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Entry: 5WBY
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HEADER    TRANSFERASE                             29-JUN-17   5WBY              
TITLE     CRYSTAL STRUCTURE OF MTOR(DELTAN)-MLST8-PRAS40(BETA-STRAND) COMPLEX   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR;                      
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: RESIDUES 1376-2549;                                        
COMPND   5 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED       
COMPND   6 PROTEIN 1,FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN,MAMMALIAN      
COMPND   7 TARGET OF RAPAMYCIN,MTOR,MECHANISTIC TARGET OF RAPAMYCIN,RAPAMYCIN   
COMPND   8 AND FKBP12 TARGET 1,RAPAMYCIN TARGET PROTEIN 1;                      
COMPND   9 EC: 2.7.11.1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: TARGET OF RAPAMYCIN COMPLEX SUBUNIT LST8;                  
COMPND  13 CHAIN: D, C;                                                         
COMPND  14 SYNONYM: TORC SUBUNIT LST8,G PROTEIN BETA SUBUNIT-LIKE,PROTEIN       
COMPND  15 GBETAL,MAMMALIAN LETHAL WITH SEC13 PROTEIN 8,MLST8;                  
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: PROLINE-RICH AKT1 SUBSTRATE 1;                             
COMPND  19 CHAIN: P, O;                                                         
COMPND  20 FRAGMENT: RESIDUES 114-207;                                          
COMPND  21 SYNONYM: 40 KDA PROLINE-RICH AKT SUBSTRATE;                          
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1;                        
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: MLST8, GBL, LST8;                                              
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: AKT1S1, PRAS40;                                                
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PET2                                      
KEYWDS    WD40, PRAS40 BETA, COMPLEX, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.PAVLETICH,H.YANG                                                  
REVDAT   2   10-JAN-18 5WBY    1       JRNL                                     
REVDAT   1   20-DEC-17 5WBY    0                                                
JRNL        AUTH   H.YANG,X.JIANG,B.LI,H.J.YANG,M.MILLER,A.YANG,A.DHAR,         
JRNL        AUTH 2 N.P.PAVLETICH                                                
JRNL        TITL   MECHANISMS OF MTORC1 ACTIVATION BY RHEB AND INHIBITION BY    
JRNL        TITL 2 PRAS40.                                                      
JRNL        REF    NATURE                        V. 552   368 2017              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29236692                                                     
JRNL        DOI    10.1038/NATURE25023                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 69072                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1707                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2082                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 34.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.4120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22243                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
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) : 98.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.89000                                             
REMARK   3    B22 (A**2) : -4.64000                                             
REMARK   3    B33 (A**2) : 5.54000                                              
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): 0.522         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.436         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.095        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22757 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 20893 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30849 ; 1.148 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 48454 ; 0.901 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2753 ; 6.290 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1090 ;37.153 ;23.963       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4008 ;16.330 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   157 ;11.396 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3386 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 25139 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4662 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 11045 ; 2.869 ; 2.326       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 11044 ; 2.869 ; 2.326       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13787 ; 4.892 ; 4.647       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 13788 ; 4.892 ; 4.648       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11712 ; 2.913 ; 2.413       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 11713 ; 2.913 ; 2.413       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 17063 ; 5.030 ; 4.772       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 25048 ; 7.811 ;51.858       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 25049 ; 7.811 ;51.863       
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 : 18                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1385       B    1442      2                      
REMARK   3           1     A   1385       A    1442      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    556 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    342 ;  3.13 ; 99.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    556 ;  4.00 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1443       B    1504      2                      
REMARK   3           1     A   1443       A    1504      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    627 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      2    A (A**2):    368 ; 11.12 ; 99.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    627 ; 10.98 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1505       B    1537      2                      
REMARK   3           1     A   1505       A    1537      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    280 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):    195 ; 12.02 ; 99.00           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    280 ; 11.04 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1538       B    1580      2                      
REMARK   3           1     A   1538       A    1580      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    387 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      4    A (A**2):    256 ;  9.90 ; 99.00           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    387 ;  8.32 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1581       B    1605      2                      
REMARK   3           1     A   1581       A    1605      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    A    (A):    226 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      5    A (A**2):    149 ;  8.32 ; 99.00           
REMARK   3   MEDIUM THERMAL     5    A (A**2):    226 ; 10.03 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1612       B    1678      2                      
REMARK   3           1     A   1612       A    1678      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    A    (A):    727 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      6    A (A**2):    397 ;  6.71 ; 99.00           
REMARK   3   MEDIUM THERMAL     6    A (A**2):    727 ;  7.89 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1679       B    1734      2                      
REMARK   3           1     A   1679       A    1734      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  7    A    (A):    545 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      7    A (A**2):    332 ;  3.43 ; 99.00           
REMARK   3   MEDIUM THERMAL     7    A (A**2):    545 ;  3.86 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1735       B    1814      2                      
REMARK   3           1     A   1735       A    1814      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  8    A    (A):    816 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      8    A (A**2):    477 ;  3.50 ; 99.00           
REMARK   3   MEDIUM THERMAL     8    A (A**2):    816 ;  4.09 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1867       B    1930      2                      
REMARK   3           1     A   1867       A    1930      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  9    A    (A):    634 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      9    A (A**2):    378 ;  2.47 ; 99.00           
REMARK   3   MEDIUM THERMAL     9    A (A**2):    634 ;  2.94 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1931       B    2001      2                      
REMARK   3           1     A   1931       A    2001      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    A    (A):    419 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 10    A    (A):    710 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     10    A (A**2):    419 ;  2.72 ; 99.00           
REMARK   3   MEDIUM THERMAL    10    A (A**2):    710 ;  3.85 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2002       B    2021      2                      
REMARK   3           1     A   2002       A    2021      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    A    (A):    120 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 11    A    (A):    187 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     11    A (A**2):    120 ;  2.91 ; 99.00           
REMARK   3   MEDIUM THERMAL    11    A (A**2):    187 ;  3.19 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2022       B    2115      2                      
REMARK   3           1     A   2022       A    2115      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    A    (A):    556 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 12    A    (A):    980 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     12    A (A**2):    556 ; 12.55 ; 99.00           
REMARK   3   MEDIUM THERMAL    12    A (A**2):    980 ; 11.39 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2116       B    2190      2                      
REMARK   3           1     A   2116       A    2190      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    A    (A):    439 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 13    A    (A):    744 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     13    A (A**2):    439 ;  4.09 ; 99.00           
REMARK   3   MEDIUM THERMAL    13    A (A**2):    744 ;  3.77 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2191       B    2212      2                      
REMARK   3           1     A   2191       A    2212      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    A    (A):    131 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 14    A    (A):    216 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     14    A (A**2):    131 ;  2.90 ; 99.00           
REMARK   3   MEDIUM THERMAL    14    A (A**2):    216 ;  4.17 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2213       B    2241      2                      
REMARK   3           1     A   2213       A    2241      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    A    (A):    169 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 15    A    (A):    281 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     15    A (A**2):    169 ;  2.93 ; 99.00           
