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Database: PDB
Entry: 5GGZ
LinkDB: 5GGZ
Original site: 5GGZ 
HEADER    CHAPERONE/CHAPERONE INHIBITOR           16-JUN-16   5GGZ              
TITLE     CRYSTAL STRUCTURE OF NOVEL INHIBITOR BOUND WITH HSP90                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: B, A, D, C;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 16-225;                                       
COMPND   5 SYNONYM: HSP90;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSSETA(DE3) PLYSS;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    HSP90, CHAPERONE-CHAPERONE INHIBITOR COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.T.CHEN,J.LI,Y.C.XU                                                  
REVDAT   1   08-MAR-17 5GGZ    0                                                
JRNL        AUTH   F.JIANG,H.J.WANG,Y.H.JIN,Q.ZHANG,Z.H.WANG,J.M.JIA,F.LIU,     
JRNL        AUTH 2 L.WANG,Q.C.BAO,D.D.LI,Q.D.YOU,X.L.XU                         
JRNL        TITL   NOVEL TETRAHYDROPYRIDO[4,3-D]PYRIMIDINES AS POTENT           
JRNL        TITL 2 INHIBITORS OF CHAPERONE HEAT SHOCK PROTEIN 90                
JRNL        REF    J. MED. CHEM.                 V.  59 10498 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27933959                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00912                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 68699                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1990                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.9268 -  4.8527    0.85     4635   138  0.1734 0.2141        
REMARK   3     2  4.8527 -  3.8531    0.87     4652   131  0.1585 0.2199        
REMARK   3     3  3.8531 -  3.3664    0.88     4733   142  0.1913 0.2557        
REMARK   3     4  3.3664 -  3.0588    0.90     4767   141  0.2124 0.2566        
REMARK   3     5  3.0588 -  2.8396    0.91     4818   148  0.2221 0.2741        
REMARK   3     6  2.8396 -  2.6722    0.91     4817   147  0.2256 0.2411        
REMARK   3     7  2.6722 -  2.5384    0.92     4901   147  0.2240 0.2791        
REMARK   3     8  2.5384 -  2.4280    0.92     4860   147  0.2295 0.3473        
REMARK   3     9  2.4280 -  2.3345    0.92     4895   150  0.2281 0.2813        
REMARK   3    10  2.3345 -  2.2540    0.93     4866   137  0.2384 0.3029        
REMARK   3    11  2.2540 -  2.1835    0.93     4952   149  0.2530 0.3667        
REMARK   3    12  2.1835 -  2.1211    0.93     4951   145  0.2596 0.3417        
REMARK   3    13  2.1211 -  2.0653    0.93     4905   148  0.2694 0.2819        
REMARK   3    14  2.0653 -  2.0149    0.75     3957   120  0.2662 0.3348        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.03                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           6809                                  
REMARK   3   ANGLE     :  1.077           9187                                  
REMARK   3   CHIRALITY :  0.045           1041                                  
REMARK   3   PLANARITY :  0.004           1161                                  
REMARK   3   DIHEDRAL  : 16.633           2525                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5GGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000735.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68734                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 0.2 M MGCL2, 26% PEG 4000,   
REMARK 280  PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.29050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     LYS B   225                                                      
REMARK 465     LYS A   225                                                      
REMARK 465     LYS C   225                                                      
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   OG   SER A   211     OE1  GLN C   133              2.14            
REMARK 500   O    HOH B   416     O    HOH B   503              2.17            
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    TYR B  38      108.13   -162.69                                   
REMARK 500    ASN B 105      -58.68   -135.17                                   
REMARK 500    ALA B 124       29.19    -76.31                                   
REMARK 500    ALA B 166     -145.32     60.93                                   
REMARK 500    SER B 211       44.46   -140.45                                   
REMARK 500    ALA A 166     -142.30     63.05                                   
REMARK 500    TYR D  38      113.16   -162.68                                   
REMARK 500    ALA D 166     -147.31     63.59                                   
REMARK 500    TYR C  38      107.40   -161.46                                   
REMARK 500    THR C  94       42.57   -108.79                                   
REMARK 500    ASN C 105      -59.69   -141.83                                   
REMARK 500    ALA C 166     -148.43     63.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6TN B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6TN A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6TN D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6TN C 301                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS BELIEVE THAT THE SEQUENCE IS CORRECT AND THERE ARE THE   
REMARK 999 TRUE IDENTITIES OF THESE RESIDUES.                                   
