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Database: PDB
Entry: 4JT6
LinkDB: 4JT6
Original site: 4JT6 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       22-MAR-13   4JT6              
TITLE     STRUCTURE OF MTORDELTAN-MLST8-PI-103 COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MTOR;                                                      
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1376-2549;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MLST8;                                                     
COMPND   8 CHAIN: D, C;                                                         
COMPND   9 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+)HYGROMYCIN;                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: MLST8;                                                         
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+)BLASTICIDIN                    
KEYWDS    KINASE, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.PAVLETICH,H.YANG                                                  
REVDAT   3   29-MAY-13 4JT6    1       JRNL                                     
REVDAT   2   15-MAY-13 4JT6    1       REMARK                                   
REVDAT   1   08-MAY-13 4JT6    0                                                
JRNL        AUTH   H.YANG,D.G.RUDGE,J.D.KOOS,B.VAIDIALINGAM,H.J.YANG,           
JRNL        AUTH 2 N.P.PAVLETICH                                                
JRNL        TITL   MTOR KINASE STRUCTURE, MECHANISM AND REGULATION.             
JRNL        REF    NATURE                        V. 497   217 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   23636326                                                     
JRNL        DOI    10.1038/NATURE12122                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42196                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1294                            
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) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2188                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.4000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22097                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.63000                                             
REMARK   3    B22 (A**2) : -2.17000                                             
REMARK   3    B33 (A**2) : 2.80000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.808         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.517         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.422        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.897                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22698 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30778 ; 1.217 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2742 ; 6.406 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1088 ;37.370 ;23.952       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3982 ;20.420 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   158 ;18.638 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3368 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17176 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 10990 ; 1.475 ; 3.245       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13723 ; 2.727 ; 7.296       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11706 ; 1.068 ; 3.299       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 17                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    B    (A):    284 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):     80 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    376 ; 0.010 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    300 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):     88 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    116 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1012 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1268 ; 0.020 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    223 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):    232 ; 4.170 ;99.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    223 ; 4.710 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    271 ; 0.010 ; 0.500           
REMARK   3   TIGHT THERMAL      2    B (A**2):    248 ; 9.500 ;99.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    271 ; 9.800 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    B    (A):    121 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      3    B (A**2):    132 ; 9.800 ;99.000           
REMARK   3   MEDIUM THERMAL     3    B (A**2):    121 ; 9.780 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    B    (A):    161 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    B (A**2):    172 ;18.720 ;99.000           
REMARK   3   MEDIUM THERMAL     4    B (A**2):    161 ;18.300 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    B    (A):    211 ; 0.030 ; 0.500           
REMARK   3   TIGHT THERMAL      5    B (A**2):    188 ;28.770 ;99.000           
REMARK   3   MEDIUM THERMAL     5    B (A**2):    211 ;25.280 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    B    (A):    204 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      6    B (A**2):    204 ;12.800 ;99.000           
REMARK   3   MEDIUM THERMAL     6    B (A**2):    204 ;12.570 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  7    B    (A):    238 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      7    B (A**2):    224 ; 3.390 ;99.000           
REMARK   3   MEDIUM THERMAL     7    B (A**2):    238 ; 3.490 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  8    B    (A):    363 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      8    B (A**2):    320 ; 3.630 ;99.000           
REMARK   3   MEDIUM THERMAL     8    B (A**2):    363 ; 4.310 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  9    B    (A):    258 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      9    B (A**2):    256 ; 4.690 ;99.000           
REMARK   3   MEDIUM THERMAL     9    B (A**2):    258 ; 4.820 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 10    B    (A):    283 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     10    B (A**2):    284 ; 5.640 ;99.000           
REMARK   3   MEDIUM THERMAL    10    B (A**2):    283 ; 5.980 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 11    B    (A):     73 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     11    B (A**2):     80 ; 6.890 ;99.000           
REMARK   3   MEDIUM THERMAL    11    B (A**2):     73 ; 6.860 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 12    B    (A):    425 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     12    B (A**2):    376 ;17.010 ;99.000           
REMARK   3   MEDIUM THERMAL    12    B (A**2):    425 ;16.760 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 13    B    (A):    293 ; 0.050 ; 0.500           
REMARK   3   TIGHT THERMAL     13    B (A**2):    300 ; 9.140 ;99.000           
REMARK   3   MEDIUM THERMAL    13    B (A**2):    293 ; 9.410 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 14    B    (A):     90 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     14    B (A**2):     88 ; 5.090 ;99.000           
REMARK   3   MEDIUM THERMAL    14    B (A**2):     90 ; 6.080 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 15    B    (A):    108 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     15    B (A**2):    116 ; 1.880 ;99.000           
REMARK   3   MEDIUM THERMAL    15    B (A**2):    108 ; 2.060 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 16    B    (A):   1055 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     16    B (A**2):   1012 ; 4.050 ;99.000           
REMARK   3   MEDIUM THERMAL    16    B (A**2):   1055 ; 4.230 ;99.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 17                                 
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 17    D    (A):   1186 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL     17    D (A**2):   1268 ; 9.950 ;99.000           
REMARK   3   MEDIUM THERMAL    17    D (A**2):   1186 ;10.450 ;99.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.30                                          
REMARK   3   ION PROBE RADIUS   : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 1.10                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES      : REFINED INDIVIDUALLY      
REMARK   4                                                                      
REMARK   4 4JT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078472.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 8.5                                
