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Entry: 4DRH
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HEADER    ISOMERASE/TRANSFERASE                   17-FEB-12   4DRH              
TITLE     CO-CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF FKBP51, RAPAMYCIN AND THE
TITLE    2 FRB FRAGMENT OF MTOR AT LOW PH                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP5;                 
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: FKBP51 FK1 DOMAIN, UNP RESIDUES 1-140;                     
COMPND   5 SYNONYM: PPIASE FKBP5, 51 KDA FK506-BINDING PROTEIN, 51 KDA FKBP,    
COMPND   6 FKBP-51, 54 KDA PROGESTERONE RECEPTOR-ASSOCIATED IMMUNOPHILIN,       
COMPND   7 ANDROGEN-REGULATED PROTEIN 6, FF1 ANTIGEN, FK506-BINDING PROTEIN 5,  
COMPND   8 FKBP-5, FKBP54, P54, HSP90-BINDING IMMUNOPHILIN, ROTAMASE;           
COMPND   9 EC: 5.2.1.8;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR;                      
COMPND  13 CHAIN: B, E;                                                         
COMPND  14 FRAGMENT: FRB DOMAIN, UNP RESIDUES 2025-2114;                        
COMPND  15 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED       
COMPND  16 PROTEIN 1, FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN, MAMMALIAN    
COMPND  17 TARGET OF RAPAMYCIN, MTOR, MECHANISTIC TARGET OF RAPAMYCIN, RAPAMYCIN
COMPND  18 AND FKBP12 TARGET 1, RAPAMYCIN TARGET PROTEIN 1;                     
COMPND  19 EC: 2.7.11.1;                                                        
COMPND  20 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: AIG6, FKBP5, FKBP51;                                           
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, MAMMALIAN TARGET OF RAPAMYCIN, KINASE, SIGNALLING, 
KEYWDS   3 IMMUNOSUPPRESSION, CANCER, ISOMERASE-TRANSFERASE COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.MAERZ,A.BRACHER,F.HAUSCH                                          
REVDAT   2   27-MAR-13 4DRH    1       JRNL                                     
REVDAT   1   06-FEB-13 4DRH    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27545                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1474                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1999                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3497                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.27                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
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): 0.246         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.061        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3819 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5165 ; 1.450 ; 2.020       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   446 ; 6.485 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   163 ;35.169 ;24.479       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   630 ;17.457 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.984 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   534 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2821 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1590 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2526 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   159 ; 0.127 ; 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):    50 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.178 ; 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):  2291 ; 0.593 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3535 ; 0.880 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1737 ; 1.567 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1630 ; 2.291 ; 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  : 14                                         
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     9        A    48                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.0650  19.4360  -6.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2308 T22:  -0.0358                                     
REMARK   3      T33:  -0.1436 T12:   0.0649                                     
REMARK   3      T13:  -0.0509 T23:  -0.0712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2312 L22:   2.8622                                     
REMARK   3      L33:   4.4652 L12:   1.7298                                     
REMARK   3      L13:  -0.0913 L23:  -0.2115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0219 S12:  -0.3262 S13:   0.2392                       
REMARK   3      S21:   0.0909 S22:   0.0569 S23:   0.2318                       
REMARK   3      S31:  -0.4010 S32:  -0.4133 S33:  -0.0787                       
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    49        A    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7600  19.2600   1.4020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3174 T22:  -0.0994                                     
REMARK   3      T33:  -0.2394 T12:  -0.0433                                     
REMARK   3      T13:  -0.0111 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7102 L22:   6.0537                                     
REMARK   3      L33:   6.4256 L12:  -0.6051                                     
REMARK   3      L13:   0.2443 L23:   1.1088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0922 S12:  -0.1826 S13:  -0.1335                       
