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Database: PDB
Entry: 6ENC
LinkDB: 6ENC
Original site: 6ENC 
HEADER    HYDROLASE                               04-OCT-17   6ENC              
TITLE     LTA4 HYDROLASE IN COMPLEX WITH COMPOUND11                             
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                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    LTA4H, INHIBITOR, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SRINIVAS                                                            
REVDAT   3   16-OCT-19 6ENC    1       REMARK                                   
REVDAT   2   31-JAN-18 6ENC    1       AUTHOR                                   
REVDAT   1   13-DEC-17 6ENC    0                                                
JRNL        AUTH   S.NUMAO,F.HASLER,C.LAGUERRE,H.SRINIVAS,N.WACK,P.JAGER,       
JRNL        AUTH 2 A.SCHMID,A.OSMONT,P.ROTHLISBERGER,J.HOUGUENADE,C.BERGSDORF,  
JRNL        AUTH 3 J.DAWSON,N.CARTE,A.HOFMANN,C.MARKERT,L.HARDAKER,A.BILLICH,   
JRNL        AUTH 4 R.M.WOLF,C.A.PENNO,B.BOLLBUCK,W.MILTZ,T.A.ROHN               
JRNL        TITL   FEASIBILITY AND PHYSIOLOGICAL RELEVANCE OF DESIGNING HIGHLY  
JRNL        TITL 2 POTENT AMINOPEPTIDASE-SPARING LEUKOTRIENE A4 HYDROLASE       
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    SCI REP                       V.   7 13591 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29051536                                                     
JRNL        DOI    10.1038/S41598-017-13490-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49716                          
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)  : 0.163                          
REMARK   3   R VALUE            (WORKING SET)  : 0.161                          
REMARK   3   FREE R VALUE                      : 0.195                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2486                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.95                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.00                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.53                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3592                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1935                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3413                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1913                   
REMARK   3   BIN FREE R VALUE                        : 0.2326                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.98                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 179                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4854                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 691                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.25450                                              
REMARK   3    B22 (A**2) : 4.81770                                              
REMARK   3    B33 (A**2) : -7.07220                                             
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) : 0.181               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.156               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.132               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.142               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.127               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5028   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6835   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1716   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 120    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 726    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5028   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 651    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6232   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.52                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.48                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   34.7078    3.6926   -0.1582           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0339 T22:   -0.0395                                    
REMARK   3     T33:   -0.0341 T12:   -0.0060                                    
REMARK   3     T13:   -0.0046 T23:    0.0018                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2567 L22:    0.5574                                    
REMARK   3     L33:    0.1855 L12:   -0.0311                                    
REMARK   3     L13:    0.0190 L23:   -0.0488                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0105 S12:    0.0027 S13:   -0.0097                     
REMARK   3     S21:   -0.0395 S22:    0.0105 S23:    0.0277                     
REMARK   3     S31:    0.0290 S32:   -0.0086 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ENC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006892.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49717                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.1 IMIDAZOLE PH 6.8,      
REMARK 280  0.1 SODIUM ACETATE, 0.005 M YBCL3, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 298K                                                    