REMARK   3   MEDIUM THERMAL    15    A (A**2):    281 ;  3.27 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2242       B    2549      2                      
REMARK   3           1     A   2242       A    2549      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    A    (A):   1500 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 16    A    (A):   2552 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     16    A (A**2):   1500 ;  3.98 ; 99.00           
REMARK   3   MEDIUM THERMAL    16    A (A**2):   2552 ;  4.65 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 17                                 
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      8       D     324      2                      
REMARK   3           1     C      8       C     324      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  17    C    (A):   1866 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 17    C    (A):   2783 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     17    C (A**2):   1866 ;  4.40 ; 99.00           
REMARK   3   MEDIUM THERMAL    17    C (A**2):   2783 ;  4.81 ; 99.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 18                                 
REMARK   3     CHAIN NAMES                    : P O                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P    187       P     196      2                      
REMARK   3           1     O    187       O     196      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  18    O    (A):     58 ;  0.00 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 18    O    (A):    110 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL     18    O (A**2):     58 ;  7.56 ; 99.00           
REMARK   3   MEDIUM THERMAL    18    O (A**2):    110 ;  7.80 ; 99.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1385        B  1442                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2750  -6.0000 -31.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6832 T22:   0.7121                                     
REMARK   3      T33:   0.4330 T12:   0.0299                                     
REMARK   3      T13:  -0.0222 T23:  -0.1788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9188 L22:   4.4820                                     
REMARK   3      L33:   5.0370 L12:   2.2317                                     
REMARK   3      L13:  -1.8000 L23:  -1.3152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1887 S12:  -0.7979 S13:   0.2498                       
REMARK   3      S21:   0.4590 S22:  -0.3951 S23:  -0.0900                       
REMARK   3      S31:  -0.2985 S32:   0.4408 S33:   0.2064                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1443        B  1504                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1380   0.4230 -25.0460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3088 T22:   1.0591                                     
REMARK   3      T33:   0.8699 T12:   0.0227                                     
REMARK   3      T13:  -0.1201 T23:  -0.0923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6637 L22:   0.5978                                     
REMARK   3      L33:   0.8208 L12:   0.9826                                     
REMARK   3      L13:  -0.3092 L23:  -0.6460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1500 S12:  -0.1480 S13:   0.5546                       
REMARK   3      S21:   0.2836 S22:  -0.1816 S23:  -0.1564                       
REMARK   3      S31:  -0.4321 S32:   0.2847 S33:   0.3316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1505        B  1678                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9020 -18.6620 -12.3000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0741 T22:   1.4255                                     
REMARK   3      T33:   0.8524 T12:  -0.0303                                     
REMARK   3      T13:   0.0528 T23:  -0.2254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3164 L22:   1.7857                                     
REMARK   3      L33:   2.1282 L12:  -0.9105                                     
REMARK   3      L13:  -1.8714 L23:   0.6556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0339 S12:  -0.1944 S13:   0.2269                       
REMARK   3      S21:   0.7175 S22:  -0.1028 S23:   0.6135                       
REMARK   3      S31:  -0.1540 S32:  -0.5975 S33:   0.1367                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1679        B  2021                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0130 -45.3880 -50.5560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2486 T22:   0.2072                                     
REMARK   3      T33:   0.1309 T12:   0.0547                                     
REMARK   3      T13:   0.0236 T23:   0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5229 L22:   1.9713                                     
REMARK   3      L33:   0.7434 L12:   1.8383                                     
REMARK   3      L13:   1.0946 L23:   0.7023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0983 S12:   0.2456 S13:  -0.0131                       
REMARK   3      S21:  -0.0077 S22:   0.0446 S23:  -0.2479                       
REMARK   3      S31:   0.1492 S32:   0.2465 S33:  -0.1430                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  2022        B  2115                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.6470 -43.2790 -84.4990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1935 T22:   1.3203                                     
REMARK   3      T33:   1.1276 T12:  -0.0092                                     
REMARK   3      T13:   0.1280 T23:   0.2394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1517 L22:   0.3369                                     
REMARK   3      L33:   3.6225 L12:   0.0485                                     
REMARK   3      L13:   0.6212 L23:   0.3294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0811 S12:   0.3193 S13:   0.0233                       
REMARK   3      S21:  -0.5169 S22:   0.0145 S23:  -0.4006                       
REMARK   3      S31:  -0.7610 S32:   0.5148 S33:   0.0666                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  2116        B  2459                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4430 -27.7960 -53.9280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1543 T22:   0.2428                                     
REMARK   3      T33:   0.1669 T12:  -0.0378                                     
REMARK   3      T13:   0.0157 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8295 L22:   3.6122                                     
REMARK   3      L33:   0.2996 L12:   0.1078                                     
REMARK   3      L13:  -0.0177 L23:  -0.9939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0663 S12:  -0.0117 S13:  -0.1720                       
REMARK   3      S21:  -0.1037 S22:  -0.0346 S23:   0.2450                       
REMARK   3      S31:   0.0724 S32:  -0.0368 S33:  -0.0316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1385        A  1442                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.4660 -27.2360 -70.9540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8068 T22:   0.8006                                     
REMARK   3      T33:   0.6798 T12:  -0.0411                                     
REMARK   3      T13:   0.0417 T23:  -0.1196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8808 L22:   4.5910                                     
REMARK   3      L33:   4.6699 L12:  -2.9488                                     
REMARK   3      L13:   1.4278 L23:  -1.8354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0654 S12:   0.7852 S13:  -0.0216                       
REMARK   3      S21:  -0.5389 S22:  -0.2808 S23:  -0.0970                       
REMARK   3      S31:   0.2340 S32:   0.3768 S33:   0.2153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1443        A  1504                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.8340 -34.0550 -77.9580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3390 T22:   1.2715                                     
REMARK   3      T33:   1.0797 T12:   0.1664                                     
REMARK   3      T13:   0.1172 T23:  -0.0883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4815 L22:   1.6814                                     
REMARK   3      L33:   2.5736 L12:   1.2762                                     
REMARK   3      L13:  -0.5833 L23:  -1.8710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0943 S12:   0.4745 S13:  -0.4970                       
REMARK   3      S21:  -0.3700 S22:  -0.0991 S23:  -0.2554                       
REMARK   3      S31:   0.6366 S32:   0.5356 S33:   0.1934                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1505        A  1678                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.3930 -15.6760 -90.1490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3969 T22:   1.6208                                     
REMARK   3      T33:   1.4017 T12:  -0.1110                                     
REMARK   3      T13:  -0.1246 T23:  -0.1048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1427 L22:   0.1444                                     
REMARK   3      L33:   0.8062 L12:  -0.0494                                     
REMARK   3      L13:   0.2157 L23:  -0.3018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0808 S12:   0.1420 S13:   0.2501                       
REMARK   3      S21:  -0.1774 S22:   0.0919 S23:   0.1486                       
REMARK   3      S31:   0.0395 S32:  -0.2833 S33:  -0.0111                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1679        A  2021                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.4140  12.7350 -53.4590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2746 T22:   0.2565                                     
REMARK   3      T33:   0.3771 T12:  -0.0632                                     
REMARK   3      T13:  -0.0643 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7748 L22:   2.3101                                     
REMARK   3      L33:   0.7338 L12:  -1.7114                                     
REMARK   3      L13:  -0.7422 L23:   0.4889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:  -0.2459 S13:   0.1722                       
REMARK   3      S21:  -0.0233 S22:   0.0692 S23:  -0.1177                       
REMARK   3      S31:  -0.1023 S32:   0.2729 S33:  -0.1080                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2022        A  2115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0710  11.3860 -19.7830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4948 T22:   1.4701                                     
REMARK   3      T33:   1.2973 T12:   0.1483                                     
REMARK   3      T13:   0.1666 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0518 L22:   0.2296                                     
REMARK   3      L33:   3.3754 L12:  -0.0096                                     
REMARK   3      L13:   0.1271 L23:  -0.7561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1392 S12:  -0.2036 S13:   0.0037                       
REMARK   3      S21:   0.2454 S22:   0.0110 S23:   0.0377                       
REMARK   3      S31:   0.2129 S32:   0.2718 S33:  -0.1503                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2116        A  2459                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.0900  -4.9410 -49.6580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1546 T22:   0.2586                                     
