GenomeNet

Database: PDB
Entry: 4Y6Z
LinkDB: 4Y6Z
Original site: 4Y6Z 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-FEB-15   4Y6Z              
TITLE     YEAST 20S PROTEASOME IN COMPLEX WITH AC-PAL-EP                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND   3 CHAIN: A, O;                                                         
COMPND   4 SYNONYM: MACROPAIN SUBUNIT Y7,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND   5 SUBUNIT Y7,PROTEASOME COMPONENT Y7,PROTEINASE YSCE SUBUNIT 7;        
COMPND   6 EC: 3.4.25.1;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND   9 CHAIN: B, P;                                                         
COMPND  10 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  11 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;     
COMPND  12 EC: 3.4.25.1;                                                        
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND  15 CHAIN: C, Q;                                                         
COMPND  16 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  17 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6; 
COMPND  18 EC: 3.4.25.1;                                                        
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  21 CHAIN: D, R;                                                         
COMPND  22 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  23 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2; 
COMPND  24 EC: 3.4.25.1;                                                        
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  27 CHAIN: E, S;                                                         
COMPND  28 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  29 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5; 
COMPND  30 EC: 3.4.25.1;                                                        
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;                  
COMPND  33 CHAIN: F, T;                                                         
COMPND  34 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  35 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;        
COMPND  36 EC: 3.4.25.1;                                                        
COMPND  37 MOL_ID: 7;                                                           
COMPND  38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  39 CHAIN: G, U;                                                         
COMPND  40 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE     
COMPND  41 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,    
COMPND  42 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;                   
COMPND  43 EC: 3.4.25.1;                                                        
COMPND  44 MOL_ID: 8;                                                           
COMPND  45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  46 CHAIN: H, V;                                                         
COMPND  47 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  48 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1; 
COMPND  49 EC: 3.4.25.1;                                                        
COMPND  50 MOL_ID: 9;                                                           
COMPND  51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  52 CHAIN: I, W;                                                         
COMPND  53 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  54 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;                              
COMPND  55 EC: 3.4.25.1;                                                        
COMPND  56 MOL_ID: 10;                                                          
COMPND  57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  58 CHAIN: J, X;                                                         
COMPND  59 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  60 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;     
COMPND  61 EC: 3.4.25.1;                                                        
COMPND  62 MOL_ID: 11;                                                          
COMPND  63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  64 CHAIN: K, Y;                                                         
COMPND  65 SYNONYM: MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  66 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2; 
COMPND  67 EC: 3.4.25.1;                                                        
COMPND  68 MOL_ID: 12;                                                          
COMPND  69 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  70 CHAIN: L, Z;                                                         
COMPND  71 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME  
COMPND  72 COMPONENT C5;                                                        
COMPND  73 EC: 3.4.25.1;                                                        
COMPND  74 MOL_ID: 13;                                                          
COMPND  75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  76 CHAIN: M, a;                                                         
COMPND  77 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  78 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4; 
COMPND  79 EC: 3.4.25.1;                                                        
COMPND  80 MOL_ID: 14;                                                          
COMPND  81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  82 CHAIN: N, b;                                                         
COMPND  83 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  84 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3; 
COMPND  85 EC: 3.4.25.1;                                                        
COMPND  86 MOL_ID: 15;                                                          
COMPND  87 MOLECULE: AC-PAL-EP;                                                 
COMPND  88 CHAIN: c, d, e, f, g, h;                                             
COMPND  89 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   8 S288C);                                                              
SOURCE   9 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  10 ORGANISM_TAXID: 559292;                                              
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  13 S288C);                                                              
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 559292;                                              
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  18 S288C);                                                              
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  20 ORGANISM_TAXID: 559292;                                              
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  23 S288C);                                                              
SOURCE  24 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  25 ORGANISM_TAXID: 559292;                                              
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  28 S288C);                                                              
SOURCE  29 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  30 ORGANISM_TAXID: 559292;                                              
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  33 S288C);                                                              
SOURCE  34 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  35 ORGANISM_TAXID: 559292;                                              
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  38 S288C);                                                              
SOURCE  39 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  40 ORGANISM_TAXID: 559292;                                              
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  43 S288C);                                                              
SOURCE  44 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  45 ORGANISM_TAXID: 559292;                                              
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  48 S288C);                                                              
SOURCE  49 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  50 ORGANISM_TAXID: 559292;                                              
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  53 S288C);                                                              
SOURCE  54 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  55 ORGANISM_TAXID: 559292;                                              
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  58 S288C);                                                              
SOURCE  59 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  60 ORGANISM_TAXID: 559292;                                              
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  63 S288C);                                                              
SOURCE  64 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  65 ORGANISM_TAXID: 559292;                                              
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  68 S288C);                                                              
SOURCE  69 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  70 ORGANISM_TAXID: 559292;                                              
SOURCE  71 MOL_ID: 15;                                                          
SOURCE  72 SYNTHETIC: YES;                                                      
SOURCE  73 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  74 ORGANISM_TAXID: 32630                                                
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX, PROTEASOME, INHIBITOR, BINDING 
KEYWDS   2 ANALYSIS                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GROLL,E.M.HUBER                                                     
REVDAT   4   10-JAN-24 4Y6Z    1       REMARK                                   
REVDAT   3   15-NOV-23 4Y6Z    1       REMARK LINK   ATOM                       
REVDAT   2   01-JUL-15 4Y6Z    1       JRNL                                     
REVDAT   1   17-JUN-15 4Y6Z    0                                                
JRNL        AUTH   E.M.HUBER,G.DE BRUIN,W.HEINEMEYER,G.PANIAGUA SORIANO,        
JRNL        AUTH 2 H.S.OVERKLEEFT,M.GROLL                                       
JRNL        TITL   SYSTEMATIC ANALYSES OF SUBSTRATE PREFERENCES OF 20S          
JRNL        TITL 2 PROTEASOMES USING PEPTIDIC EPOXYKETONE INHIBITORS.           
