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Database: PDB
Entry: 1YC1
LinkDB: 1YC1
Original site: 1YC1 
HEADER    CELL CYCLE                              21-DEC-04   1YC1              
TITLE     CRYSTAL STRUCTURES OF HUMAN HSP90ALPHA COMPLEXED WITH                 
TITLE    2 DIHYDROXYPHENYLPYRAZOLES                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL ATP BINDING DOMAIN RESIDUES 9-223;              
COMPND   5 SYNONYM: HSP 86;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSPCA, HSP90A, HSPC1;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    CELL-CYCLE, CANCER, DRUG DESIGN, CELL CYCLE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KREUSCH,S.HAN,A.BRINKER,V.ZHOU,H.CHOI,Y.HE,S.A.LESLEY,              
AUTHOR   2 J.CALDWELL,X.GU                                                      
REVDAT   2   24-FEB-09 1YC1    1       VERSN                                    
REVDAT   1   22-FEB-05 1YC1    0                                                
JRNL        AUTH   A.KREUSCH,S.HAN,A.BRINKER,V.ZHOU,H.S.CHOI,Y.HE,              
JRNL        AUTH 2 S.A.LESLEY,J.CALDWELL,X.J.GU                                 
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN HSP90ALPHA-COMPLEXED             
JRNL        TITL 2 WITH DIHYDROXYPHENYLPYRAZOLES.                               
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15  1475 2005              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   15713410                                                     
JRNL        DOI    10.1016/J.BMCL.2004.12.087                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1654342.920                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 31248                          
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 SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1553                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4877                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE                    : 0.2350                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 240                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1655                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 307                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.19000                                             
REMARK   3    B22 (A**2) : 2.15000                                              
REMARK   3    B33 (A**2) : -0.96000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.06                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.044                           
REMARK   3   BOND ANGLES            (DEGREES) : 4.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 11.54                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.430 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.260 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.290 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 46.27                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : 3129_CORRECT.PARAM                             
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : 3129_CORRECT.TOP                               
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YC1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031362.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31248                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25300                            
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: 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   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, LICL, PH 9.0, VAPOR            
REMARK 280  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       44.19300            
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       44.19300            
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       35.80550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.80550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.19300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.80550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.50000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.19300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.80550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.50000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THIS PROTEIN IS A MONOMER                                    
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -27                                                      
REMARK 465     ARG A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     SER A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     MET A   -16                                                      
REMARK 465     ALA A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     GLN A    -9                                                      
REMARK 465     GLN A    -8                                                      
REMARK 465     MET A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     ARG A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     TRP A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER 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   225                                                      
REMARK 465     ARG A   226                                                      
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: 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   O    HOH A   470     O    HOH A   687              1.94            
REMARK 500   N    GLY A   181     O    HOH A   697              2.02            
REMARK 500   N    GLN A   212     O    HOH A   705              2.07            
REMARK 500   O    LYS A   208     O    HOH A   705              2.11            
REMARK 500   O    GLN A   212     O    HOH A   706              2.13            
REMARK 500   O    HOH A   487     O    HOH A   708              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A    61     O    HIS A   210     4565     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  87   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    PHE A 213   C   -  N   -  CA  ANGL. DEV. =  17.2 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    TYR A  38      125.57    -37.65                                   
REMARK 500    ALA A 111     -125.29     52.37                                   
REMARK 500    ALA A 124       -3.72    -52.66                                   
REMARK 500    ILE A 128       -4.77    -54.94                                   
REMARK 500    ALA A 166     -147.48     66.96                                   
REMARK 500    ARG A 182      139.37   -174.86                                   
REMARK 500    SER A 211       -3.57   -146.25                                   
REMARK 500    GLN A 212       17.69    -67.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 648        DISTANCE =  5.71 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4BC A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YC3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1YC4   RELATED DB: PDB                                   
DBREF  1YC1 A    9   236  UNP    P07900   HS90A_HUMAN      8    235             
SEQADV 1YC1 MET A  -27  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ARG A  -26  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A  -25  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 SER A  -24  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -23  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -22  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -21  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -20  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -19  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 HIS A  -18  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A  -17  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 MET A  -16  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ALA A  -15  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 SER A  -14  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 MET A  -13  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 THR A  -12  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A  -11  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A  -10  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLN A   -9  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLN A   -8  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 MET A   -7  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A   -6  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ARG A   -5  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A   -4  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 LEU A   -3  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 TYR A   -2  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A   -1  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A    0  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A    1  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A    2  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 LYS A    3  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ASP A    4  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 ARG A    5  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 TRP A    6  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 GLY A    7  UNP  P07900              CLONING ARTIFACT               
SEQADV 1YC1 SER A    8  UNP  P07900              CLONING ARTIFACT               
SEQRES   1 A  264  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 A  264  SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR          
SEQRES   3 A  264  ASP ASP ASP ASP LYS ASP ARG TRP GLY SER ASP GLN PRO          
SEQRES   4 A  264  MET GLU GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA          
SEQRES   5 A  264  GLU ILE ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE          
SEQRES   6 A  264  TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER          
SEQRES   7 A  264  ASN SER SER ASP ALA LEU ASP LYS ILE ARG TYR GLU THR          
SEQRES   8 A  264  LEU THR ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU          
SEQRES   9 A  264  HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU          
SEQRES  10 A  264  THR ILE VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP          
SEQRES  11 A  264  LEU ILE ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR          
SEQRES  12 A  264  LYS ALA PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE          
SEQRES  13 A  264  SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA          
SEQRES  14 A  264  TYR LEU VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS          
SEQRES  15 A  264  ASN ASP ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY          
SEQRES  16 A  264  GLY SER PHE THR VAL ARG THR ASP THR GLY GLU PRO MET          
SEQRES  17 A  264  GLY ARG GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP          
SEQRES  18 A  264  GLN THR GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE          
SEQRES  19 A  264  VAL LYS LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR          
SEQRES  20 A  264  LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP          
SEQRES  21 A  264  ASP GLU ALA GLU                                              
HET    4BC  A 401      27                                                       
HETNAM     4BC 4-(1,3-BENZODIOXOL-5-YL)-5-(5-ETHYL-2,4-                         
HETNAM   2 4BC  DIHYDROXYPHENYL)-2H-PYRAZOLE-3-CARBOXYLIC ACID                  
FORMUL   2  4BC    C19 H16 N2 O6                                                
FORMUL   3  HOH   *307(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  GLY A   73  5                                   7    
HELIX    4   4 THR A   99  THR A  109  1                                  11    
HELIX    5   5 GLY A  114  ALA A  124  1                                  11    
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 GLU A  192  LEU A  198  5                                   7    
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  PHE A 170   N  PHE A  20           
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  ILE A  91   O  VAL A 186           
SHEET    7   A 8 ILE A  78  ASN A  83 -1  N  ILE A  81   O  THR A  90           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SITE     1 AC1 18 ASN A  51  ALA A  55  LYS A  58  ASP A  93                    
SITE     2 AC1 18 ILE A  96  GLY A  97  MET A  98  LEU A 107                    
SITE     3 AC1 18 PHE A 138  THR A 184  VAL A 186  HOH A 402                    
SITE     4 AC1 18 HOH A 411  HOH A 433  HOH A 460  HOH A 489                    
SITE     5 AC1 18 HOH A 635  HOH A 687                                          
CRYST1   71.611   89.000   88.386  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      0.013964  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011236  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011314        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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