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Database: PDB
Entry: 6FTW
LinkDB: 6FTW
Original site: 6FTW 
HEADER    HYDROLASE                               24-FEB-18   6FTW              
TITLE     CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 4D2 CATALYTIC DOMAIN WITH
TITLE    2 INHIBITOR NPD-048                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4D;           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DPDE3,PDE43;                                                
COMPND   5 EC: 3.1.4.53;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: RESIDUES 381-740                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PDE4D, DPDE3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    PHOSPHODIESTERASE, HYDROLASE, CAMP HYDROLYSIS, ALTERNATIVE SPLICING   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.SINGH,D.G.BROWN                                                   
REVDAT   5   17-JAN-24 6FTW    1       LINK                                     
REVDAT   4   04-SEP-19 6FTW    1       JRNL                                     
REVDAT   3   31-JUL-19 6FTW    1       JRNL                                     
REVDAT   2   24-JUL-19 6FTW    1       JRNL                                     
REVDAT   1   20-MAR-19 6FTW    0                                                
JRNL        AUTH   E.DE HEUVEL,A.K.SINGH,E.EDINK,T.VAN DER MEER,                
JRNL        AUTH 2 M.VAN DER WOUDE,P.SADEK,M.P.KRELL-JORGENSEN,T.VAN DEN BERGH, 
JRNL        AUTH 3 J.VEERMAN,G.CALJON,T.D.KALEJAIYE,M.WIJTMANS,L.MAES,          
JRNL        AUTH 4 H.P.DE KONING,G.JAN STERK,M.SIDERIUS,I.J.P.DE ESCH,          
JRNL        AUTH 5 D.G.BROWN,R.LEURS                                            
JRNL        TITL   ALKYNAMIDE PHTHALAZINONES AS A NEW CLASS OF TBRPDEB1         
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.              V.  27  3998 2019              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   31327675                                                     
JRNL        DOI    10.1016/J.BMC.2019.06.027                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 65.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 90714                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4729                            
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) : 2.16                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.22                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6591                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 349                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10555                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 348                                     
REMARK   3   SOLVENT ATOMS            : 551                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.56000                                              
REMARK   3    B22 (A**2) : -1.12000                                             
REMARK   3    B33 (A**2) : 0.56000                                              
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): 0.202         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.865         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11082 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10230 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14972 ; 1.761 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 23766 ; 1.091 ; 2.984       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1300 ; 5.867 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   551 ;35.182 ;24.864       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1917 ;15.593 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;19.212 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1709 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11984 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2093 ; 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):  5212 ; 3.887 ; 4.600       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5211 ; 3.885 ; 4.600       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6508 ; 5.383 ; 6.879       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6509 ; 5.383 ; 6.880       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5870 ; 4.797 ; 5.077       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5871 ; 4.796 ; 5.077       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8465 ; 6.976 ; 7.412       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13065 ; 8.333 ;55.318       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13066 ; 8.332 ;55.320       
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 6FTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008923.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
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                         : CRL                                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.160                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.06300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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: 3SL3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350, 30% ETHYLENE GLYCOL, 0.1   
REMARK 280  M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
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       49.57000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.03000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.71500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.03000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.57000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.71500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     GLY A    75                                                      
REMARK 465     SER A    76                                                      
REMARK 465     HIS A    77                                                      
REMARK 465     MET A    78                                                      
REMARK 465     ILE A    79                                                      
REMARK 465     PRO A    80                                                      
REMARK 465     GLN A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     SER A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     ALA A   417                                                      
REMARK 465     PRO A   418                                                      
REMARK 465     ASP A   419                                                      
REMARK 465     ASP A   420                                                      
REMARK 465     PRO A   421                                                      
REMARK 465     GLU A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     GLY A   424                                                      
REMARK 465     ARG A   425                                                      
REMARK 465     GLN A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     THR A   429                                                      
REMARK 465     GLU A   430                                                      
REMARK 465     LYS A   431                                                      
REMARK 465     PHE A   432                                                      
