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Entry: 5WBH
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HEADER    TRANSFERASE                             29-JUN-17   5WBH              
TITLE     STRUCTURE OF THE FRB DOMAIN OF MTOR BOUND TO A SUBSTRATE RECRUITMENT  
TITLE    2 PEPTIDE OF S6K1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR;                      
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: RESIDUES 2018-2114;                                        
COMPND   5 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED       
COMPND   6 PROTEIN 1,FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN,MAMMALIAN      
COMPND   7 TARGET OF RAPAMYCIN,MTOR,MECHANISTIC TARGET OF RAPAMYCIN,RAPAMYCIN   
COMPND   8 AND FKBP12 TARGET 1,RAPAMYCIN TARGET PROTEIN 1;                      
COMPND   9 EC: 2.7.11.1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: RIBOSOMAL PROTEIN S6 KINASE BETA-1;                        
COMPND  13 CHAIN: W;                                                            
COMPND  14 FRAGMENT: RESIDUES 412-437;                                          
COMPND  15 SYNONYM: S6K1,70 KDA RIBOSOMAL PROTEIN S6 KINASE 1,P70-S6K 1,        
COMPND  16 RIBOSOMAL PROTEIN S6 KINASE I,SERINE/THREONINE-PROTEIN KINASE 14A,P70
COMPND  17 RIBOSOMAL S6 KINASE ALPHA,P70 S6KA;                                  
COMPND  18 EC: 2.7.11.1;                                                        
COMPND  19 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: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1;                        
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: PET26;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RPS6KB1, STK14A;                                               
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: PET26                                     
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.PAVLETICH,H.YANG                                                  
REVDAT   2   18-APR-18 5WBH    1       JRNL                                     
REVDAT   1   20-DEC-17 5WBH    0                                                
JRNL        AUTH   H.YANG,X.JIANG,B.LI,H.J.YANG,M.MILLER,A.YANG,A.DHAR,         
JRNL        AUTH 2 N.P.PAVLETICH                                                
JRNL        TITL   MECHANISMS OF MTORC1 ACTIVATION BY RHEB AND INHIBITION BY    
JRNL        TITL 2 PRAS40.                                                      
JRNL        REF    NATURE                        V. 552   368 2017              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29236692                                                     
JRNL        DOI    10.1038/NATURE25023                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 61680                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1932                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3649                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 119                          
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4108                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 334                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.80000                                             
REMARK   3    B22 (A**2) : 5.45000                                              
REMARK   3    B33 (A**2) : -1.65000                                             
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): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.489         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4221 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3936 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5667 ; 1.066 ; 1.927       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8963 ; 0.892 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   479 ; 4.951 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   231 ;32.315 ;23.203       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   775 ;15.098 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;13.459 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   546 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4722 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1069 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 6                                          
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  2023        A  2116                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4270  21.3970  -8.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2634 T22:   0.1826                                     
REMARK   3      T33:   0.2078 T12:   0.0232                                     
REMARK   3      T13:   0.0230 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1130 L22:   1.2004                                     
REMARK   3      L33:   4.0271 L12:   0.6847                                     
REMARK   3      L13:   2.3089 L23:   0.4622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.2110 S13:  -0.0302                       
REMARK   3      S21:   0.0691 S22:   0.0570 S23:  -0.0650                       
REMARK   3      S31:   0.0685 S32:  -0.0158 S33:  -0.0380                       
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 :   B  2023        B  2116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6830  21.7310   1.0040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2897 T22:   0.1426                                     
REMARK   3      T33:   0.1837 T12:   0.0062                                     
REMARK   3      T13:  -0.0062 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8582 L22:   0.6614                                     
REMARK   3      L33:   2.2255 L12:  -0.7562                                     
REMARK   3      L13:  -1.4490 L23:   0.1466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0960 S12:  -0.0385 S13:  -0.1363                       