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       39.03150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.57700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.58750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.57700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.03150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.58750            
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 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
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     GLY A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 437    CG   OD1  OD2                                       
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   CE2  TYR A   383     O    HOH A   803              2.01            
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       65.74   -112.68                                   
REMARK 500    SER A  80     -130.44     50.35                                   
REMARK 500    ASN A  97       -4.89     79.78                                   
REMARK 500    GLU A 271       42.57    -74.15                                   
REMARK 500    CYS A 274      -20.74     79.03                                   
REMARK 500    TRP A 301      -61.41   -109.89                                   
REMARK 500    PHE A 432       35.70    -97.26                                   
REMARK 500    PRO A 458      174.21    -58.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1490        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH A1491        DISTANCE = 10.09 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 704  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD1                                                    
REMARK 620 2 HOH A1236   O   144.4                                              
REMARK 620 N                    1                                               
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  89.6                                              
REMARK 620 3 GLU A 318   OE1  87.6  93.4                                        
REMARK 620 4 GLU A 318   OE2 139.8  84.2  53.3                                  
REMARK 620 5 BGW A 707   O8  133.0 132.7 105.9  74.5                            
REMARK 620 6 BGW A 707   O9   95.4 108.9 157.5 124.2  56.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD1                                                    
REMARK 620 2 ASP A 481   OD2  53.4                                              
REMARK 620 3 ACT A 702   O    72.9  77.4                                        
REMARK 620 4 ACT A 702   OXT 114.8 128.0  53.0                                  
REMARK 620 5 HOH A 808   O    80.6 133.9  93.8  70.7                            
REMARK 620 6 HOH A1008   O    75.7  87.3 148.3 143.2  77.0                      
REMARK 620 7 HOH A1169   O   153.4 145.7 122.1  70.3  76.8  85.7                
REMARK 620 8 ASP A  47   OD1  72.9 125.8  81.0  65.8  13.4  86.1  87.2          
REMARK 620 9 ASP A  47   OD2  73.4 126.1  79.8  64.4  14.4  87.5  87.1   1.5    
REMARK 620 N                    1     2     3     4     5     6     7     8     
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 ACT A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BGW A 707                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6ENB   RELATED DB: PDB                                   
DBREF  6ENC A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 6ENC GLY A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 6ENC PRO A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 6ENC GLY A    0  UNP  P09960              EXPRESSION TAG                 
SEQRES   1 A  613  GLY PRO GLY PRO GLU ILE VAL ASP THR CYS SER LEU ALA          
SEQRES   2 A  613  SER PRO ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU          
SEQRES   3 A  613  ARG CYS SER VAL ASP PHE THR ARG ARG THR LEU THR GLY          
SEQRES   4 A  613  THR ALA ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU          
SEQRES   5 A  613  ARG SER LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU          
SEQRES   6 A  613  LYS VAL VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU          
SEQRES   7 A  613  GLY GLU ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE          
SEQRES   8 A  613  SER LEU PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL          
SEQRES   9 A  613  ILE GLU ILE SER PHE GLU THR SER PRO LYS SER SER ALA          
SEQRES  10 A  613  LEU GLN TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU          
SEQRES  11 A  613  HIS PRO TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS          
SEQRES  12 A  613  ARG ALA ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS          
SEQRES  13 A  613  LEU THR TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU          
SEQRES  14 A  613  VAL ALA LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO          
SEQRES  15 A  613  ASP PRO GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE          
SEQRES  16 A  613  GLN LYS VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL          
SEQRES  17 A  613  VAL GLY ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR          
SEQRES  18 A  613  LEU VAL TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA          
SEQRES  19 A  613  TYR GLU PHE SER GLU THR GLU SER MET LEU LYS ILE ALA          
