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Database: PDB
Entry: 4DRJ
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HEADER    ISOMERASE/TRANSFERASE                   17-FEB-12   4DRJ              
TITLE     O-CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF FKBP52, RAPAMYCIN AND THE 
TITLE    2 FRB FRAGMENT OF MTOR                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP4;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FK1 DOMAIN, UNP RESIDUES 1-140;                            
COMPND   5 SYNONYM: PPIASE FKBP4, 51 KDA FK506-BINDING PROTEIN, FKBP51, 52 KDA  
COMPND   6 FK506-BINDING PROTEIN, 52 KDA FKBP, FKBP-52, 59 KDA IMMUNOPHILIN,    
COMPND   7 P59, FK506-BINDING PROTEIN 4, FKBP-4, FKBP59, HSP-BINDING            
COMPND   8 IMMUNOPHILIN, HBI, IMMUNOPHILIN FKBP52, ROTAMASE, PEPTIDYL-PROLYL    
COMPND   9 CIS-TRANS ISOMERASE FKBP4, N-TERMINALLY PROCESSED;                   
COMPND  10 EC: 5.2.1.8;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR;                      
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: FRB DOMAIN, UNP RESIDUES 2025-2114;                        
COMPND  16 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED       
COMPND  17 PROTEIN 1, FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN, MAMMALIAN    
COMPND  18 TARGET OF RAPAMYCIN, MTOR, MECHANISTIC TARGET OF RAPAMYCIN, RAPAMYCIN
COMPND  19 AND FKBP12 TARGET 1, RAPAMYCIN TARGET PROTEIN 1;                     
COMPND  20 EC: 2.7.11.1;                                                        
COMPND  21 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: FKBP4, FKBP52;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTA;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1;                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTA                                
KEYWDS    FK-506 BINDING DOMAIN, HSP90 COCHAPERONE, IMMUNOPHILIN, PEPTIDYL-     
KEYWDS   2 PROLYL ISOMERASE, KINASE, SIGNALLING, MAMMALIAN TARGET OF RAPAMYCIN, 
KEYWDS   3 IMMUNOSUPPRESSION, CANCER, ISOMERASE-TRANSFERASE COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.MAERZ,A.BRACHER,F.HAUSCH                                          
REVDAT   2   27-MAR-13 4DRJ    1       JRNL                                     
REVDAT   1   06-FEB-13 4DRJ    0                                                
JRNL        AUTH   A.M.MARZ,A.K.FABIAN,C.KOZANY,A.BRACHER,F.HAUSCH              
JRNL        TITL   LARGE FK506-BINDING PROTEINS SHAPE THE PHARMACOLOGY OF       
JRNL        TITL 2 RAPAMYCIN.                                                   
JRNL        REF    MOL.CELL.BIOL.                V.  33  1357 2013              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   23358420                                                     
JRNL        DOI    10.1128/MCB.00678-12                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23105                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1233                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1657                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 96                           
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1705                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 151                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.362         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1850 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2503 ; 1.287 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   221 ; 5.860 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    79 ;32.766 ;23.924       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   306 ;16.796 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;17.345 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   262 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1403 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   859 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1278 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   130 ; 0.139 ; 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):    25 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.148 ; 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):  1123 ; 0.691 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1748 ; 0.933 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   833 ; 1.654 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   755 ; 2.460 ; 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    19        A    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4280  -1.7703 -10.3185              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0578 T22:  -0.0019                                     
REMARK   3      T33:   0.1630 T12:   0.0334                                     
REMARK   3      T13:  -0.0830 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.6637 L22:  14.7119                                     
REMARK   3      L33:  20.1436 L12:   6.0963                                     
REMARK   3      L13:  -2.0798 L23:   8.0725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2301 S12:  -0.1265 S13:  -0.1087                       