JRNL        REF    J.AM.CHEM.SOC.                V. 137  7835 2015              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   26020686                                                     
JRNL        DOI    10.1021/JACS.5B03688                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 276851                         
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14572                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 20079                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1057                         
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 49458                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 427                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.11000                                              
REMARK   3    B22 (A**2) : -5.58000                                             
REMARK   3    B33 (A**2) : 1.97000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.51000                                             
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): 0.254         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.204         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.401        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 50400 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 48202 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 68214 ; 0.938 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):110994 ; 0.809 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6306 ; 5.229 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2246 ;34.864 ;24.408       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8736 ;15.413 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   284 ;14.876 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7692 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 57112 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11268 ; 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): 25314 ; 2.306 ; 5.510       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25313 ; 2.306 ; 5.510       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31590 ; 3.078 ; 8.252       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31591 ; 3.078 ; 8.252       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 25086 ; 2.269 ; 5.838       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 25086 ; 2.269 ; 5.838       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 36625 ; 2.855 ; 8.635       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 52935 ; 3.542 ;42.700       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 52893 ; 3.529 ;42.697       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 98602 ; 0.868 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   223 ;28.804 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 97907 ;16.514 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 14                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A O                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     500      1                      
REMARK   3           1     O      1       O     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    O (A**2):   3795 ; 5.080 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B P                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     500      1                      
REMARK   3           1     P      1       P     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      2    P (A**2):   3756 ; 4.220 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C Q                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C     500      1                      
REMARK   3           1     Q      1       Q     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      3    Q (A**2):   3729 ;10.140 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D R                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      1       D     500      1                      
REMARK   3           1     R      1       R     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      4    R (A**2):   3578 ; 6.100 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E S                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E      1       E     500      1                      
REMARK   3           1     S      1       S     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      5    S (A**2):   3509 ; 5.210 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F T                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F      1       F     500      1                      
REMARK   3           1     T      1       T     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      6    T (A**2):   3749 ; 5.680 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : G U                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G      1       G     500      1                      
REMARK   3           1     U      1       U     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      7    U (A**2):   3770 ; 4.210 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H V                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H      1       H     500      1                      
REMARK   3           1     V      1       V     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      8    V (A**2):   3394 ; 3.420 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I W                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I     500      1                      
REMARK   3           1     W      1       W     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      9    W (A**2):   3119 ; 3.160 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J X                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J     500      1                      
REMARK   3           1     X      1       X     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    O    (A):   3099 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL     10    X (A**2):   3099 ; 2.740 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K Y                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      1       K     500      1                      
REMARK   3           1     Y      1       Y     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    O    (A):   3259 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL     11    Y (A**2):   3259 ; 3.640 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L Z                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L     500      1                      
REMARK   3           1     Z      1       Z     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    O    (A):   3439 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL     12    Z (A**2):   3439 ; 3.290 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M a                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M     500      1                      
REMARK   3           1     a      1       a     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    O    (A):   3618 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL     13    a (A**2):   3618 ; 3.090 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N b                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     N      1       N     500      1                      
