GenomeNet

Database: PDB
Entry: 4Y2P
LinkDB: 4Y2P
Original site: 4Y2P 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 10-FEB-15   4Y2P              
TITLE     STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH N-METHYL-1-[3- 
TITLE    2 (PYRIDIN-3-YL)PHENYL]METHANAMINE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-555;                                        
COMPND   5 EC: 3.3.2.10;                                                        
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: EPHX2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR COMPLEX, HYDROLASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.AMANO,T.YAMAGUCHI                                                   
REVDAT   1   06-MAY-15 4Y2P    0                                                
JRNL        AUTH   Y.AMANO,E.TANABE,T.YAMAGUCHI                                 
JRNL        TITL   IDENTIFICATION OF N-ETHYLMETHYLAMINE AS A NOVEL SCAFFOLD FOR 
JRNL        TITL 2 INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE BY CRYSTALLOGRAPHIC  
JRNL        TITL 3 FRAGMENT SCREENING                                           
JRNL        REF    BIOORG.MED.CHEM.              V.  23  2310 2015              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   25862210                                                     
JRNL        DOI    10.1016/J.BMC.2015.03.083                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 37865                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2765                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 120                          
REMARK   3   BIN FREE R VALUE                    : 0.2300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.190         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.162         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.195         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4448 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6026 ; 2.199 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   545 ; 6.978 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;34.615 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   783 ;18.333 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.383 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   659 ; 0.156 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3369 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2183 ; 2.863 ; 2.854       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2727 ; 3.773 ; 4.265       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2262 ; 4.450 ; 3.244       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6931 ; 9.570 ;24.310       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206760.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39866                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, AMMONIUM            
REMARK 280  DIHYDROGEN PHOSPHATE, PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      163.10133            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.55067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      122.32600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.77533            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      203.87667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      163.10133            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       81.55067            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.77533            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      122.32600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      203.87667            
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: 4390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      -93.05900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      122.32600            
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     1                                                      
REMARK 465     ASN A   548                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     HIS A   556                                                      
REMARK 465     HIS A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     HIS A   561                                                      
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   OE1  GLU A    69     OE1  GLU A    69     7465     2.12            
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  99   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A  99   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 130   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    LEU A 183   CA  -  CB  -  CG  ANGL. DEV. =  19.4 DEGREES          
REMARK 500    LEU A 183   CB  -  CG  -  CD2 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    PRO A 225   C   -  N   -  CA  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    ARG A 287   CB  -  CG  -  CD  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ARG A 287   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH1 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG A 353   CG  -  CD  -  NE  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU A 438   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 482   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A 482   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG A 482   NE  -  CZ  -  NH2 ANGL. DEV. =  10.1 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    LEU A  10      -72.99    -90.86                                   