REMARK 465     GLN A   433                                                      
REMARK 465     PHE A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     THR A   437                                                      
REMARK 465     LEU A   438                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     HIS B    77                                                      
REMARK 465     MET B    78                                                      
REMARK 465     ILE B    79                                                      
REMARK 465     PRO B    80                                                      
REMARK 465     ARG B    81                                                      
REMARK 465     PHE B    82                                                      
REMARK 465     GLY B    83                                                      
REMARK 465     VAL B    84                                                      
REMARK 465     LYS B    85                                                      
REMARK 465     THR B    86                                                      
REMARK 465     GLU B    87                                                      
REMARK 465     GLN B    88                                                      
REMARK 465     SER B   413                                                      
REMARK 465     PRO B   414                                                      
REMARK 465     SER B   415                                                      
REMARK 465     PRO B   416                                                      
REMARK 465     ALA B   417                                                      
REMARK 465     PRO B   418                                                      
REMARK 465     ASP B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     PRO B   421                                                      
REMARK 465     GLU B   422                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     GLY B   424                                                      
REMARK 465     ARG B   425                                                      
REMARK 465     GLN B   426                                                      
REMARK 465     GLY B   427                                                      
REMARK 465     GLN B   428                                                      
REMARK 465     THR B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     LYS B   431                                                      
REMARK 465     PHE B   432                                                      
REMARK 465     GLN B   433                                                      
REMARK 465     PHE B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     LEU B   436                                                      
REMARK 465     THR B   437                                                      
REMARK 465     LEU B   438                                                      
REMARK 465     GLY C    75                                                      
REMARK 465     SER C    76                                                      
REMARK 465     HIS C    77                                                      
REMARK 465     MET C    78                                                      
REMARK 465     ILE C    79                                                      
REMARK 465     PRO C    80                                                      
REMARK 465     ARG C    81                                                      
REMARK 465     PHE C    82                                                      
REMARK 465     GLY C    83                                                      
REMARK 465     VAL C    84                                                      
REMARK 465     LYS C    85                                                      
REMARK 465     THR C    86                                                      
REMARK 465     GLU C    87                                                      
REMARK 465     GLN C   412                                                      
REMARK 465     SER C   413                                                      
REMARK 465     PRO C   414                                                      
REMARK 465     SER C   415                                                      
REMARK 465     PRO C   416                                                      
REMARK 465     ALA C   417                                                      
REMARK 465     PRO C   418                                                      
REMARK 465     ASP C   419                                                      
REMARK 465     ASP C   420                                                      
REMARK 465     PRO C   421                                                      
REMARK 465     GLU C   422                                                      
REMARK 465     GLU C   423                                                      
REMARK 465     GLY C   424                                                      
REMARK 465     ARG C   425                                                      
REMARK 465     GLN C   426                                                      
REMARK 465     GLY C   427                                                      
REMARK 465     GLN C   428                                                      
REMARK 465     THR C   429                                                      
REMARK 465     GLU C   430                                                      
REMARK 465     LYS C   431                                                      
REMARK 465     PHE C   432                                                      
REMARK 465     GLN C   433                                                      
REMARK 465     PHE C   434                                                      
REMARK 465     GLU C   435                                                      
REMARK 465     LEU C   436                                                      
REMARK 465     THR C   437                                                      
REMARK 465     LEU C   438                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     SER D    76                                                      
REMARK 465     HIS D    77                                                      
REMARK 465     MET D    78                                                      
REMARK 465     ILE D    79                                                      
REMARK 465     PRO D    80                                                      
REMARK 465     ARG D    81                                                      
REMARK 465     PHE D    82                                                      
REMARK 465     GLY D    83                                                      
REMARK 465     VAL D    84                                                      
REMARK 465     LYS D    85                                                      
REMARK 465     THR D    86                                                      
REMARK 465     GLU D    87                                                      
REMARK 465     SER D   413                                                      
REMARK 465     PRO D   414                                                      
REMARK 465     SER D   415                                                      