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-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49787                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65000                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NACL, PH 8.5, HANGING DROP     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 277K, VAPOR DIFFUSION, HANGING DROP    
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       81.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.90000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.60000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.90000            
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 300 REMARK: THE BIOLOGICAL UNIT IS A HETERODIMER. THERE ARE 2            
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A & C AND CHAINS B   
REMARK 300 & D)                                                                 
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 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 APPLY THE FOLLOWING TO CHAINS: A, 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 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     ASP B  1376                                                      
REMARK 465     ASP B  1377                                                      
REMARK 465     ASN B  1378                                                      
REMARK 465     GLY B  1379                                                      
REMARK 465     ILE B  1380                                                      
REMARK 465     VAL B  1381                                                      
REMARK 465     LEU B  1382                                                      
REMARK 465     LEU B  1383                                                      
REMARK 465     GLY B  1384                                                      
REMARK 465     LYS B  1815                                                      
REMARK 465     LYS B  1816                                                      
REMARK 465     LEU B  1817                                                      
REMARK 465     ARG B  1818                                                      
REMARK 465     HIS B  1819                                                      
REMARK 465     ALA B  1820                                                      
REMARK 465     SER B  1821                                                      
REMARK 465     GLY B  1822                                                      
REMARK 465     ALA B  1823                                                      
REMARK 465     ASN B  1824                                                      
REMARK 465     ILE B  1825                                                      
REMARK 465     THR B  1826                                                      
REMARK 465     ASN B  1827                                                      
REMARK 465     ALA B  1828                                                      
REMARK 465     THR B  1829                                                      
REMARK 465     THR B  1830                                                      
REMARK 465     ALA B  1831                                                      
REMARK 465     ALA B  1832                                                      
REMARK 465     THR B  1833                                                      
REMARK 465     THR B  1834                                                      
REMARK 465     ALA B  1835                                                      
REMARK 465     ALA B  1836                                                      
REMARK 465     THR B  1837                                                      
REMARK 465     ALA B  1838                                                      
REMARK 465     THR B  1839                                                      
REMARK 465     THR B  1840                                                      
REMARK 465     THR B  1841                                                      
REMARK 465     ALA B  1842                                                      
REMARK 465     SER B  1843                                                      
REMARK 465     THR B  1844                                                      
REMARK 465     GLU B  1845                                                      
REMARK 465     GLY B  1846                                                      
REMARK 465     SER B  1847                                                      
REMARK 465     ASN B  1848                                                      
REMARK 465     SER B  1849                                                      
REMARK 465     GLU B  1850                                                      
REMARK 465     SER B  1851                                                      
REMARK 465     GLU B  1852                                                      
REMARK 465     ALA B  1853                                                      
REMARK 465     GLU B  1854                                                      
REMARK 465     SER B  1855                                                      
REMARK 465     THR B  1856                                                      
REMARK 465     GLU B  1857                                                      
REMARK 465     ASN B  1858                                                      
REMARK 465     SER B  1859                                                      
REMARK 465     PRO B  1860                                                      
REMARK 465     THR B  1861                                                      
REMARK 465     PRO B  1862                                                      
REMARK 465     SER B  1863                                                      
REMARK 465     PRO B  1864                                                      
REMARK 465     LEU B  1865                                                      
REMARK 465     GLN B  1866                                                      
REMARK 465     LYS B  2437                                                      
REMARK 465     GLY B  2438                                                      
REMARK 465     ASN B  2439                                                      
REMARK 465     LYS B  2440                                                      
REMARK 465     ARG B  2441                                                      
REMARK 465     SER B  2442                                                      
REMARK 465     ARG B  2443                                                      
REMARK 465     THR B  2444                                                      
REMARK 465     ARG B  2445                                                      
REMARK 465     THR B  2446                                                      
REMARK 465     ASP B  2447                                                      
REMARK 465     SER B  2448                                                      
REMARK 465     TYR B  2449                                                      
REMARK 465     SER B  2450                                                      
REMARK 465     ALA B  2451                                                      
REMARK 465     GLY B  2452                                                      
REMARK 465     GLN B  2453                                                      
REMARK 465     SER B  2454                                                      
REMARK 465     VAL B  2455                                                      
REMARK 465     GLU B  2456                                                      
REMARK 465     ILE B  2457                                                      
REMARK 465     LEU B  2458                                                      
REMARK 465     ASP B  2459                                                      
REMARK 465     GLY B  2460                                                      
REMARK 465     VAL B  2461                                                      
REMARK 465     GLU B  2462                                                      
REMARK 465     LEU B  2463                                                      
REMARK 465     GLY B  2464                                                      
REMARK 465     GLU B  2465                                                      
REMARK 465     PRO B  2466                                                      
REMARK 465     ALA B  2467                                                      
REMARK 465     HIS B  2468                                                      
REMARK 465     LYS B  2469                                                      
REMARK 465     LYS B  2470                                                      
REMARK 465     THR B  2471                                                      
REMARK 465     GLY B  2472                                                      
REMARK 465     THR B  2473                                                      
