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Database: PDB
Entry: 5AEN
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HEADER    HYDROLASE                               06-JAN-15   5AEN              
TITLE     STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH INHIBITOR 
TITLE    2 DIMETHYL(2- (4-PHENOXYPHENOXY)ETHYL)AMINE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A4 HYDROLASE, LEUKOTRIENE A(4);
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET 24                                     
KEYWDS    HYDROLASE, LEUKOTRIENE (LT) A4 HYDROLASE/AMINOPEPTIDASE, LTA4H        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.MOSER,S.K.WITTMANN,J.KRAMER,R.BLOCHER,J.ACHENBACH,D.POGORYELOV,     
AUTHOR   2 E.PROSCHAK                                                           
REVDAT   3   27-FEB-19 5AEN    1       REMARK                                   
REVDAT   2   11-MAR-15 5AEN    1       JRNL                                     
REVDAT   1   11-FEB-15 5AEN    0                                                
JRNL        AUTH   D.MOSER,S.K.WITTMANN,J.KRAMER,R.BLOCHER,J.ACHENBACH,         
JRNL        AUTH 2 D.POGORYELOV,E.PROSCHAK                                      
JRNL        TITL   PENG: A NEURAL GAS-BASED APPROACH FOR PHARMACOPHORE          
JRNL        TITL 2 ELUCIDATION. METHOD DESIGN, VALIDATION AND VIRTUAL SCREENING 
JRNL        TITL 3 FOR NOVEL LIGANDS OF LTA4H.                                  
JRNL        REF    J.CHEM.INF.MODEL.             V.  55   284 2015              
JRNL        REFN                   ISSN 1549-9596                               
JRNL        PMID   25625859                                                     
JRNL        DOI    10.1021/CI500618U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 53240                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4958                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.7331 -  5.7889    1.00     3355   182  0.1925 0.1632        
REMARK   3     2  5.7889 -  4.5959    1.00     3372   176  0.1612 0.1937        
REMARK   3     3  4.5959 -  4.0152    1.00     3373   176  0.1502 0.1592        
REMARK   3     4  4.0152 -  3.6482    1.00     3359   176  0.1610 0.1602        
REMARK   3     5  3.6482 -  3.3868    1.00     3368   175  0.1729 0.1943        
REMARK   3     6  3.3868 -  3.1872    1.00     3383   175  0.1892 0.1970        
REMARK   3     7  3.1872 -  3.0276    1.00     3378   179  0.1908 0.1796        
REMARK   3     8  3.0276 -  2.8958    1.00     3336   178  0.1842 0.1810        
REMARK   3     9  2.8958 -  2.7843    1.00     3377   180  0.1692 0.2039        
REMARK   3    10  2.7843 -  2.6882    1.00     3405   180  0.1671 0.1989        
REMARK   3    11  2.6882 -  2.6042    1.00     3337   181  0.1614 0.1908        
REMARK   3    12  2.6042 -  2.5298    1.00     3349   176  0.1609 0.1777        
REMARK   3    13  2.5298 -  2.4632    1.00     3347   178  0.1633 0.1934        
REMARK   3    14  2.4632 -  2.4031    1.00     3355   179  0.1575 0.1698        
REMARK   3    15  2.4031 -  2.3484    1.00     3384   174  0.1507 0.1966        
REMARK   3    16  2.3484 -  2.2985    1.00     3380   182  0.1565 0.1758        
REMARK   3    17  2.2985 -  2.2525    1.00     3392   180  0.1602 0.1833        
REMARK   3    18  2.2525 -  2.2100    1.00     3342   177  0.1588 0.1877        
REMARK   3    19  2.2100 -  2.1705    1.00     3378   183  0.1564 0.1868        
REMARK   3    20  2.1705 -  2.1337    1.00     3349   176  0.1601 0.2087        
REMARK   3    21  2.1337 -  2.0993    1.00     3397   175  0.1648 0.2013        
REMARK   3    22  2.0993 -  2.0670    1.00     3351   177  0.1667 0.1876        
REMARK   3    23  2.0670 -  2.0366    0.99     3332   176  0.1648 0.1866        
REMARK   3    24  2.0366 -  2.0079    0.98     3261   171  0.1748 0.2387        
REMARK   3    25  2.0079 -  1.9808    0.94     3139   167  0.1813 0.2126        