SEQRES  20 A  613  GLU ASP LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP          
SEQRES  21 A  613  LEU LEU VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET          
SEQRES  22 A  613  GLU ASN PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU          
SEQRES  23 A  613  ALA GLY ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU          
SEQRES  24 A  613  ILE SER HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS          
SEQRES  25 A  613  THR TRP ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL          
SEQRES  26 A  613  TYR LEU GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU          
SEQRES  27 A  613  LYS PHE ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU          
SEQRES  28 A  613  LEU GLN ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO          
SEQRES  29 A  613  PHE THR LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO          
SEQRES  30 A  613  ASP VAL ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE          
SEQRES  31 A  613  ALA LEU LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO          
SEQRES  32 A  613  GLU ILE PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS          
SEQRES  33 A  613  PHE SER TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP          
SEQRES  34 A  613  PHE LEU TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU          
SEQRES  35 A  613  ASN GLN VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY          
SEQRES  36 A  613  LEU PRO PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR          
SEQRES  37 A  613  ASN ALA CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA          
SEQRES  38 A  613  LYS GLU ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU          
SEQRES  39 A  613  LYS ASP LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA          
SEQRES  40 A  613  GLN THR LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE          
SEQRES  41 A  613  LYS ARG MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN          
SEQRES  42 A  613  ASN SER GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE          
SEQRES  43 A  613  GLN SER LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS          
SEQRES  44 A  613  MET ALA THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO          
SEQRES  45 A  613  LEU PHE LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP          
SEQRES  46 A  613  GLN ALA VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET          
SEQRES  47 A  613  HIS PRO VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS          
SEQRES  48 A  613  VAL ASP                                                      
HET     ZN  A 701       1                                                       
HET    ACT  A 702       4                                                       
HET     YB  A 703       1                                                       
HET     YB  A 704       1                                                       
HET    IMD  A 705       5                                                       
HET    IMD  A 706       5                                                       
HET    BGW  A 707      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     BGW 1-[[4-(1,3-BENZOTHIAZOL-2-YLOXY)                                 
HETNAM   2 BGW  PHENYL]METHYL]PIPERIDINE-4-CARBOXYLIC ACID                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4   YB    2(YB 3+)                                                     
FORMUL   6  IMD    2(C3 H5 N2 1+)                                               
FORMUL   8  BGW    C20 H20 N2 O3 S                                              
FORMUL   9  HOH   *691(H2 O)                                                    
HELIX    1 AA1 GLN A   79  GLY A   83  5                                   5    
HELIX    2 AA2 THR A  119  THR A  123  5                                   5    
HELIX    3 AA3 HIS A  139  ILE A  143  5                                   5    
HELIX    4 AA4 PRO A  198  ILE A  202  5                                   5    
HELIX    5 AA5 GLU A  223  GLU A  225  5                                   3    
HELIX    6 AA6 GLN A  226  PHE A  234  1                                   9    
HELIX    7 AA7 GLU A  236  GLY A  249  1                                  14    
HELIX    8 AA8 PRO A  280  LEU A  283  5                                   4    
HELIX    9 AA9 SER A  290  HIS A  299  1                                  10    
HELIX   10 AB1 THR A  310  HIS A  313  5                                   4    
HELIX   11 AB2 PHE A  314  GLY A  334  1                                  21    
HELIX   12 AB3 GLY A  334  GLY A  357  1                                  24    
HELIX   13 AB4 HIS A  360  LYS A  364  5                                   5    
HELIX   14 AB5 ASP A  373  TYR A  378  1                                   6    
HELIX   15 AB6 SER A  380  GLY A  398  1                                  19    
HELIX   16 AB7 GLY A  399  SER A  415  1                                  17    
HELIX   17 AB8 THR A  420  PHE A  432  1                                  13    
HELIX   18 AB9 LYS A  435  ASN A  440  1                                   6    
HELIX   19 AC1 ASP A  443  SER A  450  1                                   8    
HELIX   20 AC2 THR A  465  ALA A  478  1                                  14    
