  77  ASP B  84 -1  O  GLY B  78   N  LEU B 187           
SHEET    5  BA 9 ARG B 106  ARG B 110  1  O  ARG B 106   N  ARG B  81           
SHEET    6  BA 9 LEU B 142  VAL B 145  1  O  LEU B 142   N  LEU B 107           
SHEET    7  BA 9 HIS B 170  GLU B 173  1  O  HIS B 170   N  ILE B 143           
SHEET    8  BA 9 HIS B  54  ASP B  56 -1  O  HIS B  54   N  GLU B 173           
SHEET    9  BA 9 GLY B 199  PRO B 201 -1  O  SER B 200   N  ILE B  55           
SHEET    1  BB 2 SER B  90  ILE B  91  0                                        
SHEET    2  BB 2 HIS B 126  LEU B 127  1  O  HIS B 126   N  ILE B  91           
SHEET    1  CA 9 ILE C   7  ASP C   8  0                                        
SHEET    2  CA 9 VAL C 205  PRO C 208 -1  O  ILE C 206   N  ILE C   7           
SHEET    3  CA 9 GLY C 183  ILE C 188 -1  O  GLU C 186   N  ARG C 207           
SHEET    4  CA 9 VAL C  77  ASP C  84 -1  O  GLY C  78   N  LEU C 187           
SHEET    5  CA 9 ARG C 106  ARG C 110  1  O  ARG C 106   N  ARG C  81           
SHEET    6  CA 9 LEU C 142  VAL C 145  1  O  LEU C 142   N  LEU C 107           
SHEET    7  CA 9 HIS C 170  GLU C 173  1  O  HIS C 170   N  ILE C 143           
SHEET    8  CA 9 HIS C  54  ASP C  56 -1  O  HIS C  54   N  GLU C 173           
SHEET    9  CA 9 GLY C 199  PRO C 201 -1  O  SER C 200   N  ILE C  55           
SHEET    1  CB 4 SER C  27  TRP C  32  0                                        
SHEET    2  CB 4 VAL C  42  SER C  48 -1  O  VAL C  42   N  LEU C  31           
SHEET    3  CB 4 VAL D  42  MET D  47 -1  O  LEU D  45   N  MET C  47           
SHEET    4  CB 4 SER D  27  TRP D  32 -1  O  SER D  27   N  THR D  46           
SHEET    1  CC 2 SER C  90  ILE C  91  0                                        
SHEET    2  CC 2 HIS C 126  LEU C 127  1  O  HIS C 126   N  ILE C  91           
SHEET    1  DA 9 ILE D   7  ASP D   8  0                                        
SHEET    2  DA 9 VAL D 205  PRO D 208 -1  O  ILE D 206   N  ILE D   7           
SHEET    3  DA 9 GLY D 183  ILE D 188 -1  O  GLU D 186   N  ARG D 207           
SHEET    4  DA 9 VAL D  77  ASP D  84 -1  O  GLY D  78   N  LEU D 187           
SHEET    5  DA 9 ARG D 106  ARG D 110  1  O  ARG D 106   N  ARG D  81           
SHEET    6  DA 9 LEU D 142  VAL D 145  1  O  LEU D 142   N  LEU D 107           
SHEET    7  DA 9 HIS D 170  GLU D 173  1  O  HIS D 170   N  ILE D 143           
SHEET    8  DA 9 HIS D  54  ASP D  56 -1  O  HIS D  54   N  GLU D 173           
SHEET    9  DA 9 GLY D 199  PRO D 201 -1  O  SER D 200   N  ILE D  55           
SHEET    1  DB 2 SER D  90  ILE D  91  0                                        
SHEET    2  DB 2 HIS D 126  LEU D 127  1  O  HIS D 126   N  ILE D  91           
LINK         ND1 HIS A  50                ZN    ZN A 402     1555   1555  2.26  
LINK         NE2 HIS A  54                ZN    ZN A 402     1555   1555  2.39  
LINK         OD2 ASP A  56                ZN    ZN A 401     1555   1555  2.02  
LINK         OD1 ASP A  56                ZN    ZN A 402     1555   1555  2.17  
LINK         OD1 ASP A  64                MG    MG A1210     1555   1555  2.65  
LINK         NE2 HIS A 161                ZN    ZN A 401     1555   1555  2.24  
LINK         OE2 GLU A 173                ZN    ZN A 401     1555   1555  2.24  
LINK         OE1 GLU A 173                ZN    ZN A 401     1555   1555  2.67  
LINK         OE1 GLU A 173                ZN    ZN A 402     1555   1555  2.49  
LINK        ZN    ZN A 401                 O   HOH A2046     1555   1555  2.25  
LINK        ZN    ZN A 401                 O   HOH A2103     1555   1555  2.17  
LINK        ZN    ZN A 402                 O   HOH A2027     1555   1555  2.32  
LINK        ZN    ZN A 402                 O   HOH A2046     1555   1555  2.48  
LINK        MG    MG A1210                 O   HOH A2054     1555   1555  2.24  
LINK        MG    MG A1210                 O   HOH A2055     1555   1555  2.24  
LINK        MG    MG A1210                 O   HOH A2132     1555   1555  2.06  
LINK         ND1 HIS B  50                ZN    ZN B 402     1555   1555  2.40  
LINK         NE2 HIS B  54                ZN    ZN B 402     1555   1555  2.27  
LINK         OD2 ASP B  56                ZN    ZN B 401     1555   1555  2.08  
LINK         OD1 ASP B  56                ZN    ZN B 402     1555   1555  2.33  
LINK         NE2 HIS B 161                ZN    ZN B 401     1555   1555  2.20  
LINK         OE1 GLU B 173                ZN    ZN B 401     1555   1555  2.61  
LINK         OE2 GLU B 173                ZN    ZN B 401     1555   1555  2.08  
LINK         OE1 GLU B 173                ZN    ZN B 402     1555   1555  2.27  
LINK        ZN    ZN B 401                 O   HOH B2022     1555   1555  2.21  
LINK        ZN    ZN B 401                 O   HOH B2053     1555   1555  2.59  
