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Database: PDB
Entry: 4L2L
LinkDB: 4L2L
Original site: 4L2L 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           04-JUN-13   4L2L              
TITLE     HUMAN LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH LIGAND 4-(4-            
TITLE    2 BENZYLPHENYL)THIAZOL-2-AMINE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A(4) HYDROLASE;                
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4, LTA4H;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PAQN                                      
KEYWDS    METALLOPROTEIN, HYDROLASE, PROTEASE, ZINC BINDING, HYDROLASE-         
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.STSIAPANAVA,A.RINALDO-MATTHIS,J.Z.HAEGGSTROM                        
REVDAT   3   15-NOV-17 4L2L    1       REMARK                                   
REVDAT   2   23-APR-14 4L2L    1       JRNL                                     
REVDAT   1   12-MAR-14 4L2L    0                                                
JRNL        AUTH   A.STSIAPANAVA,U.OLSSON,M.WAN,T.KLEINSCHMIDT,D.RUTISHAUSER,   
JRNL        AUTH 2 R.A.ZUBAREV,B.SAMUELSSON,A.RINALDO-MATTHIS,J.Z.HAEGGSTROM    
JRNL        TITL   BINDING OF PRO-GLY-PRO AT THE ACTIVE SITE OF LEUKOTRIENE A4  
JRNL        TITL 2 HYDROLASE/AMINOPEPTIDASE AND DEVELOPMENT OF AN EPOXIDE       
JRNL        TITL 3 HYDROLASE SELECTIVE INHIBITOR.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  4227 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24591641                                                     
JRNL        DOI    10.1073/PNAS.1402136111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 73759                          
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) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3882                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4885                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.2130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4852                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 487                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.52000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.082         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.210         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5248 ; 0.023 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5035 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7185 ; 2.162 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11671 ; 0.975 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   677 ; 6.053 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   235 ;34.857 ;24.468       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   933 ;12.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.258 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   805 ; 0.138 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5928 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1198 ; 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 4L2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080101.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77641                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.648                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 8.510                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.0300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.240                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R59                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM SODIUM ACETATE, 22% (V/V) PEG      
REMARK 280  8000, 5 MM YBCL3, PH 6.5, LIQUID DIFFUSION, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.35050            
REMARK 290   SMTRY3   2  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   481    YB     YB A   703     1454     2.11            
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 A 325   CD    GLU A 325   OE2     0.073                       
REMARK 500    SER A 380   CB    SER A 380   OG     -0.109                       
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  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ASP A 257   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 331   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 338   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 426   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP A 461   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 481   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    PHE A 526   CB  -  CG  -  CD2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 537   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 573   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP A 578   CB  -  CG  -  OD1 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ASP A 606   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  79       67.34   -119.20                                   
REMARK 500    SER A  80     -131.28     43.72                                   
REMARK 500    ASN A  97       -0.70     72.95                                   
REMARK 500    SER A 222     -178.89   -172.82                                   
REMARK 500    GLU A 271       44.37    -82.22                                   
REMARK 500    CYS A 274       -5.39     72.75                                   
REMARK 500    LEU A 275       77.39   -158.26                                   
REMARK 500    LYS A 546       32.65     72.62                                   
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 A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A 707   O                                                      
REMARK 620 2 GLU A 318   OE2 102.5                                              
REMARK 620 3 HIS A 295   NE2 108.9 101.4                                        
REMARK 620 4 HIS A 299   NE2 131.7 107.1 101.6                                  
REMARK 620 5 ACT A 707   OXT  53.1 155.5  90.0  91.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 704  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD2                                                    
REMARK 620 2 ASP A 175   OD1  39.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 705  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1261   O                                                      
REMARK 620 2 ASP A 426   OD1  81.7                                              
REMARK 620 3 HOH A1256   O    81.0  64.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A 708   O                                                      
REMARK 620 2 ASP A  47   OD2  82.7                                              
REMARK 620 3 ASP A  47   OD1 131.5  52.7                                        
REMARK 620 4 ACT A 708   OXT  57.5  68.6 111.4                                  
REMARK 620 5 HOH A 913   O   127.1  77.8  66.5  69.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 706  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 825   O                                                      
REMARK 620 2 HOH A 868   O    82.0                                              
