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Database: PDB
Entry: 3B7T
LinkDB: 3B7T
Original site: 3B7T 
HEADER    HYDROLASE                               31-OCT-07   3B7T              
TITLE     [E296Q]LTA4H IN COMPLEX WITH ARG-ALA-ARG SUBSTRATE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A4, HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RAR PEPTIDE;                                               
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7T3;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    TRANSITION STATE, ANALOGUE PEPTIDE, HYDROLYSIS, ALTERNATIVE SPLICING, 
KEYWDS   2 CYTOPLASM, HYDROLASE, LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING,       
KEYWDS   3 METALLOPROTEASE, MULTIFUNCTIONAL ENZYME, PROTEASE, ZINC, TRIPEPTIDE  
KEYWDS   4 SUBSTRATE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.THOLANDER,J.HAEGGSTROM,M.THUNNISSEN,A.MUROYA,B.-P.ROQUES,M.-        
AUTHOR   2 C.FOURNIE-ZALUSKI                                                    
REVDAT   5   20-NOV-19 3B7T    1       SEQADV LINK                              
REVDAT   4   07-MAR-18 3B7T    1       REMARK                                   
REVDAT   3   24-FEB-09 3B7T    1       VERSN                                    
REVDAT   2   07-OCT-08 3B7T    1       JRNL                                     
REVDAT   1   16-SEP-08 3B7T    0                                                
JRNL        AUTH   F.THOLANDER,A.MUROYA,B.P.ROQUES,M.C.FOURNIE-ZALUSKI,         
JRNL        AUTH 2 M.M.THUNNISSEN,J.Z.HAEGGSTROM                                
JRNL        TITL   STRUCTURE-BASED DISSECTION OF THE ACTIVE SITE CHEMISTRY OF   
JRNL        TITL 2 LEUKOTRIENE A4 HYDROLASE: IMPLICATIONS FOR M1                
JRNL        TITL 3 AMINOPEPTIDASES AND INHIBITOR DESIGN.                        
JRNL        REF    CHEM.BIOL.                    V.  15   920 2008              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   18804029                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2008.07.018                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.THOLANDER,J.Z.HAEGGSTROM                                   
REMARK   1  TITL   ASSAY FOR RAPID ANALYSIS OF THE TRI-PEPTIDASE ACTIVITY OF    
REMARK   1  TITL 2 LTA4 HYDROLASE.                                              
REMARK   1  REF    PROTEINS                      V.  67  1113 2007              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  PMID   17357161                                                     
REMARK   1  DOI    10.1002/PROT.21329                                           
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.ANDBERG,M.M.THUNNISSEN,            
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON         
REMARK   1  TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND   
REMARK   1  TITL 3 AMINOPEPTIDASE SUBSTRATES.                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 279 27376 2004              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   15078870                                                     
REMARK   1  DOI    10.1074/JBC.M401031200                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,J.Z.HAEGGSTROM        
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE/AMINOPEPTIDASE. GLUTAMATE 271 IS A  
REMARK   1  TITL 2 CATALYTIC RESIDUE WITH SPECIFIC ROLES IN TWO DISTINCT ENZYME 
REMARK   1  TITL 3 MECHANISMS.                                                  
REMARK   1  REF    J.BIOL.CHEM.                  V. 277  1398 2002              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   11675384                                                     
REMARK   1  DOI    10.1074/JBC.M106577200                                       
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,B.SAMUELSSON,         
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: SELECTIVE ABROGATION OF            
REMARK   1  TITL 2 LEUKOTRIENE B4 FORMATION BY MUTATION OF ASPARTIC ACID 375.   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  99  4215 2002              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   11917124                                                     
REMARK   1  DOI    10.1073/PNAS.072090099                                       
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.M.THUNNISSEN,P.NORDLUND,J.Z.HAEGGSTROM                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN LEUKOTRIENE A(4) HYDROLASE, A     
REMARK   1  TITL 2 BIFUNCTIONAL ENZYME IN INFLAMMATION.                         
