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Database: PDB
Entry: 3WQ9
LinkDB: 3WQ9
Original site: 3WQ9 
HEADER    CHAPERONE                               23-JAN-14   3WQ9              
TITLE     CRYSTAL STRUCTURE OF HSP90-ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH 2- 
TITLE    2 (4-HYDROXY-CYCLOHEXYLAMINO)-4-[5-(4-PHENYL-IMIDAZOL-1-YL)-           
TITLE    3 ISOQUINOLIN-1-YL]-BENZAMIDE                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, UNP RESIDUES 1-236;                     
COMPND   5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN   
COMPND   6 NY-REN-38;                                                           
COMPND   7 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: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET19A                                    
KEYWDS    HYDROLASE, ATP BINDING, CHAPERONE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.T.CHONG,S.YAMASHITA,H.OSHIUMI,T.UNO,M.KITADE                        
REVDAT   1   25-FEB-15 3WQ9    0                                                
JRNL        AUTH   C.YOSHIMURA,S.YAMASHITA,H.OSHIUMI,T.UNO,Y.KAWAI,K.T.CHONG,   
JRNL        AUTH 2 Y.KODAMA,M.KITADE,S.OHKUBO                                   
JRNL        TITL   EVOLUTION OF HIGHLY SELECTIVE HSP90 / INHIBITORS BY          
JRNL        TITL 2 STRUCTURE AND THERMODYNAMICS GUIDED DESIGN                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23092                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1234                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1649                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.5160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1664                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 169                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.137         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.848         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
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):  1733 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2338 ; 1.945 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   210 ; 6.039 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    77 ;38.140 ;25.065       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   317 ;15.108 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;19.349 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   263 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1283 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1043 ; 1.290 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1685 ; 2.192 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   690 ; 3.110 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   653 ; 4.989 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3WQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096656.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24346                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 6.950                              
REMARK 200  R MERGE                    (I) : 0.02600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.04                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, 200MM NACL, 50MM TRIS PH       
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.57400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.57400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.68500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.29250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.68500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.29250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.57400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.68500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.29250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.57400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.68500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.29250            
REMARK 290   SMTRY3   8  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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -92.58500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 453  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 552  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 564  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
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 A  38      129.38    -38.10                                   
REMARK 500    ASN A  40       55.94    -96.49                                   
REMARK 500    ASN A 105      -64.48   -122.30                                   
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 YUK A 301                 
DBREF  3WQ9 A    1   236  UNP    P07900   HS90A_HUMAN      1    236             
SEQADV 3WQ9 HIS A    0  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  237  HIS MET PRO GLU GLU THR GLN THR GLN ASP GLN PRO MET          
SEQRES   2 A  237  GLU GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA GLU          
SEQRES   3 A  237  ILE ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE TYR          
SEQRES   4 A  237  SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER ASN          
SEQRES   5 A  237  SER SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER LEU          
SEQRES   6 A  237  THR ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU HIS          
SEQRES   7 A  237  ILE ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU THR          
SEQRES   8 A  237  ILE VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP LEU          
SEQRES   9 A  237  ILE ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR LYS          
SEQRES  10 A  237  ALA PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE SER          
SEQRES  11 A  237  MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA TYR          
SEQRES  12 A  237  LEU VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS ASN          
SEQRES  13 A  237  ASP ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY GLY          
SEQRES  14 A  237  SER PHE THR VAL ARG THR ASP THR GLY GLU PRO MET GLY          
SEQRES  15 A  237  ARG GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN          
SEQRES  16 A  237  THR GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL          
SEQRES  17 A  237  LYS LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR LEU          
SEQRES  18 A  237  PHE VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP ASP          
SEQRES  19 A  237  GLU ALA GLU                                                  
HET    YUK  A 301      38                                                       
HETNAM     YUK 2-[(TRANS-4-HYDROXYCYCLOHEXYL)AMINO]-4-[5-(4-PHENYL-1H-          
HETNAM   2 YUK  IMIDAZOL-1-YL)ISOQUINOLIN-1-YL]BENZAMIDE                        
FORMUL   2  YUK    C31 H29 N5 O2                                                
FORMUL   3  HOH   *169(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  ASP A   66  1                                  25    
HELIX    3   3 PRO A   67  ASP A   71  5                                   5    
HELIX    4   4 THR A   99  ASN A  105  1                                   7    
HELIX    5   5 ASN A  105  GLY A  125  1                                  21    
HELIX    6   6 ASP A  127  GLY A  135  5                                   9    
HELIX    7   7 VAL A  136  TYR A  139  5                                   4    
HELIX    8   8 SER A  140  VAL A  144  1                                   5    
HELIX    9   9 GLN A  194  LEU A  198  5                                   5    
HELIX   10  10 GLU A  199  SER A  211  1                                  13    
SHEET    1   A 8 VAL A  17  ALA A  21  0                                        
SHEET    2   A 8 SER A 169  THR A 174 -1  O  VAL A 172   N  GLU A  18           
SHEET    3   A 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4   A 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5   A 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6   A 8 THR A  88  ASP A  93 -1  N  ASP A  93   O  THR A 184           
SHEET    7   A 8 ILE A  78  ASN A  83 -1  N  ASN A  79   O  VAL A  92           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SITE     1 AC1 19 GLN A  23  SER A  52  ALA A  55  LYS A  58                    
SITE     2 AC1 19 ASP A  93  MET A  98  LEU A 103  ILE A 104                    
SITE     3 AC1 19 GLY A 108  PHE A 138  TYR A 139  TRP A 162                    
SITE     4 AC1 19 PHE A 170  THR A 184  LYS A 224  HOH A 405                    
SITE     5 AC1 19 HOH A 412  HOH A 471  HOH A 489                               
CRYST1   67.370   92.585   85.148  90.00  90.00  90.00 C 2 2 21      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      0.014843  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011744        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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