REMARK 620 3 ASP A 481   OD2 124.0  83.5                                        
REMARK 620 4 ASP A 481   OD1  74.4  71.6  49.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 705  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 426   OD1                                                    
REMARK 620 2 ASP A 426   OD2  51.0                                              
REMARK 620 3 HOH A1261   O    60.8 100.5                                        
REMARK 620 N                    1     2                                         
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1V6 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 706                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 709                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DPR   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH          
REMARK 900 INHIBITOR CAPTOPRIL                                                  
REMARK 900 RELATED ID: 3U9W   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH          
REMARK 900 INHIBITOR SC57461A                                                   
DBREF  4L2L A    0   610  UNP    P09960   LKHA4_HUMAN      1    611             
SEQRES   1 A  611  MET PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO          
SEQRES   2 A  611  ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS          
SEQRES   3 A  611  SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA          
SEQRES   4 A  611  ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER          
SEQRES   5 A  611  LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL          
SEQRES   6 A  611  VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU          
SEQRES   7 A  611  ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU          
SEQRES   8 A  611  PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU          
SEQRES   9 A  611  ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN          
SEQRES  10 A  611  TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO          
SEQRES  11 A  611  TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA          
SEQRES  12 A  611  ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR          
SEQRES  13 A  611  TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA          
SEQRES  14 A  611  LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO          
SEQRES  15 A  611  GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS          
SEQRES  16 A  611  VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY          
SEQRES  17 A  611  ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL          
SEQRES  18 A  611  TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU          
SEQRES  19 A  611  PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP          
SEQRES  20 A  611  LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU          
SEQRES  21 A  611  VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN          
SEQRES  22 A  611  PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY          
SEQRES  23 A  611  ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER          
SEQRES  24 A  611  HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP          
SEQRES  25 A  611  ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU          
SEQRES  26 A  611  GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE          
SEQRES  27 A  611  ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN          
SEQRES  28 A  611  ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR          
SEQRES  29 A  611  LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL          
SEQRES  30 A  611  ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU          
SEQRES  31 A  611  LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE          
SEQRES  32 A  611  PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER          
SEQRES  33 A  611  TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU          
SEQRES  34 A  611  TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN          
SEQRES  35 A  611  VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO          
SEQRES  36 A  611  PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA          
SEQRES  37 A  611  CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU          
SEQRES  38 A  611  ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP          
SEQRES  39 A  611  LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR          
SEQRES  40 A  611  LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG          
SEQRES  41 A  611  MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER          
SEQRES  42 A  611  GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER          
SEQRES  43 A  611  LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA          
SEQRES  44 A  611  THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE          
SEQRES  45 A  611  LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA          
SEQRES  46 A  611  VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO          
SEQRES  47 A  611  VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP          
HET     ZN  A 701       1                                                       
HET    1V6  A 702      30                                                       
HET     YB  A 703       1                                                       
HET     YB  A 704       2                                                       
HET     YB  A 705       2                                                       
HET     YB  A 706       1                                                       
HET    ACT  A 707       4                                                       
HET    ACT  A 708       4                                                       
HET    ACT  A 709       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     1V6 4-(4-BENZYLPHENYL)-1,3-THIAZOL-2-AMINE                           
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     ACT ACETATE ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  1V6    C16 H14 N2 S                                                 
FORMUL   4   YB    4(YB 3+)                                                     
FORMUL   8  ACT    3(C2 H3 O2 1-)                                               
FORMUL  11  HOH   *487(H2 O)                                                    
HELIX    1   1 GLN A   79  GLY A   83  5                                   5    
HELIX    2   2 THR A  119  THR A  123  5                                   5    
HELIX    3   3 HIS A  139  ILE A  143  5                                   5    
HELIX    4   4 TYR A  200  ILE A  202  5                                   3    
HELIX    5   5 GLU A  223  GLU A  225  5                                   3    
HELIX    6   6 GLN A  226  PHE A  234  1                                   9    
HELIX    7   7 GLU A  236  GLY A  249  1                                  14    
HELIX    8   8 PRO A  280  LEU A  283  5                                   4    
HELIX    9   9 SER A  290  HIS A  299  1                                  10    
