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Database: PDB
Entry: 4OIW
LinkDB: 4OIW
Original site: 4OIW 
HEADER    HYDROLASE                               20-JAN-14   4OIW              
TITLE     STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE M18      
TITLE    2 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE M18 FAMILY AMINOPEPTIDASE 2;                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 3.4.11.-;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;                
SOURCE   5 GENE: APEB, PA3247, PSEUDOMONAS AERUGINOSA;                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVFT1S                                    
KEYWDS    DODECAMERIC TET STRUCTURE, ASPARTYL AMINOPEPTIDASE, PSEUDOMONAS       
KEYWDS   2 AERUGINOSA, HISTIDINE MUTATION, M18 FAMILY, HYDROLASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.NGUYEN,R.PANDIAN,D.D.KIM,S.C.HA,H.J.YOON,K.S.KIM,K.H.YUN,J.H.KIM, 
AUTHOR   2 K.K.KIM                                                              
REVDAT   4   17-SEP-14 4OIW    1       JRNL                                     
REVDAT   3   23-APR-14 4OIW    1       JRNL                                     
REVDAT   2   09-APR-14 4OIW    1       JRNL                                     
REVDAT   1   02-APR-14 4OIW    0                                                
JRNL        AUTH   D.D.NGUYEN,R.PANDIAN,D.KIM,S.C.HA,H.J.YOON,K.S.KIM,K.H.YUN,  
JRNL        AUTH 2 J.H.KIM,K.K.KIM                                              
JRNL        TITL   STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE 
JRNL        TITL 2 M18 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA               
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 447   101 2014              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   24704201                                                     
JRNL        DOI    10.1016/J.BBRC.2014.03.109                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 95594                          
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) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5026                            
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) : 2.44                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4902                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 266                          
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18936                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 890                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.71000                                             
REMARK   3    B22 (A**2) : 2.53000                                              
REMARK   3    B33 (A**2) : 1.18000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.412         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.225         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.141         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.104         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19320 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 18372 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26232 ; 1.743 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 41964 ; 0.852 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2430 ; 7.387 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   966 ;37.534 ;23.168       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3036 ;15.860 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   198 ;18.817 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2922 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22404 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4698 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 4OIW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL45PX                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.7321                             
REMARK 200  MONOCHROMATOR                  : 0.17   2.3 KEV                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95594                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 4NJR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%(V/V) 2-PROPANOL, 0.1M HEPES 7.5,     
REMARK 280  0.2M MGCL2, 10MM SPERMIDINE, 0.1MM ZNCL2, MICROBATCH                
REMARK 280  CRYSTALLIZATION, TEMPERATURE 295K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.34650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.34650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       75.01000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      109.13350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       75.01000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      109.13350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.34650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       75.01000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      109.13350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       86.34650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       75.01000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      109.13350            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 81350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 151760 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -654.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, B, D, F                      
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       86.34650            
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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     SER A   269                                                      
REMARK 465     CYS A   270                                                      
REMARK 465     SER A   271                                                      
REMARK 465     HIS A   272                                                      
REMARK 465     CYS A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     ASP A   276                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     CYS A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     SER A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     ILE A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     PRO A   380                                                      
REMARK 465     ILE A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     SER B   269                                                      
REMARK 465     CYS B   270                                                      
REMARK 465     SER B   271                                                      
REMARK 465     HIS B   272                                                      
REMARK 465     CYS B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     ALA B   275                                                      
REMARK 465     ASP B   276                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     CYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     THR B   377                                                      
REMARK 465     ILE B   378                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     PRO B   380                                                      
REMARK 465     ILE B   381                                                      
REMARK 465     THR B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     SER B   384                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     SER C   269                                                      