REMARK   3      S21:   0.3729 S22:  -0.1624 S23:  -0.2951                       
REMARK   3      S31:  -0.2068 S32:  -0.1468 S33:   0.0701                       
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    87        A   140                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1680  19.8200  -4.9050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2794 T22:  -0.1553                                     
REMARK   3      T33:  -0.2656 T12:  -0.0235                                     
REMARK   3      T13:  -0.0400 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6791 L22:   4.0448                                     
REMARK   3      L33:   5.9041 L12:  -0.0186                                     
REMARK   3      L13:  -0.8345 L23:   1.2158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:  -0.0332 S13:   0.0252                       
REMARK   3      S21:   0.0036 S22:  -0.0457 S23:  -0.0908                       
REMARK   3      S31:  -0.2540 S32:   0.0354 S33:   0.0755                       
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 :   B  2018        B  2056                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3530  21.8200   2.3220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2615 T22:  -0.0779                                     
REMARK   3      T33:  -0.2273 T12:  -0.1033                                     
REMARK   3      T13:   0.0247 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6137 L22:   4.0055                                     
REMARK   3      L33:   7.3642 L12:   2.1402                                     
REMARK   3      L13:   1.9164 L23:   1.4034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:  -0.0352 S13:   0.1974                       
REMARK   3      S21:  -0.1432 S22:   0.0292 S23:   0.0312                       
REMARK   3      S31:  -0.5912 S32:   0.1967 S33:  -0.0063                       
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  2057        B  2076                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2690  24.6710  17.8030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0653 T22:   0.3512                                     
REMARK   3      T33:  -0.1609 T12:  -0.2397                                     
REMARK   3      T13:  -0.0036 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7677 L22:  17.6276                                     
REMARK   3      L33:   3.2325 L12:   8.9924                                     
REMARK   3      L13:   4.8804 L23:   2.9230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5047 S12:  -0.5133 S13:  -0.4116                       
REMARK   3      S21:   1.0733 S22:  -0.5238 S23:  -1.1718                       
REMARK   3      S31:  -0.5173 S32:   0.7868 S33:   0.0191                       
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  2077        B  2112                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7500  14.0840   7.8360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3269 T22:  -0.0252                                     
REMARK   3      T33:  -0.2890 T12:  -0.1131                                     
REMARK   3      T13:   0.0201 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1383 L22:  13.4194                                     
REMARK   3      L33:   4.0126 L12:  -1.8912                                     
REMARK   3      L13:  -0.1442 L23:   2.6846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:  -0.7516 S13:  -0.0305                       
REMARK   3      S21:  -0.0924 S22:   0.0348 S23:   0.0347                       
REMARK   3      S31:   0.0069 S32:  -0.0158 S33:  -0.0369                       
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 :   D    10        D    51                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3200  55.4070   4.4110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0150 T22:  -0.1202                                     
REMARK   3      T33:  -0.0953 T12:  -0.1153                                     
REMARK   3      T13:   0.0123 T23:  -0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9795 L22:   4.5014                                     
REMARK   3      L33:   3.4526 L12:   2.7477                                     
REMARK   3      L13:   2.6250 L23:   0.3919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0882 S12:   0.2799 S13:   0.5922                       
REMARK   3      S21:  -0.5123 S22:  -0.0468 S23:   0.5607                       
REMARK   3      S31:  -0.4763 S32:  -0.2487 S33:   0.1350                       
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 :   D    52        D   101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1310  45.9610  -2.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0057 T22:  -0.0240                                     
REMARK   3      T33:  -0.1637 T12:  -0.2259                                     
REMARK   3      T13:   0.0297 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4417 L22:   7.5912                                     
REMARK   3      L33:   4.5794 L12:   1.3512                                     
REMARK   3      L13:   2.2678 L23:   0.8410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2204 S12:   0.6936 S13:  -0.1379                       
REMARK   3      S21:  -0.6639 S22:   0.1773 S23:   0.0547                       
REMARK   3      S31:  -0.1225 S32:   0.1157 S33:   0.0431                       