REMARK   3      S21:  -0.0517 S22:   0.0513 S23:  -0.0456                       
REMARK   3      S31:   0.0692 S32:   0.0495 S33:   0.0447                       
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 :   C  2019        C  2116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2780  -0.1950 -30.0970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3133 T22:   0.0207                                     
REMARK   3      T33:   0.2900 T12:   0.0134                                     
REMARK   3      T13:   0.0153 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5667 L22:   1.5326                                     
REMARK   3      L33:   1.4070 L12:   0.2661                                     
REMARK   3      L13:   1.7476 L23:   0.2783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.1918 S13:   0.3220                       
REMARK   3      S21:   0.1001 S22:  -0.0117 S23:   0.0533                       
REMARK   3      S31:  -0.1230 S32:   0.0362 S33:   0.0315                       
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 :   D  2023        D  2116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8680  17.8540 -39.4200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2380 T22:   0.0059                                     
REMARK   3      T33:   0.1522 T12:   0.0011                                     
REMARK   3      T13:  -0.0283 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7379 L22:   2.0190                                     
REMARK   3      L33:   4.2984 L12:  -0.1032                                     
REMARK   3      L13:  -1.9590 L23:   0.4081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.1064 S13:   0.0413                       
REMARK   3      S21:  -0.0372 S22:  -0.0136 S23:  -0.0846                       
REMARK   3      S31:   0.0451 S32:  -0.0213 S33:   0.0029                       
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 :   E  2023        E  2116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0110  33.9680 -30.8670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2925 T22:   0.0375                                     
REMARK   3      T33:   0.3040 T12:   0.0300                                     
REMARK   3      T13:   0.0005 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7206 L22:   1.5949                                     
REMARK   3      L33:   2.2012 L12:   0.2751                                     
REMARK   3      L13:  -1.2508 L23:  -0.7258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0317 S12:  -0.0620 S13:  -0.1385                       
REMARK   3      S21:  -0.0071 S22:  -0.0314 S23:   0.1128                       
REMARK   3      S31:   0.0835 S32:   0.2028 S33:   0.0632                       
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 :   W   392        W   410                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9630   5.5810 -48.7580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3099 T22:   0.2324                                     
REMARK   3      T33:   0.3799 T12:   0.0219                                     
REMARK   3      T13:  -0.0044 T23:  -0.0668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4125 L22:   8.9162                                     
REMARK   3      L33:   4.4695 L12:  -3.1197                                     
REMARK   3      L13:   2.4627 L23:  -5.7735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1735 S12:   0.0981 S13:  -0.2394                       
REMARK   3      S21:  -0.3535 S22:   0.0283 S23:   0.1802                       
REMARK   3      S31:   0.2543 S32:   0.0643 S33:  -0.2017                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN USED IF PRESENT IN THE INPUT                              
REMARK   4                                                                      
REMARK   4 5WBH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228735.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97920                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66487                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1FAP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TACSIMATE, PH 7.0, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.47200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.42400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.47200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       67.42400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 6100 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 5770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 6360 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
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: 880 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7320 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, W                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 6450 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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  2016                                                      
REMARK 465     SER A  2017                                                      
REMARK 465     ARG A  2018                                                      
REMARK 465     VAL A  2019                                                      
REMARK 465     ALA A  2020                                                      
REMARK 465     ILE A  2021                                                      
REMARK 465     GLN A  2114                                                      
REMARK 465     SER A  2115                                                      
REMARK 465     GLY A  2116                                                      
REMARK 465     GLY A  2117                                                      
REMARK 465     GLY B  2016                                                      