REMARK 465     CYS C   270                                                      
REMARK 465     SER C   271                                                      
REMARK 465     HIS C   272                                                      
REMARK 465     CYS C   273                                                      
REMARK 465     GLY C   274                                                      
REMARK 465     ALA C   275                                                      
REMARK 465     ASP C   276                                                      
REMARK 465     GLY C   373                                                      
REMARK 465     CYS C   374                                                      
REMARK 465     GLY C   375                                                      
REMARK 465     SER C   376                                                      
REMARK 465     THR C   377                                                      
REMARK 465     ILE C   378                                                      
REMARK 465     GLY C   379                                                      
REMARK 465     PRO C   380                                                      
REMARK 465     ILE C   381                                                      
REMARK 465     THR C   382                                                      
REMARK 465     ALA C   383                                                      
REMARK 465     SER C   384                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     GLY D   268                                                      
REMARK 465     SER D   269                                                      
REMARK 465     CYS D   270                                                      
REMARK 465     SER D   271                                                      
REMARK 465     HIS D   272                                                      
REMARK 465     CYS D   273                                                      
REMARK 465     GLY D   274                                                      
REMARK 465     ALA D   275                                                      
REMARK 465     ASP D   276                                                      
REMARK 465     GLY D   373                                                      
REMARK 465     CYS D   374                                                      
REMARK 465     GLY D   375                                                      
REMARK 465     SER D   376                                                      
REMARK 465     THR D   377                                                      
REMARK 465     ILE D   378                                                      
REMARK 465     GLY D   379                                                      
REMARK 465     PRO D   380                                                      
REMARK 465     ILE D   381                                                      
REMARK 465     THR D   382                                                      
REMARK 465     ALA D   383                                                      
REMARK 465     SER D   384                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     SER E     0                                                      
REMARK 465     GLY E   268                                                      
REMARK 465     SER E   269                                                      
REMARK 465     CYS E   270                                                      
REMARK 465     SER E   271                                                      
REMARK 465     HIS E   272                                                      
REMARK 465     CYS E   273                                                      
REMARK 465     GLY E   274                                                      
REMARK 465     ALA E   275                                                      
REMARK 465     ASP E   276                                                      
REMARK 465     GLY E   373                                                      
REMARK 465     CYS E   374                                                      
REMARK 465     GLY E   375                                                      
REMARK 465     SER E   376                                                      
REMARK 465     THR E   377                                                      
REMARK 465     ILE E   378                                                      
REMARK 465     GLY E   379                                                      
REMARK 465     PRO E   380                                                      
REMARK 465     ILE E   381                                                      
REMARK 465     THR E   382                                                      
REMARK 465     ALA E   383                                                      
REMARK 465     SER E   384                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     SER F     0                                                      
REMARK 465     GLY F   268                                                      
REMARK 465     SER F   269                                                      
REMARK 465     CYS F   270                                                      
REMARK 465     SER F   271                                                      
REMARK 465     HIS F   272                                                      
REMARK 465     CYS F   273                                                      
REMARK 465     GLY F   274                                                      
REMARK 465     ALA F   275                                                      
REMARK 465     ASP F   276                                                      
REMARK 465     GLY F   373                                                      
REMARK 465     CYS F   374                                                      
REMARK 465     GLY F   375                                                      
REMARK 465     SER F   376                                                      
REMARK 465     THR F   377                                                      
REMARK 465     ILE F   378                                                      
REMARK 465     GLY F   379                                                      
REMARK 465     PRO F   380                                                      
REMARK 465     ILE F   381                                                      
REMARK 465     THR F   382                                                      
REMARK 465     ALA F   383                                                      
REMARK 465     SER F   384                                                      
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 A   621     O    HOH A   641              1.90            
REMARK 500   OE1  GLU A   265     O    HOH A   621              1.90            
REMARK 500   OE1  GLU F   265     O    HOH F   610              1.97            
REMARK 500   OE1  GLU E   265     O    HOH E   633              1.98            
REMARK 500   OE2  GLU C   265     O    HOH C   625              2.03            
REMARK 500   O    HOH A   664     O    HOH C   633              2.04            
REMARK 500   O    HOH F   610     O    HOH F   636              2.06            
REMARK 500   O    HOH A   752     O    HOH A   753              2.12            
REMARK 500   O    HOH E   633     O    HOH E   634              2.12            