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   8   131 2001              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1  PMID   11175901                                                     
REMARK   1  DOI    10.1038/84117                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 57183                          
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 SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1902                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6960                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 254                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4903                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.92000                                              
REMARK   3    B22 (A**2) : -5.86000                                             
REMARK   3    B33 (A**2) : 0.94000                                              
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) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.43                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 42.08                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3B7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045186.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS, XFIT                          
REMARK 200  DATA SCALING SOFTWARE          : XSCALE, XDS                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57220                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.54                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: XFIT                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1H19                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-PEPTIDE WAS CO-CRYSTALLIZED WITH     
REMARK 280  [E296Q]LTA4H BY LIQUID-LIQUID DIFFUSION IN MELTING-POINT            
REMARK 280  CAPILLARIES. A TRIS-BUFFERED (10 MM, PH 7.5) SOLUTION OF PROTEIN    
REMARK 280  AND TRIPEPTIDE, MOLAR RATIO 1:10 (~70 MICROM PROTEIN), WAS          
REMARK 280  LAYERED ON THE PRECIPITATE SOLUTION CONTAINING 28% (WEIGHT/         
REMARK 280  VOLUME) POLYETHYLENE GLYCOL (MW 8000), 50 MM NA ACETATE, 100 MM     
REMARK 280  IMIDAZOLE, PH 6.8, AND 5 MM YBCL3. CRYSTALS WERE ADDITIONALLY       
REMARK 280  SOAKED IN SOLUTIONS WITH INCREASED TRI-PEPTIDE CONCENTRATION        
REMARK 280  PRIOR TO DATA COLLECTION, LIQUID-LIQUID DIFFUSION, TEMPERATURE      
REMARK 280  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       39.24500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.95800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.89250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.95800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.24500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.89250            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  80     -134.75     45.36                                   
REMARK 500    LYS A 126       -1.92     71.43                                   
REMARK 500    ASP A 183      105.29    176.00                                   
REMARK 500    SER A 222      177.18    175.61                                   
REMARK 500    GLU A 271       46.66    -75.30                                   
REMARK 500    CYS A 274      -19.97     72.64                                   
REMARK 500    TRP A 301      -74.28   -119.97                                   
REMARK 500    LEU A 369       24.29    -73.78                                   
REMARK 500    SER A 379     -166.14   -169.99                                   
REMARK 500    PRO A 458     -177.95    -60.82                                   
REMARK 500    THR A 463      -70.49    -27.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2  98.6                                              
REMARK 620 3 GLU A 318   OE1  96.8 104.4                                        
REMARK 620 4 GLU A 318   OE2 150.8  92.3  54.2                                  
REMARK 620 5 ARG B 702   N   135.4  98.6 118.1  68.4                            
REMARK 620 6 ARG B 702   O    85.8 165.9  88.3  90.2  69.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD1                                                    
REMARK 620 2 ASP A 481   OD2  51.0                                              
REMARK 620 3 HOH A 709   O   104.9 101.4                                        
REMARK 620 4 ASP A  47   OD1 123.8  74.2  71.5                                  
REMARK 620 5 ASP A  47   OD2 123.7  73.8  72.9   1.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R59   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME COMPLEXED WITH INHIBITOR RB3041                          
REMARK 900 RELATED ID: 3B7R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7U   RELATED DB: PDB                                   
DBREF  3B7T A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 3B7T HIS A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T HIS A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T HIS A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T HIS A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T HIS A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7T GLN A  296  UNP  P09960    GLU   297 ENGINEERED                     
SEQRES   1 A  616  HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR CYS          
SEQRES   2 A  616  SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS HIS          
SEQRES   3 A  616  LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG THR          
SEQRES   4 A  616  LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN GLU          
SEQRES   5 A  616  ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP LEU          
SEQRES   6 A  616  THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL LYS          
SEQRES   7 A  616  TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER PRO          
SEQRES   8 A  616  MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN GLN          
SEQRES   9 A  616  GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO LYS          
SEQRES  10 A  616  SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR SER          
SEQRES  11 A  616  GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN ALA          
SEQRES  12 A  616  ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR PRO          
SEQRES  13 A  616  SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL PRO          
SEQRES  14 A  616  LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP GLY          
SEQRES  15 A  616  GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE TYR          
SEQRES  16 A  616  LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU ILE          
SEQRES  17 A  616  ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE GLY          
SEQRES  18 A  616  PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL GLU          
SEQRES  19 A  616  LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET LEU          
SEQRES  20 A  616  LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP GLY          
SEQRES  21 A  616  GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO TYR          
SEQRES  22 A  616  GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR PRO          
SEQRES  23 A  616  THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL ILE          
SEQRES  24 A  616  ALA HIS GLN ILE SER HIS SER TRP THR GLY ASN LEU VAL          
SEQRES  25 A  616  THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU GLY          
SEQRES  26 A  616  HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG LEU          
SEQRES  27 A  616  PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY GLY          
SEQRES  28 A  616  TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY GLU          
SEQRES  29 A  616  THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR ASP          
