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Database: PDB
Entry: 3CHQ
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HEADER    HYDROLASE                               10-MAR-08   3CHQ              
TITLE     CRYSTAL STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N5-[4-  
TITLE    2 (PHENYLMETHOXY)PHENYL]-L-GLUTAMINE                                   
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: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT3-MB4                                   
KEYWDS    EPOXIDE HYDROLASE, ALPHA-BETA PROTEIN, LEUKOTRIENE BIOSYNTHESIS,      
KEYWDS   2 METALLOPROTEASE, INHIBITOR COMPLEX, ALTERNATIVE SPLICING, CYTOPLASM, 
KEYWDS   3 METAL-BINDING, MULTIFUNCTIONAL ENZYME, ZINC, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.G.M.THUNNISSEN,M.ADLER,M.WHITLOW                                  
REVDAT   4   20-NOV-19 3CHQ    1       LINK                                     
REVDAT   3   24-FEB-09 3CHQ    1       VERSN                                    
REVDAT   2   27-MAY-08 3CHQ    1       JRNL                                     
REVDAT   1   22-APR-08 3CHQ    0                                                
JRNL        AUTH   T.A.KIRKLAND,M.ADLER,J.G.BAUMAN,M.CHEN,J.Z.HAEGGSTROM,       
JRNL        AUTH 2 B.KING,M.J.KOCHANNY,A.M.LIANG,L.MENDOZA,G.B.PHILLIPS,        
JRNL        AUTH 3 M.THUNNISSEN,L.TRINH,M.WHITLOW,B.YE,H.YE,J.PARKINSON,        
JRNL        AUTH 4 W.J.GUILFORD                                                 
JRNL        TITL   SYNTHESIS OF GLUTAMIC ACID ANALOGS AS POTENT INHIBITORS OF   
JRNL        TITL 2 LEUKOTRIENE A4 HYDROLASE.                                    
JRNL        REF    BIOORG.MED.CHEM.              V.  16  4963 2008              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   18394906                                                     
JRNL        DOI    10.1016/J.BMC.2008.03.042                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.M.G.M.THUNNISSEN,P.N.NORDLUND,J.Z.HAEGGSTROM               
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE, A       
REMARK   1  TITL 2 BIFUNCTIONAL ENZYME IN INFLAMMATION                          
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   8   131 2001              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.M.G.M.THUNNISSEN,B.ANDERSON,B.SAMUELSSON,C.-H.WONG,        
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   CRYSTAL STRUCTURES OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX    
REMARK   1  TITL 2 WITH CAPTOPRIL AND TWO COMPETITIVE TIGHT-BINDING INHIBITORS. 
REMARK   1  REF    FASEB J.                      V.  16  1648 2002              
REMARK   1  REFN                   ISSN 0892-6638                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,B.SAMUELSSON,         
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: SELECTIVE ABROGATION OF            
REMARK   1  TITL 2 LEUKOTRIENE B4 FORMATION BY MUTATION OF ASPARTIC ACID 375.   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  99  4215 2002              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.O.T.THOLANDER,M.ANDBERG,M.M.G.M.THUNNISSEN,    
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON         
REMARK   1  TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND   
REMARK   1  TITL 3 AMINOPEPTIDASE SUBSTRATES                                    
REMARK   1  REF    J.MOL.BIOL.                   V. 279 27376 2004              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2124152.530                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 45307                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1749                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : NULL                 
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.09                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4252                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE                    : 0.2924                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 148                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
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          : 33                                      
REMARK   3   SOLVENT ATOMS            : 344                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28000                                             
REMARK   3    B22 (A**2) : 0.61000                                              
REMARK   3    B33 (A**2) : -0.33000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.650                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.720 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.320 ; 2.050                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.720 ; 2.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.720 ; 3.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 52.39                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ZN.PARAM                                       
REMARK   3  PARAMETER FILE  5  : 420.PARAM                                      
REMARK   3  PARAMETER FILE  6  : IMD.PARAM                                      
REMARK   3  PARAMETER FILE  7  : ACE.PARAM                                      