REMARK   3    26  1.9808 -  1.9551    0.88     3004   156  0.1973 0.2625        
REMARK   3    27  1.9551 -  1.9306    0.82     2741   145  0.2011 0.2284        
REMARK   3    28  1.9306 -  1.9074    0.65     2226   114  0.2127 0.2465        
REMARK   3    29  1.9074 -  1.8852    0.47     1559    75  0.2248 0.2751        
REMARK   3    30  1.8852 -  1.8640    0.21      716    39  0.2436 0.3154        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           5008                                  
REMARK   3   ANGLE     :  1.245           6802                                  
REMARK   3   CHIRALITY :  0.073            756                                  
REMARK   3   PLANARITY :  0.007            865                                  
REMARK   3   DIHEDRAL  : 14.192           1840                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5AEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290062687.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.728730                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53242                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GW6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITTER OF PROTEIN SOLUTION        
REMARK 280  CONTAINING 10MM TRIS-HCL, 25MM KCL, AND 4 MG/ML TO 8 MG/ML LTA4H    
REMARK 280  (PH 8) WAS MIXED AT DIFFERENT RATIOS (0.5:1, 1:1, AND 1:2) WITH     
REMARK 280  PRECIPITATE SOLUTION CONTAINING 0:15M IMIDAZOLE, 0:1M SODIUM        
REMARK 280  ACETATE PH 6, 14% PEG-8000, AND 5MM YBCL3, AND CRYSTALLIZED AT      
REMARK 280  17:4 C FOR TWO WEEKS BY HANGING DROP VAPOR-DIFFUSION METHOD,        
REMARK 280  VAPOR DIFFUSION, HANGING 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       38.49800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.11150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.47650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.11150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.49800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.47650            
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 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 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 401    CD   OE1  OE2                                       
REMARK 470     ARG A 586    CZ   NH1  NH2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  YB     YB A   613    YB     YB A   616     1545     0.63            
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       71.84   -113.66                                   
REMARK 500    SER A  80     -127.27     42.84                                   
REMARK 500    ASN A  97       -5.22     76.44                                   
REMARK 500    LYS A 126       -2.86     76.85                                   
REMARK 500    GLU A 271       43.15    -80.63                                   
REMARK 500    CYS A 274      -12.57     76.62                                   
REMARK 500    LEU A 275       81.89   -157.15                                   
REMARK 500    PHE A 432       39.25    -99.14                                   
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 612  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 GLU A 318   OE1 100.2                                              
REMARK 620 3 HIS A 299   NE2 100.3 111.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 613  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD2                                                    
REMARK 620 2 HOH A2072   O   150.0                                              
REMARK 620 3 HOH A2073   O    78.1  94.7                                        
REMARK 620 4 HOH A2502   O    77.5 120.2 142.3                                  
REMARK 620 5 HOH A2607   O   121.8  86.2  86.7  82.3                            
REMARK 620 6 ASP A  47   OD2  77.9  84.8 129.0  72.3 143.8                      
REMARK 620 7 ASP A  47   OD1  67.9  82.1  74.9 120.5 157.2  54.5                