REMARK 500    VAL A  13      -71.50   -126.48                                   
REMARK 500    GLN A 204      -96.83   -102.62                                   
REMARK 500    GLU A 269     -139.08   -117.03                                   
REMARK 500    ASP A 335     -128.56     64.09                                   
REMARK 500    ASN A 359      -48.86     81.72                                   
REMARK 500    MET A 419       34.28    -89.02                                   
REMARK 500    LEU A 514      130.00    -39.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A  291     ASP A  292                  143.11                    
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                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   9   OD2                                                    
REMARK 620 2 ASP A  11   O    86.7                                              
REMARK 620 3 ASP A 185   OD1 114.2  85.3                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3C5 A 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Y2J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Y2Y   RELATED DB: PDB                                   
DBREF  4Y2P A    1   555  UNP    P34913   HYES_HUMAN       1    555             
SEQADV 4Y2P HIS A  556  UNP  P34913              EXPRESSION TAG                 
SEQADV 4Y2P HIS A  557  UNP  P34913              EXPRESSION TAG                 
SEQADV 4Y2P HIS A  558  UNP  P34913              EXPRESSION TAG                 
SEQADV 4Y2P HIS A  559  UNP  P34913              EXPRESSION TAG                 
SEQADV 4Y2P HIS A  560  UNP  P34913              EXPRESSION TAG                 
SEQADV 4Y2P HIS A  561  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  561  MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL          
SEQRES   2 A  561  LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR          
SEQRES   3 A  561  GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP          
SEQRES   4 A  561  ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG          
SEQRES   5 A  561  LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO          
SEQRES   6 A  561  LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA          
SEQRES   7 A  561  LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE          
SEQRES   8 A  561  PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO          
SEQRES   9 A  561  MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE          
SEQRES  10 A  561  THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG          
SEQRES  11 A  561  ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU          
SEQRES  12 A  561  LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL          
SEQRES  13 A  561  GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU          
SEQRES  14 A  561  LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE          
SEQRES  15 A  561  LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP          
SEQRES  16 A  561  LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR          
SEQRES  17 A  561  ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU          
SEQRES  18 A  561  LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO          
SEQRES  19 A  561  SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG          
SEQRES  20 A  561  VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA          
SEQRES  21 A  561  VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER          
SEQRES  22 A  561  TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR          
SEQRES  23 A  561  ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER          
SEQRES  24 A  561  SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL          
SEQRES  25 A  561  LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY          
SEQRES  26 A  561  LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY          
SEQRES  27 A  561  MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG          
SEQRES  28 A  561  VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO          
SEQRES  29 A  561  ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA          
SEQRES  30 A  561  ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO          
SEQRES  31 A  561  GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG          
SEQRES  32 A  561  THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL          
SEQRES  33 A  561  LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE          
SEQRES  34 A  561  VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL          
SEQRES  35 A  561  THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS          
SEQRES  36 A  561  LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN          
SEQRES  37 A  561  MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY          
SEQRES  38 A  561  ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU          
SEQRES  39 A  561  LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET          
SEQRES  40 A  561  GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU          
SEQRES  41 A  561  ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU          
SEQRES  42 A  561  VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA          
SEQRES  43 A  561  ARG ASN PRO PRO VAL VAL SER LYS MET HIS HIS HIS HIS          
SEQRES  44 A  561  HIS HIS                                                      