SEQRES  30 A  616  ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR GLU          
SEQRES  31 A  616  LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU LEU          
SEQRES  32 A  616  GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA TYR          
SEQRES  33 A  616  VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP ASP          
SEQRES  34 A  616  TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS VAL          
SEQRES  35 A  616  ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU TYR          
SEQRES  36 A  616  SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP MET          
SEQRES  37 A  616  THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG TRP          
SEQRES  38 A  616  ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN ALA          
SEQRES  39 A  616  THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN GLU          
SEQRES  40 A  616  PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO LEU          
SEQRES  41 A  616  GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE ASN          
SEQRES  42 A  616  ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU ARG          
SEQRES  43 A  616  LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO LEU          
SEQRES  44 A  616  ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS PHE          
SEQRES  45 A  616  THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP LYS          
SEQRES  46 A  616  SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS LYS          
SEQRES  47 A  616  ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY LYS          
SEQRES  48 A  616  ASP LEU LYS VAL ASP                                          
SEQRES   1 B    3  ARG ALA ARG                                                  
HET     ZN  A 701       1                                                       
HET     YB  A 702       1                                                       
HET     YB  A 703       1                                                       
HET    IMD  A 704       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   YB    2(YB 3+)                                                     
FORMUL   6  IMD    C3 H5 N2 1+                                                  
FORMUL   7  HOH   *31(H2 O)                                                     
HELIX    1   1 GLN A   79  GLY A   83  5                                   5    
HELIX    2   2 THR A  119  THR A  123  5                                   5    
HELIX    3   3 HIS A  139  ILE A  143  5                                   5    
HELIX    4   4 TYR A  200  ILE A  202  5                                   3    
HELIX    5   5 GLU A  223  GLU A  225  5                                   3    
HELIX    6   6 GLN A  226  PHE A  234  1                                   9    
HELIX    7   7 GLU A  236  GLY A  249  1                                  14    
HELIX    8   8 PRO A  280  LEU A  283  5                                   4    
HELIX    9   9 SER A  290  HIS A  299  1                                  10    
HELIX   10  10 THR A  310  ASP A  312  5                                   3    
HELIX   11  11 HIS A  313  GLY A  334  1                                  22    
HELIX   12  12 GLY A  334  GLY A  357  1                                  24    
HELIX   13  13 HIS A  360  LYS A  364  5                                   5    
HELIX   14  14 ASP A  373  TYR A  378  1                                   6    
HELIX   15  15 SER A  380  LEU A  397  1                                  18    
HELIX   16  16 GLY A  399  SER A  415  1                                  17    
HELIX   17  17 THR A  420  PHE A  432  1                                  13    
HELIX   18  18 LYS A  435  ASN A  440  1                                   6    
HELIX   19  19 ASP A  443  SER A  450  1                                   8    
HELIX   20  20 MET A  462  THR A  477  1                                  16    
HELIX   21  21 LYS A  479  PHE A  486  5                                   8    
HELIX   22  22 ASN A  487  LYS A  492  5                                   6    
HELIX   23  23 SER A  495  GLN A  508  1                                  14    
HELIX   24  24 PRO A  513  ASN A  525  1                                  13    
HELIX   25  25 PHE A  526  ILE A  529  5                                   4    
HELIX   26  26 ASN A  531  SER A  545  1                                  15    
HELIX   27  27 ASP A  549  GLN A  561  1                                  13    
HELIX   28  28 ARG A  563  PHE A  577  1                                  15    
HELIX   29  29 SER A  580  LYS A  592  1                                  13    
HELIX   30  30 ALA A  593  MET A  595  5                                   3    
HELIX   31  31 HIS A  596  LYS A  608  1                                  13    
SHEET    1   A 8 GLN A  69  GLU A  70  0                                        
SHEET    2   A 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3   A 8 GLU A  99  THR A 108 -1  O  SER A 105   N  GLU A  62           
SHEET    4   A 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5   A 8 CYS A  16  ASP A  28 -1  N  SER A  26   O  THR A  35           
SHEET    6   A 8 LYS A 153  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7   A 8 ARG A 186  PRO A 198 -1  O  GLN A 193   N  TYR A 156           
SHEET    8   A 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1   B 3 LEU A  49  THR A  56  0                                        
SHEET    2   B 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3   B 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1   C 4 LEU A 115  LEU A 118  0                                        
SHEET    2   C 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3   C 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4   C 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1   D 5 GLU A 210  GLY A 215  0                                        
SHEET    2   D 5 THR A 218  SER A 222 -1  O  SER A 222   N  GLU A 210           
SHEET    3   D 5 ASP A 257  VAL A 260  1  O  LEU A 258   N  TRP A 221           
SHEET    4   D 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5   D 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1   E 2 VAL A 306  ASN A 308  0                                        
SHEET    2   E 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OD2 ASP A 175                YB    YB A 703     1555   1555  2.68  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.11  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.16  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.15  
LINK         OE2 GLU A 318                ZN    ZN A 701     1555   1555  2.57  
LINK         OD1 ASP A 481                YB    YB A 702     1555   1555  2.55  
LINK         OD2 ASP A 481                YB    YB A 702     1555   1555  2.54  
LINK         N   ARG B 702                ZN    ZN A 701     1555   1555  2.29  
LINK         O   ARG B 702                ZN    ZN A 701     1555   1555  2.54  
LINK        YB    YB A 702                 O   HOH A 709     1555   1555  2.83  
LINK         OD1 ASP A  47                YB    YB A 702     1555   1545  2.56  
LINK         OD2 ASP A  47                YB    YB A 702     1555   1545  2.53  
CISPEP   1 GLN A  136    ALA A  137          0         1.10                     
CISPEP   2 ALA A  510    PRO A  511          0         0.49                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  ARG B 702                    
SITE     1 AC2  3 ASP A  47  ASP A 481  HOH A 709                               
SITE     1 AC3  4 GLY A 344  ASN A 351  GLU A 501  GLN A 508                    
CRYST1   78.490   87.785   99.916  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      0.012740  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010008        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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