REMARK 620 8 ASP A 481   OD1  46.1 156.5  69.6  72.8  75.9 118.6 109.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 614  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 121   OE1                                                    
REMARK 620 2 GLU A  70   OE1 114.3                                              
REMARK 620 3 GLU A 121   OE2  51.8  70.0                                        
REMARK 620 4 GLU A  70   OE2 114.6  54.6  67.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 615  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2446   O                                                      
REMARK 620 2 ASP A 426   OD1 123.8                                              
REMARK 620 3 HOH A2444   O   151.3  74.0                                        
REMARK 620 4 HOH A2454   O    78.6  77.0  84.9                                  
REMARK 620 5 HOH A2445   O    90.7 143.3  80.7 127.0                            
REMARK 620 6 ASP A 422   OD2  78.1  97.9 124.9 147.7  75.3                      
REMARK 620 7 ASP A 422   OD1 130.7  71.2  73.9 145.6  76.6  52.6                
REMARK 620 8 ASP A 426   OD2  72.8  52.8 126.4  77.8 147.6  74.1  93.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 616  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2072   O                                                      
REMARK 620 2 HOH A2073   O    78.4                                              
REMARK 620 3 HOH A2502   O   112.1 159.7                                        
REMARK 620 4 HOH A2607   O    72.1  80.0  86.6                                  
REMARK 620 5 ASP A 481   OD2 141.6  84.1  95.9 137.7                            
REMARK 620 6 ASP A 481   OD1 144.7  74.3  88.6  81.4  56.6                      
REMARK 620 7 ASP A  47   OD2  72.9 121.1  79.2 133.5  88.0 141.3                
REMARK 620 8 ASP A  47   OD1  68.3  69.3 130.3 133.6  73.7 120.3  52.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DP8 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 612                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 613                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 614                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 615                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 616                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 618                 
DBREF  5AEN A    3   610  UNP    P09960   LKHA4_HUMAN      4    611             
SEQRES   1 A  608  ILE VAL ASP THR CYS SER LEU ALA SER PRO ALA SER VAL          
SEQRES   2 A  608  CYS ARG THR LYS HIS LEU HIS LEU ARG CYS SER VAL ASP          
SEQRES   3 A  608  PHE THR ARG ARG THR LEU THR GLY THR ALA ALA LEU THR          
SEQRES   4 A  608  VAL GLN SER GLN GLU ASP ASN LEU ARG SER LEU VAL LEU          
SEQRES   5 A  608  ASP THR LYS ASP LEU THR ILE GLU LYS VAL VAL ILE ASN          
SEQRES   6 A  608  GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU ARG GLN SER          
SEQRES   7 A  608  TYR LYS GLY SER PRO MET GLU ILE SER LEU PRO ILE ALA          
SEQRES   8 A  608  LEU SER LYS ASN GLN GLU ILE VAL ILE GLU ILE SER PHE          
SEQRES   9 A  608  GLU THR SER PRO LYS SER SER ALA LEU GLN TRP LEU THR          
SEQRES  10 A  608  PRO GLU GLN THR SER GLY LYS GLU HIS PRO TYR LEU PHE          
SEQRES  11 A  608  SER GLN CYS GLN ALA ILE HIS CYS ARG ALA ILE LEU PRO          
SEQRES  12 A  608  CYS GLN ASP THR PRO SER VAL LYS LEU THR TYR THR ALA          
SEQRES  13 A  608  GLU VAL SER VAL PRO LYS GLU LEU VAL ALA LEU MET SER          
SEQRES  14 A  608  ALA ILE ARG ASP GLY GLU THR PRO ASP PRO GLU ASP PRO          
SEQRES  15 A  608  SER ARG LYS ILE TYR LYS PHE ILE GLN LYS VAL PRO ILE          
SEQRES  16 A  608  PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY ALA LEU GLU          
SEQRES  17 A  608  SER ARG GLN ILE GLY PRO ARG THR LEU VAL TRP SER GLU          