REMARK   3           1     b      1       b     500      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    O    (A):   3007 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL     14    b (A**2):   3007 ; 2.740 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2631 -92.5688  46.5089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0997 T22:   0.0307                                     
REMARK   3      T33:   0.0821 T12:  -0.0032                                     
REMARK   3      T13:   0.0020 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0389 L22:   0.0810                                     
REMARK   3      L33:   0.0266 L12:   0.0405                                     
REMARK   3      L13:   0.0293 L23:   0.0232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0006 S12:   0.0124 S13:  -0.0051                       
REMARK   3      S21:   0.0105 S22:   0.0066 S23:  -0.0287                       
REMARK   3      S31:   0.0001 S32:   0.0029 S33:  -0.0059                       
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     1        B   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1049 -88.4262  16.6931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0883 T22:   0.0378                                     
REMARK   3      T33:   0.0832 T12:  -0.0041                                     
REMARK   3      T13:   0.0134 T23:   0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0442 L22:   0.0355                                     
REMARK   3      L33:   0.0594 L12:   0.0351                                     
REMARK   3      L13:  -0.0028 L23:  -0.0122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:   0.0144 S13:   0.0002                       
REMARK   3      S21:  -0.0104 S22:  -0.0013 S23:  -0.0071                       
REMARK   3      S31:  -0.0072 S32:   0.0127 S33:  -0.0002                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8254 -87.9400   1.2023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0985 T22:   0.0354                                     
REMARK   3      T33:   0.0815 T12:   0.0061                                     
REMARK   3      T13:  -0.0067 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0130 L22:   0.0660                                     
REMARK   3      L33:   0.1204 L12:   0.0124                                     
REMARK   3      L13:  -0.0002 L23:  -0.0535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0053 S12:   0.0101 S13:   0.0131                       
REMARK   3      S21:  -0.0430 S22:   0.0008 S23:  -0.0047                       
REMARK   3      S31:   0.0083 S32:   0.0048 S33:  -0.0061                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3641 -90.5941  13.6003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0984 T22:   0.0362                                     
REMARK   3      T33:   0.0961 T12:   0.0049                                     
REMARK   3      T13:  -0.0185 T23:   0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0995 L22:   0.0626                                     
REMARK   3      L33:   0.0121 L12:   0.0330                                     
REMARK   3      L13:  -0.0234 L23:   0.0101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0030 S12:   0.0004 S13:   0.0170                       
REMARK   3      S21:  -0.0162 S22:  -0.0095 S23:   0.0699                       
REMARK   3      S31:  -0.0085 S32:  -0.0055 S33:   0.0125                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     3        E   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1557 -94.9038  45.7074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0669 T22:   0.0389                                     
REMARK   3      T33:   0.0943 T12:   0.0173                                     
REMARK   3      T13:   0.0270 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0410 L22:   0.0462                                     
REMARK   3      L33:   0.0003 L12:  -0.0418                                     
REMARK   3      L13:  -0.0020 L23:   0.0017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0042 S12:  -0.0046 S13:  -0.0057                       
REMARK   3      S21:   0.0120 S22:   0.0061 S23:   0.0238                       
REMARK   3      S31:   0.0024 S32:   0.0013 S33:  -0.0019                       
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 :   F     2        F   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1829 -95.4703  70.0881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0873 T22:   0.0311                                     
REMARK   3      T33:   0.0488 T12:   0.0051                                     
REMARK   3      T13:   0.0400 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0323 L22:   0.0499                                     
REMARK   3      L33:   0.0375 L12:   0.0009                                     
REMARK   3      L13:  -0.0278 L23:   0.0211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:   0.0009 S13:   0.0028                       
REMARK   3      S21:   0.0284 S22:  -0.0278 S23:   0.0250                       
REMARK   3      S31:  -0.0113 S32:  -0.0049 S33:  -0.0010                       
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 :   G     2        G   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.8053 -93.8690  71.5809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.0196                                     
REMARK   3      T33:   0.0593 T12:   0.0055                                     
REMARK   3      T13:   0.0143 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0185 L22:   0.0417                                     
REMARK   3      L33:   0.0232 L12:  -0.0170                                     
REMARK   3      L13:   0.0061 L23:   0.0168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0008 S12:   0.0022 S13:   0.0090                       
REMARK   3      S21:   0.0101 S22:  -0.0027 S23:  -0.0177                       
REMARK   3      S31:   0.0015 S32:  -0.0062 S33:   0.0036                       
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 :   H     1        H   222                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8325-130.7960  48.7377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0928 T22:   0.0283                                     
REMARK   3      T33:   0.0840 T12:   0.0038                                     
REMARK   3      T13:  -0.0063 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0028 L22:   0.0260                                     
REMARK   3      L33:   0.0186 L12:   0.0020                                     
REMARK   3      L13:  -0.0006 L23:   0.0145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0144 S12:   0.0040 S13:   0.0026                       
REMARK   3      S21:   0.0243 S22:  -0.0047 S23:  -0.0341                       
REMARK   3      S31:  -0.0018 S32:  -0.0085 S33:  -0.0097                       
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 :   I     1        I   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.7829-128.2050  21.4172              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0826 T22:   0.0400                                     
REMARK   3      T33:   0.0804 T12:  -0.0041                                     