DBREF  5GGZ B   16   225  UNP    P07900   HS90A_HUMAN     16    225             
DBREF  5GGZ A   16   225  UNP    P07900   HS90A_HUMAN     16    225             
DBREF  5GGZ D   16   225  UNP    P07900   HS90A_HUMAN     16    225             
DBREF  5GGZ C   16   225  UNP    P07900   HS90A_HUMAN     16    225             
SEQADV 5GGZ VAL B  126  UNP  P07900    ALA   126 SEE SEQUENCE DETAILS           
SEQADV 5GGZ LYS B  225  UNP  P07900    GLU   225 SEE SEQUENCE DETAILS           
SEQADV 5GGZ VAL A  126  UNP  P07900    ALA   126 SEE SEQUENCE DETAILS           
SEQADV 5GGZ LYS A  225  UNP  P07900    GLU   225 SEE SEQUENCE DETAILS           
SEQADV 5GGZ VAL D  126  UNP  P07900    ALA   126 SEE SEQUENCE DETAILS           
SEQADV 5GGZ LYS D  225  UNP  P07900    GLU   225 SEE SEQUENCE DETAILS           
SEQADV 5GGZ VAL C  126  UNP  P07900    ALA   126 SEE SEQUENCE DETAILS           
SEQADV 5GGZ LYS C  225  UNP  P07900    GLU   225 SEE SEQUENCE DETAILS           
SEQRES   1 B  210  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   2 B  210  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   3 B  210  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP          
SEQRES   4 B  210  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   5 B  210  SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU          
SEQRES   6 B  210  ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP          
SEQRES   7 B  210  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   8 B  210  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES   9 B  210  GLU ALA LEU GLN ALA GLY VAL ASP ILE SER MET ILE GLY          
SEQRES  10 B  210  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  11 B  210  GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  12 B  210  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  13 B  210  VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR          
SEQRES  14 B  210  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  15 B  210  LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS          
SEQRES  16 B  210  SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU          
SEQRES  17 B  210  LYS LYS                                                      
SEQRES   1 A  210  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   2 A  210  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   3 A  210  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP          
SEQRES   4 A  210  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   5 A  210  SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU          
SEQRES   6 A  210  ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP          
SEQRES   7 A  210  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   8 A  210  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES   9 A  210  GLU ALA LEU GLN ALA GLY VAL ASP ILE SER MET ILE GLY          
SEQRES  10 A  210  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  11 A  210  GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  12 A  210  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  13 A  210  VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR          
SEQRES  14 A  210  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  15 A  210  LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS          
SEQRES  16 A  210  SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU          
SEQRES  17 A  210  LYS LYS                                                      
SEQRES   1 D  210  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   2 D  210  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   3 D  210  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP          
SEQRES   4 D  210  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   5 D  210  SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU          
SEQRES   6 D  210  ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP          
SEQRES   7 D  210  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   8 D  210  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES   9 D  210  GLU ALA LEU GLN ALA GLY VAL ASP ILE SER MET ILE GLY          
SEQRES  10 D  210  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  11 D  210  GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  12 D  210  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  13 D  210  VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR          
SEQRES  14 D  210  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  15 D  210  LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS          