SEQRES  18 A  608  LYS GLU GLN VAL GLU LYS SER ALA TYR GLU PHE SER GLU          
SEQRES  19 A  608  THR GLU SER MET LEU LYS ILE ALA GLU ASP LEU GLY GLY          
SEQRES  20 A  608  PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU VAL LEU PRO          
SEQRES  21 A  608  PRO SER PHE PRO TYR GLY GLY MET GLU ASN PRO CYS LEU          
SEQRES  22 A  608  THR PHE VAL THR PRO THR LEU LEU ALA GLY ASP LYS SER          
SEQRES  23 A  608  LEU SER ASN VAL ILE ALA HIS GLU ILE SER HIS SER TRP          
SEQRES  24 A  608  THR GLY ASN LEU VAL THR ASN LYS THR TRP ASP HIS PHE          
SEQRES  25 A  608  TRP LEU ASN GLU GLY HIS THR VAL TYR LEU GLU ARG HIS          
SEQRES  26 A  608  ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE ARG HIS PHE          
SEQRES  27 A  608  ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN ASN SER VAL          
SEQRES  28 A  608  LYS THR PHE GLY GLU THR HIS PRO PHE THR LYS LEU VAL          
SEQRES  29 A  608  VAL ASP LEU THR ASP ILE ASP PRO ASP VAL ALA TYR SER          
SEQRES  30 A  608  SER VAL PRO TYR GLU LYS GLY PHE ALA LEU LEU PHE TYR          
SEQRES  31 A  608  LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE PHE LEU GLY          
SEQRES  32 A  608  PHE LEU LYS ALA TYR VAL GLU LYS PHE SER TYR LYS SER          
SEQRES  33 A  608  ILE THR THR ASP ASP TRP LYS ASP PHE LEU TYR SER TYR          
SEQRES  34 A  608  PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN VAL ASP TRP          
SEQRES  35 A  608  ASN ALA TRP LEU TYR SER PRO GLY LEU PRO PRO ILE LYS          
SEQRES  36 A  608  PRO ASN TYR ASP MET THR LEU THR ASN ALA CYS ILE ALA          
SEQRES  37 A  608  LEU SER GLN ARG TRP ILE THR ALA LYS GLU ASP ASP LEU          
SEQRES  38 A  608  ASN SER PHE ASN ALA THR ASP LEU LYS ASP LEU SER SER          
SEQRES  39 A  608  HIS GLN LEU ASN GLU PHE LEU ALA GLN THR LEU GLN ARG          
SEQRES  40 A  608  ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG MET GLN GLU          
SEQRES  41 A  608  VAL TYR ASN PHE ASN ALA ILE ASN ASN SER GLU ILE ARG          
SEQRES  42 A  608  PHE ARG TRP LEU ARG LEU CYS ILE GLN SER LYS TRP GLU          
SEQRES  43 A  608  ASP ALA ILE PRO LEU ALA LEU LYS MET ALA THR GLU GLN          
SEQRES  44 A  608  GLY ARG MET LYS PHE THR ARG PRO LEU PHE LYS ASP LEU          
SEQRES  45 A  608  ALA ALA PHE ASP LYS SER HIS ASP GLN ALA VAL ARG THR          
SEQRES  46 A  608  TYR GLN GLU HIS LYS ALA SER MET HIS PRO VAL THR ALA          
SEQRES  47 A  608  MET LEU VAL GLY LYS ASP LEU LYS VAL ASP                      
HET    DP8  A 611      19                                                       
HET     ZN  A 612       1                                                       
HET     YB  A 613       1                                                       
HET     YB  A 614       1                                                       
HET     YB  A 615       1                                                       
HET     YB  A 616       1                                                       
HET    IMD  A 617       5                                                       
HET    IMD  A 618       5                                                       
HETNAM     DP8 N,N-DIMETHYL-2-(4-PHENOXYPHENOXY)ETHANAMINE                      
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   2  DP8    C16 H19 N O2                                                 
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   YB    4(YB 3+)                                                     
FORMUL   8  IMD    2(C3 H5 N2 1+)                                               
FORMUL  10  HOH   *608(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  PHE A  234  1                                  12    
HELIX    6   6 GLU A  236  GLY A  249  1                                  14    
HELIX    7   7 PRO A  280  LEU A  283  5                                   4    
HELIX    8   8 SER A  290  HIS A  299  1                                  10    