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 :   D   102        D   140                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3440  43.6490   4.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0983 T22:  -0.1257                                     
REMARK   3      T33:  -0.1265 T12:  -0.1619                                     
REMARK   3      T13:   0.0624 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0373 L22:   6.7167                                     
REMARK   3      L33:   6.5224 L12:   1.0170                                     
REMARK   3      L13:   1.6879 L23:  -1.5748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0756 S12:   0.0684 S13:  -0.5692                       
REMARK   3      S21:  -0.2621 S22:   0.0152 S23:   0.1918                       
REMARK   3      S31:   0.3922 S32:  -0.0013 S33:  -0.0907                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E  2019        E  2066                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9870  24.0130  -4.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1070 T22:  -0.0743                                     
REMARK   3      T33:  -0.1560 T12:  -0.2281                                     
REMARK   3      T13:   0.0889 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5684 L22:   5.2739                                     
REMARK   3      L33:   6.7650 L12:   0.5519                                     
REMARK   3      L13:   0.0477 L23:   1.6038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1019 S12:   0.3667 S13:  -0.2060                       
REMARK   3      S21:  -0.4285 S22:   0.0724 S23:   0.0977                       
REMARK   3      S31:  -0.0839 S32:  -0.3049 S33:   0.0295                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E  2067        E  2097                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4380  23.2870 -11.8930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0760 T22:  -0.0129                                     
REMARK   3      T33:  -0.0878 T12:  -0.2931                                     
REMARK   3      T13:   0.2299 T23:  -0.0618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3361 L22:   7.6470                                     
REMARK   3      L33:  10.6877 L12:  -4.8453                                     
REMARK   3      L13:   5.1082 L23:  -3.5572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1133 S12:   0.2484 S13:  -0.3738                       
REMARK   3      S21:  -1.2517 S22:   0.1919 S23:  -0.5519                       
REMARK   3      S31:   0.4287 S32:  -0.3216 S33:  -0.3052                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E  2098        E  2112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7220  32.7220 -10.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0821 T22:  -0.0125                                     
REMARK   3      T33:  -0.2057 T12:  -0.2919                                     
REMARK   3      T13:   0.0045 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5658 L22:  13.4670                                     
REMARK   3      L33:   9.4689 L12:  -6.0987                                     
REMARK   3      L13:  -1.5230 L23:  -2.2684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5016 S12:   0.8687 S13:   0.1086                       
REMARK   3      S21:  -1.1401 S22:   0.4239 S23:   0.1426                       
REMARK   3      S31:  -0.8319 S32:  -0.1689 S33:   0.0777                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
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):  -4.9340  20.0180  -1.8330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2497 T22:  -0.1390                                     
REMARK   3      T33:  -0.2056 T12:  -0.1040                                     
REMARK   3      T13:  -0.0573 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0578 L22:   3.5546                                     
REMARK   3      L33:   7.2575 L12:  -2.4790                                     
REMARK   3      L13:   2.2816 L23:   3.3818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1843 S12:   0.2411 S13:  -0.1201                       
REMARK   3      S21:  -0.6113 S22:   0.2124 S23:  -0.3118                       
REMARK   3      S31:  -0.4904 S32:   0.0702 S33:  -0.0281                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   201        D   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8330  36.9690  -0.2930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1190 T22:   0.0781                                     
REMARK   3      T33:  -0.1040 T12:  -0.1825                                     
REMARK   3      T13:   0.0067 T23:  -0.1067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2226 L22:  10.8080                                     
REMARK   3      L33:   1.0894 L12:   3.4182                                     
REMARK   3      L13:   0.8793 L23:   1.7021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4182 S12:  -0.3875 S13:  -0.6364                       
REMARK   3      S21:  -0.1636 S22:  -0.1416 S23:  -0.2479                       
REMARK   3      S31:  -0.5667 S32:   0.1065 S33:  -0.2766                       
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 4DRH 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 RCSB070690.                                      