SEQRES  16 D  210  SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU          
SEQRES  17 D  210  LYS LYS                                                      
SEQRES   1 C  210  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   2 C  210  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   3 C  210  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP          
SEQRES   4 C  210  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   5 C  210  SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU          
SEQRES   6 C  210  ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP          
SEQRES   7 C  210  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   8 C  210  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES   9 C  210  GLU ALA LEU GLN ALA GLY VAL ASP ILE SER MET ILE GLY          
SEQRES  10 C  210  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  11 C  210  GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  12 C  210  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  13 C  210  VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR          
SEQRES  14 C  210  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  15 C  210  LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS          
SEQRES  16 C  210  SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU          
SEQRES  17 C  210  LYS LYS                                                      
HET    6TN  B 301      26                                                       
HET    6TN  A 301      26                                                       
HET    6TN  D 301      26                                                       
HET    6TN  C 301      26                                                       
HETNAM     6TN [2,4-BIS(OXIDANYL)-5-PROPAN-2-YL-PHENYL]-(2-ETHOXY-7,8-          
HETNAM   2 6TN  DIHYDRO-5~{H}-PYRIDO[4,3-D]PYRIMIDIN-6-YL)METHANONE             
FORMUL   5  6TN    4(C19 H23 N3 O4)                                             
FORMUL   9  HOH   *409(H2 O)                                                    
HELIX    1 AA1 GLN B   23  THR B   36  1                                  14    
HELIX    2 AA2 GLU B   42  ASP B   66  1                                  25    
HELIX    3 AA3 PRO B   67  ASP B   71  5                                   5    
HELIX    4 AA4 THR B   99  ASN B  105  1                                   7    
HELIX    5 AA5 ASN B  105  ALA B  111  1                                   7    
HELIX    6 AA6 ALA B  111  ALA B  124  1                                  14    
HELIX    7 AA7 ASP B  127  GLY B  135  5                                   9    
HELIX    8 AA8 VAL B  136  LEU B  143  5                                   8    
HELIX    9 AA9 GLN B  194  LEU B  198  5                                   5    
HELIX   10 AB1 GLU B  199  SER B  211  1                                  13    
HELIX   11 AB2 GLN A   23  THR A   36  1                                  14    
HELIX   12 AB3 GLU A   42  ASP A   66  1                                  25    
HELIX   13 AB4 PRO A   67  GLY A   73  5                                   7    
HELIX   14 AB5 THR A   99  LEU A  107  1                                   9    
HELIX   15 AB6 LYS A  112  ALA A  124  1                                  13    
HELIX   16 AB7 ASP A  127  GLY A  135  5                                   9    
HELIX   17 AB8 VAL A  136  LEU A  143  5                                   8    
HELIX   18 AB9 GLU A  192  LEU A  198  5                                   7    
HELIX   19 AC1 GLU A  199  LYS A  209  1                                  11    
HELIX   20 AC2 GLN D   23  THR D   36  1                                  14    
HELIX   21 AC3 GLU D   42  ASP D   66  1                                  25    
HELIX   22 AC4 PRO D   67  GLY D   73  5                                   7    
HELIX   23 AC5 THR D   99  LEU D  107  1                                   9    
HELIX   24 AC6 LYS D  112  ALA D  124  1                                  13    
HELIX   25 AC7 ASP D  127  GLY D  135  5                                   9    
HELIX   26 AC8 VAL D  136  LEU D  143  5                                   8    
HELIX   27 AC9 GLU D  192  LEU D  198  5                                   7    
HELIX   28 AD1 GLU D  199  LYS D  209  1                                  11    
HELIX   29 AD2 GLN C   23  THR C   36  1                                  14    
HELIX   30 AD3 GLU C   42  ASP C   66  1                                  25    