REMARK 465     PRO D   416                                                      
REMARK 465     ALA D   417                                                      
REMARK 465     PRO D   418                                                      
REMARK 465     ASP D   419                                                      
REMARK 465     ASP D   420                                                      
REMARK 465     PRO D   421                                                      
REMARK 465     GLU D   422                                                      
REMARK 465     GLU D   423                                                      
REMARK 465     GLY D   424                                                      
REMARK 465     ARG D   425                                                      
REMARK 465     GLN D   426                                                      
REMARK 465     GLY D   427                                                      
REMARK 465     GLN D   428                                                      
REMARK 465     THR D   429                                                      
REMARK 465     GLU D   430                                                      
REMARK 465     LYS D   431                                                      
REMARK 465     PHE D   432                                                      
REMARK 465     GLN D   433                                                      
REMARK 465     PHE D   434                                                      
REMARK 465     GLU D   435                                                      
REMARK 465     LEU D   436                                                      
REMARK 465     THR D   437                                                      
REMARK 465     LEU D   438                                                      
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   OD2  ASP C   345     NH2  ARG C   348              1.89            
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    ASP A 266   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 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    PHE A  82       92.54     86.47                                   
REMARK 500    LEU A 104      141.76    -38.63                                   
REMARK 500    ALA A 183       17.97     53.50                                   
REMARK 500    ASP A 225       13.68     54.98                                   
REMARK 500    SER A 227       51.00     37.44                                   
REMARK 500    VAL A 292       41.02   -163.66                                   
REMARK 500    SER A 294      -89.35     72.19                                   
REMARK 500    MET A 357       -1.27     70.37                                   
REMARK 500    ILE A 376      -60.39   -121.38                                   
REMARK 500    ASP B  90      -60.09     13.26                                   
REMARK 500    ASP B  98        0.63    -68.04                                   
REMARK 500    TYR B 159      -61.83   -108.22                                   
REMARK 500    ALA B 180        1.86    -65.33                                   
REMARK 500    ALA B 183       17.34     59.99                                   
REMARK 500    ASP B 225       15.62     58.53                                   
REMARK 500    SER B 227       52.00     39.37                                   
REMARK 500    GLU B 243     -166.79    -74.40                                   
REMARK 500    LEU B 319       30.34    -93.48                                   
REMARK 500    MET B 357       -0.43     84.71                                   
REMARK 500    ASN B 362       61.77   -156.85                                   
REMARK 500    ILE B 376      -59.85   -129.49                                   
REMARK 500    ALA C 183        6.30     54.98                                   
REMARK 500    ASP C 225       16.83     59.22                                   
REMARK 500    LEU C 300      -76.76   -121.63                                   
REMARK 500    ASP C 301      -59.61     98.31                                   
REMARK 500    ILE C 376      -58.21   -120.92                                   
REMARK 500    LEU D 104      134.60    -39.88                                   
REMARK 500    TYR D 159      -64.63   -108.80                                   
REMARK 500    ASN D 161     -169.22   -127.09                                   
REMARK 500    ALA D 183       14.80     55.08                                   
REMARK 500    ASN D 224       47.22     36.89                                   
REMARK 500    LEU D 319       34.39    -98.41                                   
REMARK 500    MET D 357      -11.56     79.46                                   
REMARK 500    ASN D 362       57.73   -112.54                                   
REMARK 500    ILE D 376      -60.21   -121.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 164   NE2                                                    
REMARK 620 2 HIS A 200   NE2  92.9                                              
REMARK 620 3 ASP A 201   OD2  87.8  84.8                                        
REMARK 620 4 ASP A 318   OD1  84.6  86.2 167.9                                  
REMARK 620 5 HOH A 626   O   168.1  98.5  89.9  99.4                            
REMARK 620 6 HOH A 649   O    91.0 175.8  97.0  92.5  77.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 201   OD1                                                    
REMARK 620 2 HOH A 613   O    84.3                                              
REMARK 620 3 HOH A 626   O    93.3 100.6                                        
REMARK 620 4 HOH A 628   O   164.8  86.9 100.5                                  
REMARK 620 5 HOH A 688   O    86.6  89.0 170.4  80.9                            
REMARK 620 6 HOH A 717   O    96.8 172.3  87.0  90.3  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 164   NE2                                                    
REMARK 620 2 HIS B 200   NE2  94.2                                              
REMARK 620 3 ASP B 201   OD2  86.2  88.3                                        
REMARK 620 4 ASP B 318   OD1  88.0  88.0 172.9                                  
REMARK 620 5 HOH B 626   O   171.9  93.8  94.1  92.2                            
REMARK 620 6 HOH B 673   O    93.2 170.9  97.4  87.1  78.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 201   OD1                                                    
REMARK 620 2 HOH B 614   O    85.0                                              
REMARK 620 3 HOH B 626   O    89.0  97.2                                        
REMARK 620 4 HOH B 646   O    96.1  90.6 171.1                                  
REMARK 620 5 HOH B 654   O   171.9  87.1  93.8  82.3                            
REMARK 620 6 HOH B 658   O    89.3 174.3  82.4  90.3  98.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 164   NE2                                                    
REMARK 620 2 HIS C 200   NE2  87.4                                              
REMARK 620 3 ASP C 201   OD2  88.2  85.0                                        
REMARK 620 4 ASP C 318   OD1  87.5  94.4 175.7                                  
REMARK 620 5 HOH C 625   O   170.5 102.0  91.1  93.2                            