REMARK 465     SER B  2017                                                      
REMARK 465     ARG B  2018                                                      
REMARK 465     VAL B  2019                                                      
REMARK 465     ALA B  2020                                                      
REMARK 465     ILE B  2021                                                      
REMARK 465     GLN B  2114                                                      
REMARK 465     SER B  2115                                                      
REMARK 465     GLY B  2116                                                      
REMARK 465     GLY B  2117                                                      
REMARK 465     GLY C  2016                                                      
REMARK 465     SER C  2017                                                      
REMARK 465     GLN C  2114                                                      
REMARK 465     SER C  2115                                                      
REMARK 465     GLY C  2116                                                      
REMARK 465     GLY C  2117                                                      
REMARK 465     GLY D  2016                                                      
REMARK 465     SER D  2017                                                      
REMARK 465     ARG D  2018                                                      
REMARK 465     VAL D  2019                                                      
REMARK 465     ALA D  2020                                                      
REMARK 465     ILE D  2021                                                      
REMARK 465     GLN D  2114                                                      
REMARK 465     SER D  2115                                                      
REMARK 465     GLY D  2116                                                      
REMARK 465     GLY D  2117                                                      
REMARK 465     GLY E  2016                                                      
REMARK 465     SER E  2017                                                      
REMARK 465     ARG E  2018                                                      
REMARK 465     VAL E  2019                                                      
REMARK 465     ALA E  2020                                                      
REMARK 465     ILE E  2021                                                      
REMARK 465     GLY E  2116                                                      
REMARK 465     GLY E  2117                                                      
REMARK 465     THR W   389                                                      
REMARK 465     TYR W   390                                                      
REMARK 465     VAL W   391                                                      
REMARK 465     SER W   411                                                      
REMARK 465     PRO W   412                                                      
REMARK 465     ARG W   413                                                      
REMARK 465     ARG W   414                                                      
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     ARG C2018    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG W 410    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HZ1  LYS E  2113     O    HOH E  2201              1.56            
REMARK 500   O    HOH D  2215     O    HOH D  2265              1.94            
REMARK 500   O    HOH D  2249     O    HOH D  2265              2.11            
REMARK 500   NZ   LYS E  2113     O    HOH E  2201              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2267        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A2268        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH E2266        DISTANCE =  7.26 ANGSTROMS                       
DBREF  5WBH A 2018  2114  UNP    P42345   MTOR_HUMAN    2018   2114             
DBREF  5WBH B 2018  2114  UNP    P42345   MTOR_HUMAN    2018   2114             
DBREF  5WBH C 2018  2114  UNP    P42345   MTOR_HUMAN    2018   2114             
DBREF  5WBH D 2018  2114  UNP    P42345   MTOR_HUMAN    2018   2114             
DBREF  5WBH E 2018  2114  UNP    P42345   MTOR_HUMAN    2018   2114             
DBREF  5WBH W  389   414  UNP    P23443   KS6B1_HUMAN    412    437             
SEQADV 5WBH GLY A 2016  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER A 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER A 2115  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY A 2116  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY A 2117  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY B 2016  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER B 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER B 2115  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY B 2116  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY B 2117  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY C 2016  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER C 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER C 2115  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY C 2116  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY C 2117  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY D 2016  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER D 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER D 2115  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY D 2116  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY D 2117  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY E 2016  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER E 2017  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH SER E 2115  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY E 2116  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBH GLY E 2117  UNP  P42345              EXPRESSION TAG                 