REMARK   3      S21:   0.9516 S22:   0.0379 S23:  -1.8011                       
REMARK   3      S31:   1.1941 S32:   1.1692 S33:   0.1922                       
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    30        A    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9787  -9.6257 -17.4278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1019 T22:  -0.0967                                     
REMARK   3      T33:  -0.0564 T12:   0.0460                                     
REMARK   3      T13:   0.0039 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0414 L22:   3.6461                                     
REMARK   3      L33:   4.5477 L12:   0.2742                                     
REMARK   3      L13:   1.3841 L23:  -1.0179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0915 S12:   0.4373 S13:  -0.1358                       
REMARK   3      S21:  -0.1662 S22:   0.0209 S23:  -0.6186                       
REMARK   3      S31:   0.4152 S32:   0.4000 S33:  -0.1124                       
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    70        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5071  -7.3506 -16.8163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1235 T22:  -0.1270                                     
REMARK   3      T33:  -0.1483 T12:  -0.0061                                     
REMARK   3      T13:  -0.0058 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2655 L22:   2.3199                                     
REMARK   3      L33:   5.8414 L12:   0.0287                                     
REMARK   3      L13:   0.2525 L23:  -0.2529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0653 S12:   0.4592 S13:  -0.1323                       
REMARK   3      S21:  -0.0692 S22:   0.0716 S23:  -0.2515                       
REMARK   3      S31:   0.3739 S32:   0.0301 S33:  -0.1368                       
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   115        A   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0533 -10.0272 -10.7226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1316 T22:  -0.1230                                     
REMARK   3      T33:  -0.1279 T12:  -0.0223                                     
REMARK   3      T13:  -0.0502 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0194 L22:   3.0368                                     
REMARK   3      L33:   9.7304 L12:   0.6500                                     
REMARK   3      L13:   0.3666 L23:   0.7772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1049 S12:  -0.0055 S13:  -0.2360                       
REMARK   3      S21:   0.1230 S22:   0.0057 S23:  -0.0965                       
REMARK   3      S31:   0.7224 S32:  -0.5337 S33:  -0.1106                       
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 :   B  2019        B  2056                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4001  -7.1863 -13.8277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1124 T22:  -0.1376                                     
REMARK   3      T33:   0.0569 T12:   0.0296                                     
REMARK   3      T13:   0.0536 T23:   0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4878 L22:   5.0127                                     
REMARK   3      L33:   8.8243 L12:   0.5098                                     
REMARK   3      L13:   2.5589 L23:  -1.6865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0211 S12:   0.3763 S13:   0.4971                       
REMARK   3      S21:   0.0532 S22:   0.0603 S23:   0.7613                       
REMARK   3      S31:  -0.2389 S32:  -0.4068 S33:  -0.0392                       
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 :   B  2057        B  2067                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.3301 -14.2279 -25.1460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0839 T22:   0.6316                                     
REMARK   3      T33:   0.5619 T12:   0.0809                                     
REMARK   3      T13:  -0.0857 T23:  -0.2265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  42.6260 L22:   4.5786                                     
REMARK   3      L33:  71.8690 L12:  -6.6214                                     
REMARK   3      L13:  32.4656 L23:   7.8935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0581 S12:   2.7787 S13:  -1.5939                       
REMARK   3      S21:   0.7081 S22:  -0.8712 S23:   1.3969                       
REMARK   3      S31:  -1.0863 S32:  -2.4896 S33:  -0.1868                       
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 :   B  2068        B  2098                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3363 -19.5417 -14.0426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1309 T22:  -0.1061                                     
REMARK   3      T33:  -0.0760 T12:  -0.0271                                     
REMARK   3      T13:   0.0244 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0641 L22:   4.9007                                     
REMARK   3      L33:  13.4649 L12:  -0.2758                                     