HET     MG  A 601       1                                                       
HET    3C5  A 602      15                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     3C5 N-METHYL-1-[3-(PYRIDIN-3-YL)PHENYL]METHANAMINE                   
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  3C5    C13 H14 N2                                                   
FORMUL   4  HOH   *119(H2 O)                                                    
HELIX    1 AA1 ALA A   18  PHE A   20  5                                   3    
HELIX    2 AA2 GLY A   21  ALA A   31  1                                  11    
HELIX    3 AA3 GLY A   35  LYS A   43  1                                   9    
HELIX    4 AA4 GLY A   44  GLU A   47  5                                   4    
HELIX    5 AA5 GLY A   48  LYS A   55  1                                   8    
HELIX    6 AA6 THR A   59  ALA A   78  1                                  20    
HELIX    7 AA7 SER A   87  ARG A   99  1                                  13    
HELIX    8 AA8 ASN A  102  LYS A  115  1                                  14    
HELIX    9 AA9 GLU A  132  MET A  145  1                                  14    
HELIX   10 AB1 SER A  153  GLY A  157  1                                   5    
HELIX   11 AB2 GLU A  162  LYS A  174  1                                  13    
HELIX   12 AB3 SER A  176  SER A  178  5                                   3    
HELIX   13 AB4 ILE A  186  LEU A  196  1                                  11    
HELIX   14 AB5 ASP A  205  GLY A  218  1                                  14    
HELIX   15 AB6 ASN A  233  MET A  237  5                                   5    
HELIX   16 AB7 SER A  270  ARG A  275  5                                   6    
HELIX   17 AB8 TYR A  276  ALA A  284  1                                   9    
HELIX   18 AB9 GLU A  304  TYR A  308  5                                   5    
HELIX   19 AC1 CYS A  309  GLY A  325  1                                  17    
HELIX   20 AC2 ASP A  335  TYR A  348  1                                  14    
HELIX   21 AC3 SER A  370  ALA A  377  1                                   8    
HELIX   22 AC4 ASN A  378  VAL A  380  5                                   3    
HELIX   23 AC5 PHE A  381  PHE A  387  1                                   7    
HELIX   24 AC6 GLY A  391  ASN A  400  1                                  10    
HELIX   25 AC7 ASN A  400  PHE A  409  1                                  10    
HELIX   26 AC8 ALA A  411  SER A  415  5                                   5    
HELIX   27 AC9 LYS A  421  GLY A  426  1                                   6    
HELIX   28 AD1 THR A  443  GLY A  458  1                                  16    
HELIX   29 AD2 PHE A  459  TRP A  465  1                                   7    
HELIX   30 AD3 ASN A  468  LYS A  478  1                                  11    
HELIX   31 AD4 VAL A  500  GLN A  505  5                                   6    
HELIX   32 AD5 HIS A  506  TRP A  510  5                                   5    
HELIX   33 AD6 TRP A  525  LYS A  530  1                                   6    
HELIX   34 AD7 LYS A  530  ALA A  546  1                                  17    
SHEET    1 AA1 5 PHE A 149  GLU A 152  0                                        
SHEET    2 AA1 5 THR A 118  THR A 123  1  N  ILE A 121   O  ILE A 151           
SHEET    3 AA1 5 ALA A   5  PHE A   8  1  N  PHE A   8   O  ALA A 120           
SHEET    4 AA1 5 VAL A 180  ASP A 184  1  O  VAL A 181   N  VAL A   7           
SHEET    5 AA1 5 VAL A 199  LEU A 202  1  O  ILE A 201   N  PHE A 182           
SHEET    1 AA2 2 ALA A  15  LEU A  16  0                                        
SHEET    2 AA2 2 LYS A 100  ILE A 101 -1  O  LYS A 100   N  LEU A  16           
SHEET    1 AA3 8 SER A 238  LYS A 245  0                                        
SHEET    2 AA3 8 VAL A 248  LEU A 255 -1  O  LEU A 250   N  VAL A 242           
SHEET    3 AA3 8 ARG A 287  MET A 291 -1  O  VAL A 288   N  LEU A 255           
SHEET    4 AA3 8 ALA A 260  CYS A 264  1  N  VAL A 261   O  LEU A 289           
SHEET    5 AA3 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6 AA3 8 VAL A 352  LEU A 358  1  O  ALA A 356   N  GLY A 333           
SHEET    7 AA3 8 ALA A 488  ALA A 493  1  O  VAL A 491   N  SER A 357           
SHEET    8 AA3 8 LYS A 515  ILE A 519  1  O  LYS A 515   N  ALA A 488           
LINK         OD2 ASP A   9                MG    MG A 601     1555   1555  2.61  
LINK         O   ASP A  11                MG    MG A 601     1555   1555  2.83  
LINK         OD1 ASP A 185                MG    MG A 601     1555   1555  2.45  
CISPEP   1 LEU A   16    PRO A   17          0        -9.80                     
CISPEP   2 LYS A  160    PRO A  161          0         0.37                     
CISPEP   3 PHE A  267    PRO A  268          0        -8.55                     
SITE     1 AC1  4 ASP A   9  ASP A  11  ASP A 185  ILE A 186                    
SITE     1 AC2  5 PHE A 267  ASP A 335  TYR A 383  TYR A 466                    
SITE     2 AC2  5 HOH A 771                                                     
CRYST1   93.059   93.059  244.652  90.00  90.00 120.00 P 65 2 2     12          
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      0.010746  0.006204  0.000000        0.00000                         
SCALE2      0.000000  0.012408  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004087        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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