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Database: PDB
Entry: 4NJR
LinkDB: 4NJR
Original site: 4NJR 
HEADER    HYDROLASE                               11-NOV-13   4NJR              
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;                                                   
COMPND   4 EC: 3.4.11.-;                                                        
COMPND   5 ENGINEERED: 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, PA3257;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ASPARTYL AMINOPEPTIDASE, TET SHAPE PROTEASE, DODECAMERIC PEPTIDASE,   
KEYWDS   2 DODECAMERIC TETRAHERAL SHAPE, HYDROLASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.NGUYEN,R.PANDIAN,D.Y.KIM,S.C.HA,K.H.YUN,K.S.KIM,J.H.KIM,K.K.KIM   
REVDAT   3   17-SEP-14 4NJR    1       JRNL                                     
REVDAT   2   09-APR-14 4NJR    1       JRNL                                     
REVDAT   1   02-APR-14 4NJR    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 93254                          
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) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4898                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6839                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 360                          
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13047                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 884                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.178         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.402         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13330 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 12602 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18101 ; 1.917 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28816 ; 0.938 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1691 ; 7.938 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   655 ;36.162 ;23.176       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2073 ;15.276 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   132 ;19.007 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2010 ; 0.132 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15511 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3227 ; 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 4NJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083290.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM Q270R                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98201                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10000                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.320                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M TRIS, 0.2M MAGNESIUM    
REMARK 280  CHLORIDE, 0.1M, ZINC CHLORIDE, PH 8.0, MICROBATCH METHOD,           
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       67.09350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.73645            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      109.58533            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       67.09350            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       38.73645            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.58533            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       67.09350            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       38.73645            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      109.58533            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.47290            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      219.17067            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       77.47290            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      219.17067            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       77.47290            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      219.17067            
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: 86300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 144430 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1432.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      134.18700            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       67.09350            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      116.20935            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH D 722  LIES ON A SPECIAL POSITION.                          
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     CYS A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     SER A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     CYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     THR B   377                                                      
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     CYS D   374                                                      
REMARK 465     GLY D   375                                                      
REMARK 465     SER D   376                                                      
REMARK 465     THR D   377                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS B 272    CG   ND1  CD2  CE1  NE2                             
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    THR A   382     O    GLN A   385              2.00            
REMARK 500   O    ARG C    77     O    CYS C   257              2.04            
REMARK 500   O    HOH D   626     O    HOH D   741              2.07            
REMARK 500   O    HOH B   803     O    HOH B   804              2.09            
