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Database: PDB
Entry: 3WHA
LinkDB: 3WHA
Original site: 3WHA 
HEADER    CHAPERONE/CHAPERONE INHIBITOR           23-AUG-13   3WHA              
TITLE     HSP90 ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH A TRICYCLIC INHIBITOR   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 9-236;                                        
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;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CP;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    CHAPERONE, CHAPERONE-CHAPERONE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.FUKAMI,N.ONO                                                      
REVDAT   1   29-JAN-14 3WHA    0                                                
JRNL        AUTH   A.SUDA,K.KAWASAKI,S.KOMIYAMA,Y.ISSHIKI,D.-O.YOON,S.-J.KIM,   
JRNL        AUTH 2 Y.-J.NA,K.HASEGAWA,T.A.FUKAMI,S.SATO,T.MIURA,N.ONO,          
JRNL        AUTH 3 T.YAMAZAKI,R.SAITOH,N.SHIMMA,Y.SHIRATORI,T.TSUKUDA           
JRNL        TITL   DESIGN AND SYNTHESIS OF                                      
JRNL        TITL 2 2-AMINO-6-(1H,3H-BENZO[DE]ISOCHROMEN-6-YL)-1,3,5-TRIAZINES   
JRNL        TITL 3 AS NOVEL HSP90 INHIBITORS                                    
JRNL        REF    BIOORG.MED.CHEM.              V.  22   892 2014              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   24369839                                                     
JRNL        DOI    10.1016/J.BMC.2013.11.036                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 133171                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.185                          
REMARK   3   R VALUE            (WORKING SET)  : 0.184                          
REMARK   3   FREE R VALUE                      : 0.200                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 6705                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.64                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 9800                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2153                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 9298                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2141                   
REMARK   3   BIN FREE R VALUE                        : 0.2380                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 502                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3280                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 636                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.87150                                             
REMARK   3    B22 (A**2) : 1.60200                                              
REMARK   3    B33 (A**2) : -0.73050                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.06190                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.145               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.045               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3463   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4675   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1255   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 91     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 494    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3463   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 464    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4596   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.08                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 13.96                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3WHA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096333.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133172                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.134                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : 0.04400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.29                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33000                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3B28                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22%(W/V) PEG 3350, 0.2M MGCL2, 0.1M NA   
REMARK 280  -MES, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 278K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       53.58500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.46000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.58500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.46000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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      -70.73788            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -52.91009            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       36.43212            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -52.91009            
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 MG    MG B 302  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     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     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 465     MET B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     ARG B   226                                                      
REMARK 465     ASP B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     GLU B   229                                                      
REMARK 465     VAL B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     ASP B   232                                                      
REMARK 465     ASP B   233                                                      
REMARK 465     GLU B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  16    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  16    CG   CD   OE1  OE2                                  
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    ALA A 111     -125.08     51.62                                   
REMARK 500    ALA A 166     -145.79     66.66                                   
REMARK 500    ARG A 182      143.42   -172.27                                   
REMARK 500    THR B 109      -51.07   -132.62                                   
REMARK 500    ALA B 166     -144.70     68.62                                   
REMARK 500    ARG B 182      142.78   -173.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 699   O                                                      
REMARK 620 2 HOH B 700   O    91.0                                              
REMARK 620 3 HOH B 701   O    96.0  85.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WHA A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WHA B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B28   RELATED DB: PDB                                   
DBREF  3WHA A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
DBREF  3WHA B    9   236  UNP    P07900   HS90A_HUMAN      9    236             
SEQADV 3WHA MET A    8  UNP  P07900              EXPRESSION TAG                 
SEQADV 3WHA MET B    8  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  229  MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE          
SEQRES   2 A  229  ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE          
SEQRES   3 A  229  ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG          