REMARK   3      T33:   0.4557 T12:   0.0433                                     
REMARK   3      T13:   0.0285 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8518 L22:   3.7668                                     
REMARK   3      L33:   0.2598 L12:   0.2838                                     
REMARK   3      L13:  -0.1109 L23:  -0.9213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:  -0.0242 S13:   0.2711                       
REMARK   3      S21:   0.1521 S22:   0.0222 S23:   0.1870                       
REMARK   3      S31:  -0.0946 S32:  -0.0492 S33:  -0.0197                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     8        D   324                          
REMARK   3    RESIDUE RANGE :   P   187        P   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2360   9.1040 -78.4400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:   0.1172                                     
REMARK   3      T33:   0.0135 T12:  -0.0011                                     
REMARK   3      T13:   0.0010 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6595 L22:   4.0995                                     
REMARK   3      L33:   3.8167 L12:   0.1494                                     
REMARK   3      L13:   0.1832 L23:   0.6794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1235 S12:   0.4063 S13:  -0.0032                       
REMARK   3      S21:  -0.4086 S22:   0.1485 S23:  -0.2042                       
REMARK   3      S31:  -0.0973 S32:   0.0864 S33:  -0.0250                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     8        C   324                          
REMARK   3    RESIDUE RANGE :   O   187        O   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.4820 -41.7400 -24.5370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3415 T22:   0.2790                                     
REMARK   3      T33:   0.4042 T12:   0.0280                                     
REMARK   3      T13:  -0.1224 T23:   0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1985 L22:   3.7584                                     
REMARK   3      L33:   3.4878 L12:  -0.0197                                     
REMARK   3      L13:  -0.7110 L23:   0.1605                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0732 S12:  -0.7490 S13:   0.0069                       
REMARK   3      S21:   0.6866 S22:   0.0676 S23:  -0.5158                       
REMARK   3      S31:  -0.0046 S32:   0.2047 S33:   0.0056                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5WBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228756.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97920                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69200                            
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: 4JSN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TACSIMATE, PH 7.0, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.52200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.33300            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.52200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.33300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, P                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, O                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B  1373                                                      
REMARK 465     THR B  1374                                                      
REMARK 465     GLY B  1375                                                      
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     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
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     GLY A  1373                                                      
REMARK 465     THR A  1374                                                      
REMARK 465     GLY A  1375                                                      
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     LYS A  1606                                                      
REMARK 465     LEU A  1607                                                      
REMARK 465     VAL A  1608                                                      
REMARK 465     PRO A  1609                                                      
REMARK 465     GLU A  1610                                                      
REMARK 465     ARG A  1611                                                      
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     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
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 465     GLY P   110                                                      
REMARK 465     SER P   111                                                      
REMARK 465     GLY P   112                                                      
REMARK 465     ARG P   113                                                      
REMARK 465     GLU P   114                                                      
REMARK 465     THR P   115                                                      
REMARK 465     SER P   116                                                      
REMARK 465     GLY P   117                                                      
REMARK 465     GLU P   118                                                      
REMARK 465     GLN P   119                                                      
REMARK 465     LEU P   120                                                      
REMARK 465     GLY P   121                                                      
REMARK 465     ILE P   122                                                      
REMARK 465     SER P   123                                                      
REMARK 465     ASP P   124                                                      
REMARK 465     ASN P   125                                                      
REMARK 465     GLY P   126                                                      
REMARK 465     GLY P   127                                                      
REMARK 465     LEU P   128                                                      
REMARK 465     PHE P   129                                                      
REMARK 465     VAL P   130                                                      
REMARK 465     MET P   131                                                      
REMARK 465     ASP P   132                                                      
REMARK 465     GLU P   133                                                      
REMARK 465     ASP P   134                                                      
REMARK 465     ALA P   135                                                      
REMARK 465     THR P   136                                                      
REMARK 465     LEU P   137                                                      
REMARK 465     GLN P   138                                                      
REMARK 465     ASP P   139                                                      
REMARK 465     LEU P   140                                                      
REMARK 465     PRO P   141                                                      
REMARK 465     PRO P   142                                                      
REMARK 465     PHE P   143                                                      
REMARK 465     CYS P   144                                                      
REMARK 465     GLU P   145                                                      
REMARK 465     SER P   146                                                      
REMARK 465     ASP P   147                                                      
REMARK 465     PRO P   148                                                      
REMARK 465     GLU P   149                                                      
REMARK 465     SER P   150                                                      
REMARK 465     THR P   151                                                      
REMARK 465     ASP P   152                                                      
REMARK 465     ASP P   153                                                      
REMARK 465     GLY P   154                                                      
REMARK 465     SER P   155                                                      
REMARK 465     LEU P   156                                                      
REMARK 465     SER P   157                                                      
REMARK 465     GLU P   158                                                      
REMARK 465     GLU P   159                                                      
REMARK 465     THR P   160                                                      
REMARK 465     PRO P   161                                                      
REMARK 465     ALA P   162                                                      
REMARK 465     GLY P   163                                                      
REMARK 465     PRO P   164                                                      
REMARK 465     PRO P   165                                                      
REMARK 465     THR P   166                                                      
REMARK 465     CYS P   167                                                      
REMARK 465     SER P   168                                                      
REMARK 465     VAL P   169                                                      
REMARK 465     PRO P   170                                                      
REMARK 465     PRO P   171                                                      
REMARK 465     ALA P   172                                                      
REMARK 465     SER P   173                                                      
REMARK 465     ALA P   174                                                      
REMARK 465     LEU P   175                                                      
REMARK 465     PRO P   176                                                      
REMARK 465     THR P   177                                                      
REMARK 465     GLN P   178                                                      
REMARK 465     GLN P   179                                                      
REMARK 465     TYR P   180                                                      
REMARK 465     ALA P   181                                                      
REMARK 465     LYS P   182                                                      
REMARK 465     SER P   183                                                      
REMARK 465     LEU P   184                                                      
REMARK 465     PRO P   185                                                      
REMARK 465     VAL P   186                                                      
REMARK 465     ARG P   197                                                      
REMARK 465     THR P   198                                                      
REMARK 465     GLU P   199                                                      
REMARK 465     ALA P   200                                                      
REMARK 465     ARG P   201                                                      
REMARK 465     SER P   202                                                      
REMARK 465     SER P   203                                                      
REMARK 465     ASP P   204                                                      