REMARK 500   O    HOH D   617     O    HOH D   694              2.13            
REMARK 500   O    HOH A   601     O    HOH A   643              2.16            
REMARK 500   O    GLU A   290     O    HOH A   625              2.17            
REMARK 500   O    HOH A   660     O    HOH B   768              2.18            
REMARK 500   OE2  GLU C   265     O    HOH C   616              2.18            
REMARK 500   NH2  ARG E    36     O    HOH E   690              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    GLU E 228   CD    GLU E 228   OE1     0.081                       
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    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 198   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLU B   4   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    GLY B 183   N   -  CA  -  C   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ARG B 341   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C 139   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP D 254   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    PRO D 278   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG F  68   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG F  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP F 254   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 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    ASN A  57       18.19     59.96                                   
REMARK 500    ASP A  58       28.23     43.89                                   
REMARK 500    ARG A 144      -51.67     72.22                                   
REMARK 500    LEU A 208      -61.98    -97.60                                   
REMARK 500    ASP A 254       43.76   -144.05                                   
REMARK 500    ASP A 371       30.38    -93.67                                   
REMARK 500    HIS A 401        3.65     84.74                                   
REMARK 500    ARG B   2     -119.54     85.88                                   
REMARK 500    ALA B   3      -15.51   -173.78                                   
REMARK 500    GLU B   4       82.62     92.72                                   
REMARK 500    LEU B   5      -32.36     98.14                                   
REMARK 500    ASP B  58       26.12     49.75                                   
REMARK 500    SER B  59       -8.45   -140.43                                   
REMARK 500    CYS B  87     -169.28   -164.16                                   
REMARK 500    ARG B 144      -48.51     69.34                                   
REMARK 500    ASN B 158       61.15   -162.71                                   
REMARK 500    ALA B 181      158.76    -48.61                                   
REMARK 500    LEU B 208      -64.68    -99.06                                   
REMARK 500    ASP B 254       37.54   -146.84                                   
REMARK 500    GLU B 266       23.81    -77.90                                   
REMARK 500    TYR B 316       44.72   -148.12                                   
REMARK 500    ASN B 339       35.50    -78.47                                   
REMARK 500    HIS B 401       -1.53     87.94                                   
REMARK 500    ASP C  58       21.94     48.98                                   
REMARK 500    CYS C  87     -172.22   -172.60                                   
REMARK 500    SER C 123     -163.74   -119.05                                   
REMARK 500    ARG C 144      -47.78     64.31                                   
REMARK 500    ASN C 158       69.70   -158.91                                   
REMARK 500    ALA C 181     -166.92    -67.79                                   
REMARK 500    TYR C 316       42.51   -147.58                                   
REMARK 500    ASP C 318       -9.91    -59.36                                   
REMARK 500    ASN C 339       34.79    -87.79                                   
REMARK 500    ALA C 399       36.21     71.86                                   
REMARK 500    HIS C 401        4.59     89.12                                   
REMARK 500    ASN D  57       16.99     54.44                                   
REMARK 500    ARG D 144      -55.52     66.34                                   
REMARK 500    ASN D 158       67.83   -152.86                                   
REMARK 500    ASP D 254       48.73   -143.81                                   
REMARK 500    GLU D 290      157.30    -41.65                                   
REMARK 500    TYR D 316       50.94   -144.62                                   
REMARK 500    ASN D 339       38.32    -83.51                                   
REMARK 500    THR D 344      130.15    -32.86                                   
REMARK 500    HIS D 401        2.11     86.40                                   
REMARK 500    GLU E  47      -90.96   -109.70                                   
REMARK 500    THR E  48      122.50    168.05                                   
REMARK 500    ASN E  57       12.71     56.85                                   
REMARK 500    ASN E  93       78.83   -117.35                                   
REMARK 500    SER E 123     -165.06   -126.69                                   
REMARK 500    ARG E 144      -51.50     75.01                                   
REMARK 500    ASN E 158       67.38   -155.20                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A    1     ARG A    2                  131.29                    
REMARK 500 PRO A  182     GLY A  183                  -30.91                    
REMARK 500 PHE A  366     VAL A  367                  147.52                    
REMARK 500 PRO D  182     GLY D  183                  -47.22                    
REMARK 500 PRO E  182     GLY E  183                  -30.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR F  48        22.8      L          L   OUTSIDE RANGE           
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 A 753        DISTANCE =  5.64 ANGSTROMS                       
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 F 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 266   OE2                                                    
REMARK 620 2 ASP F 236   OD2 100.4                                              
REMARK 620 3 HIS F 401   NE2  99.6  87.1                                        
REMARK 620 4 HOH F 637   O   112.0 108.6 140.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 266   OE2                                                    
REMARK 620 2 ASP A 236   OD2 109.8                                              
REMARK 620 3 HOH A 643   O   132.9 109.0                                        
REMARK 620 4 HIS A 401   NE2 123.4  89.4  82.5                                  
REMARK 620 5 HOH A 601   O    93.4  98.3  55.2 137.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 266   OE2                                                    
REMARK 620 2 ASP C 236   OD2 107.9                                              
REMARK 620 3 HIS C 401   NE2 122.5  85.6                                        
REMARK 620 4 HOH C 653   O   116.9 130.7  87.2                                  
REMARK 620 5 HOH C 618   O    88.1  97.1 146.9  66.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 266   OE2                                                    
REMARK 620 2 ASP D 236   OD2 101.9                                              
REMARK 620 3 HOH D 629   O   117.9 139.6                                        