REMARK 620 6 HOH C 658   O    94.6 176.7  97.7  83.0  76.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 201   OD1                                                    
REMARK 620 2 HOH C 607   O    76.5                                              
REMARK 620 3 HOH C 625   O    95.5  99.5                                        
REMARK 620 4 HOH C 645   O   163.4  88.3  93.5                                  
REMARK 620 5 HOH C 657   O    90.2  87.7 171.7  82.5                            
REMARK 620 6 HOH C 675   O    97.1 172.1  85.6  97.4  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 164   NE2                                                    
REMARK 620 2 HIS D 200   NE2  95.3                                              
REMARK 620 3 ASP D 201   OD2  86.8  84.7                                        
REMARK 620 4 ASP D 318   OD1  86.6  91.1 171.8                                  
REMARK 620 5 HOH D 617   O   168.2  96.4  92.4  95.0                            
REMARK 620 6 HOH D 654   O    93.7 170.6  98.1  87.2  74.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 201   OD1                                                    
REMARK 620 2 HOH D 617   O    96.5                                              
REMARK 620 3 HOH D 652   O    82.0  94.7                                        
REMARK 620 4 HOH D 671   O   168.2  89.3  87.3                                  
REMARK 620 5 HOH D 689   O    90.3 172.0  90.3  84.7                            
REMARK 620 6 HOH D 709   O    91.9  82.2 172.8  99.0  93.5                      
REMARK 620 N                    1     2     3     4     5                       
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z D 516                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6FTM   RELATED DB: PDB                                   
DBREF  6FTW A   79   438  UNP    Q08499   PDE4D_HUMAN    381    740             
DBREF  6FTW B   79   438  UNP    Q08499   PDE4D_HUMAN    381    740             
DBREF  6FTW C   79   438  UNP    Q08499   PDE4D_HUMAN    381    740             
DBREF  6FTW D   79   438  UNP    Q08499   PDE4D_HUMAN    381    740             
SEQADV 6FTW GLY A   75  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW SER A   76  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW HIS A   77  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW MET A   78  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW GLY B   75  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW SER B   76  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW HIS B   77  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW MET B   78  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW GLY C   75  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW SER C   76  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW HIS C   77  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW MET C   78  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW GLY D   75  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW SER D   76  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW HIS D   77  UNP  Q08499              EXPRESSION TAG                 
SEQADV 6FTW MET D   78  UNP  Q08499              EXPRESSION TAG                 
SEQRES   1 A  364  GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU          
SEQRES   2 A  364  GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN          
SEQRES   3 A  364  LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER          
SEQRES   4 A  364  GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE          
SEQRES   5 A  364  GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL          
SEQRES   6 A  364  ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS          
SEQRES   7 A  364  TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA          
SEQRES   8 A  364  ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR          
SEQRES   9 A  364  PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU          
SEQRES  10 A  364  ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS          
SEQRES  11 A  364  PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER          
SEQRES  12 A  364  GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU          
SEQRES  13 A  364  ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU          
SEQRES  14 A  364  GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN          
SEQRES  15 A  364  ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU          
SEQRES  16 A  364  ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP          
SEQRES  17 A  364  LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER          
SEQRES  18 A  364  GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN          
SEQRES  19 A  364  VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN          
SEQRES  20 A  364  PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP          
SEQRES  21 A  364  ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU          
SEQRES  22 A  364  ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS          
SEQRES  23 A  364  HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE          
SEQRES  24 A  364  ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP          
SEQRES  25 A  364  LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU          
SEQRES  26 A  364  GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN          
SEQRES  27 A  364  SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG          
SEQRES  28 A  364  GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU          
SEQRES   1 B  364  GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU          
SEQRES   2 B  364  GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN          
SEQRES   3 B  364  LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER          
SEQRES   4 B  364  GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE          
SEQRES   5 B  364  GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL          
SEQRES   6 B  364  ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS          
SEQRES   7 B  364  TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA          
SEQRES   8 B  364  ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR          
SEQRES   9 B  364  PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU          
SEQRES  10 B  364  ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS          
SEQRES  11 B  364  PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER          
SEQRES  12 B  364  GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU          
SEQRES  13 B  364  ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU          
SEQRES  14 B  364  GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN          
SEQRES  15 B  364  ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU          
SEQRES  16 B  364  ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP          
SEQRES  17 B  364  LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER          
SEQRES  18 B  364  GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN          
SEQRES  19 B  364  VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN          
SEQRES  20 B  364  PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP          
SEQRES  21 B  364  ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU          
SEQRES  22 B  364  ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS          