LINK        ZN    ZN B 402                 O   HOH B2016     1555   1555  2.45  
LINK        ZN    ZN B 402                 O   HOH B2022     1555   1555  2.31  
LINK         O   GLY C  38                MG    MG C1210     1555   1555  2.10  
LINK         ND1 HIS C  50                ZN    ZN C 402     1555   1555  2.24  
LINK         NE2 HIS C  54                ZN    ZN C 402     1555   1555  2.35  
LINK         OD2 ASP C  56                ZN    ZN C 401     1555   1555  2.10  
LINK         OD1 ASP C  56                ZN    ZN C 402     1555   1555  2.24  
LINK         NE2 HIS C 161                ZN    ZN C 401     1555   1555  2.27  
LINK         OE2 GLU C 173                ZN    ZN C 401     1555   1555  2.10  
LINK         OE1 GLU C 173                ZN    ZN C 401     1555   1555  2.57  
LINK         OE1 GLU C 173                ZN    ZN C 402     1555   1555  2.44  
LINK        ZN    ZN C 401                 O   HOH C2055     1555   1555  2.34  
LINK        ZN    ZN C 401                 O   HOH C2092     1555   1555  2.54  
LINK        ZN    ZN C 402                 O   HOH C2024     1555   1555  2.40  
LINK        ZN    ZN C 402                 O   HOH C2055     1555   1555  2.04  
LINK        MG    MG C1210                 O   HOH C2049     1555   1555  2.06  
LINK        MG    MG C1210                 O   HOH C2050     1555   1555  2.21  
LINK        MG    MG C1210                 O   HOH C2051     1555   1555  2.55  
LINK        MG    MG C1210                 O   HOH C2052     1555   1555  2.09  
LINK        MG    MG C1210                 O   HOH C2115     1555   1555  2.31  
LINK         ND1 HIS D  50                ZN    ZN D 402     1555   1555  2.42  
LINK         NE2 HIS D  54                ZN    ZN D 402     1555   1555  2.39  
LINK         OD2 ASP D  56                ZN    ZN D 401     1555   1555  2.08  
LINK         OD1 ASP D  56                ZN    ZN D 402     1555   1555  2.23  
LINK         NE2 HIS D 161                ZN    ZN D 401     1555   1555  2.16  
LINK         OE2 GLU D 173                ZN    ZN D 401     1555   1555  2.15  
LINK         OE1 GLU D 173                ZN    ZN D 401     1555   1555  2.62  
LINK         OE1 GLU D 173                ZN    ZN D 402     1555   1555  2.32  
LINK         O   ILE D 209                MG    MG D1210     1555   1555  2.84  
LINK        ZN    ZN D 401                 O   HOH D2033     1555   1555  2.27  
LINK        ZN    ZN D 402                 O   HOH D2022     1555   1555  2.38  
LINK        ZN    ZN D 402                 O   HOH D2033     1555   1555  2.21  
LINK        MG    MG D1210                 O   HOH D2090     1555   1555  1.79  
SITE     1 AC1  6 ASP A  56  HIS A 161  GLU A 173   ZN A 402                    
SITE     2 AC1  6 HOH A2046  HOH A2103                                          
SITE     1 AC2  7 HIS A  50  HIS A  54  ASP A  56  GLU A 173                    
SITE     2 AC2  7  ZN A 401  HOH A2027  HOH A2046                               
SITE     1 AC3  6 TRP A  20  ASP A  23  HIS A  50  HIS A  60                    
SITE     2 AC3  6 HOH A2046  VAL B  40                                          
SITE     1 AC4  6 ASP B  56  HIS B 161  GLU B 173   ZN B 402                    
SITE     2 AC4  6 HOH B2022  HOH B2053                                          
SITE     1 AC5  7 HIS B  50  HIS B  54  ASP B  56  GLU B 173                    
SITE     2 AC5  7  ZN B 401  HOH B2016  HOH B2022                               
SITE     1 AC6  6 ASP C  56  HIS C 161  GLU C 173   ZN C 402                    
SITE     2 AC6  6 HOH C2055  HOH C2092                                          
SITE     1 AC7  7 HIS C  50  HIS C  54  ASP C  56  GLU C 173                    
SITE     2 AC7  7  ZN C 401  HOH C2024  HOH C2055                               
SITE     1 AC8  5 ASP D  56  HIS D 161  GLU D 173   ZN D 402                    
SITE     2 AC8  5 HOH D2033                                                     
SITE     1 AC9  7 HIS D  50  HIS D  54  ASP D  56  GLU D 173                    
SITE     2 AC9  7  ZN D 401  HOH D2022  HOH D2033                               
SITE     1 BC1  6 GLY C  38  HOH C2049  HOH C2050  HOH C2051                    
SITE     2 BC1  6 HOH C2052  HOH C2115                                          
SITE     1 BC2  4 ASP A  64  HOH A2054  HOH A2055  HOH A2132                    
SITE     1 BC3  3 ILE D 209  HOH D2090  HOH D2091                               
CRYST1   73.695   66.561   84.061  90.00  90.24  90.00 P 1 21 1      8          
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      0.013569  0.000000  0.000057        0.00000                         
SCALE2      0.000000  0.015024  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011896        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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