REMARK 500   O    HOH D   756     O    HOH D   770              2.09            
REMARK 500   O    HOH A   738     O    HOH A   809              2.11            
REMARK 500   O    HOH D   631     O    HOH D   658              2.17            
REMARK 500   N    GLY C   379     O    HOH C   764              2.17            
REMARK 500   O    HOH C   795     O    HOH C   796              2.18            
REMARK 500   OD2  ASP D   121     O    HOH D   718              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 B 228   CD    GLU B 228   OE1     0.076                       
REMARK 500    CYS B 273   C     CYS B 273   O       0.116                       
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   2   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    VAL A 260   CB  -  CA  -  C   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    ASP A 318   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B  41   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG B  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 139   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    SER B 271   N   -  CA  -  C   ANGL. DEV. =  27.5 DEGREES          
REMARK 500    ASP B 307   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 389   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP C 187   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP C 227   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ILE C 258   N   -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    VAL C 260   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG C 300   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C 319   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    VAL C 391   CB  -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    VAL D  54   CB  -  CA  -  C   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ARG D  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG D  77   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    VAL D 260   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG D 286   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG D 389   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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    ARG A   2       15.70    168.64                                   
REMARK 500    ARG A 144      -54.04     70.81                                   
REMARK 500    ASN A 158       64.00   -160.21                                   
REMARK 500    SER A 269     -171.33     56.33                                   
REMARK 500    CYS A 270       51.42     92.00                                   
REMARK 500    HIS A 272      -19.86    -45.69                                   
REMARK 500    ASP A 276       46.97   -101.83                                   
REMARK 500    TYR A 316       48.92   -151.35                                   
REMARK 500    VAL A 386      -43.14     76.20                                   
REMARK 500    HIS A 401        2.63     82.80                                   
REMARK 500    ARG B   2      -53.43     29.15                                   
REMARK 500    CYS B  87     -174.10   -170.55                                   
REMARK 500    SER B 123     -167.14   -113.77                                   
REMARK 500    ARG B 144      -55.06     69.33                                   
REMARK 500    ASN B 158       59.98   -158.58                                   
REMARK 500    ASP B 254       41.05   -145.29                                   
REMARK 500    SER B 271      -71.77    172.48                                   
REMARK 500    CYS B 273     -138.87   -124.14                                   
REMARK 500    ALA B 275     -166.13     75.40                                   
REMARK 500    TYR B 316       43.16   -147.54                                   
REMARK 500    THR B 382      102.13    113.94                                   
REMARK 500    ALA B 383     -119.50    -66.38                                   
REMARK 500    SER B 384      101.28      0.89                                   
REMARK 500    GLN B 385      -76.65     79.03                                   
REMARK 500    HIS B 401        6.48     81.04                                   
REMARK 500    GLU C   4      -67.26     95.58                                   
REMARK 500    ASN C  57       14.28     59.55                                   
REMARK 500    SER C 123     -165.19   -114.42                                   
REMARK 500    ARG C 144      -50.11     64.37                                   
REMARK 500    ASN C 158       67.32   -165.83                                   
REMARK 500    LEU C 208      -61.19   -100.47                                   
REMARK 500    ASP C 254       44.98   -144.50                                   
REMARK 500    ILE C 258      108.47     62.00                                   
REMARK 500    TYR C 316       47.46   -145.86                                   
REMARK 500    HIS C 401        4.83     83.23                                   
REMARK 500    ASN D  57       15.72     57.60                                   
REMARK 500    SER D 123     -168.81   -114.31                                   
REMARK 500    ARG D 144      -52.95     73.65                                   
REMARK 500    ASN D 158       60.97   -162.36                                   
REMARK 500    LEU D 208      -63.55    -97.07                                   
REMARK 500    ASP D 254       40.18   -145.56                                   
REMARK 500    TYR D 316       43.07   -150.16                                   
REMARK 500    LEU D 428      -47.72   -149.05                                   
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 ARG A    2     ALA A    3                  132.20                    