REMARK 465     GLU P   205                                                      
REMARK 465     GLU P   206                                                      
REMARK 465     ASN P   207                                                      
REMARK 465     GLY O   110                                                      
REMARK 465     SER O   111                                                      
REMARK 465     GLY O   112                                                      
REMARK 465     ARG O   113                                                      
REMARK 465     GLU O   114                                                      
REMARK 465     THR O   115                                                      
REMARK 465     SER O   116                                                      
REMARK 465     GLY O   117                                                      
REMARK 465     GLU O   118                                                      
REMARK 465     GLN O   119                                                      
REMARK 465     LEU O   120                                                      
REMARK 465     GLY O   121                                                      
REMARK 465     ILE O   122                                                      
REMARK 465     SER O   123                                                      
REMARK 465     ASP O   124                                                      
REMARK 465     ASN O   125                                                      
REMARK 465     GLY O   126                                                      
REMARK 465     GLY O   127                                                      
REMARK 465     LEU O   128                                                      
REMARK 465     PHE O   129                                                      
REMARK 465     VAL O   130                                                      
REMARK 465     MET O   131                                                      
REMARK 465     ASP O   132                                                      
REMARK 465     GLU O   133                                                      
REMARK 465     ASP O   134                                                      
REMARK 465     ALA O   135                                                      
REMARK 465     THR O   136                                                      
REMARK 465     LEU O   137                                                      
REMARK 465     GLN O   138                                                      
REMARK 465     ASP O   139                                                      
REMARK 465     LEU O   140                                                      
REMARK 465     PRO O   141                                                      
REMARK 465     PRO O   142                                                      
REMARK 465     PHE O   143                                                      
REMARK 465     CYS O   144                                                      
REMARK 465     GLU O   145                                                      
REMARK 465     SER O   146                                                      
REMARK 465     ASP O   147                                                      
REMARK 465     PRO O   148                                                      
REMARK 465     GLU O   149                                                      
REMARK 465     SER O   150                                                      
REMARK 465     THR O   151                                                      
REMARK 465     ASP O   152                                                      
REMARK 465     ASP O   153                                                      
REMARK 465     GLY O   154                                                      
REMARK 465     SER O   155                                                      
REMARK 465     LEU O   156                                                      
REMARK 465     SER O   157                                                      
REMARK 465     GLU O   158                                                      
REMARK 465     GLU O   159                                                      
REMARK 465     THR O   160                                                      
REMARK 465     PRO O   161                                                      
REMARK 465     ALA O   162                                                      
REMARK 465     GLY O   163                                                      
REMARK 465     PRO O   164                                                      
REMARK 465     PRO O   165                                                      
REMARK 465     THR O   166                                                      
REMARK 465     CYS O   167                                                      
REMARK 465     SER O   168                                                      
REMARK 465     VAL O   169                                                      
REMARK 465     PRO O   170                                                      
REMARK 465     PRO O   171                                                      
REMARK 465     ALA O   172                                                      
REMARK 465     SER O   173                                                      
REMARK 465     ALA O   174                                                      
REMARK 465     LEU O   175                                                      
REMARK 465     PRO O   176                                                      
REMARK 465     THR O   177                                                      
REMARK 465     GLN O   178                                                      
REMARK 465     GLN O   179                                                      
REMARK 465     TYR O   180                                                      
REMARK 465     ALA O   181                                                      
REMARK 465     LYS O   182                                                      
REMARK 465     SER O   183                                                      
REMARK 465     LEU O   184                                                      
REMARK 465     PRO O   185                                                      
REMARK 465     VAL O   186                                                      
REMARK 465     ARG O   197                                                      
REMARK 465     THR O   198                                                      
REMARK 465     GLU O   199                                                      
REMARK 465     ALA O   200                                                      
REMARK 465     ARG O   201                                                      
REMARK 465     SER O   202                                                      
REMARK 465     SER O   203                                                      
REMARK 465     ASP O   204                                                      
REMARK 465     GLU O   205                                                      
REMARK 465     GLU O   206                                                      
REMARK 465     ASN O   207                                                      
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    PHE B1440       79.38   -107.12                                   
REMARK 500    GLU B1442      -39.73   -133.39                                   
REMARK 500    LYS B1606       41.46    -94.18                                   
REMARK 500    LEU B1607      -57.16   -157.16                                   
REMARK 500    LEU B1623      -58.17   -165.43                                   
REMARK 500    VAL B1630      -57.10    -20.96                                   
REMARK 500    ASP B1649       76.48   -116.35                                   
REMARK 500    ASP B1680       86.58     65.60                                   
REMARK 500    SER B1682       78.75    -51.95                                   
REMARK 500    VAL B1692      -51.15    -14.78                                   
REMARK 500    ARG B1709       80.86    -58.99                                   
REMARK 500    ALA B1728      -76.99    -74.96                                   
REMARK 500    SER B1785       54.89   -101.19                                   
REMARK 500    ARG B1896       89.26     54.07                                   
REMARK 500    ASN B1899       30.81   -146.77                                   
REMARK 500    GLN B1937      -34.71    -30.64                                   
REMARK 500    LYS B1981       74.05   -119.80                                   
REMARK 500    ARG B2042       77.15     58.47                                   
REMARK 500    SER B2120      133.88   -170.66                                   
REMARK 500    SER B2127       90.66   -160.18                                   
REMARK 500    SER B2165     -163.82   -110.00                                   
REMARK 500    ARG B2168       67.32     61.34                                   
REMARK 500    ASN B2262       59.56   -103.03                                   
REMARK 500    ASP B2274       38.72    -99.36                                   
REMARK 500    ARG B2339       56.93    -90.81                                   
REMARK 500    ASP B2357       90.40     58.88                                   
REMARK 500    PHE B2358       45.11   -108.18                                   
REMARK 500    PHE B2362     -169.33     59.61                                   
REMARK 500    HIS B2410       46.89   -103.66                                   
REMARK 500    TYR B2423       20.04    -79.33                                   
REMARK 500    PHE B2513      -65.97   -129.47                                   
REMARK 500    SER D  43     -176.46   -170.86                                   
REMARK 500    ASN D  74      -44.64    106.89                                   
REMARK 500    ASN D  76     -159.41    -91.94                                   
REMARK 500    LYS D  86      177.26     62.01                                   
REMARK 500    ASP D 106       13.80    -69.35                                   
REMARK 500    ARG D 115       39.80    -95.99                                   
REMARK 500    GLN D 140       -4.28     75.87                                   
REMARK 500    GLU D 170       -4.83     70.90                                   
REMARK 500    GLU D 206       94.11     71.52                                   
REMARK 500    VAL D 207      -56.91   -131.53                                   
REMARK 500    ASN D 264      116.68    173.43                                   
REMARK 500    GLU D 267       44.31   -154.23                                   
REMARK 500    SER D 268        0.46     56.78                                   
REMARK 500    SER D 269      105.60     62.06                                   
REMARK 500    ASP D 291       20.20    -79.09                                   
REMARK 500    PHE A1440       79.77   -107.36                                   
REMARK 500    GLU A1442      -34.70   -130.22                                   
REMARK 500    LEU A1623      -58.78   -164.95                                   
REMARK 500    VAL A1630      -56.72    -21.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      89 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 GLU B 1444     ILE B 1445                  142.91                    