SEQRES  23 B  364  HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE          
SEQRES  24 B  364  ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP          
SEQRES  25 B  364  LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU          
SEQRES  26 B  364  GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN          
SEQRES  27 B  364  SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG          
SEQRES  28 B  364  GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU          
SEQRES   1 C  364  GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU          
SEQRES   2 C  364  GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN          
SEQRES   3 C  364  LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER          
SEQRES   4 C  364  GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE          
SEQRES   5 C  364  GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL          
SEQRES   6 C  364  ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS          
SEQRES   7 C  364  TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA          
SEQRES   8 C  364  ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR          
SEQRES   9 C  364  PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU          
SEQRES  10 C  364  ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS          
SEQRES  11 C  364  PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER          
SEQRES  12 C  364  GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU          
SEQRES  13 C  364  ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU          
SEQRES  14 C  364  GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN          
SEQRES  15 C  364  ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU          
SEQRES  16 C  364  ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP          
SEQRES  17 C  364  LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER          
SEQRES  18 C  364  GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN          
SEQRES  19 C  364  VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN          
SEQRES  20 C  364  PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP          
SEQRES  21 C  364  ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU          
SEQRES  22 C  364  ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS          
SEQRES  23 C  364  HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE          
SEQRES  24 C  364  ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP          
SEQRES  25 C  364  LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU          
SEQRES  26 C  364  GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN          
SEQRES  27 C  364  SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG          
SEQRES  28 C  364  GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU          
SEQRES   1 D  364  GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU          
SEQRES   2 D  364  GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN          
SEQRES   3 D  364  LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER          
SEQRES   4 D  364  GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE          
SEQRES   5 D  364  GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL          
SEQRES   6 D  364  ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS          
SEQRES   7 D  364  TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA          
SEQRES   8 D  364  ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR          
SEQRES   9 D  364  PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU          
SEQRES  10 D  364  ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS          
SEQRES  11 D  364  PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER          
SEQRES  12 D  364  GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU          
SEQRES  13 D  364  ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU          
SEQRES  14 D  364  GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN          
SEQRES  15 D  364  ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU          
SEQRES  16 D  364  ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP          
SEQRES  17 D  364  LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER          
SEQRES  18 D  364  GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN          
SEQRES  19 D  364  VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN          
SEQRES  20 D  364  PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP          
SEQRES  21 D  364  ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU          
SEQRES  22 D  364  ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS          
SEQRES  23 D  364  HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE          
SEQRES  24 D  364  ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP          
SEQRES  25 D  364  LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU          
SEQRES  26 D  364  GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN          
SEQRES  27 D  364  SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG          
SEQRES  28 D  364  GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU          
HET     ZN  A 501       1                                                       
HET     MG  A 502       1                                                       
HET    EDO  A 503       4                                                       
HET    EDO  A 504       4                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET    EDO  A 507       4                                                       
HET    EDO  A 508       4                                                       
HET    EDO  A 509       4                                                       
HET    EDO  A 510       4                                                       
HET    EDO  A 511       4                                                       
HET    EDO  A 512       4                                                       
HET    EDO  A 513       4                                                       
HET    EDO  A 514       4                                                       
HET    EPE  A 515      15                                                       
HET    EDO  A 516       4                                                       
HET    E6Z  A 517      31                                                       
HET     ZN  B 501       1                                                       
HET     MG  B 502       1                                                       
HET    EDO  B 503       4                                                       
HET    EDO  B 504       4                                                       
HET    EDO  B 505       4                                                       
HET    EDO  B 506       4                                                       
HET    EDO  B 507       4                                                       
HET    EPE  B 508      15                                                       
HET    E6Z  B 509      31                                                       
HET     ZN  C 501       1                                                       
HET     MG  C 502       1                                                       
