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Database: PDB
Entry: 3QDD
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HEADER    CHAPERONE/CHAPERONE INHIBITOR           18-JAN-11   3QDD              
TITLE     HSP90A N-TERMINAL DOMAIN IN COMPLEX WITH BIIB021                      
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, HSP86, RENAL CARCINOMA ANTIGEN NY-REN-38;
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATPASE, CHAPERONE-CHAPERONE INHIBITOR COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.ARNDT,M.A.BIAMONTE                                                
REVDAT   3   26-SEP-12 3QDD    1       JRNL                                     
REVDAT   2   19-SEP-12 3QDD    1       JRNL                                     
REVDAT   1   18-JUL-12 3QDD    0                                                
JRNL        AUTH   J.SHI,R.VAN DE WATER,K.HONG,R.B.LAMER,K.W.WEICHERT,          
JRNL        AUTH 2 C.M.SANDOVAL,S.R.KASIBHATLA,M.F.BOEHM,J.CHAO,K.LUNDGREN,     
JRNL        AUTH 3 N.TIMPLE,R.LOUGH,G.IBANEZ,C.BOYKIN,F.J.BURROWS,M.R.KEHRY,    
JRNL        AUTH 4 T.J.YUN,E.K.HARNING,C.AMBROSE,J.THOMPSON,S.A.BIXLER,A.DUNAH, 
JRNL        AUTH 5 P.SNODGRASS-BELT,J.ARNDT,I.J.ENYEDY,P.LI,V.S.HONG,           
JRNL        AUTH 6 A.MCKENZIE,M.A.BIAMONTE                                      
JRNL        TITL   EC144 IS A POTENT INHIBITOR OF THE HEAT SHOCK PROTEIN 90.    
JRNL        REF    J.MED.CHEM.                   V.  55  7786 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22938030                                                     
JRNL        DOI    10.1021/JM300810X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26859                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1432                            
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1892                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1644                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.53000                                             
REMARK   3    B33 (A**2) : 0.59000                                              
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): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.579         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1710 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1155 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2309 ; 1.570 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2833 ; 0.993 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   212 ; 5.878 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    76 ;35.106 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   319 ;11.220 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;18.246 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   261 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1882 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   335 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   347 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1213 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   841 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   830 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   161 ; 0.179 ; 0.200       
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):    14 ; 0.334 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    15 ; 0.160 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.228 ; 0.200       
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):  1370 ; 1.232 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   431 ; 0.284 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1683 ; 1.395 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   800 ; 2.678 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   624 ; 3.763 ; 4.500       
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  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A    42                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2190  27.8670  16.3300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1085 T22:  -0.0110                                     
REMARK   3      T33:  -0.1545 T12:  -0.0047                                     
REMARK   3      T13:   0.0106 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9164 L22:   0.6081                                     
REMARK   3      L33:   4.8166 L12:   0.6262                                     
REMARK   3      L13:  -1.3909 L23:  -1.3969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:   0.1912 S13:   0.0150                       
REMARK   3      S21:  -0.0079 S22:   0.1009 S23:   0.0613                       
REMARK   3      S31:  -0.0467 S32:  -0.2805 S33:  -0.1021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3150  39.9590  26.3840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0939 T22:  -0.0540                                     
REMARK   3      T33:  -0.1181 T12:  -0.0041                                     
REMARK   3      T13:  -0.0149 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6289 L22:   1.9875                                     
REMARK   3      L33:   4.1599 L12:   1.0090                                     
REMARK   3      L13:   1.6513 L23:   2.3445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0665 S12:  -0.0031 S13:   0.0791                       
REMARK   3      S21:  -0.0346 S22:   0.0288 S23:  -0.0419                       
REMARK   3      S31:  -0.2246 S32:   0.0092 S33:   0.0377                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    74        A    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7820  25.3890  20.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1177 T22:  -0.0514                                     
REMARK   3      T33:  -0.0954 T12:   0.0249                                     
REMARK   3      T13:   0.0065 T23:   0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3563 L22:   5.6679                                     
REMARK   3      L33:   2.0610 L12:   1.6884                                     
REMARK   3      L13:   0.6068 L23:   2.4373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:  -0.0283 S13:  -0.3704                       
REMARK   3      S21:   0.1456 S22:   0.1234 S23:  -0.6833                       
REMARK   3      S31:   0.1812 S32:   0.2122 S33:  -0.1529                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    88        A   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6970  31.8320  28.1840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1007 T22:  -0.0226                                     
REMARK   3      T33:  -0.1350 T12:   0.0129                                     
REMARK   3      T13:  -0.0034 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1019 L22:   1.5791                                     
REMARK   3      L33:   0.9836 L12:   0.1043                                     
REMARK   3      L13:  -0.1702 L23:   0.6303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:  -0.1283 S13:   0.0238                       
REMARK   3      S21:   0.0849 S22:   0.0552 S23:   0.0448                       
REMARK   3      S31:  -0.0158 S32:  -0.0080 S33:  -0.0361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   110        A   138                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3590  38.9860  13.6860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1386 T22:  -0.0184                                     
REMARK   3      T33:  -0.1027 T12:   0.0178                                     
