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Database: PDB
Entry: 6HGX
LinkDB: 6HGX
Original site: 6HGX 
HEADER    HYDROLASE                               23-AUG-18   6HGX              
TITLE     SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH 1-(4-((4-(TERT-BUTYL)       
TITLE    2 MORPHOLIN-2-YL)METHOXY)PHENYL)-3-CYCLOHEXYLUREA                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.3.2.10,3.1.3.76;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: EPHX2;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    INHIBITOR, COMPLEX, SEH, HYDROLASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.KRAMER,D.POGORYELOV,K.HIESINGER,E.PROSCHAK                        
REVDAT   1   03-JUL-19 6HGX    0                                                
JRNL        AUTH   K.HIESINGER,J.S.KRAMER,J.ACHENBACH,D.MOSER,J.WEBER,          
JRNL        AUTH 2 S.K.WITTMANN,C.MORISSEAU,C.ANGIONI,G.GEISSLINGER,A.S.KAHNT,  
JRNL        AUTH 3 A.KAISER,A.PROSCHAK,D.STEINHILBER,D.POGORYELOV,K.WAGNER,     
JRNL        AUTH 4 B.D.HAMMOCK,E.PROSCHAK                                       
JRNL        TITL   COMPUTER-AIDED SELECTIVE OPTIMIZATION OF SIDE ACTIVITIES OF  
JRNL        TITL 2 TALINOLOL.                                                   
JRNL        REF    ACS MED.CHEM.LETT.            V.  10   899 2019              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   31223445                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.9B00075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21197                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.640                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2043                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 52.8658 -  5.3254    1.00     1372   146  0.1835 0.2197        
REMARK   3     2  5.3254 -  4.2275    1.00     1309   140  0.1409 0.2014        
REMARK   3     3  4.2275 -  3.6933    1.00     1292   137  0.1503 0.1814        
REMARK   3     4  3.6933 -  3.3556    1.00     1288   137  0.1730 0.2351        
REMARK   3     5  3.3556 -  3.1152    1.00     1280   136  0.1959 0.2402        
REMARK   3     6  3.1152 -  2.9315    1.00     1281   137  0.2457 0.3461        
REMARK   3     7  2.9315 -  2.7847    1.00     1250   134  0.2552 0.2796        
REMARK   3     8  2.7847 -  2.6635    1.00     1284   136  0.2924 0.3637        
REMARK   3     9  2.6635 -  2.5610    1.00     1269   137  0.2872 0.3495        
REMARK   3    10  2.5610 -  2.4726    1.00     1259   134  0.2769 0.2969        
REMARK   3    11  2.4726 -  2.3953    1.00     1258   134  0.2740 0.3475        
REMARK   3    12  2.3953 -  2.3268    1.00     1273   135  0.2682 0.3251        
REMARK   3    13  2.3268 -  2.2656    0.99     1254   133  0.2588 0.3020        
REMARK   3    14  2.2656 -  2.2103    1.00     1242   134  0.2793 0.3486        
REMARK   3    15  2.2103 -  2.1600    1.00     1243   133  0.2997 0.3201        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           2683                                  
REMARK   3   ANGLE     :  1.006           3647                                  
REMARK   3   CHIRALITY :  0.054            378                                  
REMARK   3   PLANARITY :  0.006            470                                  
REMARK   3   DIHEDRAL  : 24.131           1002                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 370 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0704 -13.7721 -32.8440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1972 T22:   0.2281                                     
REMARK   3      T33:   0.2800 T12:   0.0038                                     
REMARK   3      T13:   0.0410 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1190 L22:   3.5538                                     
REMARK   3      L33:   2.7071 L12:   1.0245                                     
REMARK   3      L13:  -0.1535 L23:   0.0270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0629 S12:  -0.0614 S13:  -0.1676                       
REMARK   3      S21:  -0.1444 S22:  -0.0068 S23:  -0.1623                       
REMARK   3      S31:   0.0973 S32:   0.1045 S33:   0.0330                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 399 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3155 -31.2642 -44.8033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8525 T22:   0.5614                                     
REMARK   3      T33:   0.7426 T12:  -0.1327                                     
REMARK   3      T13:   0.1040 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2975 L22:   3.2234                                     
REMARK   3      L33:   4.4811 L12:  -3.1367                                     
REMARK   3      L13:   0.6741 L23:   0.1009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4563 S12:  -0.3036 S13:  -1.4579                       
REMARK   3      S21:  -0.1793 S22:   0.5075 S23:   0.6477                       
REMARK   3      S31:   1.2944 S32:  -0.7960 S33:   0.0448                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 400 THROUGH 421 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6448 -20.8989 -43.3282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4434 T22:   0.4647                                     
REMARK   3      T33:   0.5156 T12:  -0.0246                                     
REMARK   3      T13:  -0.0879 T23:   0.0601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1845 L22:   4.3593                                     
REMARK   3      L33:   4.5688 L12:   3.0785                                     
REMARK   3      L13:  -3.9970 L23:  -1.6803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3691 S12:  -0.2598 S13:  -0.6804                       
REMARK   3      S21:  -0.3281 S22:   0.2148 S23:  -0.1537                       
REMARK   3      S31:   0.8655 S32:   0.3222 S33:   0.2054                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 547 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1692 -20.6689 -32.1476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3187 T22:   0.2527                                     