REMARK 500 ASP B 1680     PRO B 1681                  136.01                    
REMARK 500 GLU A 1444     ILE A 1445                  143.11                    
REMARK 500 ASP A 1680     PRO A 1681                  135.35                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5WBY B 1376  2549  UNP    P42345   MTOR_HUMAN    1376   2549             
DBREF  5WBY D    1   326  UNP    Q9BVC4   LST8_HUMAN       1    326             
DBREF  5WBY A 1376  2549  UNP    P42345   MTOR_HUMAN    1376   2549             
DBREF  5WBY C    1   326  UNP    Q9BVC4   LST8_HUMAN       1    326             
DBREF  5WBY P  114   207  UNP    Q96B36   AKTS1_HUMAN    114    207             
DBREF  5WBY O  114   207  UNP    Q96B36   AKTS1_HUMAN    114    207             
SEQADV 5WBY GLY B 1373  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY THR B 1374  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY GLY B 1375  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY GLY D   -1  UNP  Q9BVC4              EXPRESSION TAG                 
SEQADV 5WBY SER D    0  UNP  Q9BVC4              EXPRESSION TAG                 
SEQADV 5WBY GLY A 1373  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY THR A 1374  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY GLY A 1375  UNP  P42345              EXPRESSION TAG                 
SEQADV 5WBY GLY C   -1  UNP  Q9BVC4              EXPRESSION TAG                 
SEQADV 5WBY SER C    0  UNP  Q9BVC4              EXPRESSION TAG                 
SEQADV 5WBY GLY P  110  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY SER P  111  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY GLY P  112  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY ARG P  113  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY GLY O  110  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY SER O  111  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY GLY O  112  UNP  Q96B36              EXPRESSION TAG                 
SEQADV 5WBY ARG O  113  UNP  Q96B36              EXPRESSION TAG                 
SEQRES   1 B 1177  GLY THR GLY ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU          
SEQRES   2 B 1177  ARG ALA ALA LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS          
SEQRES   3 B 1177  TYR LYS GLU LEU GLU PHE GLN LYS GLY PRO THR PRO ALA          
SEQRES   4 B 1177  ILE LEU GLU SER LEU ILE SER ILE ASN ASN LYS LEU GLN          
SEQRES   5 B 1177  GLN PRO GLU ALA ALA ALA GLY VAL LEU GLU TYR ALA MET          
SEQRES   6 B 1177  LYS HIS PHE GLY GLU LEU GLU ILE GLN ALA THR TRP TYR          
SEQRES   7 B 1177  GLU LYS LEU HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR          
SEQRES   8 B 1177  ASP LYS LYS MET ASP THR ASN LYS ASP ASP PRO GLU LEU          
SEQRES   9 B 1177  MET LEU GLY ARG MET ARG CYS LEU GLU ALA LEU GLY GLU          
SEQRES  10 B 1177  TRP GLY GLN LEU HIS GLN GLN CYS CYS GLU LYS TRP THR          
SEQRES  11 B 1177  LEU VAL ASN ASP GLU THR GLN ALA LYS MET ALA ARG MET          
SEQRES  12 B 1177  ALA ALA ALA ALA ALA TRP GLY LEU GLY GLN TRP ASP SER          
SEQRES  13 B 1177  MET GLU GLU TYR THR CYS MET ILE PRO ARG ASP THR HIS          
SEQRES  14 B 1177  ASP GLY ALA PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN          
SEQRES  15 B 1177  ASP LEU PHE SER LEU ALA GLN GLN CYS ILE ASP LYS ALA          
SEQRES  16 B 1177  ARG ASP LEU LEU ASP ALA GLU LEU THR ALA MET ALA GLY          
SEQRES  17 B 1177  GLU SER TYR SER ARG ALA TYR GLY ALA MET VAL SER CYS          
SEQRES  18 B 1177  HIS MET LEU SER GLU LEU GLU GLU VAL ILE GLN TYR LYS          
SEQRES  19 B 1177  LEU VAL PRO GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP          
SEQRES  20 B 1177  TRP GLU ARG LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP          
SEQRES  21 B 1177  TRP GLN LYS ILE LEU MET VAL ARG SER LEU VAL VAL SER          
SEQRES  22 B 1177  PRO HIS GLU ASP MET ARG THR TRP LEU LYS TYR ALA SER          
SEQRES  23 B 1177  LEU CYS GLY LYS SER GLY ARG LEU ALA LEU ALA HIS LYS          
SEQRES  24 B 1177  THR LEU VAL LEU LEU LEU GLY VAL ASP PRO SER ARG GLN          
SEQRES  25 B 1177  LEU ASP HIS PRO LEU PRO THR VAL HIS PRO GLN VAL THR          
SEQRES  26 B 1177  TYR ALA TYR MET LYS ASN MET TRP LYS SER ALA ARG LYS          
SEQRES  27 B 1177  ILE ASP ALA PHE GLN HIS MET GLN HIS PHE VAL GLN THR          
SEQRES  28 B 1177  MET GLN GLN GLN ALA GLN HIS ALA ILE ALA THR GLU ASP          
SEQRES  29 B 1177  GLN GLN HIS LYS GLN GLU LEU HIS LYS LEU MET ALA ARG          
SEQRES  30 B 1177  CYS PHE LEU LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN          
SEQRES  31 B 1177  GLY ILE ASN GLU SER THR ILE PRO LYS VAL LEU GLN TYR          
SEQRES  32 B 1177  TYR SER ALA ALA THR GLU HIS ASP ARG SER TRP TYR LYS          
SEQRES  33 B 1177  ALA TRP HIS ALA TRP ALA VAL MET ASN PHE GLU ALA VAL          
SEQRES  34 B 1177  LEU HIS TYR LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS          
SEQRES  35 B 1177  LYS LYS LEU ARG HIS ALA SER GLY ALA ASN ILE THR ASN          
SEQRES  36 B 1177  ALA THR THR ALA ALA THR THR ALA ALA THR ALA THR THR          
SEQRES  37 B 1177  THR ALA SER THR GLU GLY SER ASN SER GLU SER GLU ALA          
SEQRES  38 B 1177  GLU SER THR GLU ASN SER PRO THR PRO SER PRO LEU GLN          
SEQRES  39 B 1177  LYS LYS VAL THR GLU ASP LEU SER LYS THR LEU LEU MET          
SEQRES  40 B 1177  TYR THR VAL PRO ALA VAL GLN GLY PHE PHE ARG SER ILE          
SEQRES  41 B 1177  SER LEU SER ARG GLY ASN ASN LEU GLN ASP THR LEU ARG          
SEQRES  42 B 1177  VAL LEU THR LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP          
SEQRES  43 B 1177  VAL ASN GLU ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN          
SEQRES  44 B 1177  ILE ASP THR TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA          
SEQRES  45 B 1177  ARG ILE ASP THR PRO ARG PRO LEU VAL GLY ARG LEU ILE          
SEQRES  46 B 1177  HIS GLN LEU LEU THR ASP ILE GLY ARG TYR HIS PRO GLN          
SEQRES  47 B 1177  ALA LEU ILE TYR PRO LEU THR VAL ALA SER LYS SER THR          
SEQRES  48 B 1177  THR THR ALA ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS          
SEQRES  49 B 1177  ASN MET CYS GLU HIS SER ASN THR LEU VAL GLN GLN ALA          
SEQRES  50 B 1177  MET MET VAL SER GLU GLU LEU ILE ARG VAL ALA ILE LEU          
SEQRES  51 B 1177  TRP HIS GLU MET TRP HIS GLU GLY LEU GLU GLU ALA SER          
SEQRES  52 B 1177  ARG LEU TYR PHE GLY GLU ARG ASN VAL LYS GLY MET PHE          
SEQRES  53 B 1177  GLU VAL LEU GLU PRO LEU HIS ALA MET MET GLU ARG GLY          
SEQRES  54 B 1177  PRO GLN THR LEU LYS GLU THR SER PHE ASN GLN ALA TYR          
SEQRES  55 B 1177  GLY ARG ASP LEU MET GLU ALA GLN GLU TRP CYS ARG LYS          
SEQRES  56 B 1177  TYR MET LYS SER GLY ASN VAL LYS ASP LEU THR GLN ALA          
SEQRES  57 B 1177  TRP ASP LEU TYR TYR HIS VAL PHE ARG ARG ILE SER LYS          
SEQRES  58 B 1177  GLN LEU PRO GLN LEU THR SER LEU GLU LEU GLN TYR VAL          
SEQRES  59 B 1177  SER PRO LYS LEU LEU MET CYS ARG ASP LEU GLU LEU ALA          
SEQRES  60 B 1177  VAL PRO GLY THR TYR ASP PRO ASN GLN PRO ILE ILE ARG          
SEQRES  61 B 1177  ILE GLN SER ILE ALA PRO SER LEU GLN VAL ILE THR SER          
SEQRES  62 B 1177  LYS GLN ARG PRO ARG LYS LEU THR LEU MET GLY SER ASN          
SEQRES  63 B 1177  GLY HIS GLU PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP          
SEQRES  64 B 1177  LEU ARG GLN ASP GLU ARG VAL MET GLN LEU PHE GLY LEU          
SEQRES  65 B 1177  VAL ASN THR LEU LEU ALA ASN ASP PRO THR SER LEU ARG          
SEQRES  66 B 1177  LYS ASN LEU SER ILE GLN ARG TYR ALA VAL ILE PRO LEU          
SEQRES  67 B 1177  SER THR ASN SER GLY LEU ILE GLY TRP VAL PRO HIS CYS          
SEQRES  68 B 1177  ASP THR LEU HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS          
SEQRES  69 B 1177  LYS LYS ILE LEU LEU ASN ILE GLU HIS ARG ILE MET LEU          
SEQRES  70 B 1177  ARG MET ALA PRO ASP TYR ASP HIS LEU THR LEU MET GLN          
SEQRES  71 B 1177  LYS VAL GLU VAL PHE GLU HIS ALA VAL ASN ASN THR ALA          
SEQRES  72 B 1177  GLY ASP ASP LEU ALA LYS LEU LEU TRP LEU LYS SER PRO          
SEQRES  73 B 1177  SER SER GLU VAL TRP PHE ASP ARG ARG THR ASN TYR THR          
SEQRES  74 B 1177  ARG SER LEU ALA VAL MET SER MET VAL GLY TYR ILE LEU          
SEQRES  75 B 1177  GLY LEU GLY ASP ARG HIS PRO SER ASN LEU MET LEU ASP          
SEQRES  76 B 1177  ARG LEU SER GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP          
SEQRES  77 B 1177  CYS PHE GLU VAL ALA MET THR ARG GLU LYS PHE PRO GLU          
SEQRES  78 B 1177  LYS ILE PRO PHE ARG LEU THR ARG MET LEU THR ASN ALA          
SEQRES  79 B 1177  MET GLU VAL THR GLY LEU ASP GLY ASN TYR ARG ILE THR          
SEQRES  80 B 1177  CYS HIS THR VAL MET GLU VAL LEU ARG GLU HIS LYS ASP          
SEQRES  81 B 1177  SER VAL MET ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO          
SEQRES  82 B 1177  LEU LEU ASN TRP ARG LEU MET ASP THR ASN THR LYS GLY          
SEQRES  83 B 1177  ASN LYS ARG SER ARG THR ARG THR ASP SER TYR SER ALA          
SEQRES  84 B 1177  GLY GLN SER VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY          
SEQRES  85 B 1177  GLU PRO ALA HIS LYS LYS THR GLY THR THR VAL PRO GLU          
SEQRES  86 B 1177  SER ILE HIS SER PHE ILE GLY ASP GLY LEU VAL LYS PRO          
SEQRES  87 B 1177  GLU ALA LEU ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG          
SEQRES  88 B 1177  VAL ARG ASP LYS LEU THR GLY ARG ASP PHE SER HIS ASP          
SEQRES  89 B 1177  ASP THR LEU ASP VAL PRO THR GLN VAL GLU LEU LEU ILE          
SEQRES  90 B 1177  LYS GLN ALA THR SER HIS GLU ASN LEU CYS GLN CYS TYR          
SEQRES  91 B 1177  ILE GLY TRP CYS PRO PHE TRP                                  
SEQRES   1 D  328  GLY SER MET ASN THR SER PRO GLY THR VAL GLY SER ASP          
SEQRES   2 D  328  PRO VAL ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL          
SEQRES   3 D  328  ARG PHE TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR          
SEQRES   4 D  328  VAL GLN HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL          
SEQRES   5 D  328  THR PRO ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN          
SEQRES   6 D  328  HIS ILE ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN          
SEQRES   7 D  328  PRO ILE ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA          
SEQRES   8 D  328  SER VAL GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR          
SEQRES   9 D  328  GLY GLY GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG          
SEQRES  10 D  328  SER ARG ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN          
SEQRES  11 D  328  ALA PRO ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA          
SEQRES  12 D  328  GLU LEU ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE          
SEQRES  13 D  328  TRP ASP LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO          
SEQRES  14 D  328  GLU PRO GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO          
SEQRES  15 D  328  ASP ALA SER TYR MET ALA ALA VAL ASN SER THR GLY ASN          
SEQRES  16 D  328  CYS TYR VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU          
SEQRES  17 D  328  VAL THR GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS          
SEQRES  18 D  328  THR ARG TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER          
SEQRES  19 D  328  THR LEU LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS          
SEQRES  20 D  328  ILE TRP ARG THR SER ASN PHE SER LEU MET THR GLU LEU          
SEQRES  21 D  328  SER ILE LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY          
SEQRES  22 D  328  TRP MET TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR          