HET    EDO  C 503       4                                                       
HET    EDO  C 504       4                                                       
HET    EDO  C 505       4                                                       
HET    EDO  C 506       4                                                       
HET    EDO  C 507       4                                                       
HET    EDO  C 508       4                                                       
HET    EDO  C 509       4                                                       
HET    EDO  C 510       4                                                       
HET    EPE  C 511      15                                                       
HET    E6Z  C 512      31                                                       
HET    EDO  C 513       4                                                       
HET     ZN  D 501       1                                                       
HET     MG  D 502       1                                                       
HET    EDO  D 503       4                                                       
HET    EDO  D 504       4                                                       
HET    EDO  D 505       4                                                       
HET    EDO  D 506       4                                                       
HET    EDO  D 507       4                                                       
HET    EDO  D 508       4                                                       
HET    EDO  D 509       4                                                       
HET    EDO  D 510       4                                                       
HET    EDO  D 511       4                                                       
HET    EDO  D 512       4                                                       
HET    EDO  D 513       4                                                       
HET    EPE  D 514      15                                                       
HET    EDO  D 515       4                                                       
HET    E6Z  D 516      31                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     E6Z 3-{5-[(4AR,8AS)-3-CYCLOHEPTYL-4-OXO-3,4,4A,5,8,8A-               
HETNAM   2 E6Z  HEXAHYDROPHTHALAZIN-1-YL]-2-METHOXYPHENYL}PROP-2-               
HETNAM   3 E6Z  YNAMIDE                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     EPE HEPES                                                            
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL   7  EDO    39(C2 H6 O2)                                                 
FORMUL  19  EPE    4(C8 H18 N2 O4 S)                                            
FORMUL  21  E6Z    4(C25 H29 N3 O3)                                             
FORMUL  60  HOH   *551(H2 O)                                                    
HELIX    1 AA1 THR A   86  LEU A   96  1                                  11    
HELIX    2 AA2 GLU A   97  LYS A  101  5                                   5    
HELIX    3 AA3 HIS A  105  SER A  113  1                                   9    
HELIX    4 AA4 ARG A  116  ARG A  129  1                                  14    
HELIX    5 AA5 ASP A  130  LYS A  136  1                                   7    
HELIX    6 AA6 PRO A  138  HIS A  152  1                                  15    
HELIX    7 AA7 ASN A  161  SER A  177  1                                  17    
HELIX    8 AA8 THR A  178  GLU A  182  5                                   5    
HELIX    9 AA9 THR A  186  HIS A  200  1                                  15    
HELIX   10 AB1 SER A  208  THR A  215  1                                   8    
HELIX   11 AB2 SER A  217  TYR A  223  1                                   7    
HELIX   12 AB3 SER A  227  LEU A  240  1                                  14    
HELIX   13 AB4 LEU A  241  GLU A  243  5                                   3    
HELIX   14 AB5 THR A  253  ALA A  270  1                                  18    
HELIX   15 AB6 THR A  271  SER A  274  5                                   4    
HELIX   16 AB7 LYS A  275  THR A  289  1                                  15    
HELIX   17 AB8 ASN A  302  LEU A  319  1                                  18    
HELIX   18 AB9 SER A  320  LYS A  324  5                                   5    
HELIX   19 AC1 PRO A  325  ARG A  350  1                                  26    
HELIX   20 AC2 ASP A  359  ALA A  363  5                                   5    
HELIX   21 AC3 SER A  364  ILE A  376  1                                  13    
HELIX   22 AC4 ILE A  376  VAL A  388  1                                  13    
HELIX   23 AC5 ALA A  392  THR A  409  1                                  18    
HELIX   24 AC6 ASP B   90  ASP B   98  1                                   9    
HELIX   25 AC7 VAL B   99  LYS B  101  5                                   3    
HELIX   26 AC8 HIS B  105  SER B  113  1                                   9    
HELIX   27 AC9 ARG B  116  ARG B  129  1                                  14    
HELIX   28 AD1 ASP B  130  LYS B  136  1                                   7    
HELIX   29 AD2 PRO B  138  HIS B  152  1                                  15    
HELIX   30 AD3 ASN B  161  SER B  177  1                                  17    
HELIX   31 AD4 THR B  178  GLU B  182  5                                   5    
HELIX   32 AD5 THR B  186  HIS B  200  1                                  15    
HELIX   33 AD6 SER B  208  THR B  215  1                                   8    
HELIX   34 AD7 SER B  217  TYR B  223  1                                   7    
HELIX   35 AD8 SER B  227  LEU B  240  1                                  14    
HELIX   36 AD9 LEU B  241  GLU B  243  5                                   3    
HELIX   37 AE1 THR B  253  ALA B  270  1                                  18    
HELIX   38 AE2 THR B  271  SER B  274  5                                   4    
HELIX   39 AE3 LYS B  275  THR B  289  1                                  15    
HELIX   40 AE4 ASN B  302  LEU B  319  1                                  18    
HELIX   41 AE5 SER B  320  LYS B  324  5                                   5    
HELIX   42 AE6 PRO B  325  ARG B  350  1                                  26    
HELIX   43 AE7 SER B  364  ILE B  376  1                                  13    
HELIX   44 AE8 ILE B  376  VAL B  388  1                                  13    
HELIX   45 AE9 ALA B  392  THR B  409  1                                  18    
HELIX   46 AF1 GLU C   89  GLU C   97  1                                   9    
HELIX   47 AF2 ASP C   98  LYS C  101  5                                   4    
HELIX   48 AF3 HIS C  105  SER C  113  1                                   9    
HELIX   49 AF4 ARG C  116  ARG C  129  1                                  14    
HELIX   50 AF5 ASP C  130  LYS C  136  1                                   7    
HELIX   51 AF6 PRO C  138  HIS C  152  1                                  15    
HELIX   52 AF7 ASN C  161  SER C  177  1                                  17    
HELIX   53 AF8 THR C  178  GLU C  182  5                                   5    
HELIX   54 AF9 THR C  186  HIS C  200  1                                  15    
HELIX   55 AG1 SER C  208  THR C  215  1                                   8    
HELIX   56 AG2 SER C  217  TYR C  223  1                                   7    
