GenomeNet

Database: PDB
Entry: 5N3W
LinkDB: 5N3W
Original site: 5N3W 
HEADER    HYDROLASE                               09-FEB-17   5N3W              
TITLE     CRYSTAL STRUCTURE OF LTA4H BOUND TO A SELECTIVE INHIBITOR AGAINST LTB4
TITLE    2 GENERATION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    HYDROLASE, INFLAMMATION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.T.WONG,C.M.LOW,R.J.SNELGROVE,S.A.HARE                               
REVDAT   2   13-SEP-17 5N3W    1       REMARK                                   
REVDAT   1   29-MAR-17 5N3W    0                                                
JRNL        AUTH   C.M.LOW,S.AKTHAR,D.F.PATEL,S.LOSER,C.T.WONG,P.L.JACKSON,     
JRNL        AUTH 2 J.E.BLALOCK,S.A.HARE,C.M.LLOYD,R.J.SNELGROVE                 
JRNL        TITL   THE DEVELOPMENT OF NOVEL LTA4H MODULATORS TO SELECTIVELY     
JRNL        TITL 2 TARGET LTB4 GENERATION.                                      
JRNL        REF    SCI REP                       V.   7 44449 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28303931                                                     
JRNL        DOI    10.1038/SREP44449                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
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) : 65.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 28048                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1536                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2009                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4844                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 437                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -4.48000                                             
REMARK   3    B33 (A**2) : 4.41000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.503         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.298         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.275         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.101        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4995 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4730 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6785 ; 1.712 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10921 ; 1.054 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   605 ; 5.842 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   221 ;36.885 ;24.389       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   855 ;16.256 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;21.864 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   753 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5571 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1134 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2424 ; 1.778 ; 2.618       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2422 ; 1.776 ; 2.617       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3027 ; 2.745 ; 3.924       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3028 ; 2.746 ; 3.925       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2571 ; 2.934 ; 2.791       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2572 ; 2.933 ; 2.791       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3759 ; 4.114 ; 4.120       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6365 ; 6.141 ;21.758       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6366 ; 6.141 ;21.758       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5N3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003475.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-15                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29612                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.14200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
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) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1SQM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 8000, 0.1 M SODIUM ACETATE,     
REMARK 280  0.15 MM IMIDAZOLE PH7.8, 5 MM YBCL3, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 291K                                              
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       39.12500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.98000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.98000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.52500            
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: 750 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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     MET A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ASP A   610                                                      
REMARK 465     VAL A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     HIS A   613                                                      
REMARK 465     HIS A   614                                                      
REMARK 465     HIS A   615                                                      
REMARK 465     HIS A   616                                                      
REMARK 465     HIS A   617                                                      
REMARK 465     HIS A   618                                                      
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  ZN     ZN A   701     OXT  ACT A   705              1.62            
REMARK 500   OD1  ASP A   257     O    HOH A   801              1.75            
REMARK 500   OH   TYR A   416     O    HOH A   802              1.91            
REMARK 500   OG   SER A   472     O    HOH A   803              2.07            
REMARK 500   O    HOH A  1182     O    HOH A  1194              2.11            
REMARK 500   O    HOH A   991     O    HOH A  1049              2.11            
REMARK 500   OD2  ASP A   257     O    HOH A   804              2.13            
REMARK 500   OD2  ASP A   461     O    HOH A   805              2.15            
REMARK 500   O    GLN A    43     O    HOH A   806              2.17            
REMARK 500   OE1  GLU A   210     O    HOH A   807              2.18            