REMARK 500 HIS A  272     CYS A  273                 -148.14                    
REMARK 500 ASP A  276     GLY A  277                  147.55                    
REMARK 500 MET B    1     ARG B    2                  118.66                    
REMARK 500 GLY C  183     GLU C  184                 -148.38                    
REMARK 500 LEU D  428     PRO D  429                  146.50                    
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    VAL A 386        24.1      L          L   OUTSIDE RANGE           
REMARK 500    SER B 271         4.0      L          L   EXPECTING SP3           
REMARK 500    CYS B 273        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER B 384        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 258        17.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 266   OE1                                                    
REMARK 620 2 ASP B 236   OD2  95.8                                              
REMARK 620 3 CO3 B 503   O3  155.3 104.6                                        
REMARK 620 4 HIS B 401   NE2 102.9  91.6  90.6                                  
REMARK 620 5 CO3 B 503   O1  102.7 107.9  58.0 145.9                            
REMARK 620 6 GLU B 266   OE2  57.7 150.6 104.4  83.4  91.5                      
REMARK 620 N                    1     2     3     4     5                       
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   OE1                                                    
REMARK 620 2 CO3 A 503   O3  158.2                                              
REMARK 620 3 ASP A 236   OD2  93.8  98.8                                        
REMARK 620 4 HIS A 401   NE2  99.5  97.3  94.0                                  
REMARK 620 5 CO3 A 503   O2   99.3  59.8 108.4 149.5                            
REMARK 620 6 GLU A 266   OE2  57.9 110.5 150.6  84.0  85.9                      
REMARK 620 N                    1     2     3     4     5                       
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  92.4                                              
REMARK 620 3 CO3 C 503   O3  151.7 113.2                                        
REMARK 620 4 HIS C 401   NE2 102.5  95.5  87.4                                  
REMARK 620 5 CO3 C 503   O1  103.6 111.3  57.0 141.3                            
REMARK 620 6 GLU C 266   OE1  56.9 146.8  99.7  81.0  89.9                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP D 236   OD2                                                    
REMARK 620 2 GLU D 266   OE2  92.6                                              
REMARK 620 3 CO3 D 503   O2  113.4 150.9                                        
REMARK 620 4 HIS D 401   NE2  94.4 104.5  87.0                                  
REMARK 620 5 CO3 D 503   O3  110.5 100.5  59.2 143.6                            
REMARK 620 6 GLU D 266   OE1 146.0  57.0 100.1  80.9  91.2                      
REMARK 620 N                    1     2     3     4     5                       
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 307   OD1                                                    
REMARK 620 2 CO3 B 503   O1  141.9                                              
REMARK 620 3 ASP B 236   OD1  96.2 111.7                                        
REMARK 620 4 HIS B  82   NE2  99.3 106.4  89.2                                  
REMARK 620 5 ASP B 307   OD2  57.5  95.0 152.7  88.3                            
REMARK 620 6 HOH B 818   O    87.4  69.2  87.5 172.8  97.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 307   OD1                                                    
REMARK 620 2 ASP D 236   OD1  97.0                                              
REMARK 620 3 CO3 D 503   O3  144.7 111.3                                        
REMARK 620 4 HIS D  82   NE2  97.6  88.5 103.6                                  
REMARK 620 5 ASP D 307   OD2  58.3 154.4  94.1  88.6                            
REMARK 620 6 HOH D 823   O    88.5  92.8  70.2 173.6  93.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 236   OD1                                                    
REMARK 620 2 CO3 A 503   O2  109.7                                              
REMARK 620 3 ASP A 307   OD1  96.2 147.3                                        
REMARK 620 4 HIS A  82   NE2  93.1  98.0 100.2                                  
REMARK 620 5 ASP A 307   OD2 153.3  96.9  58.1  85.2                            
REMARK 620 6 HOH A 823   O    93.1  76.4  82.8 172.8  91.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 236   OD1                                                    
REMARK 620 2 ASP C 307   OD1  95.7                                              
REMARK 620 3 HIS C  82   NE2  91.3  94.7                                        
REMARK 620 4 CO3 C 503   O1  114.9 141.0 107.6                                  
REMARK 620 5 ASP C 307   OD2 152.4  57.5  85.3  92.2                            
REMARK 620 6 HOH C 819   O    86.6  83.7 177.2  75.1  95.7                      
REMARK 620 N                    1     2     3     4     5                       
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 A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NJQ   RELATED DB: PDB                                   
REMARK 900 COCOPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA          
REMARK 900 WITH ZINC IN CATALYTIC SITE                                          
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: 4OIW   RELATED DB: PDB                                   
DBREF  4NJR A    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJR B    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJR C    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJR D    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