HELIX   57 AG3 SER C  227  LEU C  240  1                                  14    
HELIX   58 AG4 LEU C  241  GLU C  243  5                                   3    
HELIX   59 AG5 THR C  253  ALA C  270  1                                  18    
HELIX   60 AG6 THR C  271  SER C  274  5                                   4    
HELIX   61 AG7 LYS C  275  THR C  289  1                                  15    
HELIX   62 AG8 ASN C  302  LEU C  319  1                                  18    
HELIX   63 AG9 SER C  320  LYS C  324  5                                   5    
HELIX   64 AH1 PRO C  325  ARG C  350  1                                  26    
HELIX   65 AH2 SER C  364  ILE C  376  1                                  13    
HELIX   66 AH3 ILE C  376  VAL C  388  1                                  13    
HELIX   67 AH4 ALA C  392  THR C  409  1                                  18    
HELIX   68 AH5 GLU D   89  GLU D   97  1                                   9    
HELIX   69 AH6 HIS D  105  SER D  113  1                                   9    
HELIX   70 AH7 ARG D  116  ARG D  129  1                                  14    
HELIX   71 AH8 ASP D  130  LYS D  136  1                                   7    
HELIX   72 AH9 PRO D  138  HIS D  152  1                                  15    
HELIX   73 AI1 ASN D  161  SER D  177  1                                  17    
HELIX   74 AI2 THR D  178  GLU D  182  5                                   5    
HELIX   75 AI3 THR D  186  HIS D  200  1                                  15    
HELIX   76 AI4 SER D  208  THR D  215  1                                   8    
HELIX   77 AI5 SER D  217  TYR D  223  1                                   7    
HELIX   78 AI6 SER D  227  LEU D  240  1                                  14    
HELIX   79 AI7 LEU D  241  GLU D  243  5                                   3    
HELIX   80 AI8 THR D  253  ALA D  270  1                                  18    
HELIX   81 AI9 THR D  271  SER D  274  5                                   4    
HELIX   82 AJ1 LYS D  275  THR D  289  1                                  15    
HELIX   83 AJ2 ASN D  302  LEU D  319  1                                  18    
HELIX   84 AJ3 SER D  320  LYS D  324  5                                   5    
HELIX   85 AJ4 PRO D  325  ARG D  350  1                                  26    
HELIX   86 AJ5 SER D  364  ILE D  376  1                                  13    
HELIX   87 AJ6 ILE D  376  VAL D  388  1                                  13    
HELIX   88 AJ7 ALA D  392  SER D  408  1                                  17    
SHEET    1 AA1 2 LYS C 291  VAL C 292  0                                        
SHEET    2 AA1 2 LEU C 298  LEU C 299 -1  O  LEU C 299   N  LYS C 291           
LINK         NE2 HIS A 164                ZN    ZN A 501     1555   1555  2.22  
LINK         NE2 HIS A 200                ZN    ZN A 501     1555   1555  2.23  
LINK         OD2 ASP A 201                ZN    ZN A 501     1555   1555  2.10  
LINK         OD1 ASP A 201                MG    MG A 502     1555   1555  2.00  
LINK         OD1 ASP A 318                ZN    ZN A 501     1555   1555  2.24  
LINK        ZN    ZN A 501                 O   HOH A 626     1555   1555  2.03  
LINK        ZN    ZN A 501                 O   HOH A 649     1555   1555  2.37  
LINK        MG    MG A 502                 O   HOH A 613     1555   1555  2.31  
LINK        MG    MG A 502                 O   HOH A 626     1555   1555  2.07  
LINK        MG    MG A 502                 O   HOH A 628     1555   1555  2.24  
LINK        MG    MG A 502                 O   HOH A 688     1555   1555  2.13  
LINK        MG    MG A 502                 O   HOH A 717     1555   1555  2.08  
LINK         NE2 HIS B 164                ZN    ZN B 501     1555   1555  2.17  
LINK         NE2 HIS B 200                ZN    ZN B 501     1555   1555  2.34  
LINK         OD2 ASP B 201                ZN    ZN B 501     1555   1555  2.25  
LINK         OD1 ASP B 201                MG    MG B 502     1555   1555  1.97  
LINK         OD1 ASP B 318                ZN    ZN B 501     1555   1555  2.28  
LINK        ZN    ZN B 501                 O   HOH B 626     1555   1555  2.01  
LINK        ZN    ZN B 501                 O   HOH B 673     1555   1555  2.23  
LINK        MG    MG B 502                 O   HOH B 614     1555   1555  2.12  
LINK        MG    MG B 502                 O   HOH B 626     1555   1555  2.20  
LINK        MG    MG B 502                 O   HOH B 646     1555   1555  2.17  
LINK        MG    MG B 502                 O   HOH B 654     1555   1555  1.96  
LINK        MG    MG B 502                 O   HOH B 658     1555   1555  2.02  
LINK         NE2 HIS C 164                ZN    ZN C 501     1555   1555  2.29  
LINK         NE2 HIS C 200                ZN    ZN C 501     1555   1555  2.26  
LINK         OD2 ASP C 201                ZN    ZN C 501     1555   1555  2.33  
LINK         OD1 ASP C 201                MG    MG C 502     1555   1555  2.02  
LINK         OD1 ASP C 318                ZN    ZN C 501     1555   1555  2.18  
LINK        ZN    ZN C 501                 O   HOH C 625     1555   1555  2.15  
LINK        ZN    ZN C 501                 O   HOH C 658     1555   1555  2.16  
LINK        MG    MG C 502                 O   HOH C 607     1555   1555  2.05  
LINK        MG    MG C 502                 O   HOH C 625     1555   1555  2.09  
LINK        MG    MG C 502                 O   HOH C 645     1555   1555  2.05  
LINK        MG    MG C 502                 O   HOH C 657     1555   1555  2.18  
LINK        MG    MG C 502                 O   HOH C 675     1555   1555  2.01  
LINK         NE2 HIS D 164                ZN    ZN D 501     1555   1555  2.31  
LINK         NE2 HIS D 200                ZN    ZN D 501     1555   1555  2.16  
LINK         OD2 ASP D 201                ZN    ZN D 501     1555   1555  2.13  
LINK         OD1 ASP D 201                MG    MG D 502     1555   1555  2.07  
LINK         OD1 ASP D 318                ZN    ZN D 501     1555   1555  2.24  
LINK        ZN    ZN D 501                 O   HOH D 617     1555   1555  2.35  
LINK        ZN    ZN D 501                 O   HOH D 654     1555   1555  2.37  
LINK        MG    MG D 502                 O   HOH D 617     1555   1555  2.04  
LINK        MG    MG D 502                 O   HOH D 652     1555   1555  2.03  
LINK        MG    MG D 502                 O   HOH D 671     1555   1555  2.24  
LINK        MG    MG D 502                 O   HOH D 689     1555   1555  2.19  
LINK        MG    MG D 502                 O   HOH D 709     1555   1555  1.95  
CISPEP   1 HIS A  389    PRO A  390          0         1.62                     
CISPEP   2 HIS B  389    PRO B  390          0        -5.80                     
CISPEP   3 HIS C  389    PRO C  390          0         3.05                     
CISPEP   4 HIS D  389    PRO D  390          0        -2.50                     
SITE     1 AC1  6 HIS A 164  HIS A 200  ASP A 201  ASP A 318                    
SITE     2 AC1  6 HOH A 626  HOH A 649                                          
SITE     1 AC2  6 ASP A 201  HOH A 613  HOH A 626  HOH A 628                    
SITE     2 AC2  6 HOH A 688  HOH A 717                                          
SITE     1 AC3  5 SER A 208  PRO A 356  CYS A 358  E6Z A 517                    
SITE     2 AC3  5 HOH A 618                                                     