REMARK 500   OG1  THR A     6     O    HOH A   808              2.19            
REMARK 500   O    HOH A   810     O    HOH A  1155              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   NH2  ARG A    78     OE1  GLN A   441     2554     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 212   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 212   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  80     -131.57     46.26                                   
REMARK 500    LYS A 126       -6.82     75.39                                   
REMARK 500    CYS A 274      -11.38     74.75                                   
REMARK 500    LEU A 275       77.74   -154.79                                   
REMARK 500    THR A 281        4.85    -69.63                                   
REMARK 500    TRP A 301      -60.81   -105.57                                   
REMARK 500    PHE A 362        1.49    -64.90                                   
REMARK 500    ASN A 525       53.67     39.48                                   
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 A1236        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A1237        DISTANCE =  6.72 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                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2  92.0                                              
REMARK 620 3 GLU A 318   OE1  88.5  90.4                                        
REMARK 620 4 ACT A 705   O    92.2  88.7 178.9                                  
REMARK 620 N                    1     2     3                                   
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  52.4                                              
REMARK 620 3 HOH A 977   O    73.8  94.9                                        
REMARK 620 4 ASP A  47   OD1  69.9 118.9  86.1                                  
REMARK 620 5 ASP A  47   OD2  70.8 119.4  87.5   1.5                            
REMARK 620 6 HOH A1167   O    93.4  92.8 156.1  70.4  69.1                      
REMARK 620 7 HOH A1030   O   136.0 151.9  69.4  84.2  84.1 111.0                
REMARK 620 N                    1     2     3     4     5     6                 
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 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8KW A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 705                 
DBREF  5N3W A    0   610  UNP    P09960   LKHA4_HUMAN      1    611             
SEQADV 5N3W VAL A  611  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W ASP A  612  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  613  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  614  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  615  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  616  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  617  UNP  P09960              EXPRESSION TAG                 
SEQADV 5N3W HIS A  618  UNP  P09960              EXPRESSION TAG                 
SEQRES   1 A  619  MET PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO          
SEQRES   2 A  619  ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS          
SEQRES   3 A  619  SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA          
SEQRES   4 A  619  ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER          
SEQRES   5 A  619  LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL          
SEQRES   6 A  619  VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU          
SEQRES   7 A  619  ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU          
SEQRES   8 A  619  PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU          
SEQRES   9 A  619  ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN          
SEQRES  10 A  619  TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO          
SEQRES  11 A  619  TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA          
SEQRES  12 A  619  ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR          
SEQRES  13 A  619  TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA          
SEQRES  14 A  619  LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO          
SEQRES  15 A  619  GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS          
SEQRES  16 A  619  VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY          
SEQRES  17 A  619  ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL          
SEQRES  18 A  619  TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU          
SEQRES  19 A  619  PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP          
SEQRES  20 A  619  LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU          
SEQRES  21 A  619  VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN          
SEQRES  22 A  619  PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY          
SEQRES  23 A  619  ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER          
SEQRES  24 A  619  HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP          
SEQRES  25 A  619  ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU          
SEQRES  26 A  619  GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE          
SEQRES  27 A  619  ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN          
SEQRES  28 A  619  ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR          
SEQRES  29 A  619  LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL          
SEQRES  30 A  619  ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU          
SEQRES  31 A  619  LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE          
SEQRES  32 A  619  PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER          
SEQRES  33 A  619  TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU          
SEQRES  34 A  619  TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN          
SEQRES  35 A  619  VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO          
SEQRES  36 A  619  PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA          