SEQRES   1 A  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 A  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 A  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 A  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 A  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 A  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 A  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 A  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 A  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 A  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 A  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 A  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 A  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 A  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 A  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 A  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 A  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 A  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 A  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 A  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 A  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 A  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 A  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 A  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 A  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 A  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 A  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 A  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 A  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 A  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 A  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 A  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 A  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 B  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 B  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 B  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 B  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 B  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 B  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 B  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 B  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 B  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 B  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 B  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 B  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 B  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 B  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 B  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 B  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 B  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 B  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 B  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 B  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 B  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 B  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 B  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 B  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 B  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 B  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 B  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 B  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 B  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 B  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 B  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 B  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 B  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 C  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 C  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 C  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 C  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 C  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 C  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 C  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 C  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 C  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 C  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 C  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 C  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 C  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 C  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 C  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 C  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 C  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 C  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 C  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 C  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 C  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 C  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 C  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 C  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 C  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 C  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 C  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 C  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 C  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 C  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 C  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 C  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 C  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 D  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 D  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 D  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 D  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 D  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 D  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 D  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 D  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 D  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 D  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 D  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 D  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 D  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 D  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 D  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 D  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 D  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 D  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 D  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 D  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 D  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 D  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 D  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 D  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 D  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 D  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 D  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 D  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 D  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 D  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 D  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 D  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 D  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET    CO3  A 503       4                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET    CO3  B 503       4                                                       
HET     ZN  C 501       1                                                       
HET     ZN  C 502       1                                                       
HET    CO3  C 503       4                                                       
HET     ZN  D 501       1                                                       
HET     ZN  D 502       1                                                       
HET    CO3  D 503       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CO3 CARBONATE ION                                                    
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   7  CO3    4(C O3 2-)                                                   
FORMUL  17  HOH   *884(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 HIS A  264  GLY A  268  5                                   5    
HELIX   11  11 PRO A  278  ARG A  286  1                                   9    
HELIX   12  12 ASP A  292  GLN A  299  1                                   8    
HELIX   13  13 TYR A  316  HIS A  320  5                                   5    
HELIX   14  14 ASN A  345  SER A  359  1                                  15    
HELIX   15  15 GLY A  379  GLN A  385  1                                   7    
HELIX   16  16 HIS A  410  ALA A  424  1                                  15    
HELIX   17  17 ARG B    2  ALA B   15  1                                  14    
HELIX   18  18 THR B   18  ALA B   33  1                                  16    
HELIX   19  19 SER B   70  GLY B   75  1                                   6    
HELIX   20  20 PHE B  114  PHE B  118  5                                   5    
HELIX   21  21 ALA B  154  ASN B  158  5                                   5    
HELIX   22  22 ALA B  160  GLY B  164  5                                   5    
HELIX   23  23 ASN B  168  LEU B  173  1                                   6    
HELIX   24  24 ASP B  187  GLY B  201  1                                  15    
HELIX   25  25 ARG B  234  ALA B  251  1                                  18    
HELIX   26  26 HIS B  264  GLY B  268  5                                   5    
HELIX   27  27 PRO B  278  ARG B  286  1                                   9    
HELIX   28  28 ASP B  292  ARG B  300  1                                   9    
HELIX   29  29 TYR B  316  HIS B  320  5                                   5    
HELIX   30  30 ASN B  345  SER B  359  1                                  15    
HELIX   31  31 HIS B  410  SER B  425  1                                  16    
HELIX   32  32 ARG C    2  ALA C   15  1                                  14    
HELIX   33  33 THR C   18  ALA C   33  1                                  16    
HELIX   34  34 SER C   70  GLY C   75  1                                   6    
HELIX   35  35 PHE C  114  PHE C  118  5                                   5    
HELIX   36  36 ALA C  154  ASN C  158  5                                   5    
HELIX   37  37 ALA C  160  GLY C  164  5                                   5    
HELIX   38  38 ASN C  168  LEU C  173  1                                   6    
HELIX   39  39 ASP C  187  GLY C  201  1                                  15    
HELIX   40  40 ARG C  234  ALA C  251  1                                  18    
HELIX   41  41 HIS C  264  GLY C  268  5                                   5    
HELIX   42  42 PRO C  278  ARG C  286  1                                   9    
HELIX   43  43 ASP C  292  GLN C  299  1                                   8    
HELIX   44  44 TYR C  316  HIS C  320  5                                   5    
HELIX   45  45 ASN C  345  SER C  359  1                                  15    
HELIX   46  46 PRO C  380  GLY C  387  1                                   8    