REMARK   3  PARAMETER FILE  8  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ZN.TOP                                         
REMARK   3  TOPOLOGY FILE  5   : 420.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : IMD.TOP                                        
REMARK   3  TOPOLOGY FILE  7   : ACE.TOP                                        
REMARK   3  TOPOLOGY FILE  8   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 91.6                               
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46299                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, IMIDEAZOLE     
REMARK 280  PH 6.8, YBCL2, BESTATIN, LIQUID DIFFUSION, TEMPERATURE 298K,PH      
REMARK 280  8.00                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       34.11700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.63100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.11700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.63100            
REMARK 290   SMTRY3   4  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     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A   610                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1315     O    HOH A  1315     2665     1.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  80     -122.75     40.00                                   
REMARK 500    GLU A 182       42.30    -78.27                                   
REMARK 500    ASP A 183      -85.21    106.81                                   
REMARK 500    SER A 185       44.33    -71.19                                   
REMARK 500    GLU A 271       45.72    -79.42                                   
REMARK 500    CYS A 274      -14.03     78.10                                   
REMARK 500    LEU A 275       84.72   -153.64                                   
REMARK 500    PHE A 432       45.33   -102.17                                   
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                              YB A 803  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 107   OE1                                                    
REMARK 620 2 GLU A 107   OE2  50.4                                              
REMARK 620 3 GLU A 127   OE1  69.2  96.2                                        
REMARK 620 4 GLU A 127   OE2  69.6  98.1   2.4                                  
REMARK 620 N                    1     2     3                                   
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 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 105.2                                              
REMARK 620 3 GLU A 318   OE1 104.3 110.4                                        
REMARK 620 4 4BQ A 901   O1  108.5 118.3 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 801  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD1                                                    
REMARK 620 2 ASP A 481   OD2  51.2                                              
REMARK 620 3 HOH A1582   O    82.0  76.3                                        
REMARK 620 4 HOH A1583   O   126.3  75.2  82.5                                  
REMARK 620 5 HOH A1585   O    83.2  73.3 149.1  84.7                            
REMARK 620 6 ASP A 422   OD1 144.9  94.7  81.4  20.3  95.8                      
REMARK 620 7 ASP A 422   OD2 146.0  95.8  81.8  21.4  96.0   1.2                
REMARK 620 8 ASP A 426   OD2 145.9  96.4  79.4  22.8  98.7   3.1   2.7          
REMARK 620 N                    1     2     3     4     5     6     7           
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 YB A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4BQ A 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HS6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN        
REMARK 900 RELATED ID: 1GW6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT                   
REMARK 900 RELATED ID: 1H19   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE E271Q MUTANT                   
REMARK 900 RELATED ID: 1SQM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE R563A MUTANT                   
REMARK 900 RELATED ID: 3CHO   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 2-AMINO-N-[4-  
REMARK 900 (PHENYLMETHOXY)PHENYL]-ACETAMIDE                                     
REMARK 900 RELATED ID: 3CHP   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (3S)-3-AMINO-  
REMARK 900 4-OXO-4-[(4-PHENYLMETHOXYPHENYL)AMINO]BUTANOIC ACID                  
REMARK 900 RELATED ID: 3CHR   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 4-AMINO-N-[4-  
REMARK 900 (PHENYLMETHOXY)PHENYL]-BUTANAMIDE                                    
REMARK 900 RELATED ID: 3CHS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (2S)-2-AMINO-  
REMARK 900 5-[[4-[(2S)-2-HYDROXY-2-PHENYL-ETHOXY]PHENYL]AMINO]-5-OXO-PENTANOIC  
REMARK 900 ACID                                                                 
REMARK 900 RELATED ID: 2VJ8   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH HYDROXAMIC     
REMARK 900 ACID BASED INHIBITOR                                                 
DBREF  3CHQ A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQRES   1 A  610  PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO ALA          