REMARK 465     THR B  2474                                                      
REMARK 465     VAL B  2475                                                      
REMARK 465     PRO B  2476                                                      
REMARK 465     GLU B  2477                                                      
REMARK 465     SER B  2478                                                      
REMARK 465     ILE B  2479                                                      
REMARK 465     HIS B  2480                                                      
REMARK 465     SER B  2481                                                      
REMARK 465     PHE B  2482                                                      
REMARK 465     ILE B  2483                                                      
REMARK 465     GLY B  2484                                                      
REMARK 465     ASP B  2485                                                      
REMARK 465     GLY B  2486                                                      
REMARK 465     LEU B  2487                                                      
REMARK 465     VAL B  2488                                                      
REMARK 465     LYS B  2489                                                      
REMARK 465     PRO B  2490                                                      
REMARK 465     GLU B  2491                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     LEU D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     ASP A  1376                                                      
REMARK 465     ASP A  1377                                                      
REMARK 465     ASN A  1378                                                      
REMARK 465     GLY A  1379                                                      
REMARK 465     ILE A  1380                                                      
REMARK 465     VAL A  1381                                                      
REMARK 465     LEU A  1382                                                      
REMARK 465     LEU A  1383                                                      
REMARK 465     GLY A  1384                                                      
REMARK 465     LEU A  1607                                                      
REMARK 465     VAL A  1608                                                      
REMARK 465     PRO A  1609                                                      
REMARK 465     GLU A  1610                                                      
REMARK 465     LYS A  1815                                                      
REMARK 465     LYS A  1816                                                      
REMARK 465     LEU A  1817                                                      
REMARK 465     ARG A  1818                                                      
REMARK 465     HIS A  1819                                                      
REMARK 465     ALA A  1820                                                      
REMARK 465     SER A  1821                                                      
REMARK 465     GLY A  1822                                                      
REMARK 465     ALA A  1823                                                      
REMARK 465     ASN A  1824                                                      
REMARK 465     ILE A  1825                                                      
REMARK 465     THR A  1826                                                      
REMARK 465     ASN A  1827                                                      
REMARK 465     ALA A  1828                                                      
REMARK 465     THR A  1829                                                      
REMARK 465     THR A  1830                                                      
REMARK 465     ALA A  1831                                                      
REMARK 465     ALA A  1832                                                      
REMARK 465     THR A  1833                                                      
REMARK 465     THR A  1834                                                      
REMARK 465     ALA A  1835                                                      
REMARK 465     ALA A  1836                                                      
REMARK 465     THR A  1837                                                      
REMARK 465     ALA A  1838                                                      
REMARK 465     THR A  1839                                                      
REMARK 465     THR A  1840                                                      
REMARK 465     THR A  1841                                                      
REMARK 465     ALA A  1842                                                      
REMARK 465     SER A  1843                                                      
REMARK 465     THR A  1844                                                      
REMARK 465     GLU A  1845                                                      
REMARK 465     GLY A  1846                                                      
REMARK 465     SER A  1847                                                      
REMARK 465     ASN A  1848                                                      
REMARK 465     SER A  1849                                                      
REMARK 465     GLU A  1850                                                      
REMARK 465     SER A  1851                                                      
REMARK 465     GLU A  1852                                                      
REMARK 465     ALA A  1853                                                      
REMARK 465     GLU A  1854                                                      
REMARK 465     SER A  1855                                                      
REMARK 465     THR A  1856                                                      
REMARK 465     GLU A  1857                                                      
REMARK 465     ASN A  1858                                                      
REMARK 465     SER A  1859                                                      
REMARK 465     PRO A  1860                                                      
REMARK 465     THR A  1861                                                      
REMARK 465     PRO A  1862                                                      
REMARK 465     SER A  1863                                                      
REMARK 465     PRO A  1864                                                      
REMARK 465     LEU A  1865                                                      
REMARK 465     GLN A  1866                                                      
REMARK 465     LYS A  2437                                                      
REMARK 465     GLY A  2438                                                      
REMARK 465     ASN A  2439                                                      
REMARK 465     LYS A  2440                                                      
REMARK 465     ARG A  2441                                                      
REMARK 465     SER A  2442                                                      
REMARK 465     ARG A  2443                                                      
REMARK 465     THR A  2444                                                      
REMARK 465     ARG A  2445                                                      
REMARK 465     THR A  2446                                                      
REMARK 465     ASP A  2447                                                      
REMARK 465     SER A  2448                                                      
REMARK 465     TYR A  2449                                                      
REMARK 465     SER A  2450                                                      
REMARK 465     ALA A  2451                                                      
REMARK 465     GLY A  2452                                                      
REMARK 465     GLN A  2453                                                      
REMARK 465     SER A  2454                                                      
REMARK 465     VAL A  2455                                                      
REMARK 465     GLU A  2456                                                      
REMARK 465     ILE A  2457                                                      
REMARK 465     LEU A  2458                                                      
REMARK 465     ASP A  2459                                                      
REMARK 465     GLY A  2460                                                      
REMARK 465     VAL A  2461                                                      
REMARK 465     GLU A  2462                                                      
REMARK 465     LEU A  2463                                                      