REMARK   3      L13:   1.1641 L23:  -5.2036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0574 S12:   0.4993 S13:  -0.1352                       
REMARK   3      S21:  -0.2047 S22:   0.1224 S23:   0.4303                       
REMARK   3      S31:   0.3178 S32:  -0.2313 S33:  -0.0649                       
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 :   B  2099        B  2114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.9983 -12.2340 -22.2210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0942 T22:   0.1096                                     
REMARK   3      T33:  -0.1430 T12:  -0.0820                                     
REMARK   3      T13:  -0.0111 T23:   0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5503 L22:  11.5020                                     
REMARK   3      L33:  13.9717 L12:   0.7524                                     
REMARK   3      L13:   0.4182 L23:  -4.4869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1935 S12:   1.3221 S13:   0.2896                       
REMARK   3      S21:  -0.8330 S22:   0.1662 S23:   0.2121                       
REMARK   3      S31:  -0.1937 S32:   0.7853 S33:   0.0273                       
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   201        A   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9323  -8.5738 -13.1352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1529 T22:  -0.1078                                     
REMARK   3      T33:  -0.1994 T12:  -0.0075                                     
REMARK   3      T13:  -0.0131 T23:   0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1561 L22:   4.2415                                     
REMARK   3      L33:   2.3710 L12:   3.6762                                     
REMARK   3      L13:   0.4920 L23:   0.4307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0612 S12:   0.1893 S13:   0.2681                       
REMARK   3      S21:   0.0990 S22:   0.0541 S23:   0.1201                       
REMARK   3      S31:   0.0091 S32:  -0.1404 S33:  -0.1152                       
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 4DRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070692.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-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) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24366                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.186                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : 0.04400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 3FAP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS, 1.95M (NH4)2SO4, PH 6.5,   
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.26150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.07100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.49450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.07100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.26150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.49450            
REMARK 290   SMTRY3   4  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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     GLY B  2017                                                      
REMARK 465     ALA B  2018                                                      
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  21    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  72    CG   OD1  OD2                                       
REMARK 470     ARG A  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     ASP A  75    CG   OD1  OD2                                       
REMARK 470     GLU B2022    CG   CD   OE1  OE2                                  
REMARK 470     GLU B2025    CG   CD   OE1  OE2                                  
REMARK 470     GLU B2029    CG   CD   OE1  OE2                                  
REMARK 470     LEU B2065    CG   CD1  CD2                                       
REMARK 470     THR B2068    OG1  CG2                                            
REMARK 470     SER B2069    OG                                                  
REMARK 470     GLN B2072    CG   CD   OE1  NE2                                  
REMARK 470     LYS B2095    CG   CD   CE   NZ                                   
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    MET A  20       34.46   -149.80                                   
REMARK 500    ALA A 112     -112.80   -140.85                                   
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 RAP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DRI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DRJ   RELATED DB: PDB                                   
DBREF  4DRJ A    1   140  UNP    Q02790   FKBP4_HUMAN      1    140             
DBREF  4DRJ B 2025  2114  UNP    P42345   MTOR_HUMAN    2025   2114             
SEQADV 4DRJ GLY A   -3  UNP  Q02790              EXPRESSION TAG                 
SEQADV 4DRJ ALA A   -2  UNP  Q02790              EXPRESSION TAG                 
SEQADV 4DRJ MET A   -1  UNP  Q02790              EXPRESSION TAG                 
SEQADV 4DRJ GLY A    0  UNP  Q02790              EXPRESSION TAG                 
