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Database: PDB
Entry: 3FUJ
LinkDB: 3FUJ
Original site: 3FUJ 
HEADER    HYDROLASE                               14-JAN-09   3FUJ              
TITLE     LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 5-[2-(1H-PYRROL-1-           
TITLE    2 YL)ETHOXY]-1H-INDOLE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUKOTRIENE A(4) HYDROLASE, LTA-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: BL21-AI/PRARE;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    LEUKOTRIENE A4 HYDROLASE, LTA4H, FRAGMENT CRYSTALLOGRAPHY,            
KEYWDS   2 FRAGMENTS OF LIFE, FOL, ALTERNATIVE SPLICING, CYTOPLASM,             
KEYWDS   3 HYDROLASE, LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING,                  
KEYWDS   4 METALLOPROTEASE, MULTIFUNCTIONAL ENZYME, POLYMORPHISM,               
KEYWDS   5 PROTEASE, ZINC                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.R.DAVIES                                                            
REVDAT   2   15-SEP-09 3FUJ    1       JRNL                                     
REVDAT   1   28-JUL-09 3FUJ    0                                                
JRNL        AUTH   D.R.DAVIES,B.MAMAT,O.T.MAGNUSSON,J.CHRISTENSEN,              
JRNL        AUTH 2 M.H.HARALDSSON,R.MISHRA,B.PEASE,E.HANSEN,J.SINGH,            
JRNL        AUTH 3 D.ZEMBOWER,H.KIM,A.S.KISELYOV,A.B.BURGIN,                    
JRNL        AUTH 4 M.E.GURNEY,L.J.STEWART                                       
JRNL        TITL   DISCOVERY OF LEUKOTRIENE A4 HYDROLASE INHIBITORS             
JRNL        TITL 2 USING METABOLOMICS BIASED FRAGMENT CRYSTALLOGRAPHY.          
JRNL        REF    J.MED.CHEM.                   V.  52  4694 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19618939                                                     
JRNL        DOI    10.1021/JM900259H                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 53163                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2706                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2971                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 166                          
REMARK   3   BIN FREE R VALUE                    : 0.2350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4847                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 410                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.36000                                             
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 1.12000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.138         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.126         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.078         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.552         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5004 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6798 ; 1.453 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   607 ; 5.886 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   221 ;36.142 ;24.389       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   856 ;13.412 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;19.776 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   754 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3774 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  3039 ; 0.787 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4935 ; 1.415 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1965 ; 2.579 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1862 ; 4.188 ; 4.500       
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3FUJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051058.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97000                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3FH7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 8000, 100 MM IMIDAZOLE PH        
REMARK 280  6.5, 100 MM NA ACETATE, 5 MM YBCL3, CRYSTAL SOAKED OVERNIGHT        
REMARK 280  WITH 15 MM 5-[2-(1H-PYRROL-1-YL)ETHOXY]-1H-INDOLE, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.25800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.80450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.69750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.80450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.25800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.69750            
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     MET A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ASP A   610                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   245     O    HOH A   994              1.85            
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       69.29   -113.37                                   
REMARK 500    SER A  80     -133.05     51.07                                   
REMARK 500    ASN A  97       -4.85     81.50                                   
REMARK 500    SER A 112      123.29    -39.43                                   
REMARK 500    ASP A 183       96.81   -170.64                                   
REMARK 500    PRO A 184       -9.52    -58.74                                   
REMARK 500    GLU A 271       42.02    -80.65                                   
REMARK 500    CYS A 274      -15.60     71.16                                   
REMARK 500    PHE A 432       43.32    -98.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     VAL A 585        21.9      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2 102.5                                              
REMARK 620 3 GLU A 318   OE1  98.1 105.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   CG                                                     
REMARK 620 2 ASP A 481   OD1  26.6                                              
REMARK 620 3 ASP A 481   OD2  27.1  53.7                                        
REMARK 620 4 ACT A 801   OXT  77.0  74.8  80.4                                  
REMARK 620 5 HOH A 795   O   105.4  78.8 132.4  90.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 702                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 00G A 710                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 801                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 802                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 803                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FH7   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH INHIBITOR 4-[(2S)-          
REMARK 900 2-{[4-(4-CHLOROPHENOXY)PHENOXY]METHYL}PYRROLIDIN-1-YL]               
REMARK 900 BUTANOATE                                                            
REMARK 900 RELATED ID: 3FTS   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH RESVERATROL                 