REMARK 465     GLY A  2464                                                      
REMARK 465     GLU A  2465                                                      
REMARK 465     PRO A  2466                                                      
REMARK 465     ALA A  2467                                                      
REMARK 465     HIS A  2468                                                      
REMARK 465     LYS A  2469                                                      
REMARK 465     LYS A  2470                                                      
REMARK 465     THR A  2471                                                      
REMARK 465     GLY A  2472                                                      
REMARK 465     THR A  2473                                                      
REMARK 465     THR A  2474                                                      
REMARK 465     VAL A  2475                                                      
REMARK 465     PRO A  2476                                                      
REMARK 465     GLU A  2477                                                      
REMARK 465     SER A  2478                                                      
REMARK 465     ILE A  2479                                                      
REMARK 465     HIS A  2480                                                      
REMARK 465     SER A  2481                                                      
REMARK 465     PHE A  2482                                                      
REMARK 465     ILE A  2483                                                      
REMARK 465     GLY A  2484                                                      
REMARK 465     ASP A  2485                                                      
REMARK 465     GLY A  2486                                                      
REMARK 465     LEU A  2487                                                      
REMARK 465     VAL A  2488                                                      
REMARK 465     LYS A  2489                                                      
REMARK 465     PRO A  2490                                                      
REMARK 465     GLU A  2491                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     LEU C   325                                                      
REMARK 465     GLY C   326                                                      
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   OE2  GLU B  2015     OG   SER B  2127              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU B1416      -51.79   -120.57                                   
REMARK 500    LEU B1423       19.27    -68.14                                   
REMARK 500    GLN B1424       43.69     33.46                                   
REMARK 500    GLU B1444     -178.46     48.72                                   
REMARK 500    ILE B1445      105.94     50.36                                   
REMARK 500    HIS B1454       11.52     49.13                                   
REMARK 500    ASN B1470     -142.53    -79.98                                   
REMARK 500    LYS B1471     -132.01   -120.30                                   
REMARK 500    ASP B1473       86.22     51.84                                   
REMARK 500    LEU B1503       52.44     28.15                                   
REMARK 500    MET B1512      -56.11    -24.20                                   
REMARK 500    GLN B1525       86.32    -31.08                                   
REMARK 500    ALA B1579       80.71    -69.63                                   
REMARK 500    TYR B1583     -156.41    -78.96                                   
REMARK 500    SER B1584       45.58    -74.03                                   
REMARK 500    ARG B1622       39.67    -76.00                                   
REMARK 500    LEU B1623      -64.41   -137.51                                   
REMARK 500    VAL B1630      -72.65      2.63                                   
REMARK 500    MET B1650      -67.31      9.79                                   
REMARK 500    ASP B1680      149.32    -32.50                                   
REMARK 500    PRO B1681       56.48    -63.08                                   
REMARK 500    SER B1682       63.47     12.43                                   
REMARK 500    GLN B1684       91.55    -68.50                                   
REMARK 500    PRO B1688      149.37    -39.56                                   
REMARK 500    SER B1707     -160.59    -66.06                                   
REMARK 500    ARG B1709       76.52    -55.72                                   
REMARK 500    ALA B1728      -77.41    -84.54                                   
REMARK 500    THR B1734      -53.19    -22.47                                   
REMARK 500    GLU B1735       39.45    -60.54                                   
REMARK 500    ASP B1736       78.33   -152.34                                   
REMARK 500    ARG B1784      -71.57     55.77                                   
REMARK 500    TRP B1786      107.01     90.89                                   
REMARK 500    ARG B1896      110.81     33.97                                   
REMARK 500    ASN B1898       59.74   -147.06                                   
REMARK 500    TYR B1913       55.74   -113.11                                   
REMARK 500    ASP B1933      -65.85    -24.62                                   
REMARK 500    THR B1934      -61.22    -21.15                                   
REMARK 500    ASP B1947       38.65    -71.95                                   
REMARK 500    HIS B1968       74.26     36.18                                   
REMARK 500    GLN B1970      -58.88    107.45                                   
REMARK 500    ARG B1987      -76.98    -62.55                                   
REMARK 500    GLU B2000       23.91    -66.71                                   
REMARK 500    HIS B2001      -46.12   -168.07                                   
REMARK 500    SER B2002       42.22   -142.23                                   
REMARK 500    GLU B2041      -14.61   -145.22                                   
REMARK 500    ASN B2093     -106.87    -77.71                                   
REMARK 500    VAL B2094      -17.58    146.64                                   
REMARK 500    PRO B2116        6.28    -68.19                                   
REMARK 500    PRO B2141      119.50    -32.41                                   
REMARK 500    ASN B2147      -29.28     86.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     204 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B 1914     HIS B 1915                 -136.26                    
REMARK 500 PRO D  169     GLU D  170                  125.74                    
REMARK 500 GLY A 1914     HIS A 1915                 -137.87                    
REMARK 500 PRO C  169     GLU C  170                  126.36                    
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    MET B1650        24.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS B1915        17.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS B1968        24.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS B2401        24.5      L          L   OUTSIDE RANGE           
REMARK 500    SER D 269        24.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A1915        16.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS A1968        24.1      L          L   OUTSIDE RANGE           
REMARK 500    HIS A2401        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER C 269        25.0      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 X6K B 2601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X6K A 2601                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JSN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JSV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JSX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JT5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JSP   RELATED DB: PDB                                   
DBREF  4JT6 B 1376  2549  UNP    P42345   MTOR_HUMAN    1376   2549             
DBREF  4JT6 D    1   326  UNP    Q9BVC4   LST8_HUMAN       1    326             
DBREF  4JT6 A 1376  2549  UNP    P42345   MTOR_HUMAN    1376   2549             
DBREF  4JT6 C    1   326  UNP    Q9BVC4   LST8_HUMAN       1    326             
SEQRES   1 B 1174  ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU ARG ALA ALA          
SEQRES   2 B 1174  LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS TYR LYS GLU          
SEQRES   3 B 1174  LEU GLU PHE GLN LYS GLY PRO THR PRO ALA ILE LEU GLU          
SEQRES   4 B 1174  SER LEU ILE SER ILE ASN ASN LYS LEU GLN GLN PRO GLU          
SEQRES   5 B 1174  ALA ALA ALA GLY VAL LEU GLU TYR ALA MET LYS HIS PHE          