HELIX    9   9 THR A  310  ASP A  312  5                                   3    
HELIX   10  10 HIS A  313  GLY A  334  1                                  22    
HELIX   11  11 GLY A  334  GLY A  357  1                                  24    
HELIX   12  12 HIS A  360  LYS A  364  5                                   5    
HELIX   13  13 ASP A  373  TYR A  378  1                                   6    
HELIX   14  14 SER A  380  LEU A  397  1                                  18    
HELIX   15  15 GLY A  399  SER A  415  1                                  17    
HELIX   16  16 THR A  420  PHE A  432  1                                  13    
HELIX   17  17 LYS A  435  ASN A  440  1                                   6    
HELIX   18  18 ASP A  443  SER A  450  1                                   8    
HELIX   19  19 THR A  465  ALA A  478  1                                  14    
HELIX   20  20 LYS A  479  PHE A  486  5                                   8    
HELIX   21  21 ASN A  487  LYS A  492  5                                   6    
HELIX   22  22 SER A  495  GLN A  508  1                                  14    
HELIX   23  23 PRO A  513  ASN A  525  1                                  13    
HELIX   24  24 PHE A  526  ILE A  529  5                                   4    
HELIX   25  25 ASN A  531  SER A  545  1                                  15    
HELIX   26  26 TRP A  547  ASP A  549  5                                   3    
HELIX   27  27 ALA A  550  GLN A  561  1                                  12    
HELIX   28  28 ARG A  563  PHE A  577  1                                  15    
HELIX   29  29 SER A  580  LYS A  592  1                                  13    
HELIX   30  30 ALA A  593  MET A  595  5                                   3    
HELIX   31  31 HIS A  596  LYS A  608  1                                  13    
SHEET    1  AA 8 GLN A  69  GLU A  70  0                                        
SHEET    2  AA 8 LEU A  59  ILE A  66 -1  O  ILE A  66   N  GLN A  69           
SHEET    3  AA 8 GLU A  99  THR A 108 -1  O  GLU A 103   N  VAL A  65           
SHEET    4  AA 8 THR A  33  SER A  44 -1  O  LEU A  34   N  THR A 108           
SHEET    5  AA 8 CYS A  16  ASP A  28 -1  O  ARG A  17   N  GLN A  43           
SHEET    6  AA 8 LEU A 154  PRO A 163  1  O  THR A 155   N  LEU A  21           
SHEET    7  AA 8 ASP A 183  ILE A 197 -1  O  LYS A 187   N  VAL A 162           
SHEET    8  AA 8 ILE A 173  ASP A 180 -1  O  ILE A 173   N  ILE A 192           
SHEET    1  AB 3 LEU A  49  LEU A  54  0                                        
SHEET    2  AB 3 MET A  86  LEU A  94 -1  O  MET A  86   N  LEU A  54           
SHEET    3  AB 3 TYR A  73  LEU A  75 -1  O  ALA A  74   N  GLU A  87           
SHEET    1  AC 4 LEU A 115  LEU A 118  0                                        
SHEET    2  AC 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3  AC 4 LEU A 204  GLY A 207 -1  O  LEU A 204   N  SER A 133           
SHEET    4  AC 4 VAL A 167  MET A 170 -1  O  VAL A 167   N  GLY A 207           
SHEET    1  AD 5 GLU A 210  GLY A 215  0                                        
SHEET    2  AD 5 THR A 218  SER A 222 -1  O  THR A 218   N  ILE A 214           
SHEET    3  AD 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4  AD 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5  AD 5 GLY A 269  MET A 270 -1  O  MET A 270   N  PHE A 277           
SHEET    1  AE 2 VAL A 306  ASN A 308  0                                        
SHEET    2  AE 2 LYS A 417  ILE A 419  1  O  LYS A 417   N  THR A 307           
LINK        ZN    ZN A 612                 NE2 HIS A 295     1555   1555  2.11  
LINK        ZN    ZN A 612                 OE1 GLU A 318     1555   1555  2.03  
LINK        ZN    ZN A 612                 NE2 HIS A 299     1555   1555  2.08  
LINK        YB    YB A 613                 OD2 ASP A 481     1555   1555  2.79  