SEQRES  23 D  328  ILE VAL THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP          
SEQRES  24 D  328  CYS VAL GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY          
SEQRES  25 D  328  HIS GLN LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER          
SEQRES  26 D  328  VAL LEU GLY                                                  
SEQRES   1 A 1177  GLY THR GLY ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU          
SEQRES   2 A 1177  ARG ALA ALA LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS          
SEQRES   3 A 1177  TYR LYS GLU LEU GLU PHE GLN LYS GLY PRO THR PRO ALA          
SEQRES   4 A 1177  ILE LEU GLU SER LEU ILE SER ILE ASN ASN LYS LEU GLN          
SEQRES   5 A 1177  GLN PRO GLU ALA ALA ALA GLY VAL LEU GLU TYR ALA MET          
SEQRES   6 A 1177  LYS HIS PHE GLY GLU LEU GLU ILE GLN ALA THR TRP TYR          
SEQRES   7 A 1177  GLU LYS LEU HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR          
SEQRES   8 A 1177  ASP LYS LYS MET ASP THR ASN LYS ASP ASP PRO GLU LEU          
SEQRES   9 A 1177  MET LEU GLY ARG MET ARG CYS LEU GLU ALA LEU GLY GLU          
SEQRES  10 A 1177  TRP GLY GLN LEU HIS GLN GLN CYS CYS GLU LYS TRP THR          
SEQRES  11 A 1177  LEU VAL ASN ASP GLU THR GLN ALA LYS MET ALA ARG MET          
SEQRES  12 A 1177  ALA ALA ALA ALA ALA TRP GLY LEU GLY GLN TRP ASP SER          
SEQRES  13 A 1177  MET GLU GLU TYR THR CYS MET ILE PRO ARG ASP THR HIS          
SEQRES  14 A 1177  ASP GLY ALA PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN          
SEQRES  15 A 1177  ASP LEU PHE SER LEU ALA GLN GLN CYS ILE ASP LYS ALA          
SEQRES  16 A 1177  ARG ASP LEU LEU ASP ALA GLU LEU THR ALA MET ALA GLY          
SEQRES  17 A 1177  GLU SER TYR SER ARG ALA TYR GLY ALA MET VAL SER CYS          
SEQRES  18 A 1177  HIS MET LEU SER GLU LEU GLU GLU VAL ILE GLN TYR LYS          
SEQRES  19 A 1177  LEU VAL PRO GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP          
SEQRES  20 A 1177  TRP GLU ARG LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP          
SEQRES  21 A 1177  TRP GLN LYS ILE LEU MET VAL ARG SER LEU VAL VAL SER          
SEQRES  22 A 1177  PRO HIS GLU ASP MET ARG THR TRP LEU LYS TYR ALA SER          
SEQRES  23 A 1177  LEU CYS GLY LYS SER GLY ARG LEU ALA LEU ALA HIS LYS          
SEQRES  24 A 1177  THR LEU VAL LEU LEU LEU GLY VAL ASP PRO SER ARG GLN          
SEQRES  25 A 1177  LEU ASP HIS PRO LEU PRO THR VAL HIS PRO GLN VAL THR          
SEQRES  26 A 1177  TYR ALA TYR MET LYS ASN MET TRP LYS SER ALA ARG LYS          
SEQRES  27 A 1177  ILE ASP ALA PHE GLN HIS MET GLN HIS PHE VAL GLN THR          
SEQRES  28 A 1177  MET GLN GLN GLN ALA GLN HIS ALA ILE ALA THR GLU ASP          
SEQRES  29 A 1177  GLN GLN HIS LYS GLN GLU LEU HIS LYS LEU MET ALA ARG          
SEQRES  30 A 1177  CYS PHE LEU LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN          
SEQRES  31 A 1177  GLY ILE ASN GLU SER THR ILE PRO LYS VAL LEU GLN TYR          
SEQRES  32 A 1177  TYR SER ALA ALA THR GLU HIS ASP ARG SER TRP TYR LYS          
SEQRES  33 A 1177  ALA TRP HIS ALA TRP ALA VAL MET ASN PHE GLU ALA VAL          
SEQRES  34 A 1177  LEU HIS TYR LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS          
SEQRES  35 A 1177  LYS LYS LEU ARG HIS ALA SER GLY ALA ASN ILE THR ASN          
SEQRES  36 A 1177  ALA THR THR ALA ALA THR THR ALA ALA THR ALA THR THR          
SEQRES  37 A 1177  THR ALA SER THR GLU GLY SER ASN SER GLU SER GLU ALA          
SEQRES  38 A 1177  GLU SER THR GLU ASN SER PRO THR PRO SER PRO LEU GLN          
SEQRES  39 A 1177  LYS LYS VAL THR GLU ASP LEU SER LYS THR LEU LEU MET          
SEQRES  40 A 1177  TYR THR VAL PRO ALA VAL GLN GLY PHE PHE ARG SER ILE          
SEQRES  41 A 1177  SER LEU SER ARG GLY ASN ASN LEU GLN ASP THR LEU ARG          
SEQRES  42 A 1177  VAL LEU THR LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP          
SEQRES  43 A 1177  VAL ASN GLU ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN          
SEQRES  44 A 1177  ILE ASP THR TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA          
SEQRES  45 A 1177  ARG ILE ASP THR PRO ARG PRO LEU VAL GLY ARG LEU ILE          
SEQRES  46 A 1177  HIS GLN LEU LEU THR ASP ILE GLY ARG TYR HIS PRO GLN          
SEQRES  47 A 1177  ALA LEU ILE TYR PRO LEU THR VAL ALA SER LYS SER THR          
SEQRES  48 A 1177  THR THR ALA ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS          
SEQRES  49 A 1177  ASN MET CYS GLU HIS SER ASN THR LEU VAL GLN GLN ALA          
SEQRES  50 A 1177  MET MET VAL SER GLU GLU LEU ILE ARG VAL ALA ILE LEU          
SEQRES  51 A 1177  TRP HIS GLU MET TRP HIS GLU GLY LEU GLU GLU ALA SER          
SEQRES  52 A 1177  ARG LEU TYR PHE GLY GLU ARG ASN VAL LYS GLY MET PHE          
SEQRES  53 A 1177  GLU VAL LEU GLU PRO LEU HIS ALA MET MET GLU ARG GLY          
SEQRES  54 A 1177  PRO GLN THR LEU LYS GLU THR SER PHE ASN GLN ALA TYR          
SEQRES  55 A 1177  GLY ARG ASP LEU MET GLU ALA GLN GLU TRP CYS ARG LYS          
SEQRES  56 A 1177  TYR MET LYS SER GLY ASN VAL LYS ASP LEU THR GLN ALA          
SEQRES  57 A 1177  TRP ASP LEU TYR TYR HIS VAL PHE ARG ARG ILE SER LYS          
SEQRES  58 A 1177  GLN LEU PRO GLN LEU THR SER LEU GLU LEU GLN TYR VAL          
SEQRES  59 A 1177  SER PRO LYS LEU LEU MET CYS ARG ASP LEU GLU LEU ALA          
SEQRES  60 A 1177  VAL PRO GLY THR TYR ASP PRO ASN GLN PRO ILE ILE ARG          
SEQRES  61 A 1177  ILE GLN SER ILE ALA PRO SER LEU GLN VAL ILE THR SER          
SEQRES  62 A 1177  LYS GLN ARG PRO ARG LYS LEU THR LEU MET GLY SER ASN          
SEQRES  63 A 1177  GLY HIS GLU PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP          
SEQRES  64 A 1177  LEU ARG GLN ASP GLU ARG VAL MET GLN LEU PHE GLY LEU          
SEQRES  65 A 1177  VAL ASN THR LEU LEU ALA ASN ASP PRO THR SER LEU ARG          
SEQRES  66 A 1177  LYS ASN LEU SER ILE GLN ARG TYR ALA VAL ILE PRO LEU          
SEQRES  67 A 1177  SER THR ASN SER GLY LEU ILE GLY TRP VAL PRO HIS CYS          
SEQRES  68 A 1177  ASP THR LEU HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS          
SEQRES  69 A 1177  LYS LYS ILE LEU LEU ASN ILE GLU HIS ARG ILE MET LEU          
SEQRES  70 A 1177  ARG MET ALA PRO ASP TYR ASP HIS LEU THR LEU MET GLN          
SEQRES  71 A 1177  LYS VAL GLU VAL PHE GLU HIS ALA VAL ASN ASN THR ALA          
SEQRES  72 A 1177  GLY ASP ASP LEU ALA LYS LEU LEU TRP LEU LYS SER PRO          
SEQRES  73 A 1177  SER SER GLU VAL TRP PHE ASP ARG ARG THR ASN TYR THR          
SEQRES  74 A 1177  ARG SER LEU ALA VAL MET SER MET VAL GLY TYR ILE LEU          
SEQRES  75 A 1177  GLY LEU GLY ASP ARG HIS PRO SER ASN LEU MET LEU ASP          
SEQRES  76 A 1177  ARG LEU SER GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP          
SEQRES  77 A 1177  CYS PHE GLU VAL ALA MET THR ARG GLU LYS PHE PRO GLU          
SEQRES  78 A 1177  LYS ILE PRO PHE ARG LEU THR ARG MET LEU THR ASN ALA          
SEQRES  79 A 1177  MET GLU VAL THR GLY LEU ASP GLY ASN TYR ARG ILE THR          
SEQRES  80 A 1177  CYS HIS THR VAL MET GLU VAL LEU ARG GLU HIS LYS ASP          
SEQRES  81 A 1177  SER VAL MET ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO          
SEQRES  82 A 1177  LEU LEU ASN TRP ARG LEU MET ASP THR ASN THR LYS GLY          
SEQRES  83 A 1177  ASN LYS ARG SER ARG THR ARG THR ASP SER TYR SER ALA          
SEQRES  84 A 1177  GLY GLN SER VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY          
SEQRES  85 A 1177  GLU PRO ALA HIS LYS LYS THR GLY THR THR VAL PRO GLU          
SEQRES  86 A 1177  SER ILE HIS SER PHE ILE GLY ASP GLY LEU VAL LYS PRO          
SEQRES  87 A 1177  GLU ALA LEU ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG          
SEQRES  88 A 1177  VAL ARG ASP LYS LEU THR GLY ARG ASP PHE SER HIS ASP          
SEQRES  89 A 1177  ASP THR LEU ASP VAL PRO THR GLN VAL GLU LEU LEU ILE          
SEQRES  90 A 1177  LYS GLN ALA THR SER HIS GLU ASN LEU CYS GLN CYS TYR          
SEQRES  91 A 1177  ILE GLY TRP CYS PRO PHE TRP                                  
SEQRES   1 C  328  GLY SER MET ASN THR SER PRO GLY THR VAL GLY SER ASP          
SEQRES   2 C  328  PRO VAL ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL          
SEQRES   3 C  328  ARG PHE TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR          
SEQRES   4 C  328  VAL GLN HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL          
SEQRES   5 C  328  THR PRO ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN          
SEQRES   6 C  328  HIS ILE ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN          
SEQRES   7 C  328  PRO ILE ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA          
SEQRES   8 C  328  SER VAL GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR          
SEQRES   9 C  328  GLY GLY GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG          
SEQRES  10 C  328  SER ARG ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN          
SEQRES  11 C  328  ALA PRO ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA          
SEQRES  12 C  328  GLU LEU ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE          
SEQRES  13 C  328  TRP ASP LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO          
SEQRES  14 C  328  GLU PRO GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO          
SEQRES  15 C  328  ASP ALA SER TYR MET ALA ALA VAL ASN SER THR GLY ASN          
SEQRES  16 C  328  CYS TYR VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU          
SEQRES  17 C  328  VAL THR GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS          
SEQRES  18 C  328  THR ARG TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER          
SEQRES  19 C  328  THR LEU LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS          
SEQRES  20 C  328  ILE TRP ARG THR SER ASN PHE SER LEU MET THR GLU LEU          
SEQRES  21 C  328  SER ILE LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY          
SEQRES  22 C  328  TRP MET TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR          
SEQRES  23 C  328  ILE VAL THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP          
SEQRES  24 C  328  CYS VAL GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY          
SEQRES  25 C  328  HIS GLN LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER          
SEQRES  26 C  328  VAL LEU GLY                                                  
SEQRES   1 P   98  GLY SER GLY ARG GLU THR SER GLY GLU GLN LEU GLY ILE          
SEQRES   2 P   98  SER ASP ASN GLY GLY LEU PHE VAL MET ASP GLU ASP ALA          
SEQRES   3 P   98  THR LEU GLN ASP LEU PRO PRO PHE CYS GLU SER ASP PRO          
SEQRES   4 P   98  GLU SER THR ASP ASP GLY SER LEU SER GLU GLU THR PRO          
SEQRES   5 P   98  ALA GLY PRO PRO THR CYS SER VAL PRO PRO ALA SER ALA          
SEQRES   6 P   98  LEU PRO THR GLN GLN TYR ALA LYS SER LEU PRO VAL SER          
SEQRES   7 P   98  VAL PRO VAL TRP GLY PHE LYS GLU LYS ARG THR GLU ALA          
SEQRES   8 P   98  ARG SER SER ASP GLU GLU ASN                                  
SEQRES   1 O   98  GLY SER GLY ARG GLU THR SER GLY GLU GLN LEU GLY ILE          
SEQRES   2 O   98  SER ASP ASN GLY GLY LEU PHE VAL MET ASP GLU ASP ALA          
SEQRES   3 O   98  THR LEU GLN ASP LEU PRO PRO PHE CYS GLU SER ASP PRO          
SEQRES   4 O   98  GLU SER THR ASP ASP GLY SER LEU SER GLU GLU THR PRO          
SEQRES   5 O   98  ALA GLY PRO PRO THR CYS SER VAL PRO PRO ALA SER ALA          
SEQRES   6 O   98  LEU PRO THR GLN GLN TYR ALA LYS SER LEU PRO VAL SER          
SEQRES   7 O   98  VAL PRO VAL TRP GLY PHE LYS GLU LYS ARG THR GLU ALA          
SEQRES   8 O   98  ARG SER SER ASP GLU GLU ASN                                  