HELIX   47  47 HIS C  410  ALA C  424  1                                  15    
HELIX   48  48 ARG D    2  SER D   16  1                                  15    
HELIX   49  49 THR D   18  ALA D   33  1                                  16    
HELIX   50  50 SER D   70  GLY D   75  1                                   6    
HELIX   51  51 PHE D  114  PHE D  118  5                                   5    
HELIX   52  52 ALA D  154  ASN D  158  5                                   5    
HELIX   53  53 ALA D  160  GLY D  164  5                                   5    
HELIX   54  54 ASN D  168  LEU D  173  1                                   6    
HELIX   55  55 ASP D  187  GLY D  201  1                                  15    
HELIX   56  56 ARG D  234  ALA D  251  1                                  18    
HELIX   57  57 HIS D  264  GLY D  268  5                                   5    
HELIX   58  58 PRO D  278  ARG D  286  1                                   9    
HELIX   59  59 ASP D  292  GLN D  299  1                                   8    
HELIX   60  60 TYR D  316  HIS D  320  5                                   5    
HELIX   61  61 ASN D  345  SER D  359  1                                  15    
HELIX   62  62 GLY D  379  GLY D  387  1                                   9    
HELIX   63  63 HIS D  410  ALA D  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 257   N  ARG A  65           
SHEET    5   A 9 PHE A  76  HIS 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  VAL A 391   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  SER A 213   N  ALA A 125           
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  ALA A 407   N  ILE A 230           
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 ASN B 256  THR B 262 -1  O  LEU B 259   N  ALA B  63           
SHEET    5   E 9 PHE B  76  HIS B  82  1  N  VAL B  79   O  VAL B 260           
SHEET    6   E 9 LEU B 302  ALA B 306  1  O  VAL B 304   N  LEU B  78           
SHEET    7   E 9 THR B 390  GLY B 394  1  O  VAL B 391   N  SER B 305           
SHEET    8   E 9 VAL B 333  LYS B 335 -1  N  LYS B 335   O  ASP B 392           
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  TYR B 109   N  CYS B  87           
SHEET    3   F 3 ILE B 176  GLN B 179 -1  O  ALA B 178   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  ASP B 209   N  THR B 129           
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  62   N  VAL C  54           
SHEET    4   I 9 LEU C 259  THR C 262 -1  O  LEU C 259   N  ALA C  63           
SHEET    5   I 9 ARG C  77  HIS 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 THR C 390  GLY C 394  1  O  VAL C 391   N  SER C 305           
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  ALA C 178   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  PHE C 130   O  GLU C 137           
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  ALA C 231   N  ALA C 221           
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  62   N  VAL D  54           
SHEET    4   M 9 ASN D 256  THR D 262 -1  O  LEU D 259   N  ALA D  63           
SHEET    5   M 9 PHE D  76  HIS D  82  1  N  ARG D  77   O  ASN D 256           
SHEET    6   M 9 LEU D 302  ALA D 306  1  O  VAL D 304   N  LEU D  78           
SHEET    7   M 9 THR D 390  GLY D 394  1  O  VAL D 391   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 3 CYS D  87  ARG D  98  0                                        
SHEET    2   N 3 PHE D 101  TYR D 109 -1  O  GLN D 103   N  ILE D  96           
SHEET    3   N 3 ILE D 176  GLN D 179 -1  O  ALA D 178   N  LEU D 102           
SHEET    1   O 3 LYS D 135  ASP D 142  0                                        
SHEET    2   O 3 LEU D 122  ALA D 132 -1  N  VAL D 128   O  ARG D 139           
SHEET    3   O 3 VAL D 206  ASP D 216 -1  O  ASP D 209   N  THR D 129           
SHEET    1   P 5 ALA D 221  VAL D 223  0                                        
SHEET    2   P 5 PHE D 229  GLY D 232 -1  O  ALA D 231   N  ALA D 221           
SHEET    3   P 5 GLU D 405  GLY D 408 -1  O  ALA D 407   N  ILE D 230           
SHEET    4   P 5 PRO D 396  PHE D 398 -1  N  PHE D 398   O  LEU D 406           
SHEET    5   P 5 ALA D 309  HIS D 310  1  N  ALA D 309   O  THR D 397           
LINK         OE1 GLU B 266                ZN    ZN B 502     1555   1555  1.82  
LINK         OE1 GLU A 266                ZN    ZN A 501     1555   1555  1.96  
LINK         OE2 GLU C 266                ZN    ZN C 501     1555   1555  1.96  
LINK        ZN    ZN A 501                 O3  CO3 A 503     1555   1555  1.97  
LINK         OD2 ASP C 236                ZN    ZN C 501     1555   1555  1.97  
LINK         OD2 ASP D 236                ZN    ZN D 501     1555   1555  1.97  
LINK         OE2 GLU D 266                ZN    ZN D 501     1555   1555  1.98  
LINK         OD2 ASP A 236                ZN    ZN A 501     1555   1555  2.00  
LINK         OD1 ASP B 307                ZN    ZN B 501     1555   1555  2.00  
LINK         OD2 ASP B 236                ZN    ZN B 502     1555   1555  2.02  
LINK         OD1 ASP D 307                ZN    ZN D 502     1555   1555  2.04  
LINK         OD1 ASP A 236                ZN    ZN A 502     1555   1555  2.07  
LINK         OD1 ASP D 236                ZN    ZN D 502     1555   1555  2.08  
LINK         OD1 ASP C 236                ZN    ZN C 502     1555   1555  2.08  
LINK        ZN    ZN B 502                 O3  CO3 B 503     1555   1555  2.08  
LINK        ZN    ZN D 501                 O2  CO3 D 503     1555   1555  2.08  
LINK        ZN    ZN B 501                 O1  CO3 B 503     1555   1555  2.08  
LINK         OD1 ASP C 307                ZN    ZN C 502     1555   1555  2.10  