LINK        YB    YB A 613                 O   HOH A2072     1555   1545  2.31  
LINK        YB    YB A 613                 O   HOH A2073     1555   1545  2.52  
LINK        YB    YB A 613                 O   HOH A2502     1555   1555  2.84  
LINK        YB    YB A 613                 O   HOH A2607     1555   1545  2.55  
LINK        YB    YB A 613                 OD2 ASP A  47     1555   1545  2.50  
LINK        YB    YB A 613                 OD1 ASP A  47     1555   1545  2.41  
LINK        YB    YB A 613                 OD1 ASP A 481     1555   1555  2.84  
LINK        YB    YB A 614                 OE1 GLU A 121     1555   1555  2.63  
LINK        YB    YB A 614                 OE1 GLU A  70     1555   3544  2.45  
LINK        YB    YB A 614                 OE2 GLU A 121     1555   1555  2.39  
LINK        YB    YB A 614                 OE2 GLU A  70     1555   3544  2.43  
LINK        YB    YB A 615                 O   HOH A2446     1555   1555  2.52  
LINK        YB    YB A 615                 OD1 ASP A 426     1555   1555  2.55  
LINK        YB    YB A 615                 O   HOH A2444     1555   1555  2.54  
LINK        YB    YB A 615                 O   HOH A2454     1555   1555  2.69  
LINK        YB    YB A 615                 O   HOH A2445     1555   1555  2.66  
LINK        YB    YB A 615                 OD2 ASP A 422     1555   1555  2.54  
LINK        YB    YB A 615                 OD1 ASP A 422     1555   1555  2.50  
LINK        YB    YB A 615                 OD2 ASP A 426     1555   1555  2.40  
LINK        YB    YB A 616                 O   HOH A2072     1555   1555  2.93  
LINK        YB    YB A 616                 O   HOH A2073     1555   1555  2.70  
LINK        YB    YB A 616                 O   HOH A2502     1555   1565  2.45  
LINK        YB    YB A 616                 O   HOH A2607     1555   1555  2.71  
LINK        YB    YB A 616                 OD2 ASP A 481     1555   1565  2.29  
LINK        YB    YB A 616                 OD1 ASP A 481     1555   1565  2.37  
LINK        YB    YB A 616                 OD2 ASP A  47     1555   1555  2.51  
LINK        YB    YB A 616                 OD1 ASP A  47     1555   1555  2.57  
CISPEP   1 GLN A  136    ALA A  137          0         0.69                     
CISPEP   2 ALA A  510    PRO A  511          0         4.11                     
SITE     1 AC1 11 GLN A 136  TYR A 267  GLY A 269  MET A 270                    
SITE     2 AC1 11 TRP A 311  PHE A 314  VAL A 367  PRO A 374                    
SITE     3 AC1 11 ALA A 377  TYR A 378  TYR A 383                               
SITE     1 AC2  5 HIS A 295  HIS A 299  GLU A 318  TYR A 383                    
SITE     2 AC2  5 HOH A2342                                                     
SITE     1 AC3  6 ASP A  47  ASP A 481  HOH A2072  HOH A2073                    
SITE     2 AC3  6 HOH A2502  HOH A2607                                          
SITE     1 AC4  2 GLU A  70  GLU A 121                                          
SITE     1 AC5  6 ASP A 422  ASP A 426  HOH A2444  HOH A2445                    
SITE     2 AC5  6 HOH A2446  HOH A2454                                          
SITE     1 AC6  6 ASP A  47  ASP A 481  HOH A2072  HOH A2073                    
SITE     2 AC6  6 HOH A2502  HOH A2607                                          
SITE     1 AC7  7 GLY A 344  GLY A 347  GLU A 348  ASN A 351                    
SITE     2 AC7  7 GLU A 501  ALA A 504  GLN A 508                               
SITE     1 AC8  7 SER A 288  LEU A 289  SER A 496  HIS A 497                    
SITE     2 AC8  7 ASN A 500  ASN A 531  HOH A2608                               
CRYST1   76.996   86.953   98.223  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      0.012988  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011500  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010181        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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