HELIX    1 AA1 GLU B 1385  GLY B 1407  1                                  23    
HELIX    2 AA2 THR B 1409  LYS B 1422  1                                  14    
HELIX    3 AA3 GLN B 1425  PHE B 1440  1                                  16    
HELIX    4 AA4 ILE B 1445  LEU B 1453  1                                   9    
HELIX    5 AA5 GLU B 1455  ASN B 1470  1                                  16    
HELIX    6 AA6 ASP B 1473  GLY B 1488  1                                  16    
HELIX    7 AA7 GLU B 1489  GLU B 1499  1                                  11    
HELIX    8 AA8 ASN B 1505  GLY B 1524  1                                  20    
HELIX    9 AA9 GLN B 1525  ILE B 1536  1                                  12    
HELIX   10 AB1 THR B 1540  GLN B 1554  1                                  15    
HELIX   11 AB2 LEU B 1556  MET B 1578  1                                  23    
HELIX   12 AB3 ALA B 1586  LYS B 1606  1                                  21    
HELIX   13 AB4 ARG B 1612  GLY B 1625  1                                  14    
HELIX   14 AB5 ILE B 1629  SER B 1641  1                                  13    
HELIX   15 AB6 ASP B 1649  GLY B 1664  1                                  16    
HELIX   16 AB7 ARG B 1665  GLY B 1678  1                                  14    
HELIX   17 AB8 HIS B 1693  SER B 1707  1                                  15    
HELIX   18 AB9 ARG B 1709  HIS B 1730  1                                  22    
HELIX   19 AC1 GLN B 1737  GLN B 1762  1                                  26    
HELIX   20 AC2 SER B 1767  ASP B 1783  1                                  17    
HELIX   21 AC3 TRP B 1786  LYS B 1814  1                                  29    
HELIX   22 AC4 LYS B 1868  LEU B 1894  1                                  27    
HELIX   23 AC5 ASN B 1899  GLY B 1914  1                                  16    
HELIX   24 AC6 TRP B 1916  ILE B 1930  1                                  15    
HELIX   25 AC7 GLN B 1931  GLN B 1937  5                                   7    
HELIX   26 AC8 VAL B 1938  ALA B 1944  1                                   7    
HELIX   27 AC9 ARG B 1950  TYR B 1967  1                                  18    
HELIX   28 AD1 HIS B 1968  ALA B 1971  5                                   4    
HELIX   29 AD2 LEU B 1972  LYS B 1981  1                                  10    
HELIX   30 AD3 THR B 1984  ILE B 2021  1                                  38    
HELIX   31 AD4 LEU B 2022  PHE B 2039  1                                  18    
HELIX   32 AD5 ASN B 2043  ARG B 2060  1                                  18    
HELIX   33 AD6 THR B 2064  TYR B 2074  1                                  11    
HELIX   34 AD7 TYR B 2074  GLY B 2092  1                                  19    
HELIX   35 AD8 ASN B 2093  LEU B 2115  1                                  23    
HELIX   36 AD9 LEU B 2123  SER B 2127  1                                   5    
HELIX   37 AE1 SER B 2127  CYS B 2133  1                                   7    
HELIX   38 AE2 LEU B 2192  ASP B 2212  1                                  21    
HELIX   39 AE3 ASP B 2212  LYS B 2218  1                                   7    
HELIX   40 AE4 LEU B 2246  LYS B 2257  1                                  12    
HELIX   41 AE5 ASN B 2262  ALA B 2272  1                                  11    
HELIX   42 AE6 ASP B 2274  LEU B 2278  5                                   5    
HELIX   43 AE7 THR B 2279  ASN B 2293  1                                  15    
HELIX   44 AE8 ASP B 2297  SER B 2307  1                                  11    
HELIX   45 AE9 SER B 2309  GLY B 2335  1                                  27    
HELIX   46 AF1 GLU B 2363  ARG B 2368  1                                   6    
HELIX   47 AF2 THR B 2380  MET B 2387  1                                   8    
HELIX   48 AF3 GLY B 2394  HIS B 2410  1                                  17    
HELIX   49 AF4 HIS B 2410  TYR B 2423  1                                  14    
HELIX   50 AF5 ASN B 2428  ASP B 2433  1                                   6    
HELIX   51 AF6 THR B 2434  THR B 2436  5                                   3    
HELIX   52 AF7 LEU B 2493  GLY B 2510  1                                  18    
HELIX   53 AF8 ASP B 2520  SER B 2534  1                                  15    
HELIX   54 AF9 SER B 2534  CYS B 2541  1                                   8    
HELIX   55 AG1 TYR B 2542  CYS B 2546  5                                   5    
HELIX   56 AG2 ARG A 1386  GLY A 1407  1                                  22    
HELIX   57 AG3 THR A 1409  LYS A 1422  1                                  14    
HELIX   58 AG4 GLN A 1425  PHE A 1440  1                                  16    
HELIX   59 AG5 ILE A 1445  LEU A 1453  1                                   9    
HELIX   60 AG6 GLU A 1455  ASN A 1470  1                                  16    
HELIX   61 AG7 ASP A 1473  GLY A 1488  1                                  16    
HELIX   62 AG8 GLU A 1489  GLU A 1499  1                                  11    
HELIX   63 AG9 ASN A 1505  GLY A 1524  1                                  20    
HELIX   64 AH1 GLN A 1525  ILE A 1536  1                                  12    
HELIX   65 AH2 THR A 1540  GLN A 1554  1                                  15    
HELIX   66 AH3 LEU A 1556  MET A 1578  1                                  23    
HELIX   67 AH4 ALA A 1586  ILE A 1603  1                                  18    
HELIX   68 AH5 GLU A 1613  GLY A 1625  1                                  13    
HELIX   69 AH6 ILE A 1629  SER A 1641  1                                  13    
HELIX   70 AH7 ASP A 1649  GLY A 1664  1                                  16    
HELIX   71 AH8 ARG A 1665  GLY A 1678  1                                  14    
HELIX   72 AH9 HIS A 1693  SER A 1707  1                                  15    
HELIX   73 AI1 ARG A 1709  HIS A 1730  1                                  22    
HELIX   74 AI2 GLN A 1737  GLN A 1762  1                                  26    
HELIX   75 AI3 SER A 1767  ASP A 1783  1                                  17    
HELIX   76 AI4 TRP A 1786  LYS A 1814  1                                  29    
HELIX   77 AI5 LYS A 1868  LEU A 1894  1                                  27    
HELIX   78 AI6 ASN A 1899  GLY A 1914  1                                  16    
HELIX   79 AI7 TRP A 1916  ILE A 1930  1                                  15    
HELIX   80 AI8 GLN A 1931  GLN A 1937  5                                   7    
HELIX   81 AI9 VAL A 1938  ALA A 1944  1                                   7    
HELIX   82 AJ1 ARG A 1950  TYR A 1967  1                                  18    
HELIX   83 AJ2 LEU A 1972  SER A 1980  1                                   9    
HELIX   84 AJ3 THR A 1984  ILE A 2021  1                                  38    
HELIX   85 AJ4 LEU A 2022  PHE A 2039  1                                  18    
HELIX   86 AJ5 ASN A 2043  ARG A 2060  1                                  18    
HELIX   87 AJ6 THR A 2064  TYR A 2074  1                                  11    
HELIX   88 AJ7 TYR A 2074  GLY A 2092  1                                  19    
HELIX   89 AJ8 ASN A 2093  LEU A 2115  1                                  23    
HELIX   90 AJ9 LEU A 2123  SER A 2127  1                                   5    
HELIX   91 AK1 SER A 2127  CYS A 2133  1                                   7    
HELIX   92 AK2 LEU A 2192  ASP A 2212  1                                  21    
HELIX   93 AK3 ASP A 2212  LYS A 2218  1                                   7    
HELIX   94 AK4 LEU A 2246  LYS A 2257  1                                  12    
HELIX   95 AK5 ASN A 2262  ALA A 2272  1                                  11    
HELIX   96 AK6 ASP A 2274  LEU A 2278  5                                   5    
HELIX   97 AK7 THR A 2279  ASN A 2293  1                                  15    
HELIX   98 AK8 ASP A 2297  SER A 2307  1                                  11    
HELIX   99 AK9 SER A 2309  GLY A 2335  1                                  27    
HELIX  100 AL1 GLU A 2363  ARG A 2368  1                                   6    
HELIX  101 AL2 THR A 2380  MET A 2387  1                                   8    
HELIX  102 AL3 GLY A 2394  HIS A 2410  1                                  17    
HELIX  103 AL4 HIS A 2410  TYR A 2423  1                                  14    
HELIX  104 AL5 ASN A 2428  ASP A 2433  1                                   6    
HELIX  105 AL6 THR A 2434  THR A 2436  5                                   3    
HELIX  106 AL7 LEU A 2493  GLY A 2510  1                                  18    
HELIX  107 AL8 ASP A 2520  SER A 2534  1                                  15    
HELIX  108 AL9 SER A 2534  CYS A 2541  1                                   8    
HELIX  109 AM1 TYR A 2542  CYS A 2546  5                                   5    
SHEET    1 AA1 4 SER B2120  GLU B2122  0                                        
SHEET    2 AA1 4 SER B2159  VAL B2162 -1  O  LEU B2160   N  LEU B2121           
SHEET    3 AA1 4 ARG B2170  GLY B2176 -1  O  LYS B2171   N  GLN B2161           
SHEET    4 AA1 4 ILE B2153  ILE B2156 -1  N  SER B2155   O  MET B2175           
SHEET    1 AA2 6 SER B2120  GLU B2122  0                                        
SHEET    2 AA2 6 SER B2159  VAL B2162 -1  O  LEU B2160   N  LEU B2121           
SHEET    3 AA2 6 ARG B2170  GLY B2176 -1  O  LYS B2171   N  GLN B2161           
SHEET    4 AA2 6 GLU B2181  LYS B2187 -1  O  PHE B2184   N  LEU B2172           
SHEET    5 AA2 6 GLY B2235  GLY B2238 -1  O  ILE B2237   N  LEU B2185           
SHEET    6 AA2 6 VAL B2227  PRO B2229 -1  N  ILE B2228   O  LEU B2236           
SHEET    1 AA3 3 CYS B2243  THR B2245  0                                        
SHEET    2 AA3 3 LEU B2344  ASP B2347 -1  O  LEU B2346   N  ASP B2244           
SHEET    3 AA3 3 ILE B2353  HIS B2355 -1  O  LEU B2354   N  MET B2345           
SHEET    1 AA4 4 CYS D  34  GLN D  39  0                                        
SHEET    2 AA4 4 THR D  23  TRP D  27 -1  N  PHE D  26   O  ARG D  36           
SHEET    3 AA4 4 VAL D  13  GLY D  19 -1  N  THR D  17   O  ARG D  25           
SHEET    4 AA4 4 VAL D 315  ASP D 322 -1  O  ALA D 319   N  ALA D  16           
SHEET    1 AA5 4 ALA D  47  VAL D  50  0                                        
SHEET    2 AA5 4 MET D  56  ALA D  60 -1  O  ALA D  58   N  GLU D  49           
SHEET    3 AA5 4 ILE D  65  ASP D  69 -1  O  ARG D  66   N  ALA D  59           
SHEET    4 AA5 4 PRO D  77  SER D  80 -1  O  ILE D  78   N  MET D  67           
SHEET    1 AA6 4 ILE D  88  PHE D  93  0                                        
SHEET    2 AA6 4 TRP D  99  GLY D 104 -1  O  TYR D 101   N  GLY D  92           
SHEET    3 AA6 4 THR D 108  ASP D 113 -1  O  TRP D 112   N  MET D 100           
SHEET    4 AA6 4 ARG D 123  GLN D 126 -1  O  PHE D 125   N  ALA D 109           
SHEET    1 AA7 5 ILE D 131  LEU D 136  0                                        
SHEET    2 AA7 5 GLU D 142  ASP D 147 -1  O  ILE D 144   N  CYS D 135           
SHEET    3 AA7 5 ILE D 152  ASP D 156 -1  O  HIS D 153   N  VAL D 145           
SHEET    4 AA7 5 ASN D 162  ILE D 166 -1  O  GLU D 163   N  ILE D 154           
SHEET    5 AA7 5 VAL P 190  TRP P 191  1  O  VAL P 190   N  ILE D 166           
SHEET    1 AA8 4 ILE D 173  ILE D 178  0                                        
SHEET    2 AA8 4 TYR D 184  ASN D 189 -1  O  ALA D 186   N  HIS D 177           
SHEET    3 AA8 4 CYS D 194  LEU D 199 -1  O  TRP D 197   N  MET D 185           
SHEET    4 AA8 4 LEU D 210  ILE D 216 -1  O  ILE D 211   N  ASN D 198           
SHEET    1 AA9 4 ALA D 223  PHE D 228  0                                        