REMARK 620 4 HIS D 401   NE2 107.9  86.6  87.5                                  
REMARK 620 5 HOH D 631   O   123.8  90.6  62.5 127.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 266   OE2                                                    
REMARK 620 2 ASP E 236   OD2  92.8                                              
REMARK 620 3 HIS E 401   NE2 105.5  90.7                                        
REMARK 620 4 HOH E 635   O   108.9  96.2 144.5                                  
REMARK 620 5 HOH E 632   O   105.4 161.3  88.6  74.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 236   OD2                                                    
REMARK 620 2 GLU B 266   OE2 101.2                                              
REMARK 620 3 HIS B 401   NE2  94.6 115.0                                        
REMARK 620 4 HOH B 635   O   139.6 109.4  95.7                                  
REMARK 620 5 HOH B 601   O   100.1  97.3 141.0  51.2                            
REMARK 620 N                    1     2     3     4                             
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 501                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OID   RELATED DB: PDB                                   
REMARK 900 D236A MUTATION FROM ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS          
REMARK 900 AERUGINOSA                                                           
REMARK 900 RELATED ID: 4NJR   RELATED DB: PDB                                   
REMARK 900 ZNZNPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA          
REMARK 900 WITH ZINC IN CATALYTIC SITE                                          
REMARK 900 RELATED ID: 4NJQ   RELATED DB: PDB                                   
REMARK 900 COCOPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA          
REMARK 900 WITH ZINC IN CATALYTIC SITE                                          
DBREF  4OIW A    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4OIW B    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4OIW C    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4OIW D    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4OIW E    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4OIW F    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
SEQADV 4OIW GLY A   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER A    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA A   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQADV 4OIW GLY B   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER B    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA B   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQADV 4OIW GLY C   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER C    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA C   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQADV 4OIW GLY D   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER D    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA D   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQADV 4OIW GLY E   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER E    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA E   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQADV 4OIW GLY F   -1  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW SER F    0  UNP  Q9HYZ3              EXPRESSION TAG                 
SEQADV 4OIW ALA F   82  UNP  Q9HYZ3    HIS    82 ENGINEERED MUTATION            
SEQRES   1 A  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 A  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 A  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 A  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 A  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 A  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 A  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 A  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 A  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 A  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 A  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 A  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 A  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 A  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 A  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 A  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 A  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 A  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 A  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 A  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 A  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 A  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 A  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 A  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 A  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 A  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 A  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 A  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 A  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 A  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 A  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 A  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 A  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 A  431  LEU PRO                                                      
SEQRES   1 B  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 B  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 B  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 B  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 B  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 B  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 B  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 B  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 B  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 B  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 B  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 B  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 B  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 B  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 B  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 B  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 B  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 B  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 B  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 B  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 B  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 B  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 B  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 B  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 B  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 B  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 B  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 B  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 B  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 B  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 B  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 B  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 B  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 B  431  LEU PRO                                                      