SEQRES   4 A  229  GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE          
SEQRES   5 A  229  ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER          
SEQRES   6 A  229  GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN          
SEQRES   7 A  229  ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET          
SEQRES   8 A  229  THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA          
SEQRES   9 A  229  LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA          
SEQRES  10 A  229  GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY          
SEQRES  11 A  229  PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL          
SEQRES  12 A  229  ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU          
SEQRES  13 A  229  SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR          
SEQRES  14 A  229  GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS          
SEQRES  15 A  229  LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG          
SEQRES  16 A  229  ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY          
SEQRES  17 A  229  TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS          
SEQRES  18 A  229  GLU VAL SER ASP ASP GLU ALA GLU                              
SEQRES   1 B  229  MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE          
SEQRES   2 B  229  ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE          
SEQRES   3 B  229  ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG          
SEQRES   4 B  229  GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE          
SEQRES   5 B  229  ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER          
SEQRES   6 B  229  GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN          
SEQRES   7 B  229  ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET          
SEQRES   8 B  229  THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA          
SEQRES   9 B  229  LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA          
SEQRES  10 B  229  GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY          
SEQRES  11 B  229  PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL          
SEQRES  12 B  229  ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU          
SEQRES  13 B  229  SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR          
SEQRES  14 B  229  GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS          
SEQRES  15 B  229  LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG          
SEQRES  16 B  229  ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY          
SEQRES  17 B  229  TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS          
SEQRES  18 B  229  GLU VAL SER ASP ASP GLU ALA GLU                              
HET    GOL  A 301       6                                                       
HET    WHA  A 302      28                                                       
HET    WHA  B 301      28                                                       
HET     MG  B 302       1                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     WHA 4-{[4-AMINO-6-(5-CHLORO-1H,3H-BENZO[DE]ISOCHROMEN-6-             
HETNAM   2 WHA  YL)-1,3,5-TRIAZIN-2-YL]SULFANYL}BUTANAMIDE                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  WHA    2(C19 H18 CL N5 O2 S)                                        
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  HOH   *636(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  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  LEU A  143  5                                   8    
HELIX    8   8 GLU A  192  LEU A  198  5                                   7    
HELIX    9   9 GLU A  199  SER A  211  1                                  13    
HELIX   10  10 GLN B   23  THR B   36  1                                  14    
HELIX   11  11 ASN B   40  GLU B   42  5                                   3    
HELIX   12  12 ILE B   43  ASP B   66  1                                  24    
HELIX   13  13 PRO B   67  ASP B   71  5                                   5    
HELIX   14  14 THR B   99  THR B  109  1                                  11    
HELIX   15  15 ALA B  111  ALA B  124  1                                  14    
HELIX   16  16 ASP B  127  GLY B  135  5                                   9    
HELIX   17  17 VAL B  136  LEU B  143  5                                   8    
HELIX   18  18 GLU B  192  LEU B  198  5                                   7    
HELIX   19  19 GLU B  199  SER B  211  1                                  13    
SHEET    1   A 8 GLU A  18  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  LEU A  89   O  LEU A 188           
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           
SHEET    1   B 8 GLU B  18  ALA B  21  0                                        
SHEET    2   B 8 SER B 169  THR B 174 -1  O  PHE B 170   N  PHE B  20           
SHEET    3   B 8 TYR B 160  SER B 164 -1  N  ALA B 161   O  ARG B 173           
SHEET    4   B 8 ALA B 145  LYS B 153 -1  N  VAL B 150   O  TRP B 162           
SHEET    5   B 8 GLY B 183  LEU B 190 -1  O  ILE B 187   N  THR B 149           
SHEET    6   B 8 THR B  88  ASP B  93 -1  N  LEU B  89   O  LEU B 188           
SHEET    7   B 8 ILE B  78  ASN B  83 -1  N  ASN B  79   O  VAL B  92           
SHEET    8   B 8 ILE B 218  LEU B 220  1  O  THR B 219   N  LEU B  80           
LINK        MG    MG B 302                 O   HOH B 699     1555   1555  2.04  
LINK        MG    MG B 302                 O   HOH B 700     1555   1555  2.07  
LINK        MG    MG B 302                 O   HOH B 701     1555   1555  2.03  
LINK        MG    MG B 302                 O   HOH B 699     1555   2554  2.04  
LINK        MG    MG B 302                 O   HOH B 700     1555   2554  2.07  
LINK        MG    MG B 302                 O   HOH B 701     1555   2554  2.03  
SITE     1 AC1  8 ASP A  54  ASP A  57  LYS A 112  SER A 113                    
SITE     2 AC1  8 GLY A 114  HOH A 559  HOH A 567  HOH A 571                    
SITE     1 AC2 20 SER A  52  ASP A  54  ALA A  55  LYS A  58                    
SITE     2 AC2 20 ASP A  93  ILE A  96  GLY A  97  MET A  98                    
SITE     3 AC2 20 ASN A 106  LEU A 107  GLY A 135  PHE A 138                    
SITE     4 AC2 20 TYR A 139  THR A 184  HOH A 401  HOH A 403                    
SITE     5 AC2 20 HOH A 408  HOH A 410  HOH A 414  HOH A 670                    
SITE     1 AC3 17 ALA B  55  ASP B  93  ILE B  96  GLY B  97                    
SITE     2 AC3 17 MET B  98  ASN B 106  LEU B 107  PHE B 138                    
SITE     3 AC3 17 TYR B 139  THR B 184  HOH B 401  HOH B 403                    
SITE     4 AC3 17 HOH B 404  HOH B 409  HOH B 417  HOH B 630                    
SITE     5 AC3 17 HOH B 670                                                     
SITE     1 AC4  3 HOH B 699  HOH B 700  HOH B 701                               
CRYST1  107.170   98.920   64.240  90.00 124.55  90.00 C 1 2 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      0.009331  0.000000  0.006425        0.00000                         
SCALE2      0.000000  0.010109  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018900        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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