REMARK   3      T33:   0.3145 T12:  -0.0535                                     
REMARK   3      T13:   0.0280 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9719 L22:   2.9229                                     
REMARK   3      L33:   2.2203 L12:  -0.1512                                     
REMARK   3      L13:   0.0138 L23:  -0.1670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0899 S12:  -0.0144 S13:  -0.2692                       
REMARK   3      S21:  -0.1751 S22:   0.0851 S23:   0.0734                       
REMARK   3      S31:   0.2147 S32:  -0.1057 S33:  -0.0214                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6HGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011561.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0-6.55                           
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21319                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.362                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.41                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.01600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.390                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6FR2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN SOLUTION PROTEIN (5-10      
REMARK 280  MG/ML , 50 MM NACL, 50 MM SODIUM PHOSPHATE, 10% GLYCEROL (98%),     
REMARK 280  2 MM DTT AT PH 7.4) WAS MIXED IN DIFFERENT RATIOS (2/1, 1/1, 1/2)   
REMARK 280  WITH PRECIPITANT SOLUTION (23 %-28 % (W/V) POLYETHYLENGLYCOL        
REMARK 280  (PEG) 6000, 70 MM AMMONIUM ACETAT, 200 MM MAGNESIUM ACETAT, 100     
REMARK 280  MM SODIUM CACODYLATE AT PH 6.1-6.5), VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.90000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       52.85000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.90000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.85000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.90000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       52.85000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.90000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       52.85000            
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: 100 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 744  LIES ON A SPECIAL POSITION.                          
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   219                                                      
REMARK 465     ALA A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     LEU A   222                                                      
REMARK 465     ASN A   223                                                      
REMARK 465     THR A   224                                                      
REMARK 465     PRO A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     LEU A   228                                                      
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     LEU A   556                                                      
REMARK 465     LEU A   557                                                      
REMARK 465     GLU A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     HIS A   561                                                      
REMARK 465     HIS A   562                                                      
REMARK 465     HIS A   563                                                      
REMARK 465     HIS A   564                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     LYS A 421    CG   CD   CE   NZ                                   
REMARK 470     GLU A 424    CG   CD   OE1  OE2                                  
REMARK 470     TRP A 510    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 510    CZ3  CH2                                            
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 231     -161.28   -100.02                                   
REMARK 500    GLU A 269     -140.63   -127.03                                   
REMARK 500    ASP A 335     -129.30     61.95                                   
REMARK 500    ASN A 359      -48.62     81.89                                   
REMARK 500    PRO A 367        1.15    -69.30                                   
REMARK 500    GLU A 435       76.27   -112.67                                   
REMARK 500    MET A 503       -9.90    -56.14                                   
REMARK 500    HIS A 513       30.12    -97.53                                   
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 A 812        DISTANCE =  6.14 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                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 509   OD1                                                    
REMARK 620 2 ASP A 509   OD2  55.6                                              
REMARK 620 N                    1                                               
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 G3T A 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6HGV   RELATED DB: PDB                                   
REMARK 900 6HGV CONTAINS THE SAME PROTEIN IN COMPLEX WITH TALINOLOL             
DBREF  6HGX A  222   555  UNP    P34913   HYES_HUMAN     222    555             
SEQADV 6HGV MET A  219  UNP  P34913              INITIATING METHIONINE          
SEQADV 6HGV ALA A  220  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV SER A  221  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV LEU A  556  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV LEU A  557  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV GLU A  558  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  559  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  560  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  561  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  562  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  563  UNP  P34913              EXPRESSION TAG                 