HELIX   31 AD4 PRO C   67  ASP C   71  5                                   5    
HELIX   32 AD5 THR C   99  ASN C  105  1                                   7    
HELIX   33 AD6 ASN C  105  ALA C  124  1                                  20    
HELIX   34 AD7 ASP C  127  GLY C  135  5                                   9    
HELIX   35 AD8 VAL C  136  LEU C  143  5                                   8    
HELIX   36 AD9 GLU C  192  LEU C  198  5                                   7    
HELIX   37 AE1 GLU C  199  SER C  211  1                                  13    
SHEET    1 AA1 8 GLU B  18  ALA B  21  0                                        
SHEET    2 AA1 8 SER B 169  THR B 174 -1  O  PHE B 170   N  PHE B  20           
SHEET    3 AA1 8 TYR B 160  SER B 164 -1  N  ALA B 161   O  ARG B 173           
SHEET    4 AA1 8 ALA B 145  LYS B 153 -1  N  VAL B 150   O  TRP B 162           
SHEET    5 AA1 8 GLY B 183  LEU B 190 -1  O  ILE B 187   N  THR B 149           
SHEET    6 AA1 8 THR B  88  ASP B  93 -1  N  ILE B  91   O  VAL B 186           
SHEET    7 AA1 8 ILE B  78  ASN B  83 -1  N  ASN B  83   O  THR B  88           
SHEET    8 AA1 8 ILE B 218  LEU B 220  1  O  THR B 219   N  LEU B  80           
SHEET    1 AA2 8 GLU A  18  ALA A  21  0                                        
SHEET    2 AA2 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3 AA2 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4 AA2 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5 AA2 8 GLY A 183  LEU A 190 -1  O  LYS A 185   N  ILE A 151           
SHEET    6 AA2 8 THR A  88  ASP A  93 -1  N  LEU A  89   O  LEU A 188           
SHEET    7 AA2 8 ILE A  78  ASN A  83 -1  N  ILE A  81   O  THR A  90           
SHEET    8 AA2 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SHEET    1 AA3 8 GLU D  18  ALA D  21  0                                        
SHEET    2 AA3 8 SER D 169  THR D 174 -1  O  PHE D 170   N  PHE D  20           
SHEET    3 AA3 8 TYR D 160  SER D 164 -1  N  ALA D 161   O  ARG D 173           
SHEET    4 AA3 8 ALA D 145  LYS D 153 -1  N  VAL D 150   O  TRP D 162           
SHEET    5 AA3 8 GLY D 183  LEU D 190 -1  O  LYS D 185   N  ILE D 151           
SHEET    6 AA3 8 THR D  88  ASP D  93 -1  N  ILE D  91   O  VAL D 186           
SHEET    7 AA3 8 ILE D  78  ASN D  83 -1  N  ILE D  81   O  THR D  90           
SHEET    8 AA3 8 ILE D 218  LEU D 220  1  O  THR D 219   N  ILE D  78           
SHEET    1 AA4 8 GLU C  18  ALA C  21  0                                        
SHEET    2 AA4 8 SER C 169  THR C 174 -1  O  PHE C 170   N  PHE C  20           
SHEET    3 AA4 8 TYR C 160  SER C 164 -1  N  ALA C 161   O  ARG C 173           
SHEET    4 AA4 8 ALA C 145  LYS C 153 -1  N  VAL C 150   O  TRP C 162           
SHEET    5 AA4 8 GLY C 183  LEU C 190 -1  O  ILE C 187   N  THR C 149           
SHEET    6 AA4 8 THR C  88  ASP C  93 -1  N  ILE C  91   O  VAL C 186           
SHEET    7 AA4 8 ILE C  78  ASN C  83 -1  N  ASN C  83   O  THR C  88           
SHEET    8 AA4 8 ILE C 218  LEU C 220  1  O  THR C 219   N  ILE C  78           
SITE     1 AC1 15 ASN B  51  ALA B  55  LYS B  58  ASP B  93                    
SITE     2 AC1 15 ILE B  96  GLY B  97  MET B  98  LEU B 107                    
SITE     3 AC1 15 PHE B 138  THR B 184  VAL B 186  HOH B 405                    
SITE     4 AC1 15 HOH B 444  HOH B 457  TYR D  61                               
SITE     1 AC2 11 ASN A  51  ALA A  55  ASP A  93  ILE A  96                    
SITE     2 AC2 11 GLY A  97  PHE A 138  THR A 184  VAL A 186                    
SITE     3 AC2 11 HOH A 409  HOH A 438  TYR C  61                               
SITE     1 AC3 11 TYR B  61  ASN D  51  ALA D  55  ASP D  93                    
SITE     2 AC3 11 ILE D  96  GLY D  97  PHE D 138  THR D 184                    
SITE     3 AC3 11 VAL D 186  HOH D 421  HOH D 452                               
SITE     1 AC4 14 TYR A  61  ASN C  51  ALA C  55  LYS C  58                    
SITE     2 AC4 14 ASP C  93  ILE C  96  GLY C  97  MET C  98                    
SITE     3 AC4 14 LEU C 107  PHE C 138  THR C 184  VAL C 186                    
SITE     4 AC4 14 HOH C 414  HOH C 437                                          
CRYST1   66.841   88.581   99.382  90.00  90.08  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014961  0.000000  0.000022        0.00000                         
SCALE2      0.000000  0.011289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010062        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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