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                             : 3.5                                
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) : 0.9814                             
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   : 29100                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 89.803                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.51900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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: PDB ENTRY 1FAP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRIC ACID  2M (NH4)2SO4, PH       
REMARK 280  3.5, VAPOR DIFFUSION, TEMPERATURE 293K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -Y,-X,-Z+2/3                                            
REMARK 290       5555   -X+Y,Y,-Z+1/3                                           
REMARK 290       6555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.51433            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.02867            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       71.02867            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.51433            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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 O1   SO4 A 205  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     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     THR A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY B  2017                                                      
REMARK 465     LYS B  2113                                                      
REMARK 465     GLN B  2114                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ASN D     9                                                      
REMARK 465     GLY E  2017                                                      
REMARK 465     ALA E  2018                                                      
REMARK 465     ARG E  2060                                                      
REMARK 465     GLY E  2061                                                      
REMARK 465     PRO E  2062                                                      
REMARK 465     GLN E  2063                                                      
REMARK 465     THR E  2064                                                      
REMARK 465     LYS E  2113                                                      
REMARK 465     GLN E  2114                                                      
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     ASN A   9    CG   OD1  ND2                                       
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 140    CG   CD   OE1  OE2                                  
REMARK 470     ARG B2042    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B2059    CG   CD   OE1  OE2                                  
REMARK 470     ARG B2060    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D  10    CG   OD1  ND2                                       
REMARK 470     ARG D  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  83    CG   CD   CE   NZ                                   
REMARK 470     GLU D 140    CG   CD   OE1  OE2                                  
REMARK 470     MET E2019    CG   SD   CE                                        
REMARK 470     LEU E2065    CG   CD1  CD2                                       
REMARK 470     LYS E2066    CG   CD   CE   NZ                                   
REMARK 470     GLU E2067    CG   CD   OE1  OE2                                  
REMARK 470     GLN E2072    CG   CD   OE1  NE2                                  
REMARK 470     ARG E2076    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E2083    CG   CD   OE1  OE2                                  
REMARK 470     LYS E2090    CG   CD   CE   NZ                                   
REMARK 470     LYS E2095    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    ASN A  74     -138.11     72.99                                   
REMARK 500    ALA A 112     -108.38   -132.28                                   
REMARK 500    PRO B2062      119.10    -16.80                                   
REMARK 500    ASN D  74      -98.41   -119.02                                   
REMARK 500    ALA D 112     -110.72   -136.13                                   
REMARK 500    LYS D 121       85.54   -158.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS D 121        23.3      L          L   OUTSIDE RANGE           