REMARK   3      T13:   0.0187 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0125 L22:   0.0455                                     
REMARK   3      L33:   0.0692 L12:   0.0183                                     
REMARK   3      L13:   0.0264 L23:   0.0453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:   0.0044 S13:  -0.0045                       
REMARK   3      S21:  -0.0303 S22:  -0.0070 S23:  -0.0272                       
REMARK   3      S31:  -0.0275 S32:   0.0059 S33:   0.0069                       
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 :   J     1        J   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2675-127.3256  -0.2838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0973 T22:   0.0414                                     
REMARK   3      T33:   0.0761 T12:   0.0004                                     
REMARK   3      T13:   0.0041 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0668 L22:   0.1447                                     
REMARK   3      L33:   0.0823 L12:   0.0182                                     
REMARK   3      L13:   0.0733 L23:   0.0080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:   0.0096 S13:   0.0064                       
REMARK   3      S21:  -0.0327 S22:  -0.0064 S23:  -0.0037                       
REMARK   3      S31:  -0.0059 S32:   0.0088 S33:   0.0074                       
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 :   K     1        K   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3017-131.5804   2.5551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1115 T22:   0.0309                                     
REMARK   3      T33:   0.0837 T12:  -0.0040                                     
REMARK   3      T13:  -0.0130 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0833 L22:   0.0604                                     
REMARK   3      L33:   0.0510 L12:  -0.0464                                     
REMARK   3      L13:   0.0446 L23:  -0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0037 S12:   0.0116 S13:   0.0074                       
REMARK   3      S21:  -0.0446 S22:   0.0021 S23:   0.0204                       
REMARK   3      S31:   0.0017 S32:   0.0013 S33:  -0.0058                       
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 :   L     1        L   222                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3309-134.9087  28.6949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0828 T22:   0.0319                                     
REMARK   3      T33:   0.1064 T12:   0.0063                                     
REMARK   3      T13:  -0.0021 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1145 L22:   0.1051                                     
REMARK   3      L33:   0.1665 L12:   0.0986                                     
REMARK   3      L13:   0.0656 L23:   0.0323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0122 S12:  -0.0114 S13:   0.0077                       
REMARK   3      S21:   0.0045 S22:  -0.0071 S23:   0.0486                       
REMARK   3      S31:   0.0047 S32:  -0.0163 S33:  -0.0051                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   224                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8535-138.5072  60.6449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0838 T22:   0.0390                                     
REMARK   3      T33:   0.0758 T12:   0.0035                                     
REMARK   3      T13:   0.0230 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0659 L22:   0.2406                                     
REMARK   3      L33:   0.0587 L12:  -0.0565                                     
REMARK   3      L13:   0.0614 L23:  -0.0513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:  -0.0112 S13:   0.0079                       
REMARK   3      S21:   0.0459 S22:  -0.0092 S23:   0.0315                       
REMARK   3      S31:   0.0007 S32:  -0.0066 S33:   0.0024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9522-134.7382  71.1004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1105 T22:   0.0342                                     
REMARK   3      T33:   0.0604 T12:  -0.0001                                     
REMARK   3      T13:  -0.0064 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0918 L22:   0.1696                                     
REMARK   3      L33:   0.0434 L12:  -0.0489                                     
REMARK   3      L13:  -0.0430 L23:  -0.0311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:  -0.0175 S13:   0.0024                       
REMARK   3      S21:   0.0529 S22:   0.0043 S23:   0.0058                       
REMARK   3      S31:  -0.0114 S32:   0.0046 S33:  -0.0088                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     1        O   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7837-207.4340  36.9921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1031 T22:   0.0338                                     
REMARK   3      T33:   0.0919 T12:  -0.0064                                     
REMARK   3      T13:  -0.0116 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0873 L22:   0.1063                                     
REMARK   3      L33:   0.0851 L12:   0.0139                                     
REMARK   3      L13:  -0.0099 L23:   0.0893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:   0.0065 S13:  -0.0007                       
REMARK   3      S21:   0.0109 S22:  -0.0071 S23:   0.0225                       
REMARK   3      S31:   0.0221 S32:  -0.0125 S33:   0.0029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     1        P   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5061-206.3585   6.8927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1094 T22:   0.0387                                     
REMARK   3      T33:   0.0936 T12:  -0.0003                                     
REMARK   3      T13:  -0.0231 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0959 L22:   0.0198                                     
REMARK   3      L33:   0.0816 L12:   0.0269                                     
REMARK   3      L13:   0.0033 L23:  -0.0234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:   0.0171 S13:  -0.0059                       
REMARK   3      S21:  -0.0053 S22:  -0.0034 S23:   0.0000                       
REMARK   3      S31:   0.0027 S32:  -0.0191 S33:   0.0091                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     1        Q   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9399-204.4007  -8.8389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1225 T22:   0.0270                                     
REMARK   3      T33:   0.0682 T12:   0.0177                                     
REMARK   3      T13:  -0.0022 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0209 L22:   0.0928                                     
REMARK   3      L33:   0.1207 L12:  -0.0026                                     
REMARK   3      L13:   0.0228 L23:   0.0512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:   0.0017 S13:  -0.0222                       
REMARK   3      S21:  -0.0639 S22:  -0.0098 S23:   0.0432                       