SEQRES   1 C  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 C  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 C  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 C  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 C  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 C  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 C  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 C  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 C  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 C  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 C  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 C  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 C  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 C  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 C  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 C  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 C  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 C  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 C  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 C  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 C  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 C  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 C  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 C  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 C  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 C  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 C  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 C  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 C  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 C  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 C  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 C  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 C  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 C  431  LEU PRO                                                      
SEQRES   1 D  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 D  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 D  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 D  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 D  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 D  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 D  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 D  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 D  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 D  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 D  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 D  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 D  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 D  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 D  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 D  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 D  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 D  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 D  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 D  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 D  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 D  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 D  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 D  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 D  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 D  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 D  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 D  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 D  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 D  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 D  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 D  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 D  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 D  431  LEU PRO                                                      
SEQRES   1 E  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 E  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 E  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 E  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 E  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 E  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 E  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 E  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 E  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 E  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 E  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 E  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 E  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 E  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 E  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 E  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 E  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 E  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 E  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 E  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 E  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 E  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 E  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 E  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 E  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 E  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 E  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 E  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 E  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 E  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 E  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 E  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 E  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 E  431  LEU PRO                                                      
SEQRES   1 F  431  GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP          
SEQRES   2 F  431  PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA          
SEQRES   3 F  431  SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG          
SEQRES   4 F  431  LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY          
SEQRES   5 F  431  ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA          
SEQRES   6 F  431  ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE          
SEQRES   7 F  431  ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG          
SEQRES   8 F  431  VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU          
SEQRES   9 F  431  GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA          
SEQRES  10 F  431  PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL          
SEQRES  11 F  431  THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL          
SEQRES  12 F  431  ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA          
SEQRES  13 F  431  ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE          
SEQRES  14 F  431  ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU          
SEQRES  15 F  431  ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP          
SEQRES  16 F  431  GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL          
SEQRES  17 F  431  VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER          
SEQRES  18 F  431  ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY          
SEQRES  19 F  431  ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU          
SEQRES  20 F  431  GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE          
SEQRES  21 F  431  LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER          
SEQRES  22 F  431  HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU          