HELIX   10  10 THR A  310  ASP A  312  5                                   3    
HELIX   11  11 HIS A  313  GLY A  334  1                                  22    
HELIX   12  12 GLY A  334  GLY A  357  1                                  24    
HELIX   13  13 HIS A  360  LYS A  364  5                                   5    
HELIX   14  14 ASP A  373  TYR A  378  1                                   6    
HELIX   15  15 SER A  380  GLY A  398  1                                  19    
HELIX   16  16 GLY A  399  SER A  415  1                                  17    
HELIX   17  17 THR A  420  PHE A  432  1                                  13    
HELIX   18  18 LYS A  435  ASN A  440  1                                   6    
HELIX   19  19 ASP A  443  SER A  450  1                                   8    
HELIX   20  20 THR A  465  ALA A  478  1                                  14    
HELIX   21  21 LYS A  479  PHE A  486  5                                   8    
HELIX   22  22 ASN A  487  LYS A  492  5                                   6    
HELIX   23  23 SER A  495  GLN A  508  1                                  14    
HELIX   24  24 PRO A  513  ASN A  525  1                                  13    
HELIX   25  25 PHE A  526  ILE A  529  5                                   4    
HELIX   26  26 ASN A  531  SER A  545  1                                  15    
HELIX   27  27 ASP A  549  GLN A  561  1                                  13    
HELIX   28  28 ARG A  563  PHE A  577  1                                  15    
HELIX   29  29 PHE A  577  LYS A  592  1                                  16    
HELIX   30  30 ALA A  593  MET A  595  5                                   3    
HELIX   31  31 HIS A  596  LYS A  608  1                                  13    
SHEET    1   A 8 GLN A  69  GLU A  70  0                                        
SHEET    2   A 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3   A 8 GLU A  99  THR A 108 -1  O  GLU A 103   N  VAL A  65           
SHEET    4   A 8 THR A  33  SER A  44 -1  N  VAL A  42   O  ILE A 100           
SHEET    5   A 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6   A 8 LYS A 153  PRO A 163  1  O  THR A 157   N  LEU A  23           
SHEET    7   A 8 ARG A 186  PRO A 198 -1  O  GLN A 193   N  TYR A 156           
SHEET    8   A 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1   B 3 LEU A  49  THR A  56  0                                        
SHEET    2   B 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3   B 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1   C 4 LEU A 115  LEU A 118  0                                        
SHEET    2   C 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3   C 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4   C 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1   D 5 GLU A 210  GLY A 215  0                                        
SHEET    2   D 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3   D 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4   D 5 LEU A 275  VAL A 278  1  O  VAL A 278   N  LEU A 259           
SHEET    5   D 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1   E 2 VAL A 306  ASN A 308  0                                        
SHEET    2   E 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK        ZN    ZN A 701                 O   ACT A 707     1555   1555  1.89  
LINK         OE2 GLU A 318                ZN    ZN A 701     1555   1555  2.01  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.03  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.04  
LINK         OD2 ASP A 175                YB  A YB A 704     1555   1555  2.08  
LINK        YB  B YB A 705                 O   HOH A1261     1555   1555  2.13  
LINK        YB    YB A 703                 O   ACT A 708     1555   1555  2.17  
LINK        YB    YB A 706                 O   HOH A 825     1555   1555  2.28  
LINK         OD1 ASP A 426                YB  B YB A 705     1555   1555  2.31  
LINK        YB    YB A 706                 O   HOH A 868     1555   1555  2.38  
LINK         OD2 ASP A  47                YB    YB A 703     1555   1555  2.42  
LINK         OD1 ASP A  47                YB    YB A 703     1555   1555  2.46  
LINK         OD1 ASP A 426                YB  A YB A 705     1555   1555  2.52  
LINK        YB    YB A 703                 OXT ACT A 708     1555   1555  2.56  
LINK         OD2 ASP A 481                YB    YB A 706     1555   1555  2.56  
LINK         OD2 ASP A 426                YB  A YB A 705     1555   1555  2.62  
LINK        ZN    ZN A 701                 OXT ACT A 707     1555   1555  2.64  
LINK        YB    YB A 703                 O   HOH A 913     1555   1555  2.64  
LINK         OD1 ASP A 481                YB    YB A 706     1555   1555  2.69  
LINK         OD2 ASP A 175                YB  B YB A 704     1555   1555  2.83  
LINK        YB  B YB A 705                 O   HOH A1256     1555   1555  3.06  
LINK        YB  A YB A 705                 O   HOH A1261     1555   1555  3.13  
LINK         OD1 ASP A 175                YB  A YB A 704     1555   1555  3.38  
CISPEP   1 GLN A  136    ALA A  137          0        -0.32                     
CISPEP   2 ALA A  510    PRO A  511          0        -1.88                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  ACT A 707                    
SITE     1 AC2 17 GLN A 136  TYR A 267  TRP A 311  PHE A 314                    
SITE     2 AC2 17 PHE A 362  LYS A 364  LEU A 365  VAL A 367                    
SITE     3 AC2 17 LEU A 369  PRO A 374  ASP A 375  ALA A 377                    
SITE     4 AC2 17 TYR A 378  VAL A 381  PRO A 382  HOH A 801                    
SITE     5 AC2 17 HOH A 802                                                     
SITE     1 AC3  6 ASP A  47  ASP A 481  ACT A 708  HOH A 825                    
SITE     2 AC3  6 HOH A 868  HOH A 913                                          
SITE     1 AC4  1 ASP A 175                                                     
SITE     1 AC5  3 ASP A 426  HOH A1256  HOH A1261                               
SITE     1 AC6  6 ASP A  47  ASP A 481  ACT A 708  HOH A 825                    
SITE     2 AC6  6 HOH A 868  HOH A 913                                          
SITE     1 AC7 10 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC7 10 HIS A 299  GLU A 318  TYR A 383   ZN A 701                    
SITE     3 AC7 10 HOH A 916  HOH A1259                                          
SITE     1 AC8  8 ASP A  47  LYS A 479  ASP A 481   YB A 703                    
SITE     2 AC8  8  YB A 706  HOH A 825  HOH A 852  HOH A 913                    
SITE     1 AC9  6 GLY A 268  TYR A 378  ARG A 563  LYS A 565                    
SITE     2 AC9  6 HOH A 881  HOH A1207                                          
CRYST1   66.171   76.701   67.215  90.00  98.43  90.00 P 1 21 1      2          
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      0.015112  0.000000  0.002241        0.00000                         
SCALE2      0.000000  0.013038  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015040        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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