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RAP D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2206                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DRI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DRJ   RELATED DB: PDB                                   
DBREF  4DRH A    1   140  UNP    Q13451   FKBP5_HUMAN      1    140             
DBREF  4DRH B 2025  2114  UNP    P42345   MTOR_HUMAN    2025   2114             
DBREF  4DRH D    1   140  UNP    Q13451   FKBP5_HUMAN      1    140             
DBREF  4DRH E 2025  2114  UNP    P42345   MTOR_HUMAN    2025   2114             
SEQADV 4DRH GLY A   -3  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH ALA A   -2  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH MET A   -1  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH GLY A    0  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH GLY B 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH ALA B 2018  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH MET B 2019  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH ASP B 2020  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH PRO B 2021  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH GLU B 2022  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH PHE B 2023  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH MET B 2024  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH GLY D   -3  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH ALA D   -2  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH MET D   -1  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH GLY D    0  UNP  Q13451              EXPRESSION TAG                 
SEQADV 4DRH GLY E 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH ALA E 2018  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH MET E 2019  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH ASP E 2020  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH PRO E 2021  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH GLU E 2022  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH PHE E 2023  UNP  P42345              EXPRESSION TAG                 
SEQADV 4DRH MET E 2024  UNP  P42345              EXPRESSION TAG                 
SEQRES   1 A  144  GLY ALA MET GLY MET THR THR ASP GLU GLY ALA LYS ASN          
SEQRES   2 A  144  ASN GLU GLU SER PRO THR ALA THR VAL ALA GLU GLN GLY          
SEQRES   3 A  144  GLU ASP ILE THR SER LYS LYS ASP ARG GLY VAL LEU LYS          
SEQRES   4 A  144  ILE VAL LYS ARG VAL GLY ASN GLY GLU GLU THR PRO MET          
SEQRES   5 A  144  ILE GLY ASP LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU          
SEQRES   6 A  144  SER ASN GLY LYS LYS PHE ASP SER SER HIS ASP ARG ASN          
SEQRES   7 A  144  GLU PRO PHE VAL PHE SER LEU GLY LYS GLY GLN VAL ILE          
SEQRES   8 A  144  LYS ALA TRP ASP ILE GLY VAL ALA THR MET LYS LYS GLY          
SEQRES   9 A  144  GLU ILE CYS HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR          
SEQRES  10 A  144  GLY SER ALA GLY SER LEU PRO LYS ILE PRO SER ASN ALA          
SEQRES  11 A  144  THR LEU PHE PHE GLU ILE GLU LEU LEU ASP 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                                  
SEQRES   1 D  144  GLY ALA MET GLY MET THR THR ASP GLU GLY ALA LYS ASN          
SEQRES   2 D  144  ASN GLU GLU SER PRO THR ALA THR VAL ALA GLU GLN GLY          
SEQRES   3 D  144  GLU ASP ILE THR SER LYS LYS ASP ARG GLY VAL LEU LYS          
SEQRES   4 D  144  ILE VAL LYS ARG VAL GLY ASN GLY GLU GLU THR PRO MET          
SEQRES   5 D  144  ILE GLY ASP LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU          
SEQRES   6 D  144  SER ASN GLY LYS LYS PHE ASP SER SER HIS ASP ARG ASN          
SEQRES   7 D  144  GLU PRO PHE VAL PHE SER LEU GLY LYS GLY GLN VAL ILE          
SEQRES   8 D  144  LYS ALA TRP ASP ILE GLY VAL ALA THR MET LYS LYS GLY          
SEQRES   9 D  144  GLU ILE CYS HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR          
SEQRES  10 D  144  GLY SER ALA GLY SER LEU PRO LYS ILE PRO SER ASN ALA          
SEQRES  11 D  144  THR LEU PHE PHE GLU ILE GLU LEU LEU ASP PHE LYS GLY          
SEQRES  12 D  144  GLU                                                          
SEQRES   1 E   98  GLY ALA MET ASP PRO GLU PHE MET GLU MET TRP HIS GLU          
SEQRES   2 E   98  GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU ARG          
SEQRES   3 E   98  ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU HIS          
SEQRES   4 E   98  ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU THR          
SEQRES   5 E   98  SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU ALA          