SEQRES  23 F  431  ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA          
SEQRES  24 F  431  ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS          
SEQRES  25 F  431  GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN          
SEQRES  26 F  431  HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE          
SEQRES  27 F  431  ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA          
SEQRES  28 F  431  GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO          
SEQRES  29 F  431  VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY          
SEQRES  30 F  431  SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL          
SEQRES  31 F  431  ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS          
SEQRES  32 F  431  SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS          
SEQRES  33 F  431  LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU          
SEQRES  34 F  431  LEU PRO                                                      
HET     ZN  A 501       1                                                       
HET     ZN  B 501       1                                                       
HET     ZN  C 501       1                                                       
HET     ZN  D 501       1                                                       
HET     ZN  E 501       1                                                       
HET     ZN  F 501       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL  13  HOH   *890(H2 O)                                                    
HELIX    1   1 ARG A    2  ALA A   15  1                                  14    
HELIX    2   2 THR A   18  ALA A   33  1                                  16    
HELIX    3   3 SER A   70  GLY A   75  1                                   6    
HELIX    4   4 PHE A  114  PHE A  118  5                                   5    
HELIX    5   5 ALA A  154  ASN A  158  5                                   5    
HELIX    6   6 ALA A  160  GLY A  164  5                                   5    
HELIX    7   7 ASN A  168  LEU A  173  1                                   6    
HELIX    8   8 ASP A  187  GLY A  201  1                                  15    
HELIX    9   9 ARG A  234  ALA A  251  1                                  18    
HELIX   10  10 PRO A  278  LEU A  287  1                                  10    
HELIX   11  11 ASP A  292  GLN A  299  1                                   8    
HELIX   12  12 TYR A  316  HIS A  320  5                                   5    
HELIX   13  13 ASN A  345  SER A  359  1                                  15    
HELIX   14  14 HIS A  410  ALA A  424  1                                  15    
HELIX   15  15 ASN B    6  ALA B   15  1                                  10    
HELIX   16  16 THR B   18  ALA B   33  1                                  16    
HELIX   17  17 SER B   70  GLY B   75  1                                   6    
HELIX   18  18 PHE B  114  PHE B  118  5                                   5    
HELIX   19  19 ALA B  154  ASN B  158  5                                   5    
HELIX   20  20 ALA B  160  GLY B  164  5                                   5    
HELIX   21  21 ASN B  168  LEU B  173  1                                   6    
HELIX   22  22 ASP B  187  GLY B  201  1                                  15    
HELIX   23  23 ARG B  234  ALA B  251  1                                  18    
HELIX   24  24 PRO B  278  LEU B  287  1                                  10    
HELIX   25  25 ASP B  292  ARG B  300  1                                   9    
HELIX   26  26 TYR B  316  HIS B  320  5                                   5    
HELIX   27  27 ASN B  345  SER B  359  1                                  15    
HELIX   28  28 HIS B  410  ALA B  424  1                                  15    
HELIX   29  29 ARG C    2  ALA C   15  1                                  14    
HELIX   30  30 THR C   18  ALA C   33  1                                  16    
HELIX   31  31 SER C   70  GLY C   75  1                                   6    
HELIX   32  32 PHE C  114  PHE C  118  5                                   5    
HELIX   33  33 ALA C  154  ASN C  158  5                                   5    
HELIX   34  34 ALA C  160  GLY C  164  5                                   5    
HELIX   35  35 ASN C  168  LEU C  173  1                                   6    
HELIX   36  36 ASP C  187  GLY C  201  1                                  15    
HELIX   37  37 ARG C  234  ALA C  251  1                                  18    
HELIX   38  38 PRO C  278  LEU C  287  1                                  10    
HELIX   39  39 ASP C  292  ARG C  300  1                                   9    
HELIX   40  40 TYR C  316  HIS C  320  5                                   5    
HELIX   41  41 ASN C  345  SER C  359  1                                  15    
HELIX   42  42 HIS C  410  ALA C  424  1                                  15    
HELIX   43  43 ARG D    2  SER D   16  1                                  15    
HELIX   44  44 THR D   18  ALA D   33  1                                  16    
HELIX   45  45 SER D   70  GLY D   75  1                                   6    
HELIX   46  46 PHE D  114  PHE D  118  5                                   5    
HELIX   47  47 ALA D  154  ASN D  158  5                                   5    
HELIX   48  48 ALA D  160  GLY D  164  5                                   5    
HELIX   49  49 ASN D  168  LEU D  173  1                                   6    
HELIX   50  50 ASP D  187  GLY D  201  1                                  15    
HELIX   51  51 ARG D  234  ALA D  251  1                                  18    
HELIX   52  52 PRO D  278  ARG D  286  1                                   9    
HELIX   53  53 ASP D  292  ARG D  300  1                                   9    
HELIX   54  54 TYR D  316  HIS D  320  5                                   5    
HELIX   55  55 ASN D  345  SER D  359  1                                  15    
HELIX   56  56 HIS D  410  ALA D  424  1                                  15    
HELIX   57  57 ARG E    2  SER E   16  1                                  15    
HELIX   58  58 THR E   18  ALA E   33  1                                  16    
HELIX   59  59 SER E   70  GLY E   75  1                                   6    
HELIX   60  60 PHE E  114  PHE E  118  5                                   5    
HELIX   61  61 ALA E  154  ASN E  158  5                                   5    
HELIX   62  62 ALA E  160  GLY E  164  5                                   5    
HELIX   63  63 ASN E  168  LEU E  173  1                                   6    
HELIX   64  64 ASP E  187  GLY E  201  1                                  15    
HELIX   65  65 ARG E  234  ALA E  251  1                                  18    
HELIX   66  66 PRO E  278  ARG E  286  1                                   9    
HELIX   67  67 ASP E  292  GLN E  299  1                                   8    
HELIX   68  68 TYR E  316  HIS E  320  5                                   5    
HELIX   69  69 ASN E  345  GLU E  360  1                                  16    
HELIX   70  70 HIS E  410  ALA E  424  1                                  15    
HELIX   71  71 ARG F    2  SER F   16  1                                  15    
HELIX   72  72 THR F   18  ALA F   33  1                                  16    
HELIX   73  73 SER F   70  GLY F   75  1                                   6    
HELIX   74  74 PHE F  114  PHE F  118  5                                   5    