REMARK   3      S31:  -0.0060 S32:   0.0043 S33:  -0.0004                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     1        R   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4394-203.8556   3.7455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0644 T22:   0.0250                                     
REMARK   3      T33:   0.0815 T12:   0.0282                                     
REMARK   3      T13:   0.0191 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0483 L22:   0.1159                                     
REMARK   3      L33:   0.0361 L12:  -0.0202                                     
REMARK   3      L13:  -0.0304 L23:  -0.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:  -0.0088 S13:   0.0004                       
REMARK   3      S21:  -0.0396 S22:  -0.0177 S23:  -0.0298                       
REMARK   3      S31:   0.0089 S32:   0.0104 S33:   0.0147                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     3        S   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.2377-205.0471  35.9212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0845 T22:   0.0397                                     
REMARK   3      T33:   0.1283 T12:   0.0227                                     
REMARK   3      T13:  -0.0049 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0540 L22:   0.0410                                     
REMARK   3      L33:   0.0169 L12:  -0.0377                                     
REMARK   3      L13:  -0.0204 L23:   0.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.0129 S13:  -0.0058                       
REMARK   3      S21:   0.0076 S22:   0.0245 S23:  -0.0386                       
REMARK   3      S31:   0.0131 S32:   0.0083 S33:  -0.0243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     2        T   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0575-208.6703  60.1677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1393 T22:   0.0179                                     
REMARK   3      T33:   0.1063 T12:  -0.0009                                     
REMARK   3      T13:  -0.0473 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1031 L22:   0.0514                                     
REMARK   3      L33:   0.0055 L12:   0.0712                                     
REMARK   3      L13:  -0.0065 L23:  -0.0012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0343 S12:  -0.0126 S13:  -0.0349                       
REMARK   3      S21:   0.0332 S22:  -0.0140 S23:  -0.0383                       
REMARK   3      S31:   0.0132 S32:  -0.0033 S33:  -0.0204                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     2        U   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5294-210.6409  61.5892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1197 T22:   0.0303                                     
REMARK   3      T33:   0.0859 T12:  -0.0022                                     
REMARK   3      T13:  -0.0164 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0086 L22:   0.1211                                     
REMARK   3      L33:   0.0826 L12:  -0.0256                                     
REMARK   3      L13:  -0.0008 L23:   0.0118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0015 S12:  -0.0113 S13:   0.0028                       
REMARK   3      S21:   0.0169 S22:   0.0093 S23:   0.0020                       
REMARK   3      S31:   0.0072 S32:  -0.0038 S33:  -0.0077                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V     1        V   222                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3803-170.2078  45.7101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.0318                                     
REMARK   3      T33:   0.0976 T12:  -0.0096                                     
REMARK   3      T13:   0.0037 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0014 L22:   0.0364                                     
REMARK   3      L33:   0.0427 L12:  -0.0013                                     
REMARK   3      L13:  -0.0004 L23:   0.0181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:  -0.0007 S13:  -0.0013                       
REMARK   3      S21:   0.0042 S22:  -0.0142 S23:   0.0472                       
REMARK   3      S31:   0.0129 S32:  -0.0032 S33:   0.0049                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1625-168.0677  18.2925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0899 T22:   0.0323                                     
REMARK   3      T33:   0.0925 T12:   0.0010                                     
REMARK   3      T13:  -0.0103 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0400 L22:   0.0383                                     
REMARK   3      L33:   0.1791 L12:   0.0047                                     
REMARK   3      L13:   0.0792 L23:  -0.0174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0077 S12:  -0.0008 S13:   0.0008                       
REMARK   3      S21:  -0.0209 S22:  -0.0034 S23:   0.0226                       
REMARK   3      S31:   0.0277 S32:  -0.0059 S33:  -0.0042                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4874-165.2245  -3.4819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1211 T22:   0.0360                                     
REMARK   3      T33:   0.0833 T12:   0.0025                                     
REMARK   3      T13:  -0.0163 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0723 L22:   0.0636                                     
REMARK   3      L33:   0.0100 L12:   0.0063                                     
REMARK   3      L13:  -0.0239 L23:   0.0043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.0049 S13:  -0.0005                       
REMARK   3      S21:  -0.0343 S22:  -0.0087 S23:   0.0371                       
REMARK   3      S31:  -0.0059 S32:   0.0039 S33:   0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     1        Y   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.4869-161.5352  -0.1996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0695 T22:   0.0296                                     
REMARK   3      T33:   0.0529 T12:   0.0143                                     
REMARK   3      T13:   0.0327 T23:  -0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0405 L22:   0.0977                                     
REMARK   3      L33:   0.1465 L12:   0.0098                                     
REMARK   3      L13:   0.0579 L23:   0.0882                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:   0.0181 S13:  -0.0057                       
REMARK   3      S21:  -0.0259 S22:  -0.0080 S23:  -0.0315                       
REMARK   3      S31:   0.0188 S32:   0.0083 S33:  -0.0151                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     1        Z   222                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3111-162.7010  25.9824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0658 T22:   0.0362                                     
REMARK   3      T33:   0.0811 T12:   0.0153                                     
REMARK   3      T13:   0.0137 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0558 L22:   0.2059                                     
REMARK   3      L33:   0.0137 L12:   0.0556                                     
REMARK   3      L13:  -0.0090 L23:  -0.0446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:   0.0054 S13:  -0.0066                       
REMARK   3      S21:  -0.0073 S22:   0.0027 S23:  -0.0381                       