SEQRES   6 B 1174  GLY GLU LEU GLU ILE GLN ALA THR TRP TYR GLU LYS LEU          
SEQRES   7 B 1174  HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR ASP LYS LYS          
SEQRES   8 B 1174  MET ASP THR ASN LYS ASP ASP PRO GLU LEU MET LEU GLY          
SEQRES   9 B 1174  ARG MET ARG CYS LEU GLU ALA LEU GLY GLU TRP GLY GLN          
SEQRES  10 B 1174  LEU HIS GLN GLN CYS CYS GLU LYS TRP THR LEU VAL ASN          
SEQRES  11 B 1174  ASP GLU THR GLN ALA LYS MET ALA ARG MET ALA ALA ALA          
SEQRES  12 B 1174  ALA ALA TRP GLY LEU GLY GLN TRP ASP SER MET GLU GLU          
SEQRES  13 B 1174  TYR THR CYS MET ILE PRO ARG ASP THR HIS ASP GLY ALA          
SEQRES  14 B 1174  PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN ASP LEU PHE          
SEQRES  15 B 1174  SER LEU ALA GLN GLN CYS ILE ASP LYS ALA ARG ASP LEU          
SEQRES  16 B 1174  LEU ASP ALA GLU LEU THR ALA MET ALA GLY GLU SER TYR          
SEQRES  17 B 1174  SER ARG ALA TYR GLY ALA MET VAL SER CYS HIS MET LEU          
SEQRES  18 B 1174  SER GLU LEU GLU GLU VAL ILE GLN TYR LYS LEU VAL PRO          
SEQRES  19 B 1174  GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP TRP GLU ARG          
SEQRES  20 B 1174  LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP TRP GLN LYS          
SEQRES  21 B 1174  ILE LEU MET VAL ARG SER LEU VAL VAL SER PRO HIS GLU          
SEQRES  22 B 1174  ASP MET ARG THR TRP LEU LYS TYR ALA SER LEU CYS GLY          
SEQRES  23 B 1174  LYS SER GLY ARG LEU ALA LEU ALA HIS LYS THR LEU VAL          
SEQRES  24 B 1174  LEU LEU LEU GLY VAL ASP PRO SER ARG GLN LEU ASP HIS          
SEQRES  25 B 1174  PRO LEU PRO THR VAL HIS PRO GLN VAL THR TYR ALA TYR          
SEQRES  26 B 1174  MET LYS ASN MET TRP LYS SER ALA ARG LYS ILE ASP ALA          
SEQRES  27 B 1174  PHE GLN HIS MET GLN HIS PHE VAL GLN THR MET GLN GLN          
SEQRES  28 B 1174  GLN ALA GLN HIS ALA ILE ALA THR GLU ASP GLN GLN HIS          
SEQRES  29 B 1174  LYS GLN GLU LEU HIS LYS LEU MET ALA ARG CYS PHE LEU          
SEQRES  30 B 1174  LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN GLY ILE ASN          
SEQRES  31 B 1174  GLU SER THR ILE PRO LYS VAL LEU GLN TYR TYR SER ALA          
SEQRES  32 B 1174  ALA THR GLU HIS ASP ARG SER TRP TYR LYS ALA TRP HIS          
SEQRES  33 B 1174  ALA TRP ALA VAL MET ASN PHE GLU ALA VAL LEU HIS TYR          
SEQRES  34 B 1174  LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS LYS LYS LEU          
SEQRES  35 B 1174  ARG HIS ALA SER GLY ALA ASN ILE THR ASN ALA THR THR          
SEQRES  36 B 1174  ALA ALA THR THR ALA ALA THR ALA THR THR THR ALA SER          
SEQRES  37 B 1174  THR GLU GLY SER ASN SER GLU SER GLU ALA GLU SER THR          
SEQRES  38 B 1174  GLU ASN SER PRO THR PRO SER PRO LEU GLN LYS LYS VAL          
SEQRES  39 B 1174  THR GLU ASP LEU SER LYS THR LEU LEU MET TYR THR VAL          
SEQRES  40 B 1174  PRO ALA VAL GLN GLY PHE PHE ARG SER ILE SER LEU SER          
SEQRES  41 B 1174  ARG GLY ASN ASN LEU GLN ASP THR LEU ARG VAL LEU THR          
SEQRES  42 B 1174  LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP VAL ASN GLU          
SEQRES  43 B 1174  ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN ILE ASP THR          
SEQRES  44 B 1174  TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA ARG ILE ASP          
SEQRES  45 B 1174  THR PRO ARG PRO LEU VAL GLY ARG LEU ILE HIS GLN LEU          
SEQRES  46 B 1174  LEU THR ASP ILE GLY ARG TYR HIS PRO GLN ALA LEU ILE          
SEQRES  47 B 1174  TYR PRO LEU THR VAL ALA SER LYS SER THR THR THR ALA          
SEQRES  48 B 1174  ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS ASN MET CYS          
SEQRES  49 B 1174  GLU HIS SER ASN THR LEU VAL GLN GLN ALA MET MET VAL          
SEQRES  50 B 1174  SER GLU GLU LEU ILE ARG VAL ALA ILE LEU TRP HIS GLU          
SEQRES  51 B 1174  MET TRP HIS GLU GLY LEU GLU GLU ALA SER ARG LEU TYR          
SEQRES  52 B 1174  PHE GLY GLU ARG ASN VAL LYS GLY MET PHE GLU VAL LEU          
SEQRES  53 B 1174  GLU PRO LEU HIS ALA MET MET GLU ARG GLY PRO GLN THR          
SEQRES  54 B 1174  LEU LYS GLU THR SER PHE ASN GLN ALA TYR GLY ARG ASP          
SEQRES  55 B 1174  LEU MET GLU ALA GLN GLU TRP CYS ARG LYS TYR MET LYS          
SEQRES  56 B 1174  SER GLY ASN VAL LYS ASP LEU THR GLN ALA TRP ASP LEU          
SEQRES  57 B 1174  TYR TYR HIS VAL PHE ARG ARG ILE SER LYS GLN LEU PRO          
SEQRES  58 B 1174  GLN LEU THR SER LEU GLU LEU GLN TYR VAL SER PRO LYS          
SEQRES  59 B 1174  LEU LEU MET CYS ARG ASP LEU GLU LEU ALA VAL PRO GLY          
SEQRES  60 B 1174  THR TYR ASP PRO ASN GLN PRO ILE ILE ARG ILE GLN SER          
SEQRES  61 B 1174  ILE ALA PRO SER LEU GLN VAL ILE THR SER LYS GLN ARG          
SEQRES  62 B 1174  PRO ARG LYS LEU THR LEU MET GLY SER ASN GLY HIS GLU          
SEQRES  63 B 1174  PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP LEU ARG GLN          
SEQRES  64 B 1174  ASP GLU ARG VAL MET GLN LEU PHE GLY LEU VAL ASN THR          
SEQRES  65 B 1174  LEU LEU ALA ASN ASP PRO THR SER LEU ARG LYS ASN LEU          
SEQRES  66 B 1174  SER ILE GLN ARG TYR ALA VAL ILE PRO LEU SER THR ASN          
SEQRES  67 B 1174  SER GLY LEU ILE GLY TRP VAL PRO HIS CYS ASP THR LEU          
SEQRES  68 B 1174  HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS LYS LYS ILE          
SEQRES  69 B 1174  LEU LEU ASN ILE GLU HIS ARG ILE MET LEU ARG MET ALA          
SEQRES  70 B 1174  PRO ASP TYR ASP HIS LEU THR LEU MET GLN LYS VAL GLU          
SEQRES  71 B 1174  VAL PHE GLU HIS ALA VAL ASN ASN THR ALA GLY ASP ASP          
SEQRES  72 B 1174  LEU ALA LYS LEU LEU TRP LEU LYS SER PRO SER SER GLU          
SEQRES  73 B 1174  VAL TRP PHE ASP ARG ARG THR ASN TYR THR ARG SER LEU          
SEQRES  74 B 1174  ALA VAL MET SER MET VAL GLY TYR ILE LEU GLY LEU GLY          
SEQRES  75 B 1174  ASP ARG HIS PRO SER ASN LEU MET LEU ASP ARG LEU SER          
SEQRES  76 B 1174  GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP CYS PHE GLU          
SEQRES  77 B 1174  VAL ALA MET THR ARG GLU LYS PHE PRO GLU LYS ILE PRO          
SEQRES  78 B 1174  PHE ARG LEU THR ARG MET LEU THR ASN ALA MET GLU VAL          
SEQRES  79 B 1174  THR GLY LEU ASP GLY ASN TYR ARG ILE THR CYS HIS THR          
SEQRES  80 B 1174  VAL MET GLU VAL LEU ARG GLU HIS LYS ASP SER VAL MET          
SEQRES  81 B 1174  ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO LEU LEU ASN          
SEQRES  82 B 1174  TRP ARG LEU MET ASP THR ASN THR LYS GLY ASN LYS ARG          
SEQRES  83 B 1174  SER ARG THR ARG THR ASP SER TYR SER ALA GLY GLN SER          
SEQRES  84 B 1174  VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY GLU PRO ALA          
SEQRES  85 B 1174  HIS LYS LYS THR GLY THR THR VAL PRO GLU SER ILE HIS          
SEQRES  86 B 1174  SER PHE ILE GLY ASP GLY LEU VAL LYS PRO GLU ALA LEU          
SEQRES  87 B 1174  ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG VAL ARG ASP          
SEQRES  88 B 1174  LYS LEU THR GLY ARG ASP PHE SER HIS ASP ASP THR LEU          
SEQRES  89 B 1174  ASP VAL PRO THR GLN VAL GLU LEU LEU ILE LYS GLN ALA          
SEQRES  90 B 1174  THR SER HIS GLU ASN LEU CYS GLN CYS TYR ILE GLY TRP          
SEQRES  91 B 1174  CYS PRO PHE TRP                                              
SEQRES   1 D  326  MET ASN THR SER PRO GLY THR VAL GLY SER ASP PRO VAL          
SEQRES   2 D  326  ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL ARG PHE          
SEQRES   3 D  326  TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR VAL GLN          
SEQRES   4 D  326  HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL THR PRO          
SEQRES   5 D  326  ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN HIS ILE          
SEQRES   6 D  326  ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN PRO ILE          
SEQRES   7 D  326  ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA SER VAL          
SEQRES   8 D  326  GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR GLY GLY          
SEQRES   9 D  326  GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG SER ARG          
SEQRES  10 D  326  ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN ALA PRO          
SEQRES  11 D  326  ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA GLU LEU          
SEQRES  12 D  326  ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE TRP ASP          
SEQRES  13 D  326  LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO GLU PRO          
SEQRES  14 D  326  GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO ASP ALA          
SEQRES  15 D  326  SER TYR MET ALA ALA VAL ASN SER THR GLY ASN CYS TYR          
SEQRES  16 D  326  VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU VAL THR          
SEQRES  17 D  326  GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS THR ARG          
SEQRES  18 D  326  TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER THR LEU          
SEQRES  19 D  326  LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS ILE TRP          