HELIX   75  75 ALA F  154  ASN F  158  5                                   5    
HELIX   76  76 ALA F  160  GLY F  164  5                                   5    
HELIX   77  77 ASN F  168  LEU F  173  1                                   6    
HELIX   78  78 ASP F  187  GLY F  201  1                                  15    
HELIX   79  79 ARG F  234  ALA F  251  1                                  18    
HELIX   80  80 PRO F  278  ARG F  286  1                                   9    
HELIX   81  81 ASP F  292  GLN F  299  1                                   8    
HELIX   82  82 TYR F  316  HIS F  320  5                                   5    
HELIX   83  83 ASN F  345  SER F  359  1                                  15    
HELIX   84  84 HIS F  410  ALA F  424  1                                  15    
SHEET    1   A 9 ARG A  36  ARG A  37  0                                        
SHEET    2   A 9 ARG A  51  ARG A  56  1  O  ARG A  51   N  ARG A  36           
SHEET    3   A 9 SER A  60  ARG A  65 -1  O  ILE A  64   N  TYR A  52           
SHEET    4   A 9 ASN A 256  THR A 262 -1  O  CYS A 261   N  LEU A  61           
SHEET    5   A 9 PHE A  76  ALA A  82  1  N  VAL A  79   O  VAL A 260           
SHEET    6   A 9 LEU A 302  ALA A 306  1  O  VAL A 304   N  LEU A  78           
SHEET    7   A 9 THR A 390  GLY A 394  1  O  ILE A 393   N  SER A 305           
SHEET    8   A 9 VAL A 333  LYS A 335 -1  N  LYS A 335   O  ASP A 392           
SHEET    9   A 9 GLN A 364  PHE A 366  1  O  GLN A 364   N  ILE A 334           
SHEET    1   B 3 CYS A  87  ARG A  98  0                                        
SHEET    2   B 3 PHE A 101  TYR A 109 -1  O  TYR A 109   N  CYS A  87           
SHEET    3   B 3 ILE A 176  GLN A 179 -1  O  ALA A 178   N  LEU A 102           
SHEET    1   C 3 LYS A 135  ASP A 142  0                                        
SHEET    2   C 3 LEU A 122  ALA A 132 -1  N  PHE A 130   O  GLU A 137           
SHEET    3   C 3 VAL A 206  ASP A 216 -1  O  ASP A 209   N  THR A 129           
SHEET    1   D 5 ALA A 221  VAL A 223  0                                        
SHEET    2   D 5 PHE A 229  GLY A 232 -1  O  ALA A 231   N  ALA A 221           
SHEET    3   D 5 GLU A 405  GLY A 408 -1  O  GLU A 405   N  GLY A 232           
SHEET    4   D 5 PRO A 396  PHE A 398 -1  N  PHE A 398   O  LEU A 406           
SHEET    5   D 5 ALA A 309  HIS A 310  1  N  ALA A 309   O  THR A 397           
SHEET    1   E 9 ARG B  36  ARG B  37  0                                        
SHEET    2   E 9 ARG B  51  ARG B  56  1  O  ARG B  51   N  ARG B  36           
SHEET    3   E 9 SER B  60  ARG B  65 -1  O  ILE B  64   N  TYR B  52           
SHEET    4   E 9 CYS B 257  THR B 262 -1  O  CYS B 261   N  LEU B  61           
SHEET    5   E 9 ARG B  77  ALA B  82  1  N  ARG B  77   O  ILE B 258           
SHEET    6   E 9 LEU B 302  ALA B 306  1  O  VAL B 304   N  LEU B  78           
SHEET    7   E 9 ARG B 389  GLY B 394  1  O  ARG B 389   N  LEU B 303           
SHEET    8   E 9 VAL B 333  LYS B 335 -1  N  VAL B 333   O  GLY B 394           
SHEET    9   E 9 GLN B 364  PHE B 366  1  O  GLN B 364   N  ILE B 334           
SHEET    1   F 3 CYS B  87  ARG B  98  0                                        
SHEET    2   F 3 PHE B 101  TYR B 109 -1  O  GLN B 103   N  ILE B  96           
SHEET    3   F 3 ILE B 176  GLN B 179 -1  O  ILE B 177   N  LEU B 102           
SHEET    1   G 3 LYS B 135  ASP B 142  0                                        
SHEET    2   G 3 LEU B 122  ALA B 132 -1  N  PHE B 130   O  GLU B 137           
SHEET    3   G 3 VAL B 206  ASP B 216 -1  O  SER B 213   N  ALA B 125           
SHEET    1   H 5 ALA B 221  VAL B 223  0                                        
SHEET    2   H 5 PHE B 229  GLY B 232 -1  O  ALA B 231   N  ALA B 221           
SHEET    3   H 5 GLU B 405  GLY B 408 -1  O  ALA B 407   N  ILE B 230           
SHEET    4   H 5 PRO B 396  PHE B 398 -1  N  PHE B 398   O  LEU B 406           
SHEET    5   H 5 ALA B 309  HIS B 310  1  N  ALA B 309   O  THR B 397           
SHEET    1   I 9 ARG C  36  ARG C  37  0                                        
SHEET    2   I 9 ARG C  51  ARG C  56  1  O  ARG C  51   N  ARG C  36           
SHEET    3   I 9 SER C  60  ARG C  65 -1  O  ILE C  64   N  TYR C  52           
SHEET    4   I 9 CYS C 257  THR C 262 -1  O  CYS C 261   N  LEU C  61           
SHEET    5   I 9 ARG C  77  ALA C  82  1  N  VAL C  79   O  VAL C 260           
SHEET    6   I 9 LEU C 302  ALA C 306  1  O  VAL C 304   N  LEU C  78           
SHEET    7   I 9 ARG C 389  GLY C 394  1  O  ARG C 389   N  LEU C 303           
SHEET    8   I 9 VAL C 333  LYS C 335 -1  N  LYS C 335   O  ASP C 392           
SHEET    9   I 9 GLN C 364  PHE C 366  1  O  GLN C 364   N  ILE C 334           
SHEET    1   J 3 CYS C  87  ARG C  98  0                                        
SHEET    2   J 3 PHE C 101  TYR C 109 -1  O  TYR C 109   N  CYS C  87           
SHEET    3   J 3 ILE C 176  GLN C 179 -1  O  ILE C 177   N  LEU C 102           
SHEET    1   K 3 LYS C 135  ASP C 142  0                                        
SHEET    2   K 3 LEU C 122  ALA C 132 -1  N  VAL C 128   O  ARG C 139           
SHEET    3   K 3 VAL C 206  ASP C 216 -1  O  ASP C 209   N  THR C 129           
SHEET    1   L 5 ALA C 221  VAL C 223  0                                        
SHEET    2   L 5 PHE C 229  GLY C 232 -1  O  PHE C 229   N  VAL C 223           
SHEET    3   L 5 GLU C 405  GLY C 408 -1  O  ALA C 407   N  ILE C 230           
SHEET    4   L 5 PRO C 396  PHE C 398 -1  N  PHE C 398   O  LEU C 406           
SHEET    5   L 5 ALA C 309  HIS C 310  1  N  ALA C 309   O  THR C 397           
SHEET    1   M 9 ARG D  36  ARG D  37  0                                        
SHEET    2   M 9 ARG D  51  ARG D  56  1  O  ARG D  51   N  ARG D  36           
SHEET    3   M 9 SER D  60  ARG D  65 -1  O  ILE D  64   N  TYR D  52           
SHEET    4   M 9 CYS D 257  THR D 262 -1  O  CYS D 261   N  LEU D  61           
SHEET    5   M 9 ARG D  77  ALA D  82  1  N  ARG D  77   O  ILE D 258           
SHEET    6   M 9 LEU D 302  ALA D 306  1  O  ALA D 306   N  GLY D  80           
SHEET    7   M 9 THR D 390  GLY D 394  1  O  ILE D 393   N  SER D 305           
SHEET    8   M 9 VAL D 333  LYS D 335 -1  N  LYS D 335   O  ASP D 392           
SHEET    9   M 9 GLN D 364  PHE D 366  1  O  GLN D 364   N  ILE D 334           
SHEET    1   N 6 LYS D 135  ASP D 142  0                                        
SHEET    2   N 6 LEU D 122  ALA D 132 -1  N  PHE D 130   O  GLU D 137           
SHEET    3   N 6 VAL D 206  ASP D 216 -1  O  ASP D 209   N  THR D 129           
SHEET    4   N 6 CYS D  87  ARG D  98 -1  N  LEU D  88   O  PHE D 214           
SHEET    5   N 6 PHE D 101  TYR D 109 -1  O  TYR D 109   N  CYS D  87           
SHEET    6   N 6 ILE D 176  GLN D 179 -1  O  ILE D 177   N  LEU D 102           
SHEET    1   O 5 ALA D 221  VAL D 223  0                                        
SHEET    2   O 5 PHE D 229  GLY D 232 -1  O  ALA D 231   N  ALA D 221           
SHEET    3   O 5 GLU D 405  GLY D 408 -1  O  ALA D 407   N  ILE D 230           
SHEET    4   O 5 PRO D 396  PHE D 398 -1  N  PHE D 398   O  LEU D 406           
SHEET    5   O 5 ALA D 309  HIS D 310  1  N  ALA D 309   O  THR D 397           
SHEET    1   P 9 ARG E  36  ARG E  37  0                                        
SHEET    2   P 9 ARG E  51  ARG E  56  1  O  ARG E  51   N  ARG E  36           
SHEET    3   P 9 SER E  60  ARG E  65 -1  O  ILE E  64   N  TYR E  52           