SHEET    2 AA9 4 LEU D 234  SER D 239 -1  O  ALA D 236   N  ARG D 227           
SHEET    3 AA9 4 THR D 243  ARG D 248 -1  O  LYS D 245   N  THR D 237           
SHEET    4 AA9 4 LEU D 254  SER D 259 -1  O  LEU D 258   N  CYS D 244           
SHEET    1 AB1 4 MET D 273  PHE D 278  0                                        
SHEET    2 AB1 4 TYR D 284  SER D 289 -1  O  ALA D 288   N  GLY D 275           
SHEET    3 AB1 4 LEU D 293  CYS D 298 -1  O  TRP D 297   N  ILE D 285           
SHEET    4 AB1 4 ILE D 304  GLY D 309 -1  O  TYR D 308   N  ALA D 294           
SHEET    1 AB2 4 SER A2120  GLU A2122  0                                        
SHEET    2 AB2 4 SER A2159  VAL A2162 -1  O  LEU A2160   N  LEU A2121           
SHEET    3 AB2 4 ARG A2170  GLY A2176 -1  O  LYS A2171   N  GLN A2161           
SHEET    4 AB2 4 ILE A2153  ILE A2156 -1  N  SER A2155   O  MET A2175           
SHEET    1 AB3 6 SER A2120  GLU A2122  0                                        
SHEET    2 AB3 6 SER A2159  VAL A2162 -1  O  LEU A2160   N  LEU A2121           
SHEET    3 AB3 6 ARG A2170  GLY A2176 -1  O  LYS A2171   N  GLN A2161           
SHEET    4 AB3 6 GLU A2181  LYS A2187 -1  O  PHE A2184   N  LEU A2172           
SHEET    5 AB3 6 GLY A2235  GLY A2238 -1  O  ILE A2237   N  LEU A2185           
SHEET    6 AB3 6 VAL A2227  PRO A2229 -1  N  ILE A2228   O  LEU A2236           
SHEET    1 AB4 3 CYS A2243  THR A2245  0                                        
SHEET    2 AB4 3 LEU A2344  ASP A2347 -1  O  LEU A2346   N  ASP A2244           
SHEET    3 AB4 3 ILE A2353  HIS A2355 -1  O  LEU A2354   N  MET A2345           
SHEET    1 AB5 4 CYS C  34  GLN C  39  0                                        
SHEET    2 AB5 4 THR C  23  TRP C  27 -1  N  PHE C  26   O  ARG C  36           
SHEET    3 AB5 4 VAL C  13  GLY C  19 -1  N  THR C  17   O  ARG C  25           
SHEET    4 AB5 4 VAL C 315  ASP C 322 -1  O  ALA C 319   N  ALA C  16           
SHEET    1 AB6 4 ALA C  47  VAL C  50  0                                        
SHEET    2 AB6 4 MET C  56  ALA C  60 -1  O  ALA C  58   N  GLU C  49           
SHEET    3 AB6 4 ILE C  65  ASP C  69 -1  O  ARG C  66   N  ALA C  59           
SHEET    4 AB6 4 PRO C  77  SER C  80 -1  O  ILE C  78   N  MET C  67           
SHEET    1 AB7 4 ILE C  88  PHE C  93  0                                        
SHEET    2 AB7 4 TRP C  99  GLY C 104 -1  O  TYR C 101   N  GLY C  92           
SHEET    3 AB7 4 THR C 108  ASP C 113 -1  O  TRP C 112   N  MET C 100           
SHEET    4 AB7 4 ARG C 123  GLN C 126 -1  O  PHE C 125   N  ALA C 109           
SHEET    1 AB8 5 ILE C 131  LEU C 136  0                                        
SHEET    2 AB8 5 GLU C 142  ASP C 147 -1  O  ILE C 144   N  CYS C 135           
SHEET    3 AB8 5 ILE C 152  ASP C 156 -1  O  HIS C 153   N  VAL C 145           
SHEET    4 AB8 5 ASN C 162  ILE C 166 -1  O  GLU C 163   N  ILE C 154           
SHEET    5 AB8 5 VAL O 190  TRP O 191  1  O  VAL O 190   N  ILE C 166           
SHEET    1 AB9 4 ILE C 173  ILE C 178  0                                        
SHEET    2 AB9 4 TYR C 184  ASN C 189 -1  O  ALA C 186   N  HIS C 177           
SHEET    3 AB9 4 CYS C 194  LEU C 199 -1  O  TRP C 197   N  MET C 185           
SHEET    4 AB9 4 LEU C 210  ILE C 216 -1  O  ILE C 211   N  ASN C 198           
SHEET    1 AC1 4 ALA C 223  PHE C 228  0                                        
SHEET    2 AC1 4 LEU C 234  SER C 239 -1  O  ALA C 236   N  ARG C 227           
SHEET    3 AC1 4 THR C 243  ARG C 248 -1  O  LYS C 245   N  THR C 237           
SHEET    4 AC1 4 LEU C 254  SER C 259 -1  O  LEU C 258   N  CYS C 244           
SHEET    1 AC2 4 MET C 273  PHE C 278  0                                        
SHEET    2 AC2 4 TYR C 284  SER C 289 -1  O  ALA C 288   N  GLY C 275           
SHEET    3 AC2 4 LEU C 293  CYS C 298 -1  O  TRP C 297   N  ILE C 285           
SHEET    4 AC2 4 ILE C 304  GLY C 309 -1  O  TYR C 308   N  ALA C 294           
CRYST1  138.926  163.044  206.666  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      0.007198  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004839        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.999973 -0.007384  0.000186      -69.72169    1                    
MTRIX2   2 -0.007386 -0.999823  0.017318      -31.59790    1                    
MTRIX3   2  0.000058 -0.017319 -0.999850     -102.92092    1                    
MTRIX1   3  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   3  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   3  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   4  0.999676 -0.012174 -0.022333      -71.61633    1                    
MTRIX2   4 -0.011942 -0.999873  0.010510      -31.80653    1                    
MTRIX3   4 -0.022458 -0.010240 -0.999695     -100.87634    1                    
MTRIX1   5  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   5  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   5  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   6  0.999834 -0.006294 -0.017069      -70.89630    1                    
MTRIX2   6 -0.006308 -0.999980 -0.000781      -33.26179    1                    
MTRIX3   6 -0.017064  0.000889 -0.999854     -100.96297    1                    
MTRIX1   7  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   7  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   7  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   8  0.999633 -0.020611 -0.017579      -71.45419    1                    
MTRIX2   8 -0.020801 -0.999726 -0.010739      -33.15848    1                    
MTRIX3   8 -0.017353  0.011101 -0.999788     -100.76271    1                    
MTRIX1   9  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   9  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   9  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  10  0.999792  0.004595 -0.019854      -71.01669    1                    
MTRIX2  10  0.004865 -0.999896  0.013548      -32.98035    1                    
MTRIX3  10 -0.019790 -0.013642 -0.999711     -101.17468    1                    
MTRIX1  11  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  11  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  11  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  12  0.999847  0.007430 -0.015861      -70.58942    1                    
MTRIX2  12  0.007578 -0.999928  0.009288      -33.77645    1                    
MTRIX3  12 -0.015791 -0.009407 -0.999831     -101.10145    1                    
MTRIX1  13  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  13  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  13  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  14  0.999770  0.020708 -0.005645      -69.57171    1                    
MTRIX2  14  0.020927 -0.998899  0.041993      -32.41103    1                    
MTRIX3  14 -0.004769 -0.042101 -0.999102     -102.54208    1                    
MTRIX1  15  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  15  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  15  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  16  0.999949  0.005613 -0.008454      -69.74738    1                    
MTRIX2  16  0.005913 -0.999340  0.035846      -31.27895    1                    
MTRIX3  16 -0.008247 -0.035894 -0.999322     -102.33206    1                    
MTRIX1  17  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  17  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  17  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  18  0.999991  0.003362 -0.002580      -69.43109    1                    
MTRIX2  18  0.003420 -0.999736  0.022699      -31.62110    1                    
MTRIX3  18 -0.002503 -0.022708 -0.999739     -103.19502    1                    
MTRIX1  19  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  19  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  19  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  20  0.999986  0.004790 -0.002046      -69.40063    1                    
MTRIX2  20  0.004825 -0.999835  0.017532      -31.93521    1                    
MTRIX3  20 -0.001962 -0.017542 -0.999844     -103.38629    1                    
MTRIX1  21  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  21  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  21  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  22  0.999960  0.008668  0.002178      -69.31293    1                    
MTRIX2  22  0.008613 -0.999672  0.024131      -31.88753    1                    
MTRIX3  22  0.002386 -0.024111 -0.999706     -103.47797    1                    
MTRIX1  23  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  23  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  23  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  24  0.999829  0.013438 -0.012708      -69.91234    1                    
MTRIX2  24  0.013793 -0.999505  0.028265      -31.87374    1                    
MTRIX3  24 -0.012322 -0.028436 -0.999520     -102.91549    1                    
MTRIX1  25  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  25  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  25  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  26  0.999966  0.008156  0.001065      -69.34023    1                    
MTRIX2  26  0.008131 -0.999718  0.022324      -31.89483    1                    
MTRIX3  26  0.001247 -0.022315 -0.999750     -103.45585    1                    
MTRIX1  27  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  27  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  27  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  28  0.999999  0.001063  0.000381      -69.29395    1                    
MTRIX2  28  0.001052 -0.999588  0.028693      -31.25392    1                    
MTRIX3  28  0.000411 -0.028693 -0.999588     -103.34526    1                    
MTRIX1  29  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  29  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  29  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  30  0.999959  0.007712 -0.004753      -69.59023    1                    
MTRIX2  30  0.007873 -0.999364  0.034765      -31.38136    1                    
MTRIX3  30 -0.004482 -0.034801 -0.999384     -102.99180    1                    
MTRIX1  31  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  31  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  31  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  32  0.999949  0.010037 -0.000649      -69.31687    1                    
MTRIX2  32  0.010048 -0.999736  0.020651      -32.35940    1                    
MTRIX3  32 -0.000442 -0.020657 -0.999786     -103.13526    1                    
MTRIX1  33  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  33  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  33  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  34  0.999955  0.004915  0.008095      -69.15533    1                    
MTRIX2  34  0.004914 -0.999988  0.000132      -32.97868    1                    
MTRIX3  34  0.008095 -0.000092 -0.999967     -103.12711    1                    
MTRIX1  35  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  35  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  35  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  36  0.998327 -0.034430  0.046460      -69.00101    1                    
MTRIX2  36 -0.034160 -0.999395 -0.006587      -29.43128    1                    
MTRIX3  36  0.046659  0.004989 -0.998898     -106.35061    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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