SEQRES   2 A  610  SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS SER          
SEQRES   3 A  610  VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA ALA          
SEQRES   4 A  610  LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER LEU          
SEQRES   5 A  610  VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL VAL          
SEQRES   6 A  610  ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU ARG          
SEQRES   7 A  610  GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU PRO          
SEQRES   8 A  610  ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU ILE          
SEQRES   9 A  610  SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN TRP          
SEQRES  10 A  610  LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO TYR          
SEQRES  11 A  610  LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA ILE          
SEQRES  12 A  610  LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR TYR          
SEQRES  13 A  610  THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA LEU          
SEQRES  14 A  610  MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO GLU          
SEQRES  15 A  610  ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS VAL          
SEQRES  16 A  610  PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY ALA          
SEQRES  17 A  610  LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL TRP          
SEQRES  18 A  610  SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU PHE          
SEQRES  19 A  610  SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP LEU          
SEQRES  20 A  610  GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU VAL          
SEQRES  21 A  610  LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN PRO          
SEQRES  22 A  610  CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY ASP          
SEQRES  23 A  610  LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER HIS          
SEQRES  24 A  610  SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP ASP          
SEQRES  25 A  610  HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU GLU          
SEQRES  26 A  610  ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE ARG          
SEQRES  27 A  610  HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN ASN          
SEQRES  28 A  610  SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR LYS          
SEQRES  29 A  610  LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL ALA          
SEQRES  30 A  610  TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU LEU          
SEQRES  31 A  610  PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE PHE          
SEQRES  32 A  610  LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER TYR          
SEQRES  33 A  610  LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU TYR          
SEQRES  34 A  610  SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN VAL          
SEQRES  35 A  610  ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO PRO          
SEQRES  36 A  610  ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA CYS          
SEQRES  37 A  610  ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU ASP          
SEQRES  38 A  610  ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP LEU          
SEQRES  39 A  610  SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR LEU          
SEQRES  40 A  610  GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG MET          
SEQRES  41 A  610  GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER GLU          
SEQRES  42 A  610  ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER LYS          
SEQRES  43 A  610  TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA THR          
SEQRES  44 A  610  GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE LYS          
SEQRES  45 A  610  ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA VAL          
SEQRES  46 A  610  ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO VAL          
SEQRES  47 A  610  THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP              
HET     ZN  A 701       1                                                       
HET     YB  A 801       1                                                       
HET     YB  A 802       1                                                       
HET     YB  A 803       1                                                       
HET    IMD  A 850       5                                                       
HET    4BQ  A 901      24                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     4BQ (2S)-2-AMINO-5-OXO-5-[(4-PHENYLMETHOXYPHENYL)                    
HETNAM   2 4BQ  AMINO]PENTANOIC ACID                                            
HETSYN     4BQ N-[4-(PHENYLMETHOXY)PHENYL]-L-GLUTAMINE                          
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    3(YB 3+)                                                     
FORMUL   6  IMD    C3 H5 N2 1+                                                  
FORMUL   7  4BQ    C18 H20 N2 O4                                                
FORMUL   8  HOH   *344(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  PHE A  234  1                                  12    
HELIX    6   6 GLU A  236  GLY A  249  1                                  14    