SEQRES  20 D  326  ARG THR SER ASN PHE SER LEU MET THR GLU LEU SER ILE          
SEQRES  21 D  326  LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY TRP MET          
SEQRES  22 D  326  TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR ILE VAL          
SEQRES  23 D  326  THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP CYS VAL          
SEQRES  24 D  326  GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY HIS GLN          
SEQRES  25 D  326  LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER VAL LEU          
SEQRES  26 D  326  GLY                                                          
SEQRES   1 A 1174  ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU ARG ALA ALA          
SEQRES   2 A 1174  LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS TYR LYS GLU          
SEQRES   3 A 1174  LEU GLU PHE GLN LYS GLY PRO THR PRO ALA ILE LEU GLU          
SEQRES   4 A 1174  SER LEU ILE SER ILE ASN ASN LYS LEU GLN GLN PRO GLU          
SEQRES   5 A 1174  ALA ALA ALA GLY VAL LEU GLU TYR ALA MET LYS HIS PHE          
SEQRES   6 A 1174  GLY GLU LEU GLU ILE GLN ALA THR TRP TYR GLU LYS LEU          
SEQRES   7 A 1174  HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR ASP LYS LYS          
SEQRES   8 A 1174  MET ASP THR ASN LYS ASP ASP PRO GLU LEU MET LEU GLY          
SEQRES   9 A 1174  ARG MET ARG CYS LEU GLU ALA LEU GLY GLU TRP GLY GLN          
SEQRES  10 A 1174  LEU HIS GLN GLN CYS CYS GLU LYS TRP THR LEU VAL ASN          
SEQRES  11 A 1174  ASP GLU THR GLN ALA LYS MET ALA ARG MET ALA ALA ALA          
SEQRES  12 A 1174  ALA ALA TRP GLY LEU GLY GLN TRP ASP SER MET GLU GLU          
SEQRES  13 A 1174  TYR THR CYS MET ILE PRO ARG ASP THR HIS ASP GLY ALA          
SEQRES  14 A 1174  PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN ASP LEU PHE          
SEQRES  15 A 1174  SER LEU ALA GLN GLN CYS ILE ASP LYS ALA ARG ASP LEU          
SEQRES  16 A 1174  LEU ASP ALA GLU LEU THR ALA MET ALA GLY GLU SER TYR          
SEQRES  17 A 1174  SER ARG ALA TYR GLY ALA MET VAL SER CYS HIS MET LEU          
SEQRES  18 A 1174  SER GLU LEU GLU GLU VAL ILE GLN TYR LYS LEU VAL PRO          
SEQRES  19 A 1174  GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP TRP GLU ARG          
SEQRES  20 A 1174  LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP TRP GLN LYS          
SEQRES  21 A 1174  ILE LEU MET VAL ARG SER LEU VAL VAL SER PRO HIS GLU          
SEQRES  22 A 1174  ASP MET ARG THR TRP LEU LYS TYR ALA SER LEU CYS GLY          
SEQRES  23 A 1174  LYS SER GLY ARG LEU ALA LEU ALA HIS LYS THR LEU VAL          
SEQRES  24 A 1174  LEU LEU LEU GLY VAL ASP PRO SER ARG GLN LEU ASP HIS          
SEQRES  25 A 1174  PRO LEU PRO THR VAL HIS PRO GLN VAL THR TYR ALA TYR          
SEQRES  26 A 1174  MET LYS ASN MET TRP LYS SER ALA ARG LYS ILE ASP ALA          
SEQRES  27 A 1174  PHE GLN HIS MET GLN HIS PHE VAL GLN THR MET GLN GLN          
SEQRES  28 A 1174  GLN ALA GLN HIS ALA ILE ALA THR GLU ASP GLN GLN HIS          
SEQRES  29 A 1174  LYS GLN GLU LEU HIS LYS LEU MET ALA ARG CYS PHE LEU          
SEQRES  30 A 1174  LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN GLY ILE ASN          
SEQRES  31 A 1174  GLU SER THR ILE PRO LYS VAL LEU GLN TYR TYR SER ALA          
SEQRES  32 A 1174  ALA THR GLU HIS ASP ARG SER TRP TYR LYS ALA TRP HIS          
SEQRES  33 A 1174  ALA TRP ALA VAL MET ASN PHE GLU ALA VAL LEU HIS TYR          
SEQRES  34 A 1174  LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS LYS LYS LEU          
SEQRES  35 A 1174  ARG HIS ALA SER GLY ALA ASN ILE THR ASN ALA THR THR          
SEQRES  36 A 1174  ALA ALA THR THR ALA ALA THR ALA THR THR THR ALA SER          
SEQRES  37 A 1174  THR GLU GLY SER ASN SER GLU SER GLU ALA GLU SER THR          
SEQRES  38 A 1174  GLU ASN SER PRO THR PRO SER PRO LEU GLN LYS LYS VAL          
SEQRES  39 A 1174  THR GLU ASP LEU SER LYS THR LEU LEU MET TYR THR VAL          
SEQRES  40 A 1174  PRO ALA VAL GLN GLY PHE PHE ARG SER ILE SER LEU SER          
SEQRES  41 A 1174  ARG GLY ASN ASN LEU GLN ASP THR LEU ARG VAL LEU THR          
SEQRES  42 A 1174  LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP VAL ASN GLU          
SEQRES  43 A 1174  ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN ILE ASP THR          
SEQRES  44 A 1174  TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA ARG ILE ASP          
SEQRES  45 A 1174  THR PRO ARG PRO LEU VAL GLY ARG LEU ILE HIS GLN LEU          
SEQRES  46 A 1174  LEU THR ASP ILE GLY ARG TYR HIS PRO GLN ALA LEU ILE          
SEQRES  47 A 1174  TYR PRO LEU THR VAL ALA SER LYS SER THR THR THR ALA          
SEQRES  48 A 1174  ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS ASN MET CYS          
SEQRES  49 A 1174  GLU HIS SER ASN THR LEU VAL GLN GLN ALA MET MET VAL          
SEQRES  50 A 1174  SER GLU GLU LEU ILE ARG VAL ALA ILE LEU TRP HIS GLU          
SEQRES  51 A 1174  MET TRP HIS GLU GLY LEU GLU GLU ALA SER ARG LEU TYR          
SEQRES  52 A 1174  PHE GLY GLU ARG ASN VAL LYS GLY MET PHE GLU VAL LEU          
SEQRES  53 A 1174  GLU PRO LEU HIS ALA MET MET GLU ARG GLY PRO GLN THR          
SEQRES  54 A 1174  LEU LYS GLU THR SER PHE ASN GLN ALA TYR GLY ARG ASP          
SEQRES  55 A 1174  LEU MET GLU ALA GLN GLU TRP CYS ARG LYS TYR MET LYS          
SEQRES  56 A 1174  SER GLY ASN VAL LYS ASP LEU THR GLN ALA TRP ASP LEU          
SEQRES  57 A 1174  TYR TYR HIS VAL PHE ARG ARG ILE SER LYS GLN LEU PRO          
SEQRES  58 A 1174  GLN LEU THR SER LEU GLU LEU GLN TYR VAL SER PRO LYS          
SEQRES  59 A 1174  LEU LEU MET CYS ARG ASP LEU GLU LEU ALA VAL PRO GLY          
SEQRES  60 A 1174  THR TYR ASP PRO ASN GLN PRO ILE ILE ARG ILE GLN SER          
SEQRES  61 A 1174  ILE ALA PRO SER LEU GLN VAL ILE THR SER LYS GLN ARG          
SEQRES  62 A 1174  PRO ARG LYS LEU THR LEU MET GLY SER ASN GLY HIS GLU          
SEQRES  63 A 1174  PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP LEU ARG GLN          
SEQRES  64 A 1174  ASP GLU ARG VAL MET GLN LEU PHE GLY LEU VAL ASN THR          
SEQRES  65 A 1174  LEU LEU ALA ASN ASP PRO THR SER LEU ARG LYS ASN LEU          
SEQRES  66 A 1174  SER ILE GLN ARG TYR ALA VAL ILE PRO LEU SER THR ASN          
SEQRES  67 A 1174  SER GLY LEU ILE GLY TRP VAL PRO HIS CYS ASP THR LEU          
SEQRES  68 A 1174  HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS LYS LYS ILE          
SEQRES  69 A 1174  LEU LEU ASN ILE GLU HIS ARG ILE MET LEU ARG MET ALA          
SEQRES  70 A 1174  PRO ASP TYR ASP HIS LEU THR LEU MET GLN LYS VAL GLU          
SEQRES  71 A 1174  VAL PHE GLU HIS ALA VAL ASN ASN THR ALA GLY ASP ASP          
SEQRES  72 A 1174  LEU ALA LYS LEU LEU TRP LEU LYS SER PRO SER SER GLU          
SEQRES  73 A 1174  VAL TRP PHE ASP ARG ARG THR ASN TYR THR ARG SER LEU          
SEQRES  74 A 1174  ALA VAL MET SER MET VAL GLY TYR ILE LEU GLY LEU GLY          
SEQRES  75 A 1174  ASP ARG HIS PRO SER ASN LEU MET LEU ASP ARG LEU SER          
SEQRES  76 A 1174  GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP CYS PHE GLU          
SEQRES  77 A 1174  VAL ALA MET THR ARG GLU LYS PHE PRO GLU LYS ILE PRO          
SEQRES  78 A 1174  PHE ARG LEU THR ARG MET LEU THR ASN ALA MET GLU VAL          
SEQRES  79 A 1174  THR GLY LEU ASP GLY ASN TYR ARG ILE THR CYS HIS THR          
SEQRES  80 A 1174  VAL MET GLU VAL LEU ARG GLU HIS LYS ASP SER VAL MET          
SEQRES  81 A 1174  ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO LEU LEU ASN          
SEQRES  82 A 1174  TRP ARG LEU MET ASP THR ASN THR LYS GLY ASN LYS ARG          
SEQRES  83 A 1174  SER ARG THR ARG THR ASP SER TYR SER ALA GLY GLN SER          
SEQRES  84 A 1174  VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY GLU PRO ALA          
SEQRES  85 A 1174  HIS LYS LYS THR GLY THR THR VAL PRO GLU SER ILE HIS          
SEQRES  86 A 1174  SER PHE ILE GLY ASP GLY LEU VAL LYS PRO GLU ALA LEU          
SEQRES  87 A 1174  ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG VAL ARG ASP          
SEQRES  88 A 1174  LYS LEU THR GLY ARG ASP PHE SER HIS ASP ASP THR LEU          
SEQRES  89 A 1174  ASP VAL PRO THR GLN VAL GLU LEU LEU ILE LYS GLN ALA          
SEQRES  90 A 1174  THR SER HIS GLU ASN LEU CYS GLN CYS TYR ILE GLY TRP          
SEQRES  91 A 1174  CYS PRO PHE TRP                                              
SEQRES   1 C  326  MET ASN THR SER PRO GLY THR VAL GLY SER ASP PRO VAL          
SEQRES   2 C  326  ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL ARG PHE          
SEQRES   3 C  326  TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR VAL GLN          
SEQRES   4 C  326  HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL THR PRO          
SEQRES   5 C  326  ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN HIS ILE          
SEQRES   6 C  326  ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN PRO ILE          
SEQRES   7 C  326  ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA SER VAL          
SEQRES   8 C  326  GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR GLY GLY          