SEQRES  37 A  619  CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU          
SEQRES  38 A  619  ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP          
SEQRES  39 A  619  LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR          
SEQRES  40 A  619  LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG          
SEQRES  41 A  619  MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER          
SEQRES  42 A  619  GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER          
SEQRES  43 A  619  LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA          
SEQRES  44 A  619  THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE          
SEQRES  45 A  619  LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA          
SEQRES  46 A  619  VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO          
SEQRES  47 A  619  VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP          
SEQRES  48 A  619  VAL ASP HIS HIS HIS HIS HIS HIS                              
HET     ZN  A 701       1                                                       
HET     YB  A 702       1                                                       
HET    IMD  A 703       5                                                       
HET    8KW  A 704      18                                                       
HET    ACT  A 705       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     8KW 3-[2-(2-HYDROXYPHENYL)ETHYL]-5-METHOXY-PHENOL                    
HETNAM     ACT ACETATE ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    YB 3+                                                        
FORMUL   4  IMD    C3 H5 N2 1+                                                  
FORMUL   5  8KW    C15 H16 O3                                                   
FORMUL   6  ACT    C2 H3 O2 1-                                                  
FORMUL   7  HOH   *437(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 TYR A  200  ILE A  202  5                                   3    
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  SER A  300  1                                  11    
HELIX   10 AB1 THR A  310  ASP A  312  5                                   3    
HELIX   11 AB2 HIS A  313  GLY A  334  1                                  22    
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  LEU A  397  1                                  18    
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  VAL A  442  1                                   8    
HELIX   19 AC1 ASP A  443  SER A  450  1                                   8    
HELIX   20 AC2 THR A  465  THR A  477  1                                  13    
HELIX   21 AC3 LYS A  479  PHE A  486  5                                   8    
HELIX   22 AC4 ASN A  487  LEU A  491  5                                   5    
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 ASP A  549  GLN A  561  1                                  13    
HELIX   28 AD1 ARG A  563  PHE A  577  1                                  15    
HELIX   29 AD2 SER A  580  LYS A  592  1                                  13    
HELIX   30 AD3 HIS A  596  LEU A  607  1                                  12    
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  SER A 105   N  LYS A  63           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  HIS A  22   O  ALA A  39           
SHEET    6 AA1 8 LYS A 153  PRO A 163  1  O  GLU A 159   N  CYS A  25           
SHEET    7 AA1 8 ARG A 186  PRO A 198 -1  O  LYS A 187   N  VAL A 162           
SHEET    8 AA1 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1 AA2 3 LEU A  49  LEU A  54  0                                        
SHEET    2 AA2 3 MET A  86  LEU A  94 -1  O  MET A  86   N  LEU A  54           
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  LEU A 258   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  THR A 276   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 VAL A 306  ASN A 308  0                                        
SHEET    2 AA5 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.12  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.28  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  1.88  
LINK         OD1 ASP A 481                YB    YB A 702     1555   1555  2.62  
LINK         OD2 ASP A 481                YB    YB A 702     1555   1555  2.29  
LINK        ZN    ZN A 701                 O   ACT A 705     1555   1555  2.53  
LINK        YB    YB A 702                 O   HOH A 977     1555   1555  2.43  
LINK         OD1 ASP A  47                YB    YB A 702     1555   1565  2.61  
LINK         OD2 ASP A  47                YB    YB A 702     1555   1565  2.64  
LINK        YB    YB A 702                 O   HOH A1167     1555   1545  2.84  
LINK        YB    YB A 702                 O   HOH A1030     1555   1545  2.33  
CISPEP   1 GLN A  136    ALA A  137          0         2.84                     
CISPEP   2 ALA A  510    PRO A  511          0         6.47                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  ACT A 705                    
SITE     1 AC2  5 ASP A  47  ASP A 481  HOH A 977  HOH A1030                    
SITE     2 AC2  5 HOH A1167                                                     
SITE     1 AC3  8 GLY A 344  GLY A 347  GLU A 348  ASN A 351                    
SITE     2 AC3  8 GLU A 501  ALA A 504  GLN A 505  GLN A 508                    
SITE     1 AC4 10 GLN A 136  ALA A 137  TYR A 267  TRP A 311                    
SITE     2 AC4 10 PHE A 314  VAL A 367  PRO A 374  ASP A 375                    
SITE     3 AC4 10 ALA A 377  TYR A 378                                          
SITE     1 AC5 10 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC5 10 HIS A 299  GLU A 318  TYR A 383   ZN A 701                    
SITE     3 AC5 10 HOH A 852  HOH A1124                                          
CRYST1   78.250   87.050   99.960  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      0.012780  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011488  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010004        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system