SEQRES   6 E   98  GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN VAL          
SEQRES   7 E   98  LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS VAL          
SEQRES   8 E   98  PHE ARG ARG ILE SER LYS GLN                                  
HET    RAP  A 201      65                                                       
HET    SO4  A 202       5                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET    SO4  A 205       5                                                       
HET    SO4  A 206       5                                                       
HET    SO4  A 207       5                                                       
HET    SO4  A 208       5                                                       
HET    SO4  B2201       5                                                       
HET    SO4  B2202       5                                                       
HET    SO4  B2203       5                                                       
HET    SO4  B2204       5                                                       
HET    RAP  D 201      65                                                       
HET    SO4  D 202       5                                                       
HET    SO4  D 203       5                                                       
HET    SO4  D 204       5                                                       
HET    SO4  D 205       5                                                       
HET    SO4  E2201       5                                                       
HET    SO4  E2202       5                                                       
HET    SO4  E2203       5                                                       
HET    SO4  E2204       5                                                       
HET    SO4  E2205       5                                                       
HET    SO4  E2206       5                                                       
HETNAM     RAP RAPAMYCIN IMMUNOSUPPRESSANT DRUG                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  RAP    2(C51 H79 N O13)                                             
FORMUL   6  SO4    21(O4 S 2-)                                                  
FORMUL  28  HOH   *89(H2 O)                                                     
HELIX    1   1 SER A   13  GLY A   22  1                                  10    
HELIX    2   2 ILE A   87  ALA A   95  1                                   9    
HELIX    3   3 PRO A  109  ALA A  112  5                                   4    
HELIX    4   4 ASP B 2020  ARG B 2042  1                                  23    
HELIX    5   5 ASN B 2043  ARG B 2060  1                                  18    
HELIX    6   6 THR B 2064  GLY B 2092  1                                  29    
HELIX    7   7 ASN B 2093  SER B 2112  1                                  20    
HELIX    8   8 SER D   13  GLY D   22  1                                  10    
HELIX    9   9 ILE D   87  THR D   96  1                                  10    
HELIX   10  10 PRO D  109  ALA D  112  5                                   4    
HELIX   11  11 ASP E 2020  ARG E 2042  1                                  23    
HELIX   12  12 ASN E 2043  MET E 2058  1                                  16    
HELIX   13  13 LYS E 2066  GLY E 2092  1                                  27    
HELIX   14  14 ASN E 2093  SER E 2112  1                                  20    
SHEET    1   A 6 GLU A  23  ASP A  24  0                                        
SHEET    2   A 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  GLU A  23           
SHEET    3   A 6 ILE A 102  CYS A 107 -1  O  HIS A 104   N  ILE 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 LYS A  52  LEU A  61 -1  N  LYS A  60   O  PHE A 129           
SHEET    6   A 6 LYS A  66  ASP A  68 -1  O  PHE A  67   N  GLY A  59           
SHEET    1   B 6 GLU A  23  ASP A  24  0                                        
SHEET    2   B 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  GLU A  23           
SHEET    3   B 6 ILE A 102  CYS A 107 -1  O  HIS A 104   N  ILE 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 LYS A  52  LEU A  61 -1  N  LYS A  60   O  PHE A 129           
SHEET    6   B 6 PHE A  77  SER A  80 -1  O  PHE A  77   N  VAL A  55           
SHEET    1   C 6 GLU D  23  ASP D  24  0                                        
SHEET    2   C 6 VAL D  33  ARG D  39 -1  O  LYS D  35   N  GLU D  23           
SHEET    3   C 6 ILE D 102  CYS D 107 -1  O  HIS D 104   N  ILE D  36           