SHEET    4   P 9 CYS E 257  THR E 262 -1  O  CYS E 261   N  LEU E  61           
SHEET    5   P 9 ARG E  77  ALA E  82  1  N  ARG E  77   O  ILE E 258           
SHEET    6   P 9 LEU E 302  ALA E 306  1  O  ALA E 306   N  GLY E  80           
SHEET    7   P 9 THR E 390  GLY E 394  1  O  ILE E 393   N  SER E 305           
SHEET    8   P 9 VAL E 333  LYS E 335 -1  N  VAL E 333   O  GLY E 394           
SHEET    9   P 9 GLN E 364  PHE E 366  1  O  GLN E 364   N  ILE E 334           
SHEET    1   Q 3 CYS E  87  ARG E  98  0                                        
SHEET    2   Q 3 PHE E 101  TYR E 109 -1  O  TYR E 109   N  CYS E  87           
SHEET    3   Q 3 ILE E 176  GLN E 179 -1  O  ALA E 178   N  LEU E 102           
SHEET    1   R 3 LYS E 135  ASP E 142  0                                        
SHEET    2   R 3 LEU E 122  ALA E 132 -1  N  PHE E 130   O  GLU E 137           
SHEET    3   R 3 VAL E 206  ASP E 216 -1  O  SER E 213   N  ALA E 125           
SHEET    1   S 5 ALA E 221  VAL E 223  0                                        
SHEET    2   S 5 PHE E 229  GLY E 232 -1  O  ALA E 231   N  ALA E 221           
SHEET    3   S 5 GLU E 405  GLY E 408 -1  O  ALA E 407   N  ILE E 230           
SHEET    4   S 5 PRO E 396  PHE E 398 -1  N  PHE E 398   O  LEU E 406           
SHEET    5   S 5 ALA E 309  HIS E 310  1  N  ALA E 309   O  THR E 397           
SHEET    1   T 9 ARG F  36  ARG F  37  0                                        
SHEET    2   T 9 ARG F  51  ARG F  56  1  O  ARG F  51   N  ARG F  36           
SHEET    3   T 9 SER F  60  ARG F  65 -1  O  ILE F  62   N  VAL F  54           
SHEET    4   T 9 CYS F 257  THR F 262 -1  O  CYS F 257   N  ARG F  65           
SHEET    5   T 9 ARG F  77  ALA F  82  1  N  VAL F  79   O  VAL F 260           
SHEET    6   T 9 LEU F 302  ALA F 306  1  O  VAL F 304   N  LEU F  78           
SHEET    7   T 9 THR F 390  GLY F 394  1  O  VAL F 391   N  SER F 305           
SHEET    8   T 9 VAL F 333  LYS F 335 -1  N  LYS F 335   O  ASP F 392           
SHEET    9   T 9 GLN F 364  PHE F 366  1  O  GLN F 364   N  ILE F 334           
SHEET    1   U 3 CYS F  87  ARG F  98  0                                        
SHEET    2   U 3 PHE F 101  TYR F 109 -1  O  TYR F 109   N  CYS F  87           
SHEET    3   U 3 ILE F 176  GLN F 179 -1  O  ILE F 177   N  LEU F 102           
SHEET    1   V 3 LYS F 135  ASP F 142  0                                        
SHEET    2   V 3 LEU F 122  ALA F 132 -1  N  PHE F 130   O  GLU F 137           
SHEET    3   V 3 VAL F 206  ASP F 216 -1  O  ASP F 209   N  THR F 129           
SHEET    1   W 5 ALA F 221  VAL F 223  0                                        
SHEET    2   W 5 PHE F 229  GLY F 232 -1  O  ALA F 231   N  ALA F 221           
SHEET    3   W 5 GLU F 405  GLY F 408 -1  O  ALA F 407   N  ILE F 230           
SHEET    4   W 5 PRO F 396  PHE F 398 -1  N  PHE F 398   O  LEU F 406           
SHEET    5   W 5 ALA F 309  HIS F 310  1  N  ALA F 309   O  THR F 397           
LINK         OE2 GLU F 266                ZN    ZN F 501     1555   1555  1.78  
LINK         OE2 GLU A 266                ZN    ZN A 501     1555   1555  1.93  
LINK         OD2 ASP A 236                ZN    ZN A 501     1555   1555  1.96  
LINK         OE2 GLU C 266                ZN    ZN C 501     1555   1555  1.97  
LINK         OE2 GLU D 266                ZN    ZN D 501     1555   1555  2.00  
LINK         OE2 GLU E 266                ZN    ZN E 501     1555   1555  2.03  
LINK         OD2 ASP E 236                ZN    ZN E 501     1555   1555  2.03  
LINK         OD2 ASP B 236                ZN    ZN B 501     1555   1555  2.05  
LINK         OE2 GLU B 266                ZN    ZN B 501     1555   1555  2.08  
LINK         NE2 HIS B 401                ZN    ZN B 501     1555   1555  2.10  
LINK         OD2 ASP F 236                ZN    ZN F 501     1555   1555  2.10  
LINK         OD2 ASP C 236                ZN    ZN C 501     1555   1555  2.13  
LINK         OD2 ASP D 236                ZN    ZN D 501     1555   1555  2.13  
LINK        ZN    ZN A 501                 O   HOH A 643     1555   1555  2.14  
LINK         NE2 HIS C 401                ZN    ZN C 501     1555   1555  2.23  
LINK         NE2 HIS A 401                ZN    ZN A 501     1555   1555  2.28  
LINK        ZN    ZN C 501                 O   HOH C 653     1555   1555  2.28  
LINK        ZN    ZN D 501                 O   HOH D 629     1555   1555  2.29  
LINK         NE2 HIS E 401                ZN    ZN E 501     1555   1555  2.30  
LINK         NE2 HIS F 401                ZN    ZN F 501     1555   1555  2.34  
LINK         NE2 HIS D 401                ZN    ZN D 501     1555   1555  2.36  
LINK        ZN    ZN F 501                 O   HOH F 637     1555   1555  2.39  
LINK        ZN    ZN D 501                 O   HOH D 631     1555   1555  2.42  
LINK        ZN    ZN E 501                 O   HOH E 635     1555   1555  2.43  
LINK        ZN    ZN C 501                 O   HOH C 618     1555   1555  2.43  
LINK        ZN    ZN B 501                 O   HOH B 635     1555   1555  2.44  
LINK        ZN    ZN A 501                 O   HOH A 601     1555   1555  2.48  
LINK        ZN    ZN E 501                 O   HOH E 632     1555   1555  2.59  
LINK        ZN    ZN B 501                 O   HOH B 601     1555   1555  2.69  
CISPEP   1 ASP A  236    ASN A  237          0        -0.64                     
CISPEP   2 ARG B    2    ALA B    3          0        -0.52                     
CISPEP   3 ALA B    3    GLU B    4          0         3.72                     
CISPEP   4 GLU B    4    LEU B    5          0       -26.03                     
CISPEP   5 PRO B  182    GLY B  183          0       -30.00                     
CISPEP   6 ASP B  236    ASN B  237          0         1.21                     
CISPEP   7 PRO C  182    GLY C  183          0        -1.68                     
CISPEP   8 ASP C  236    ASN C  237          0        -2.13                     
CISPEP   9 GLY C  277    PRO C  278          0        -7.49                     
CISPEP  10 ASP D  236    ASN D  237          0         6.65                     
CISPEP  11 ASP E  236    ASN E  237          0         2.55                     
CISPEP  12 PRO F  182    GLY F  183          0         2.86                     
CISPEP  13 ASP F  236    ASN F  237          0        -0.39                     
SITE     1 AC1  5 ASP A 236  GLU A 266  HIS A 401  HOH A 601                    
SITE     2 AC1  5 HOH A 643                                                     
SITE     1 AC2  5 ASP B 236  GLU B 266  HIS B 401  HOH B 601                    
SITE     2 AC2  5 HOH B 635                                                     
SITE     1 AC3  5 ASP C 236  GLU C 266  HIS C 401  HOH C 618                    
SITE     2 AC3  5 HOH C 653                                                     
SITE     1 AC4  5 ASP D 236  GLU D 266  HIS D 401  HOH D 629                    
SITE     2 AC4  5 HOH D 631                                                     
SITE     1 AC5  5 ASP E 236  GLU E 266  HIS E 401  HOH E 632                    
SITE     2 AC5  5 HOH E 635                                                     
SITE     1 AC6  4 ASP F 236  GLU F 266  HIS F 401  HOH F 637                    
CRYST1  150.020  218.267  172.693  90.00  90.00  90.00 C 2 2 21     48          
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      0.006666  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005791        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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