LINK        ZN    ZN A 502                 O2  CO3 A 503     1555   1555  2.12  
LINK         NE2 HIS B 401                ZN    ZN B 502     1555   1555  2.13  
LINK         OD1 ASP B 236                ZN    ZN B 501     1555   1555  2.13  
LINK         OD1 ASP A 307                ZN    ZN A 502     1555   1555  2.16  
LINK        ZN    ZN D 502                 O3  CO3 D 503     1555   1555  2.16  
LINK         NE2 HIS A 401                ZN    ZN A 501     1555   1555  2.16  
LINK         NE2 HIS C  82                ZN    ZN C 502     1555   1555  2.17  
LINK         NE2 HIS D  82                ZN    ZN D 502     1555   1555  2.17  
LINK        ZN    ZN C 501                 O3  CO3 C 503     1555   1555  2.18  
LINK        ZN    ZN B 502                 O1  CO3 B 503     1555   1555  2.19  
LINK         NE2 HIS C 401                ZN    ZN C 501     1555   1555  2.20  
LINK         NE2 HIS B  82                ZN    ZN B 501     1555   1555  2.20  
LINK         NE2 HIS A  82                ZN    ZN A 502     1555   1555  2.20  
LINK         NE2 HIS D 401                ZN    ZN D 501     1555   1555  2.21  
LINK        ZN    ZN C 502                 O1  CO3 C 503     1555   1555  2.22  
LINK        ZN    ZN D 501                 O3  CO3 D 503     1555   1555  2.25  
LINK        ZN    ZN A 501                 O2  CO3 A 503     1555   1555  2.28  
LINK        ZN    ZN C 501                 O1  CO3 C 503     1555   1555  2.28  
LINK         OD2 ASP A 307                ZN    ZN A 502     1555   1555  2.35  
LINK         OE1 GLU D 266                ZN    ZN D 501     1555   1555  2.40  
LINK         OD2 ASP B 307                ZN    ZN B 501     1555   1555  2.42  
LINK         OD2 ASP D 307                ZN    ZN D 502     1555   1555  2.43  
LINK         OD2 ASP C 307                ZN    ZN C 502     1555   1555  2.44  
LINK         OE2 GLU A 266                ZN    ZN A 501     1555   1555  2.47  
LINK         OE1 GLU C 266                ZN    ZN C 501     1555   1555  2.49  
LINK         OE2 GLU B 266                ZN    ZN B 502     1555   1555  2.55  
LINK        ZN    ZN B 501                 O   HOH B 818     1555   1555  2.29  
LINK        ZN    ZN C 502                 O   HOH C 819     1555   1555  2.33  
LINK        ZN    ZN D 502                 O   HOH D 823     1555   1555  2.34  
LINK        ZN    ZN A 502                 O   HOH A 823     1555   1555  2.39  
CISPEP   1 ASP A  236    ASN A  237          0         3.19                     
CISPEP   2 GLY A  274    ALA A  275          0       -16.57                     
CISPEP   3 ASP B  236    ASN B  237          0         6.55                     
CISPEP   4 HIS B  272    CYS B  273          0        21.98                     
CISPEP   5 ASP B  276    GLY B  277          0       -14.71                     
CISPEP   6 SER B  384    GLN B  385          0       -27.30                     
CISPEP   7 ASP C  236    ASN C  237          0         6.93                     
CISPEP   8 ASP D  236    ASN D  237          0         4.73                     
SITE     1 AC1  5 ASP A 236  GLU A 266  HIS A 401   ZN A 502                    
SITE     2 AC1  5 CO3 A 503                                                     
SITE     1 AC2  6 HIS A  82  ASP A 236  ASP A 307   ZN A 501                    
SITE     2 AC2  6 CO3 A 503  HOH A 823                                          
SITE     1 AC3 10 HIS A  82  ASP A 236  GLU A 265  GLU A 266                    
SITE     2 AC3 10 ASP A 307  HIS A 401   ZN A 501   ZN A 502                    
SITE     3 AC3 10 HOH A 823  HIS D 156                                          
SITE     1 AC4  6 HIS B  82  ASP B 236  ASP B 307   ZN B 502                    
SITE     2 AC4  6 CO3 B 503  HOH B 818                                          
SITE     1 AC5  5 ASP B 236  GLU B 266  HIS B 401   ZN B 501                    
SITE     2 AC5  5 CO3 B 503                                                     
SITE     1 AC6 11 HIS B  82  ASP B 236  GLU B 265  GLU B 266                    
SITE     2 AC6 11 ASP B 307  PRO B 380  HIS B 401   ZN B 501                    
SITE     3 AC6 11  ZN B 502  HOH B 818  HIS C 156                               
SITE     1 AC7  5 ASP C 236  GLU C 266  HIS C 401   ZN C 502                    
SITE     2 AC7  5 CO3 C 503                                                     
SITE     1 AC8  6 HIS C  82  ASP C 236  ASP C 307   ZN C 501                    
SITE     2 AC8  6 CO3 C 503  HOH C 819                                          
SITE     1 AC9 10 HIS B 156  HIS C  82  ASP C 236  GLU C 265                    
SITE     2 AC9 10 GLU C 266  ASP C 307  HIS C 401   ZN C 501                    
SITE     3 AC9 10  ZN C 502  HOH C 819                                          
SITE     1 BC1  5 ASP D 236  GLU D 266  HIS D 401   ZN D 502                    
SITE     2 BC1  5 CO3 D 503                                                     
SITE     1 BC2  6 HIS D  82  ASP D 236  ASP D 307   ZN D 501                    
SITE     2 BC2  6 CO3 D 503  HOH D 823                                          
SITE     1 BC3 10 HIS A 156  HIS D  82  ASP D 236  GLU D 265                    
SITE     2 BC3 10 GLU D 266  ASP D 307  HIS D 401   ZN D 501                    
SITE     3 BC3 10  ZN D 502  HOH D 823                                          
CRYST1  134.187  134.187  328.756  90.00  90.00 120.00 H 3          36          
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      0.007452  0.004303  0.000000        0.00000                         
SCALE2      0.000000  0.008605  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003042        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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