SITE     1 AC4  5 ASN A 115  ALA A 155  ASN A 161  ASN A 162                    
SITE     2 AC4  5 ARG A 335                                                     
SITE     1 AC5  5 THR A 186  GLU A 189  SER A 259  MET A 263                    
SITE     2 AC5  5 EDO A 512                                                     
SITE     1 AC6  6 GLU A 218  HOH A 722  HIS C 152  LYS C 239                    
SITE     2 AC6  6 LEU C 240  HOH C 614                                          
SITE     1 AC7  4 LEU A 175  THR A 178  TRP A 384  ASP A 391                    
SITE     1 AC8  3 THR A 134  LYS A 136  EDO A 509                               
SITE     1 AC9  5 THR A 134  PHE A 135  ASN A 251  GLN A 256                    
SITE     2 AC9  5 EDO A 508                                                     
SITE     1 AD1  4 HIS A 152  GLU A 243  SER C 217  ARG C 350                    
SITE     1 AD2  6 PHE A 238  PHE A 249  ARG A 257  ARG A 261                    
SITE     2 AD2  6 HOH A 633  HOH A 642                                          
SITE     1 AD3  6 SER A 259  LYS A 262  TYR A 303  EDO A 505                    
SITE     2 AD3  6 EDO A 514  HOH A 660                                          
SITE     1 AD4  7 ARG A 116  GLU A 150  ASP A 151  TYR A 153                    
SITE     2 AD4  7 HOH A 604  HOH A 719  EDO C 510                               
SITE     1 AD5  3 EDO A 512  HOH A 602  HOH A 721                               
SITE     1 AD6  9 HIS A 105  VAL A 106  PHE A 107  ARG A 108                    
SITE     2 AD6  9 GLU A 111  GLN A 327  LEU A 328  GLN A 331                    
SITE     3 AD6  9 HOH A 691                                                     
SITE     1 AD7  5 LYS A 262  ASP A 266  HOH A 700  HOH B 619                    
SITE     2 AD7  5 HOH B 655                                                     
SITE     1 AD8 15 MET A 273  ASP A 318  LEU A 319  THR A 333                    
SITE     2 AD8 15 ILE A 336  MET A 337  MET A 357  SER A 368                    
SITE     3 AD8 15 GLN A 369  PHE A 372  ILE A 376  EDO A 503                    
SITE     4 AD8 15 HOH A 618  HOH A 693  HOH A 717                               
SITE     1 AD9  6 HIS B 164  HIS B 200  ASP B 201  ASP B 318                    
SITE     2 AD9  6 HOH B 626  HOH B 673                                          
SITE     1 AE1  6 ASP B 201  HOH B 614  HOH B 626  HOH B 646                    
SITE     2 AE1  6 HOH B 654  HOH B 658                                          
SITE     1 AE2  3 SER B 208  PRO B 356  HOH B 630                               
SITE     1 AE3  5 GLU B 218  EDO B 507  HOH B 632  MET C 222                    
SITE     2 AE3  5 LYS D 239                                                     
SITE     1 AE4  4 ASN B 115  ALA B 155  ASN B 162  ARG B 335                    
SITE     1 AE5  6 PHE B 211  ASN B 214  GLU B 347  MET B 352                    
SITE     2 AE5  6 GLU B 353  SER B 355                                          
SITE     1 AE6  3 GLU B 218  EDO B 504  LYS D 239                               
SITE     1 AE7  8 HIS B 105  VAL B 106  PHE B 107  ARG B 108                    
SITE     2 AE7  8 GLU B 111  GLN B 327  LEU B 328  GLN B 331                    
SITE     1 AE8 11 MET B 273  ASP B 318  ILE B 336  MET B 337                    
SITE     2 AE8 11 MET B 357  VAL B 365  SER B 368  GLN B 369                    
SITE     3 AE8 11 PHE B 372  HOH B 671  HOH B 673                               
SITE     1 AE9  6 HIS C 164  HIS C 200  ASP C 201  ASP C 318                    
SITE     2 AE9  6 HOH C 625  HOH C 658                                          
SITE     1 AF1  6 ASP C 201  HOH C 607  HOH C 625  HOH C 645                    
SITE     2 AF1  6 HOH C 657  HOH C 675                                          
SITE     1 AF2  4 PHE C 249  ARG C 257  HOH C 605  HOH C 653                    
SITE     1 AF3  4 LEU C 175  THR C 178  TRP C 384  ALA C 392                    
SITE     1 AF4  3 LYS A 239  MET B 222  GLU C 218                               
SITE     1 AF5  3 THR C 148  HIS C 152  GLU C 243                               
SITE     1 AF6  5 ASN C 115  ARG C 116  GLU C 150  ASP C 151                    
SITE     2 AF6  5 TYR C 153                                                     
SITE     1 AF7  3 PRO C 356  E6Z C 512  HOH C 638                               
SITE     1 AF8  3 LYS C 262  ASP C 266  ASP D 225                               
SITE     1 AF9  5 GLY A 114  ASN A 115  EDO A 513  ARG C 342                    
SITE     2 AF9  5 HOH C 619                                                     
SITE     1 AG1  8 HIS C 105  VAL C 106  PHE C 107  ARG C 108                    
SITE     2 AG1  8 GLU C 111  GLN C 327  LEU C 328  GLN C 331                    
SITE     1 AG2 12 HIS C 160  MET C 273  LEU C 319  ILE C 336                    
SITE     2 AG2 12 MET C 337  MET C 357  SER C 368  GLN C 369                    
SITE     3 AG2 12 PHE C 372  EDO C 508  HOH C 638  HOH C 656                    
SITE     1 AG3  3 ASN C 214  GLU C 353  GLN D 258                               
SITE     1 AG4  6 HIS D 164  HIS D 200  ASP D 201  ASP D 318                    
SITE     2 AG4  6 HOH D 617  HOH D 654                                          
SITE     1 AG5  6 ASP D 201  HOH D 617  HOH D 652  HOH D 671                    
SITE     2 AG5  6 HOH D 689  HOH D 709                                          
SITE     1 AG6  4 SER D 294  SER D 295  HOH D 609  HOH D 660                    
SITE     1 AG7  4 PHE D 340  PRO D 356  CYS D 358  E6Z D 516                    
SITE     1 AG8  5 PHE D 238  ARG D 257  ARG D 261  HOH D 647                    
SITE     2 AG8  5 HOH D 672                                                     
SITE     1 AG9  4 HOH C 621  LYS D 262  ASP D 266  HOH D 657                    
SITE     1 AH1  4 ASN D 115  ALA D 155  ASN D 161  ASN D 162                    
SITE     1 AH2  6 LEU D 175  THR D 178  TRP D 384  VAL D 388                    
SITE     2 AH2  6 ASP D 391  HOH D 662                                          
SITE     1 AH3  6 GLN D 250  LEU D 252  THR D 253  ARG D 257                    
SITE     2 AH3  6 HOH D 632  HOH D 728                                          
SITE     1 AH4  4 ARG D 129  LEU D 131  ASP D 187  ILE D 190                    
SITE     1 AH5  1 GLU D 182                                                     
SITE     1 AH6  1 GLN D 393                                                     
SITE     1 AH7  1 ASP D  98                                                     
SITE     1 AH8  7 ASP C 394  HIS D 105  VAL D 106  PHE D 107                    
SITE     2 AH8  7 ARG D 108  LEU D 328  GLN D 331                               
SITE     1 AH9  2 HIS D 152  GLU D 243                                          
SITE     1 AI1 10 MET D 273  ASP D 318  LEU D 319  ILE D 336                    
SITE     2 AI1 10 MET D 337  MET D 357  SER D 368  GLN D 369                    
SITE     3 AI1 10 PHE D 372  EDO D 504                                          
CRYST1   99.140  111.430  160.060  90.00  90.00  90.00 P 21 21 21   16          
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      0.010087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008974  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006248        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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