SEQRES   1 A  102  GLY SER ARG VAL ALA ILE LEU TRP HIS GLU MET TRP HIS          
SEQRES   2 A  102  GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU          
SEQRES   3 A  102  ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU          
SEQRES   4 A  102  HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU          
SEQRES   5 A  102  THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU          
SEQRES   6 A  102  ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN          
SEQRES   7 A  102  VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS          
SEQRES   8 A  102  VAL PHE ARG ARG ILE SER LYS GLN SER GLY GLY                  
SEQRES   1 B  102  GLY SER ARG VAL ALA ILE LEU TRP HIS GLU MET TRP HIS          
SEQRES   2 B  102  GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU          
SEQRES   3 B  102  ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU          
SEQRES   4 B  102  HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU          
SEQRES   5 B  102  THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU          
SEQRES   6 B  102  ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN          
SEQRES   7 B  102  VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS          
SEQRES   8 B  102  VAL PHE ARG ARG ILE SER LYS GLN SER GLY GLY                  
SEQRES   1 C  102  GLY SER ARG VAL ALA ILE LEU TRP HIS GLU MET TRP HIS          
SEQRES   2 C  102  GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU          
SEQRES   3 C  102  ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU          
SEQRES   4 C  102  HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU          
SEQRES   5 C  102  THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU          
SEQRES   6 C  102  ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN          
SEQRES   7 C  102  VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS          
SEQRES   8 C  102  VAL PHE ARG ARG ILE SER LYS GLN SER GLY GLY                  
SEQRES   1 D  102  GLY SER ARG VAL ALA ILE LEU TRP HIS GLU MET TRP HIS          
SEQRES   2 D  102  GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU          
SEQRES   3 D  102  ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU          
SEQRES   4 D  102  HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU          
SEQRES   5 D  102  THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU          
SEQRES   6 D  102  ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN          
SEQRES   7 D  102  VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS          
SEQRES   8 D  102  VAL PHE ARG ARG ILE SER LYS GLN SER GLY GLY                  
SEQRES   1 E  102  GLY SER ARG VAL ALA ILE LEU TRP HIS GLU MET TRP HIS          
SEQRES   2 E  102  GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY GLU          
SEQRES   3 E  102  ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO LEU          
SEQRES   4 E  102  HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS GLU          
SEQRES   5 E  102  THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET GLU          
SEQRES   6 E  102  ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY ASN          
SEQRES   7 E  102  VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR HIS          
SEQRES   8 E  102  VAL PHE ARG ARG ILE SER LYS GLN SER GLY GLY                  
SEQRES   1 W   26  THR TYR VAL ALA PRO SER VAL LEU GLU SER VAL LYS GLU          
SEQRES   2 W   26  LYS PHE SER PHE GLU PRO LYS ILE ARG SER PRO ARG ARG          
FORMUL   7  HOH   *334(H2 O)                                                    
HELIX    1 AA1 LEU A 2022  GLY A 2040  1                                  19    
HELIX    2 AA2 ASN A 2043  GLY A 2061  1                                  19    
HELIX    3 AA3 THR A 2064  GLY A 2092  1                                  29    
HELIX    4 AA4 ASN A 2093  LYS A 2113  1                                  21    
HELIX    5 AA5 TRP B 2023  ARG B 2042  1                                  20    
HELIX    6 AA6 ASN B 2043  MET B 2057  1                                  15    
HELIX    7 AA7 THR B 2064  GLY B 2092  1                                  29    
HELIX    8 AA8 ASN B 2093  LYS B 2113  1                                  21    
HELIX    9 AA9 LEU C 2022  ARG C 2042  1                                  21    
HELIX   10 AB1 ASN C 2043  ARG C 2060  1                                  18    
HELIX   11 AB2 THR C 2064  GLY C 2092  1                                  29    
HELIX   12 AB3 ASN C 2093  LYS C 2113  1                                  21    
HELIX   13 AB4 TRP D 2023  ARG D 2042  1                                  20    
HELIX   14 AB5 ASN D 2043  ARG D 2060  1                                  18    
HELIX   15 AB6 THR D 2064  GLY D 2092  1                                  29    
HELIX   16 AB7 ASN D 2093  SER D 2112  1                                  20    
HELIX   17 AB8 TRP E 2023  GLY E 2040  1                                  18    
HELIX   18 AB9 ASN E 2043  GLY E 2061  1                                  19    
HELIX   19 AC1 THR E 2064  GLY E 2092  1                                  29    
HELIX   20 AC2 ASN E 2093  SER E 2115  1                                  23    
HELIX   21 AC3 SER W  394  VAL W  399  1                                   6    
HELIX   22 AC4 LYS W  400  SER W  404  5                                   5    
HELIX   23 AC5 PHE W  405  ILE W  409  5                                   5    
CRYST1   60.613   80.944  134.848  90.00  90.00  90.00 P 2 21 21    20          
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      0.016498  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012354  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007416        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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