REMARK   3      S31:   0.0089 S32:   0.0002 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   a     1        a   223                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.4401-164.6130  58.1746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0969 T22:   0.0385                                     
REMARK   3      T33:   0.0779 T12:   0.0017                                     
REMARK   3      T13:  -0.0101 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0238 L22:   0.2953                                     
REMARK   3      L33:   0.0134 L12:  -0.0546                                     
REMARK   3      L13:  -0.0016 L23:  -0.0042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0018 S12:  -0.0130 S13:  -0.0198                       
REMARK   3      S21:   0.0448 S22:   0.0063 S23:  -0.0261                       
REMARK   3      S31:   0.0112 S32:   0.0040 S33:  -0.0081                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   b     1        b   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4392-170.1217  68.1556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1000 T22:   0.0334                                     
REMARK   3      T33:   0.0616 T12:  -0.0060                                     
REMARK   3      T13:   0.0145 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0558 L22:   0.1680                                     
REMARK   3      L33:   0.0888 L12:   0.0121                                     
REMARK   3      L13:   0.0549 L23:   0.0835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.0051 S13:  -0.0089                       
REMARK   3      S21:   0.0440 S22:  -0.0007 S23:  -0.0142                       
REMARK   3      S31:   0.0212 S32:   0.0025 S33:  -0.0008                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4Y6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206955.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT. SI(111)     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 291423                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 1RYP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, 0.1 M MES, PH      
REMARK 280  6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      150.78500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 34-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,         
REMARK 350                    AND CHAINS: d, e, f, g, h                         
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     MET B     0                                                      
REMARK 465     LYS B   245                                                      
REMARK 465     LYS B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 465     GLU B   248                                                      
REMARK 465     ASP B   249                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     ASP B   255                                                      
REMARK 465     MET B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     GLN C   241                                                      
REMARK 465     GLN C   242                                                      
REMARK 465     GLU C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     ASP C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     LYS C   247                                                      
REMARK 465     LYS C   248                                                      
REMARK 465     LYS C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     ASN C   251                                                      
REMARK 465     HIS C   252                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     PHE D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     THR D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLU D    -1                                                      
REMARK 465     TYR D     0                                                      
REMARK 465     GLY D   118                                                      
REMARK 465     ALA D   119                                                      
REMARK 465     SER D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     GLU D   123                                                      
REMARK 465     ARG D   124                                                      
REMARK 465     SER D   243                                                      
REMARK 465     PRO D   244                                                      
REMARK 465     GLU D   245                                                      
REMARK 465     GLU D   246                                                      
REMARK 465     ALA D   247                                                      
REMARK 465     ASP D   248                                                      
REMARK 465     VAL D   249                                                      
REMARK 465     GLU D   250                                                      
REMARK 465     MET D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     MET E     0                                                      
REMARK 465     PHE E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     MET F    -3                                                      
REMARK 465     THR F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     ILE F     0                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     GLY F   245                                                      
REMARK 465     ASP F   246                                                      
REMARK 465     ASP F   247                                                      
REMARK 465     ASP F   248                                                      
REMARK 465     GLU F   249                                                      
REMARK 465     ASP F   250                                                      
REMARK 465     GLU F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     ASP F   253                                                      
REMARK 465     SER F   254                                                      
REMARK 465     ASP F   255                                                      
REMARK 465     ASN F   256                                                      
REMARK 465     VAL F   257                                                      
REMARK 465     MET F   258                                                      
REMARK 465     SER F   259                                                      
REMARK 465     SER F   260                                                      
REMARK 465     ASP F   261                                                      
REMARK 465     ASP F   262                                                      
REMARK 465     GLU F   263                                                      
REMARK 465     ASN F   264                                                      
REMARK 465     ALA F   265                                                      
REMARK 465     PRO F   266                                                      
REMARK 465     VAL F   267                                                      
REMARK 465     ALA F   268                                                      
REMARK 465     THR F   269                                                      