HELIX   21 AC3 LYS A  479  PHE A  486  5                                   8    
HELIX   22 AC4 ASN A  487  LYS A  492  5                                   6    
HELIX   23 AC5 SER A  495  GLN A  508  1                                  14    
HELIX   24 AC6 PRO A  513  ASN A  525  1                                  13    
HELIX   25 AC7 PHE A  526  ILE A  529  5                                   4    
HELIX   26 AC8 ASN A  531  SER A  545  1                                  15    
HELIX   27 AC9 TRP A  547  ASP A  549  5                                   3    
HELIX   28 AD1 ALA A  550  GLN A  561  1                                  12    
HELIX   29 AD2 ARG A  563  PHE A  577  1                                  15    
HELIX   30 AD3 SER A  580  LYS A  592  1                                  13    
HELIX   31 AD4 ALA A  593  MET A  595  5                                   3    
HELIX   32 AD5 HIS A  596  LYS A  608  1                                  13    
SHEET    1 AA1 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA1 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA1 8 GLU A  99  THR A 108 -1  O  GLU A 103   N  VAL A  65           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  VAL A  42   O  ILE A 100           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6 AA1 8 LEU A 154  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7 AA1 8 ASP A 183  ILE A 197 -1  O  GLN A 193   N  TYR A 156           
SHEET    8 AA1 8 ILE A 173  ASP A 180 -1  N  THR A 178   O  ILE A 188           
SHEET    1 AA2 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA2 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA2 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA3 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA3 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3 AA3 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA3 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1 AA4 5 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3 AA4 5 ASP A 257  VAL A 260  1  O  VAL A 260   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  VAL A 278   N  LEU A 259           
SHEET    5 AA4 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1 AA5 2 THR A 307  ASN A 308  0                                        
SHEET    2 AA5 2 SER A 418  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OD1 ASP A 175                YB    YB A 704     1555   1555  2.31  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.28  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.24  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.08  
LINK         OE2 GLU A 318                ZN    ZN A 701     1555   1555  2.67  
LINK         OD1 ASP A 481                YB    YB A 703     1555   1555  2.43  
LINK         OD2 ASP A 481                YB    YB A 703     1555   1555  2.54  
LINK        ZN    ZN A 701                 O8  BGW A 707     1555   1555  2.15  
LINK        ZN    ZN A 701                 O9  BGW A 707     1555   1555  2.57  
LINK         O   ACT A 702                YB    YB A 703     1555   1555  2.42  
LINK         OXT ACT A 702                YB    YB A 703     1555   1555  2.54  
LINK        YB    YB A 703                 O   HOH A 808     1555   1555  2.38  
LINK        YB    YB A 703                 O   HOH A1008     1555   1555  2.36  
LINK        YB    YB A 703                 O   HOH A1169     1555   1555  2.57  
LINK         OD1 ASP A  47                YB    YB A 703     1555   1545  2.44  
LINK         OD2 ASP A  47                YB    YB A 703     1555   1545  2.32  
LINK        YB    YB A 704                 O   HOH A1236     1555   4545  2.74  
CISPEP   1 GLN A  136    ALA A  137          0         1.23                     
CISPEP   2 ALA A  510    PRO A  511          0         1.85                     
SITE     1 AC1  6 HIS A 295  HIS A 299  GLU A 318  TYR A 383                    
SITE     2 AC1  6 BGW A 707  HOH A 803                                          
SITE     1 AC2  9 ASP A  47  ASN A  48  ARG A 174  LYS A 479                    
SITE     2 AC2  9 ASP A 481   YB A 703  HOH A 808  HOH A 835                    
SITE     3 AC2  9 HOH A1169                                                     
SITE     1 AC3  6 ASP A  47  ASP A 481  ACT A 702  HOH A 808                    
SITE     2 AC3  6 HOH A1008  HOH A1169                                          
SITE     1 AC4  2 ASP A 175  HOH A1236                                          
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  7 SER A 288  LEU A 289  SER A 496  HIS A 497                    
SITE     2 AC6  7 ASN A 500  ASN A 531  GLU A 533                               
SITE     1 AC7 19 GLN A 136  TYR A 267  GLY A 269  MET A 270                    
SITE     2 AC7 19 GLU A 271  HIS A 295  GLU A 296  TRP A 311                    
SITE     3 AC7 19 PHE A 314  GLU A 318  VAL A 367  LEU A 369                    
SITE     4 AC7 19 PRO A 374  ASP A 375  ALA A 377  TYR A 378                    
SITE     5 AC7 19 TYR A 383   ZN A 701  HOH A 807                               
CRYST1   78.063   87.175   99.154  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      0.012810  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010085        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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