SEQRES   9 C  326  GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG SER ARG          
SEQRES  10 C  326  ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN ALA PRO          
SEQRES  11 C  326  ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA GLU LEU          
SEQRES  12 C  326  ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE TRP ASP          
SEQRES  13 C  326  LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO GLU PRO          
SEQRES  14 C  326  GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO ASP ALA          
SEQRES  15 C  326  SER TYR MET ALA ALA VAL ASN SER THR GLY ASN CYS TYR          
SEQRES  16 C  326  VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU VAL THR          
SEQRES  17 C  326  GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS THR ARG          
SEQRES  18 C  326  TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER THR LEU          
SEQRES  19 C  326  LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS ILE TRP          
SEQRES  20 C  326  ARG THR SER ASN PHE SER LEU MET THR GLU LEU SER ILE          
SEQRES  21 C  326  LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY TRP MET          
SEQRES  22 C  326  TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR ILE VAL          
SEQRES  23 C  326  THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP CYS VAL          
SEQRES  24 C  326  GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY HIS GLN          
SEQRES  25 C  326  LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER VAL LEU          
SEQRES  26 C  326  GLY                                                          
HET    X6K  B2601      26                                                       
HET    X6K  A2601      26                                                       
HETNAM     X6K 3-(4-MORPHOLIN-4-YLPYRIDO[3',2':4,5]FURO[3,2-                    
HETNAM   2 X6K  D]PYRIMIDIN-2-YL)PHENOL                                         
HETSYN     X6K PI-103                                                           
FORMUL   5  X6K    2(C19 H16 N4 O3)                                             
HELIX    1   1 GLU B 1385  GLY B 1407  1                                  23    
HELIX    2   2 THR B 1409  LEU B 1423  1                                  15    
HELIX    3   3 GLN B 1425  PHE B 1440  1                                  16    
HELIX    4   4 ILE B 1445  LEU B 1453  1                                   9    
HELIX    5   5 GLU B 1455  ASN B 1470  1                                  16    
HELIX    6   6 ASP B 1473  GLY B 1488  1                                  16    
HELIX    7   7 GLU B 1489  GLU B 1499  1                                  11    
HELIX    8   8 ASP B 1506  LEU B 1523  1                                  18    
HELIX    9   9 GLN B 1525  CYS B 1534  1                                  10    
HELIX   10  10 THR B 1540  ASP B 1555  1                                  16    
HELIX   11  11 LEU B 1556  ALA B 1573  1                                  18    
HELIX   12  12 GLY B 1588  TYR B 1605  1                                  18    
HELIX   13  13 GLU B 1613  GLY B 1625  1                                  13    
HELIX   14  14 ILE B 1629  LEU B 1642  1                                  14    
HELIX   15  15 SER B 1645  MET B 1650  1                                   6    
HELIX   16  16 MET B 1650  GLY B 1664  1                                  15    
HELIX   17  17 ARG B 1665  GLY B 1678  1                                  14    
HELIX   18  18 HIS B 1693  SER B 1707  1                                  15    
HELIX   19  19 ARG B 1709  HIS B 1730  1                                  22    
HELIX   20  20 GLN B 1737  GLY B 1763  1                                  27    
HELIX   21  21 SER B 1767  ARG B 1784  1                                  18    
HELIX   22  22 TRP B 1786  LYS B 1814  1                                  29    
HELIX   23  23 LYS B 1868  SER B 1893  1                                  26    
HELIX   24  24 ASN B 1899  TYR B 1913  1                                  15    
HELIX   25  25 TRP B 1916  ILE B 1930  1                                  15    
HELIX   26  26 ILE B 1932  GLN B 1937  5                                   6    
HELIX   27  27 VAL B 1938  ALA B 1944  1                                   7    
HELIX   28  28 ARG B 1950  TYR B 1967  1                                  18    
HELIX   29  29 LEU B 1972  LYS B 1981  1                                  10    
HELIX   30  30 THR B 1984  ILE B 2021  1                                  38    
HELIX   31  31 LEU B 2022  GLY B 2040  1                                  19    
HELIX   32  32 ASN B 2043  ARG B 2060  1                                  18    
HELIX   33  33 THR B 2064  GLY B 2092  1                                  29    
HELIX   34  34 LYS B 2095  LEU B 2115  1                                  21    
HELIX   35  35 PRO B 2116  LEU B 2118  5                                   3    
HELIX   36  36 LEU B 2123  SER B 2127  1                                   5    
HELIX   37  37 SER B 2127  CYS B 2133  1                                   7    
HELIX   38  38 LEU B 2192  ASP B 2212  1                                  21    
HELIX   39  39 ASP B 2212  LYS B 2218  1                                   7    
HELIX   40  40 LEU B 2246  LYS B 2257  1                                  12    
HELIX   41  41 ASN B 2262  ALA B 2272  1                                  11    
HELIX   42  42 ASP B 2274  LEU B 2278  5                                   5    
HELIX   43  43 THR B 2279  ASN B 2292  1                                  14    
HELIX   44  44 ASP B 2298  SER B 2307  1                                  10    
HELIX   45  45 SER B 2310  LEU B 2334  1                                  25    
HELIX   46  46 GLU B 2363  ARG B 2368  1                                   6    
HELIX   47  47 THR B 2380  MET B 2387  1                                   8    
HELIX   48  48 GLY B 2394  HIS B 2410  1                                  17    
HELIX   49  49 HIS B 2410  TYR B 2423  1                                  14    
HELIX   50  50 LEU B 2427  THR B 2436  5                                  10    
HELIX   51  51 LEU B 2493  THR B 2509  1                                  17    
HELIX   52  52 ASP B 2520  SER B 2534  1                                  15    
HELIX   53  53 SER B 2534  CYS B 2539  1                                   6    
HELIX   54  54 TYR B 2542  CYS B 2546  5                                   5    
HELIX   55  55 ARG A 1386  GLY A 1407  1                                  22    
HELIX   56  56 THR A 1409  LEU A 1423  1                                  15    
HELIX   57  57 GLN A 1425  PHE A 1440  1                                  16    
HELIX   58  58 ILE A 1445  LEU A 1453  1                                   9    
HELIX   59  59 GLU A 1455  ASN A 1470  1                                  16    
HELIX   60  60 ASP A 1473  GLY A 1488  1                                  16    
HELIX   61  61 GLU A 1489  GLU A 1499  1                                  11    
HELIX   62  62 ASP A 1506  LEU A 1523  1                                  18    
HELIX   63  63 GLN A 1525  CYS A 1534  1                                  10    
HELIX   64  64 THR A 1540  GLN A 1554  1                                  15    
HELIX   65  65 LEU A 1556  ALA A 1573  1                                  18    
HELIX   66  66 ALA A 1573  MET A 1578  1                                   6    
HELIX   67  67 GLY A 1588  TYR A 1605  1                                  18    
HELIX   68  68 GLU A 1613  GLY A 1625  1                                  13    
HELIX   69  69 ILE A 1629  LEU A 1642  1                                  14    
HELIX   70  70 SER A 1645  MET A 1650  1                                   6    
HELIX   71  71 MET A 1650  GLY A 1664  1                                  15    
HELIX   72  72 ARG A 1665  GLY A 1678  1                                  14    
HELIX   73  73 HIS A 1693  SER A 1707  1                                  15    
HELIX   74  74 ARG A 1709  HIS A 1730  1                                  22    
HELIX   75  75 GLN A 1737  GLY A 1763  1                                  27    
HELIX   76  76 SER A 1767  ARG A 1784  1                                  18    
HELIX   77  77 TRP A 1786  LYS A 1814  1                                  29    
HELIX   78  78 LYS A 1868  SER A 1893  1                                  26    
HELIX   79  79 ASN A 1899  TYR A 1913  1                                  15    
HELIX   80  80 TRP A 1916  ILE A 1930  1                                  15    
HELIX   81  81 ILE A 1932  GLN A 1937  5                                   6    
HELIX   82  82 VAL A 1938  ALA A 1944  1                                   7    
HELIX   83  83 ARG A 1950  TYR A 1967  1                                  18    
HELIX   84  84 LEU A 1972  LYS A 1981  1                                  10    