REMARK 465     ASN F   270                                                      
REMARK 465     ALA F   271                                                      
REMARK 465     ASN F   272                                                      
REMARK 465     ALA F   273                                                      
REMARK 465     THR F   274                                                      
REMARK 465     THR F   275                                                      
REMARK 465     ASP F   276                                                      
REMARK 465     GLN F   277                                                      
REMARK 465     GLU F   278                                                      
REMARK 465     GLY F   279                                                      
REMARK 465     ASP F   280                                                      
REMARK 465     ILE F   281                                                      
REMARK 465     HIS F   282                                                      
REMARK 465     LEU F   283                                                      
REMARK 465     GLU F   284                                                      
REMARK 465     MET G    -8                                                      
REMARK 465     SER G    -7                                                      
REMARK 465     GLY G    -6                                                      
REMARK 465     ALA G    -5                                                      
REMARK 465     ALA G    -4                                                      
REMARK 465     ALA G    -3                                                      
REMARK 465     ALA G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     ALA G     0                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     ASP G   243                                                      
REMARK 465     ILE H   223                                                      
REMARK 465     GLN H   224                                                      
REMARK 465     GLU H   225                                                      
REMARK 465     GLU H   226                                                      
REMARK 465     GLN H   227                                                      
REMARK 465     VAL H   228                                                      
REMARK 465     ASP H   229                                                      
REMARK 465     ILE H   230                                                      
REMARK 465     THR H   231                                                      
REMARK 465     ALA H   232                                                      
REMARK 465     MET I     0                                                      
REMARK 465     GLN J   196                                                      
REMARK 465     ALA J   197                                                      
REMARK 465     GLN J   198                                                      
REMARK 465     THR M   -12                                                      
REMARK 465     GLN M   -11                                                      
REMARK 465     ILE M   -10                                                      
REMARK 465     ALA M    -9                                                      
REMARK 465     ASN M    -8                                                      
REMARK 465     ALA M    -7                                                      
REMARK 465     GLY M    -6                                                      
REMARK 465     ALA M    -5                                                      
REMARK 465     SER M    -4                                                      
REMARK 465     PRO M    -3                                                      
REMARK 465     MET M    -2                                                      
REMARK 465     VAL M    -1                                                      
REMARK 465     ASN M     0                                                      
REMARK 465     MET P     0                                                      
REMARK 465     LYS P   245                                                      
REMARK 465     LYS P   246                                                      
REMARK 465     ASP P   247                                                      
REMARK 465     GLU P   248                                                      
REMARK 465     ASP P   249                                                      
REMARK 465     GLU P   250                                                      
REMARK 465     GLU P   251                                                      
REMARK 465     ALA P   252                                                      
REMARK 465     ASP P   253                                                      
REMARK 465     GLU P   254                                                      
REMARK 465     ASP P   255                                                      
REMARK 465     MET P   256                                                      
REMARK 465     LYS P   257                                                      
REMARK 465     MET Q    -1                                                      
REMARK 465     SER Q     0                                                      
REMARK 465     GLN Q   241                                                      
REMARK 465     GLN Q   242                                                      
REMARK 465     GLU Q   243                                                      
REMARK 465     GLN Q   244                                                      
REMARK 465     ASP Q   245                                                      
REMARK 465     LYS Q   246                                                      
REMARK 465     LYS Q   247                                                      
REMARK 465     LYS Q   248                                                      
REMARK 465     LYS Q   249                                                      
REMARK 465     SER Q   250                                                      
REMARK 465     ASN Q   251                                                      
REMARK 465     HIS Q   252                                                      
REMARK 465     MET R    -7                                                      
REMARK 465     PHE R    -6                                                      
REMARK 465     LEU R    -5                                                      
REMARK 465     THR R    -4                                                      
REMARK 465     ARG R    -3                                                      
REMARK 465     SER R    -2                                                      
REMARK 465     GLU R    -1                                                      
REMARK 465     TYR R     0                                                      
REMARK 465     GLY R   118                                                      
REMARK 465     ALA R   119                                                      
REMARK 465     SER R   120                                                      
REMARK 465     GLY R   121                                                      