SEQADV 6HGV HIS A  564  UNP  P34913              EXPRESSION TAG                 
SEQRES   1 A  346  MET ALA SER LEU ASN THR PRO ALA PRO LEU PRO THR SER          
SEQRES   2 A  346  CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL          
SEQRES   3 A  346  LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER          
SEQRES   4 A  346  GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER          
SEQRES   5 A  346  TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN          
SEQRES   6 A  346  ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR          
SEQRES   7 A  346  GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS          
SEQRES   8 A  346  MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP          
SEQRES   9 A  346  LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP          
SEQRES  10 A  346  TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR          
SEQRES  11 A  346  PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO          
SEQRES  12 A  346  PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER          
SEQRES  13 A  346  ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE          
SEQRES  14 A  346  GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN          
SEQRES  15 A  346  LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP          
SEQRES  16 A  346  GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY          
SEQRES  17 A  346  GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER          
SEQRES  18 A  346  ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN          
SEQRES  19 A  346  GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP          
SEQRES  20 A  346  TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS          
SEQRES  21 A  346  SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL          
SEQRES  22 A  346  THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER          
SEQRES  23 A  346  GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY          
SEQRES  24 A  346  HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS          
SEQRES  25 A  346  PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP          
SEQRES  26 A  346  SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET LEU          
SEQRES  27 A  346  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET     MG  A 601       1                                                       
HET    G3T  A 602      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     G3T 1-[4-[[(2~{S})-4-~{TERT}-BUTYLMORPHOLIN-2-                       
HETNAM   2 G3T  YL]METHOXY]PHENYL]-3-CYCLOHEXYL-UREA                            
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  G3T    C22 H35 N3 O3                                                
FORMUL   4  HOH   *112(H2 O)                                                    
HELIX    1 AA1 ASN A  233  MET A  237  5                                   5    
HELIX    2 AA2 SER A  270  ARG A  275  5                                   6    
HELIX    3 AA3 GLN A  277  ALA A  284  1                                   8    
HELIX    4 AA4 GLU A  304  TYR A  308  5                                   5    
HELIX    5 AA5 CYS A  309  GLY A  325  1                                  17    
HELIX    6 AA6 ASP A  335  TYR A  348  1                                  14    
HELIX    7 AA7 SER A  370  ALA A  377  1                                   8    
HELIX    8 AA8 ASN A  378  VAL A  380  5                                   3    
HELIX    9 AA9 PHE A  381  PHE A  387  1                                   7    
HELIX   10 AB1 GLY A  391  GLN A  399  1                                   9    
HELIX   11 AB2 ASN A  400  PHE A  409  1                                  10    
HELIX   12 AB3 ALA A  411  SER A  415  5                                   5    
HELIX   13 AB4 LYS A  421  GLY A  426  1                                   6    
HELIX   14 AB5 THR A  443  GLY A  458  1                                  16    
HELIX   15 AB6 PHE A  459  ASN A  464  1                                   6    
HELIX   16 AB7 TRP A  465  ARG A  467  5                                   3    
HELIX   17 AB8 ASN A  468  LYS A  478  1                                  11    
HELIX   18 AB9 VAL A  500  GLN A  505  5                                   6    
HELIX   19 AC1 HIS A  506  TRP A  510  5                                   5    
HELIX   20 AC2 TRP A  525  LYS A  530  1                                   6    
HELIX   21 AC3 LYS A  530  ALA A  546  1                                  17    
SHEET    1 AA1 8 SER A 238  LYS A 245  0                                        
SHEET    2 AA1 8 VAL A 248  LEU A 255 -1  O  LEU A 250   N  VAL A 242           
SHEET    3 AA1 8 ARG A 287  ASP A 292 -1  O  VAL A 288   N  LEU A 255           
SHEET    4 AA1 8 ALA A 260  CYS A 264  1  N  VAL A 261   O  LEU A 289           
SHEET    5 AA1 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6 AA1 8 VAL A 352  LEU A 358  1  O  LEU A 358   N  GLY A 333           
SHEET    7 AA1 8 ALA A 488  ALA A 493  1  O  VAL A 491   N  SER A 357           
SHEET    8 AA1 8 LEU A 514  ILE A 519  1  O  ILE A 519   N  THR A 492           
LINK         OD1 ASP A 509                MG    MG A 601     1555   1555  2.57  
LINK         OD2 ASP A 509                MG    MG A 601     1555   1555  1.98  
CISPEP   1 PHE A  267    PRO A  268          0        -8.39                     
SITE     1 AC1  2 HIS A 506  ASP A 509                                          
SITE     1 AC2 11 PHE A 267  ASP A 335  TRP A 336  MET A 339                    
SITE     2 AC2 11 ILE A 375  TYR A 383  GLN A 384  MET A 419                    
SITE     3 AC2 11 TYR A 466  MET A 469  HIS A 524                               
CRYST1   79.800   92.000  105.700  90.00  90.00  90.00 I 2 2 2       8          
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      0.012531  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009461        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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