HELIX    7   7 PRO A  280  LEU A  283  5                                   4    
HELIX    8   8 SER A  290  HIS A  299  1                                  10    
HELIX    9   9 THR A  310  ASP A  312  5                                   3    
HELIX   10  10 HIS A  313  GLY A  334  1                                  22    
HELIX   11  11 GLY A  334  GLY A  357  1                                  24    
HELIX   12  12 HIS A  360  LYS A  364  5                                   5    
HELIX   13  13 ASP A  373  TYR A  378  1                                   6    
HELIX   14  14 SER A  380  LEU A  397  1                                  18    
HELIX   15  15 GLY A  399  SER A  415  1                                  17    
HELIX   16  16 THR A  420  PHE A  432  1                                  13    
HELIX   17  17 LYS A  435  ASN A  440  1                                   6    
HELIX   18  18 ASP A  443  SER A  450  1                                   8    
HELIX   19  19 THR A  465  ALA A  478  1                                  14    
HELIX   20  20 LYS A  479  PHE A  486  5                                   8    
HELIX   21  21 ASN A  487  LYS A  492  5                                   6    
HELIX   22  22 SER A  495  GLN A  508  1                                  14    
HELIX   23  23 PRO A  513  ASN A  525  1                                  13    
HELIX   24  24 PHE A  526  ILE A  529  5                                   4    
HELIX   25  25 ASN A  531  SER A  545  1                                  15    
HELIX   26  26 TRP A  547  ASP A  549  5                                   3    
HELIX   27  27 ALA A  550  GLN A  561  1                                  12    
HELIX   28  28 ARG A  563  PHE A  577  1                                  15    
HELIX   29  29 SER A  580  LYS A  592  1                                  13    
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 107   N  THR A  60           
SHEET    4   A 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
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  SER A 161   N  VAL A  27           
SHEET    7   A 8 ARG A 186  PRO A 198 -1  O  LYS A 187   N  VAL A 162           
SHEET    8   A 8 ILE A 173  PRO A 179 -1  N  ASP A 175   O  LYS A 190           
SHEET    1   B 3 LEU A  49  THR A  56  0                                        
SHEET    2   B 3 SER A  84  LEU A  94 -1  O  LEU A  90   N  ARG A  50           
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  VAL A 260   N  TRP A 221           
SHEET    4   D 5 LEU A 275  VAL A 278  1  O  THR A 276   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         OE1 GLU A 107                YB    YB A 803     1555   1555  2.36  
LINK         OE2 GLU A 107                YB    YB A 803     1555   1555  2.74  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.16  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.12  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.05  
LINK         OD1 ASP A 481                YB    YB A 801     1555   1555  2.36  
LINK         OD2 ASP A 481                YB    YB A 801     1555   1555  2.68  
LINK        ZN    ZN A 701                 O1  4BQ A 901     1555   1555  2.15  
LINK        YB    YB A 801                 O   HOH A1582     1555   1555  2.34  
LINK        YB    YB A 801                 O   HOH A1583     1555   1555  2.44  
LINK        YB    YB A 801                 O   HOH A1585     1555   1555  2.52  
LINK         OE1 GLU A 127                YB    YB A 803     1555   2565  3.30  
LINK         OE1 GLU A 127                YB    YB A 802     1555   2565  2.46  
LINK         OE2 GLU A 127                YB    YB A 803     1555   2565  2.57  
LINK         OD1 ASP A 422                YB    YB A 801     1555   4457  2.54  
LINK         OD2 ASP A 422                YB    YB A 801     1555   4457  2.49  
LINK         OD2 ASP A 426                YB    YB A 801     1555   4457  2.51  
CISPEP   1 GLN A  136    ALA A  137          0         2.26                     
CISPEP   2 ALA A  510    PRO A  511          0         1.11                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  TYR A 383                    
SITE     1 AC2  6 ASP A 422  ASP A 426  ASP A 481  HOH A1582                    
SITE     2 AC2  6 HOH A1583  HOH A1585                                          
SITE     1 AC3  1 GLU A 127                                                     
SITE     1 AC4  2 GLU A 107  GLU A 127                                          
SITE     1 AC5  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC5  6 ALA A 504  GLN A 508                                          
SITE     1 AC6 16 GLN A 136  ALA A 137  TYR A 267  GLY A 269                    
SITE     2 AC6 16 GLU A 271  HIS A 295  GLU A 296  HIS A 299                    
SITE     3 AC6 16 TRP A 311  PHE A 314  GLU A 318  PRO A 374                    
SITE     4 AC6 16 ASP A 375  ALA A 377  TYR A 378  TYR A 383                    
CRYST1   68.234  133.262   84.591  90.00  90.00  90.00 P 21 21 2     4          
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      0.014655  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011822        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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