HELIX   85  85 THR A 1984  ILE A 2021  1                                  38    
HELIX   86  86 LEU A 2022  GLY A 2040  1                                  19    
HELIX   87  87 ASN A 2043  ARG A 2060  1                                  18    
HELIX   88  88 THR A 2064  GLY A 2092  1                                  29    
HELIX   89  89 LYS A 2095  LEU A 2115  1                                  21    
HELIX   90  90 PRO A 2116  LEU A 2118  5                                   3    
HELIX   91  91 LEU A 2123  SER A 2127  1                                   5    
HELIX   92  92 SER A 2127  CYS A 2133  1                                   7    
HELIX   93  93 LEU A 2192  ASP A 2212  1                                  21    
HELIX   94  94 ASP A 2212  LYS A 2218  1                                   7    
HELIX   95  95 LEU A 2246  LYS A 2257  1                                  12    
HELIX   96  96 ASN A 2262  ALA A 2272  1                                  11    
HELIX   97  97 ASP A 2274  LEU A 2278  5                                   5    
HELIX   98  98 THR A 2279  ASN A 2292  1                                  14    
HELIX   99  99 ASP A 2297  SER A 2307  1                                  11    
HELIX  100 100 SER A 2310  GLY A 2335  1                                  26    
HELIX  101 101 GLU A 2363  ARG A 2368  1                                   6    
HELIX  102 102 THR A 2380  MET A 2387  1                                   8    
HELIX  103 103 GLY A 2394  HIS A 2410  1                                  17    
HELIX  104 104 HIS A 2410  TYR A 2423  1                                  14    
HELIX  105 105 LEU A 2427  THR A 2436  5                                  10    
HELIX  106 106 LEU A 2493  THR A 2509  1                                  17    
HELIX  107 107 ASP A 2520  SER A 2534  1                                  15    
HELIX  108 108 SER A 2534  CYS A 2539  1                                   6    
HELIX  109 109 TYR A 2542  CYS A 2546  5                                   5    
SHEET    1   A 3 LEU B2121  GLU B2122  0                                        
SHEET    2   A 3 SER B2159  VAL B2162 -1  O  LEU B2160   N  LEU B2121           
SHEET    3   A 3 ARG B2170  LYS B2171 -1  O  LYS B2171   N  GLN B2161           
SHEET    1   B 3 ILE B2153  ILE B2156  0                                        
SHEET    2   B 3 THR B2173  GLY B2176 -1  O  MET B2175   N  SER B2155           
SHEET    3   B 3 GLU B2181  VAL B2183 -1  O  PHE B2182   N  LEU B2174           
SHEET    1   C 2 VAL B2227  PRO B2229  0                                        
SHEET    2   C 2 GLY B2235  ILE B2237 -1  O  LEU B2236   N  ILE B2228           
SHEET    1   D 3 CYS B2243  THR B2245  0                                        
SHEET    2   D 3 LEU B2344  ASP B2347 -1  O  LEU B2346   N  ASP B2244           
SHEET    3   D 3 ILE B2353  HIS B2355 -1  O  LEU B2354   N  MET B2345           
SHEET    1   E 4 CYS D  34  GLN D  39  0                                        
SHEET    2   E 4 THR D  23  TRP D  27 -1  N  PHE D  26   O  ARG D  36           
SHEET    3   E 4 VAL D  13  GLY D  19 -1  N  THR D  17   O  ARG D  25           
SHEET    4   E 4 VAL D 315  ASP D 322 -1  O  ALA D 319   N  ALA D  16           
SHEET    1   F 3 ALA D  47  VAL D  50  0                                        
SHEET    2   F 3 ILE D  57  ALA D  60 -1  O  ALA D  58   N  GLU D  49           
SHEET    3   F 3 ILE D  65  TYR D  68 -1  O  ARG D  66   N  ALA D  59           
SHEET    1   G 4 ILE D  88  HIS D  94  0                                        
SHEET    2   G 4 TRP D  99  GLY D 104 -1  O  TYR D 101   N  GLY D  92           
SHEET    3   G 4 THR D 108  ASP D 113 -1  O  TRP D 112   N  MET D 100           
SHEET    4   G 4 ARG D 123  GLN D 126 -1  O  PHE D 125   N  ALA D 109           
SHEET    1   H 4 ILE D 131  LEU D 136  0                                        
SHEET    2   H 4 GLU D 142  ASP D 147 -1  O  ILE D 144   N  CYS D 135           
SHEET    3   H 4 ILE D 152  ASP D 156 -1  O  HIS D 153   N  VAL D 145           
SHEET    4   H 4 ASN D 162  LEU D 165 -1  O  GLU D 163   N  ILE D 154           
SHEET    1   I 4 ILE D 173  ILE D 178  0                                        
SHEET    2   I 4 TYR D 184  ASN D 189 -1  O  ALA D 186   N  HIS D 177           
SHEET    3   I 4 CYS D 194  LEU D 199 -1  O  TYR D 195   N  ALA D 187           
SHEET    4   I 4 LEU D 210  ILE D 216 -1  O  LYS D 213   N  VAL D 196           
SHEET    1   J 4 ALA D 223  PHE D 228  0                                        
SHEET    2   J 4 LEU D 234  SER D 239 -1  O  ALA D 236   N  ARG D 227           
SHEET    3   J 4 THR D 243  ARG D 248 -1  O  TRP D 247   N  LEU D 235           
SHEET    4   J 4 LEU D 254  SER D 259 -1  O  MET D 255   N  ILE D 246           
SHEET    1   K 4 MET D 273  PHE D 278  0                                        
SHEET    2   K 4 TYR D 284  SER D 289 -1  O  ALA D 288   N  GLY D 275           
SHEET    3   K 4 LEU D 293  CYS D 298 -1  O  TRP D 297   N  ILE D 285           
SHEET    4   K 4 GLU D 303  GLY D 309 -1  O  ARG D 306   N  LEU D 296           
SHEET    1   L 3 LEU A2121  GLU A2122  0                                        
SHEET    2   L 3 SER A2159  VAL A2162 -1  O  LEU A2160   N  LEU A2121           
SHEET    3   L 3 ARG A2170  LYS A2171 -1  O  LYS A2171   N  GLN A2161           
SHEET    1   M 3 ILE A2153  ILE A2156  0                                        
SHEET    2   M 3 THR A2173  GLY A2176 -1  O  MET A2175   N  SER A2155           
SHEET    3   M 3 GLU A2181  VAL A2183 -1  O  PHE A2182   N  LEU A2174           
SHEET    1   N 2 VAL A2227  PRO A2229  0                                        
SHEET    2   N 2 GLY A2235  ILE A2237 -1  O  LEU A2236   N  ILE A2228           
SHEET    1   O 3 CYS A2243  THR A2245  0                                        
SHEET    2   O 3 LEU A2344  ASP A2347 -1  O  LEU A2346   N  ASP A2244           
SHEET    3   O 3 ILE A2353  HIS A2355 -1  O  LEU A2354   N  MET A2345           
SHEET    1   P 4 CYS C  34  GLN C  39  0                                        
SHEET    2   P 4 THR C  23  TRP C  27 -1  N  PHE C  26   O  ARG C  36           
SHEET    3   P 4 VAL C  13  GLY C  19 -1  N  THR C  17   O  ARG C  25           
SHEET    4   P 4 VAL C 315  ASP C 322 -1  O  ALA C 319   N  ALA C  16           
SHEET    1   Q 3 ALA C  47  VAL C  50  0                                        
SHEET    2   Q 3 ILE C  57  ALA C  60 -1  O  ALA C  58   N  GLU C  49           
SHEET    3   Q 3 ILE C  65  TYR C  68 -1  O  ARG C  66   N  ALA C  59           
SHEET    1   R 4 ILE C  88  HIS C  94  0                                        
SHEET    2   R 4 TRP C  99  GLY C 104 -1  O  TYR C 101   N  GLY C  92           
SHEET    3   R 4 THR C 108  ASP C 113 -1  O  TRP C 112   N  MET C 100           
SHEET    4   R 4 ARG C 123  GLN C 126 -1  O  PHE C 125   N  ALA C 109           
SHEET    1   S 4 ILE C 131  LEU C 136  0                                        
SHEET    2   S 4 GLU C 142  ASP C 147 -1  O  ILE C 144   N  CYS C 135           
SHEET    3   S 4 ILE C 152  ASP C 156 -1  O  HIS C 153   N  VAL C 145           
SHEET    4   S 4 ASN C 162  LEU C 165 -1  O  LEU C 165   N  ILE C 152           
SHEET    1   T 4 ILE C 173  ILE C 178  0                                        
SHEET    2   T 4 TYR C 184  ASN C 189 -1  O  ALA C 186   N  HIS C 177           
SHEET    3   T 4 CYS C 194  LEU C 199 -1  O  TYR C 195   N  ALA C 187           
SHEET    4   T 4 LEU C 210  ILE C 216 -1  O  LYS C 213   N  VAL C 196           
SHEET    1   U 4 ALA C 223  PHE C 228  0                                        
SHEET    2   U 4 LEU C 234  SER C 239 -1  O  ALA C 236   N  ARG C 227           
SHEET    3   U 4 THR C 243  ARG C 248 -1  O  TRP C 247   N  LEU C 235           
SHEET    4   U 4 LEU C 254  SER C 259 -1  O  MET C 255   N  ILE C 246           
SHEET    1   V 4 MET C 273  PHE C 278  0                                        
SHEET    2   V 4 TYR C 284  SER C 289 -1  O  ALA C 288   N  GLY C 275           
SHEET    3   V 4 LEU C 293  CYS C 298 -1  O  TRP C 297   N  ILE C 285           
SHEET    4   V 4 GLU C 303  GLY C 309 -1  O  ARG C 306   N  LEU C 296           
SITE     1 AC1 10 LEU B2185  GLU B2190  ASP B2195  TYR B2225                    
SITE     2 AC1 10 ILE B2237  GLY B2238  TRP B2239  VAL B2240                    
SITE     3 AC1 10 ILE B2356  ASP B2357                                          
SITE     1 AC2  9 LEU A2185  GLU A2190  ASP A2195  TYR A2225                    
SITE     2 AC2  9 GLY A2238  TRP A2239  VAL A2240  ILE A2356                    
SITE     3 AC2  9 ASP A2357                                                     
CRYST1  139.400  163.200  207.800  90.00  90.00  90.00 P 2 21 21     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007174  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006127  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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