REMARK 900 RELATED ID: 3FTU   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH DIHYDRORESVERATROL          
REMARK 900 RELATED ID: 3FTV   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT N-                 
REMARK 900 (PYRIDIN-3-YLMETHYL)ANILINE                                          
REMARK 900 RELATED ID: 3FTW   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENTS N-                
REMARK 900 (PYRIDIN-3-YLMETHYL)ANILINE AND ACETATE                              
REMARK 900 RELATED ID: 3FTX   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH DIHYDRORESVERATROL          
REMARK 900 AND BESTATIN                                                         
REMARK 900 RELATED ID: 3FTY   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 3-                 
REMARK 900 (BENZYLOXY)PYRIDIN-2-AMINE                                           
REMARK 900 RELATED ID: 3FTZ   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 2-                 
REMARK 900 (PYRIDIN-3-YLMETHOXY)ANILINE                                         
REMARK 900 RELATED ID: 3FU0   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 4-(4-              
REMARK 900 FLUOROBENZOYL)PYRIDINE                                               
REMARK 900 RELATED ID: 3FU3   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 4-(2-              
REMARK 900 AMINO-1,3-THIAZOL-4-YL)PHENOL                                        
REMARK 900 RELATED ID: 3FU5   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (5-THIOPHEN-2-              
REMARK 900 YLTHIOPHEN-2-YL)METHYLAMINE                                          
REMARK 900 RELATED ID: 3FU6   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT (4-                
REMARK 900 THIOPHEN-2-YLPHENYL)METHANAMINE                                      
REMARK 900 RELATED ID: 3FUD   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N-METHYL-1-(2-              
REMARK 900 THIOPHEN-2-YLPHENYL)METHANAMINE                                      
REMARK 900 RELATED ID: 3FUE   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-                 
REMARK 900 CHLOROINDOLE AND BESTATIN                                            
REMARK 900 RELATED ID: 3FUF   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-                 
REMARK 900 FLUOROINDOLE AND BESTATIN                                            
REMARK 900 RELATED ID: 3FUH   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-                 
REMARK 900 HYDROXYINDOLE AND BESTATIN                                           
REMARK 900 RELATED ID: 3FUI   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N-BENZYL-4-[(2R)-           
REMARK 900 PYRROLIDIN-2-YLMETHOXY]ANILINE                                       
REMARK 900 RELATED ID: 3FUK   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 1-[2-(1H-INDOL-5-           
REMARK 900 YLOXY)ETHYL]PIPERIDINE-4-CARBOXYLIC ACID                             
REMARK 900 RELATED ID: 3FUL   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH PYRIDIN-4-YL[4-(2-          
REMARK 900 PYRROLIDIN-1-YLETHOXY)PHENYL]METHANONE                               
REMARK 900 RELATED ID: 3FUM   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (R)-PYRIDIN-4-              
REMARK 900 YL[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]METHANOL                        
REMARK 900 RELATED ID: 3FUN   RELATED DB: PDB                                   
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH {4-[(2R)-                   
REMARK 900 PYRROLIDIN-2-YLMETHOXY]PHENYL}(4-THIOPHEN-3-YLPHENYL)                
REMARK 900 METHANONE                                                            
DBREF  3FUJ 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     YB  A 702       1                                                       
HET    00G  A 710      17                                                       
HET    ACT  A 801       4                                                       
HET    IMD  A 802       5                                                       
HET    IMD  A 803       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     00G 5-[2-(1H-PYRROL-1-YL)ETHOXY]-1H-INDOLE                           
HETNAM     ACT ACETATE ION                                                      
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    YB 3+                                                        
FORMUL   4  00G    C14 H14 N2 O                                                 
FORMUL   5  ACT    C2 H3 O2 1-                                                  
FORMUL   6  IMD    2(C3 H5 N2 1+)                                               
FORMUL   8  HOH   *410(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 PRO A  198  ILE A  202  5                                   5    
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  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 LEU A 154  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7   A 8 ARG A 186  ILE A 197 -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  SER A 222   N  GLU A 210           
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         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.16  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.19  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.13  
LINK         CG  ASP A 481                YB    YB A 702     1555   1555  2.78  
LINK         OD1 ASP A 481                YB    YB A 702     1555   1555  2.48  
LINK         OD2 ASP A 481                YB    YB A 702     1555   1555  2.40  
LINK        YB    YB A 702                 OXT ACT A 801     1555   1555  2.40  
LINK        YB    YB A 702                 O   HOH A 795     1555   1555  2.40  
CISPEP   1 GLN A  136    ALA A  137          0        -2.36                     
CISPEP   2 ALA A  510    PRO A  511          0         6.97                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  HOH A 884                    
SITE     1 AC2  5 ASP A  47  ASP A 481  HOH A 795  ACT A 801                    
SITE     2 AC2  5 HOH A 806                                                     
SITE     1 AC3  8 GLN A 136  ALA A 137  TYR A 267  TRP A 311                    
SITE     2 AC3  8 PHE A 314  PRO A 374  TYR A 378  TYR A 383                    
SITE     1 AC4  5 ASP A  47  LYS A 479  ASP A 481  HOH A 680                    
SITE     2 AC4  5  YB A 702                                                     
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  8 SER A 288  LEU A 289  SER A 496  HIS A 497                    
SITE     2 AC6  8 ASN A 500  ASN A 531  GLU A 533  HOH A 979                    
CRYST1   78.516   87.395   99.609  90.00  90.00  90.00 P 21 21 21    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      0.012736  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010039        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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