REMARK   3      T13:  -0.0165 T23:   0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4467 L22:   2.9301                                     
REMARK   3      L33:   4.5004 L12:  -2.1238                                     
REMARK   3      L13:  -0.5703 L23:   0.3573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.2686 S13:   0.6190                       
REMARK   3      S21:  -0.1166 S22:  -0.0249 S23:  -0.0060                       
REMARK   3      S31:  -0.2493 S32:  -0.4286 S33:   0.0143                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   139        A   184                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5890  25.6190  27.9910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1129 T22:  -0.0267                                     
REMARK   3      T33:  -0.1306 T12:   0.0013                                     
REMARK   3      T13:  -0.0049 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7184 L22:   1.1573                                     
REMARK   3      L33:   1.4358 L12:   0.6282                                     
REMARK   3      L13:   0.0912 L23:  -0.0546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.1324 S13:  -0.1877                       
REMARK   3      S21:   0.0887 S22:  -0.0065 S23:  -0.1246                       
REMARK   3      S31:   0.0656 S32:  -0.0607 S33:  -0.0484                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   185        A   207                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9620  23.6930  10.2790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1083 T22:  -0.0137                                     
REMARK   3      T33:  -0.1300 T12:   0.0060                                     
REMARK   3      T13:   0.0157 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1586 L22:   1.5488                                     
REMARK   3      L33:   3.2492 L12:   0.2810                                     
REMARK   3      L13:  -0.8203 L23:  -0.4010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1529 S12:   0.1880 S13:  -0.2763                       
REMARK   3      S21:  -0.1124 S22:  -0.0161 S23:  -0.0441                       
REMARK   3      S31:   0.3101 S32:   0.1108 S33:   0.1690                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   208        A   223                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9220  34.4400  13.3360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1271 T22:  -0.0002                                     
REMARK   3      T33:  -0.1368 T12:  -0.0205                                     
REMARK   3      T13:   0.0361 T23:   0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3370 L22:   4.5897                                     
REMARK   3      L33:   2.6665 L12:  -0.4714                                     
REMARK   3      L13:  -0.1276 L23:   0.2390                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0042 S12:   0.2555 S13:   0.0921                       
REMARK   3      S21:  -0.3172 S22:   0.0248 S23:  -0.1845                       
REMARK   3      S31:  -0.0770 S32:   0.1077 S33:  -0.0205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   999        A   999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5340  33.2460  24.8170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1121 T22:   0.0134                                     
REMARK   3      T33:  -0.1212 T12:   0.0044                                     
REMARK   3      T13:   0.0004 T23:   0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.6389 L22:   8.1521                                     
REMARK   3      L33:  10.6025 L12:  10.5721                                     
REMARK   3      L13:  14.6574 L23:   8.8322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.1344 S13:  -0.2408                       
REMARK   3      S21:   0.0666 S22:   0.2083 S23:   0.0061                       
REMARK   3      S31:   0.1446 S32:  -0.0423 S33:  -0.1746                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3QDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063502.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.629                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.05200                            
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) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45400                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE, 20% PEG2000     
REMARK 280  MME, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
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+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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       33.31250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.53200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.60250            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.31250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.53200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.60250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.31250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.53200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.60250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.31250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.53200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.60250            
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 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 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 420  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     GLU A    16                                                      
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: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A  38   CD1   TYR A  38   CE1    -0.101                       
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    ALA A 166     -145.32     64.14                                   
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 94M A 999                 
DBREF  3QDD A    1   236  UNP    P07900   HS90A_HUMAN      1    236             
SEQADV 3QDD 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    94M  A 999      22                                                       
HETNAM     94M 6-CHLORO-9-[(4-METHOXY-3,5-DIMETHYLPYRIDIN-2-YL)                 
HETNAM   2 94M  METHYL]-9H-PURIN-2-AMINE                                        
FORMUL   2  94M    C14 H15 CL N6 O                                              
FORMUL   3  HOH   *263(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  ALA A  124  1                                  20    
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    
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 GLN A 159  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  LYS A 185   N  ILE A 151           
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  ASN A  79   O  VAL A  92           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  ILE A  78           
SITE     1 AC1 15 ASN A  51  ALA A  55  ASP A  93  ILE A  96                    
SITE     2 AC1 15 GLY A  97  MET A  98  LEU A 103  LEU A 107                    
SITE     3 AC1 15 PHE A 138  TRP A 162  THR A 184  HOH A 269                    
SITE     4 AC1 15 HOH A 272  HOH A 273  HOH A 350                               
CRYST1   66.625   91.064   99.205  90.00  90.00  90.00 I 2 2 2       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      0.015009  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010080        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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