SEQADV 4DRJ GLY B 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ ALA B 2018  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ MET B 2019  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ ASP B 2020  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ PRO B 2021  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ GLU B 2022  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ PHE B 2023  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRJ MET B 2024  UNP  P42345              EXPRESSION TAG                 
SEQRES   1 A  144  GLY ALA MET GLY MET THR ALA GLU GLU MET LYS ALA THR          
SEQRES   2 A  144  GLU SER GLY ALA GLN SER ALA PRO LEU PRO MET GLU GLY          
SEQRES   3 A  144  VAL ASP ILE SER PRO LYS GLN ASP GLU GLY VAL LEU LYS          
SEQRES   4 A  144  VAL ILE LYS ARG GLU GLY THR GLY THR GLU MET PRO MET          
SEQRES   5 A  144  ILE GLY ASP ARG VAL PHE VAL HIS TYR THR GLY TRP LEU          
SEQRES   6 A  144  LEU ASP GLY THR LYS PHE ASP SER SER LEU ASP ARG LYS          
SEQRES   7 A  144  ASP LYS PHE SER PHE ASP LEU GLY LYS GLY GLU VAL ILE          
SEQRES   8 A  144  LYS ALA TRP ASP ILE ALA ILE ALA THR MET LYS VAL GLY          
SEQRES   9 A  144  GLU VAL CYS HIS ILE THR CYS LYS PRO GLU TYR ALA TYR          
SEQRES  10 A  144  GLY SER ALA GLY SER PRO PRO LYS ILE PRO PRO ASN ALA          
SEQRES  11 A  144  THR LEU VAL PHE GLU VAL GLU LEU PHE GLU PHE LYS GLY          
SEQRES  12 A  144  GLU                                                          
SEQRES   1 B   98  GLY ALA MET ASP PRO GLU PHE MET GLU MET TRP HIS GLU          
SEQRES   2 B   98  GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU ARG          
SEQRES   3 B   98  ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU HIS          
SEQRES   4 B   98  ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU THR          
SEQRES   5 B   98  SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU ALA          
SEQRES   6 B   98  GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN VAL          
SEQRES   7 B   98  LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS VAL          
SEQRES   8 B   98  PHE ARG ARG ILE SER LYS GLN                                  
HET    RAP  A 201      65                                                       
HET    SO4  A 202       5                                                       
HETNAM     RAP RAPAMYCIN IMMUNOSUPPRESSANT DRUG                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  RAP    C51 H79 N O13                                                
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *151(H2 O)                                                    
HELIX    1   1 ILE A   87  ALA A   95  1                                   9    
HELIX    2   2 PRO A  109  ALA A  112  5                                   4    
HELIX    3   3 ASP B 2020  ARG B 2042  1                                  23    
HELIX    4   4 ASN B 2043  ARG B 2060  1                                  18    
HELIX    5   5 THR B 2064  GLY B 2092  1                                  29    
HELIX    6   6 ASN B 2093  LYS B 2113  1                                  21    
SHEET    1   A 6 VAL A  23  ASP A  24  0                                        
SHEET    2   A 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23           
SHEET    3   A 6 VAL A 102  CYS A 107 -1  O  HIS A 104   N  VAL A  36           
SHEET    4   A 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107           
SHEET    5   A 6 ARG A  52  LEU A  61 -1  N  PHE A  54   O  PHE A 135           
SHEET    6   A 6 LYS A  66  SER A  69 -1  O  ASP A  68   N  GLY A  59           
SHEET    1   B 6 VAL A  23  ASP A  24  0                                        
SHEET    2   B 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23           
SHEET    3   B 6 VAL A 102  CYS A 107 -1  O  HIS A 104   N  VAL A  36           
SHEET    4   B 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107           
SHEET    5   B 6 ARG A  52  LEU A  61 -1  N  PHE A  54   O  PHE A 135           
SHEET    6   B 6 PHE A  77  ASP A  80 -1  O  PHE A  77   N  VAL A  55           
CISPEP   1 PRO A  119    PRO A  120          0        -0.70                     
SITE     1 AC1 24 TYR A  57  PHE A  67  ASP A  68  PHE A  77                    
SITE     2 AC1 24 GLY A  84  GLU A  85  VAL A  86  ILE A  87                    
SITE     3 AC1 24 TRP A  90  TYR A 113  LYS A 121  PHE A 130                    
SITE     4 AC1 24 HOH A 324  HOH A 332  HOH A 347  HOH A 401                    
SITE     5 AC1 24 LEU B2031  GLU B2032  SER B2035  PHE B2039                    
SITE     6 AC1 24 THR B2098  ASP B2102  TYR B2105  PHE B2108                    
SITE     1 AC2  7 ARG A  52  PHE A  54  SER A  78  HOH A 339                    
SITE     2 AC2  7 HOH A 390  ARG B2109  LYS B2113                               
CRYST1   58.523   62.989   70.142  90.00  90.00  90.00 P 21 21 21    4          
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      0.017087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015876  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014257        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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