SHEET    4   C 6 LEU D 128  LYS D 138 -1  O  LEU D 128   N  CYS D 107           
SHEET    5   C 6 LYS D  52  LEU D  61 -1  N  LYS D  60   O  PHE D 129           
SHEET    6   C 6 LYS D  66  ASP D  68 -1  O  ASP D  68   N  GLY D  59           
SHEET    1   D 6 GLU D  23  ASP D  24  0                                        
SHEET    2   D 6 VAL D  33  ARG D  39 -1  O  LYS D  35   N  GLU D  23           
SHEET    3   D 6 ILE D 102  CYS D 107 -1  O  HIS D 104   N  ILE D  36           
SHEET    4   D 6 LEU D 128  LYS D 138 -1  O  LEU D 128   N  CYS D 107           
SHEET    5   D 6 LYS D  52  LEU D  61 -1  N  LYS D  60   O  PHE D 129           
SHEET    6   D 6 PHE D  77  SER D  80 -1  O  PHE D  77   N  VAL D  55           
CISPEP   1 LEU A  119    PRO A  120          0         2.23                     
CISPEP   2 LEU D  119    PRO D  120          0        -1.32                     
SITE     1 AC1 21 TYR A  57  PHE A  67  ASP A  68  HIS A  71                    
SITE     2 AC1 21 PHE A  77  GLY A  84  GLN A  85  VAL A  86                    
SITE     3 AC1 21 ILE A  87  TRP A  90  TYR A 113  LYS A 121                    
SITE     4 AC1 21 PHE A 130  LEU B2031  SER B2035  PHE B2039                    
SITE     5 AC1 21 THR B2098  TRP B2101  ASP B2102  TYR B2105                    
SITE     6 AC1 21 PHE B2108                                                     
SITE     1 AC2  9 ASP A  68  SER A  69  SER A  70  LYS A 121                    
SITE     2 AC2  9 HOH A 309  HOH A 319  HOH A 320  LYS B2095                    
SITE     3 AC2  9 THR B2098                                                     
SITE     1 AC3  3 LYS A  58  LYS A  60  LYS A  66                               
SITE     1 AC4  5 SER A  13  PRO A  14  THR A  15  LYS A  60                    
SITE     2 AC4  5 HOH A 317                                                     
SITE     1 AC5  2 ARG A  31  LYS A 108                                          
SITE     1 AC6  4 LYS A  52  TYR A  54  SER B2069  ARG B2110                    
SITE     1 AC7  4 THR A  26  SER A  27  LYS A  28  TYR A 111                    
SITE     1 AC8  6 GLU A  12  PRO A  14  LYS A  38  HIS A 104                    
SITE     2 AC8  6 HOH A 324  HOH A 326                                          
SITE     1 AC9  5 LYS A  99  ASP A 136  THR B2064  LEU B2065                    
SITE     2 AC9  5 HOH B2321                                                     
SITE     1 BC1  2 LYS B2045  ARG B2086                                          
SITE     1 BC2  2 TYR B2074  ARG B2110                                          
SITE     1 BC3  7 GLU A  75  GLN B2072  ARG B2076  HIS B2106                    
SITE     2 BC3  7 ARG B2109  HOH B2308  HOH B2325                               
SITE     1 BC4 22 HOH B2316  TYR D  57  PHE D  67  ASP D  68                    
SITE     2 BC4 22 HIS D  71  PHE D  77  GLY D  84  GLN D  85                    
SITE     3 BC4 22 VAL D  86  ILE D  87  TRP D  90  TYR D 113                    
SITE     4 BC4 22 PHE D 130  LEU E2031  SER E2035  ARG E2036                    
SITE     5 BC4 22 PHE E2039  THR E2098  TRP E2101  ASP E2102                    
SITE     6 BC4 22 TYR E2105  PHE E2108                                          
SITE     1 BC5  4 SER D  13  PRO D  14  THR D  15  LYS D  60                    
SITE     1 BC6  4 GLU D  12  PRO D  14  LYS D  38  HIS D 104                    
SITE     1 BC7  5 PHE D  67  ASP D  68  SER D  69  SER D  70                    
SITE     2 BC7  5 HOH D 317                                                     
SITE     1 BC8  3 LYS D  58  LYS D  60  LYS D  66                               
SITE     1 BC9  4 TYR E2105  HIS E2106  ARG E2109  HOH E2302                    
SITE     1 CC1  3 LYS E2045  ARG E2086  HOH E2307                               
SITE     1 CC2  3 LYS D  52  TYR D  54  ARG E2109                               
SITE     1 CC3  6 HIS B2028  GLU B2029  GLU B2032  HIS E2028                    
SITE     2 CC3  6 GLU E2029  GLU E2032                                          
SITE     1 CC4  2 GLN E2082  HOH E2305                                          
SITE     1 CC5  3 ARG D  39  ASP E2077  HIS E2106                               
CRYST1  103.678  103.678  106.543  90.00  90.00 120.00 P 31 1 2     12          
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      0.009645  0.005569  0.000000        0.00000                         
SCALE2      0.000000  0.011137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009386        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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