REMARK 465     GLU R   122                                                      
REMARK 465     GLU R   123                                                      
REMARK 465     ARG R   124                                                      
REMARK 465     SER R   243                                                      
REMARK 465     PRO R   244                                                      
REMARK 465     GLU R   245                                                      
REMARK 465     GLU R   246                                                      
REMARK 465     ALA R   247                                                      
REMARK 465     ASP R   248                                                      
REMARK 465     VAL R   249                                                      
REMARK 465     GLU R   250                                                      
REMARK 465     MET R   251                                                      
REMARK 465     SER R   252                                                      
REMARK 465     MET S     0                                                      
REMARK 465     PHE S     1                                                      
REMARK 465     ARG S     2                                                      
REMARK 465     MET T    -3                                                      
REMARK 465     THR T    -2                                                      
REMARK 465     SER T    -1                                                      
REMARK 465     ILE T     0                                                      
REMARK 465     GLY T     1                                                      
REMARK 465     GLY T   245                                                      
REMARK 465     ASP T   246                                                      
REMARK 465     ASP T   247                                                      
REMARK 465     ASP T   248                                                      
REMARK 465     GLU T   249                                                      
REMARK 465     ASP T   250                                                      
REMARK 465     GLU T   251                                                      
REMARK 465     ASP T   252                                                      
REMARK 465     ASP T   253                                                      
REMARK 465     SER T   254                                                      
REMARK 465     ASP T   255                                                      
REMARK 465     ASN T   256                                                      
REMARK 465     VAL T   257                                                      
REMARK 465     MET T   258                                                      
REMARK 465     SER T   259                                                      
REMARK 465     SER T   260                                                      
REMARK 465     ASP T   261                                                      
REMARK 465     ASP T   262                                                      
REMARK 465     GLU T   263                                                      
REMARK 465     ASN T   264                                                      
REMARK 465     ALA T   265                                                      
REMARK 465     PRO T   266                                                      
REMARK 465     VAL T   267                                                      
REMARK 465     ALA T   268                                                      
REMARK 465     THR T   269                                                      
REMARK 465     ASN T   270                                                      
REMARK 465     ALA T   271                                                      
REMARK 465     ASN T   272                                                      
REMARK 465     ALA T   273                                                      
REMARK 465     THR T   274                                                      
REMARK 465     THR T   275                                                      
REMARK 465     ASP T   276                                                      
REMARK 465     GLN T   277                                                      
REMARK 465     GLU T   278                                                      
REMARK 465     GLY T   279                                                      
REMARK 465     ASP T   280                                                      
REMARK 465     ILE T   281                                                      
REMARK 465     HIS T   282                                                      
REMARK 465     LEU T   283                                                      
REMARK 465     GLU T   284                                                      
REMARK 465     MET U    -8                                                      
REMARK 465     SER U    -7                                                      
REMARK 465     GLY U    -6                                                      
REMARK 465     ALA U    -5                                                      
REMARK 465     ALA U    -4                                                      
REMARK 465     ALA U    -3                                                      
REMARK 465     ALA U    -2                                                      
REMARK 465     SER U    -1                                                      
REMARK 465     ALA U     0                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     ASP U   243                                                      
REMARK 465     ILE V   223                                                      
REMARK 465     GLN V   224                                                      
REMARK 465     GLU V   225                                                      
REMARK 465     GLU V   226                                                      
REMARK 465     GLN V   227                                                      
REMARK 465     VAL V   228                                                      
REMARK 465     ASP V   229                                                      
REMARK 465     ILE V   230                                                      
REMARK 465     THR V   231                                                      
REMARK 465     ALA V   232                                                      
REMARK 465     MET W     0                                                      
REMARK 465     GLN X   196                                                      
REMARK 465     ALA X   197                                                      
REMARK 465     GLN X   198                                                      
REMARK 465     THR a   -12                                                      
REMARK 465     GLN a   -11                                                      
REMARK 465     ILE a   -10                                                      
REMARK 465     ALA a    -9                                                      
REMARK 465     ASN a    -8                                                      
REMARK 465     ALA a    -7                                                      
REMARK 465     GLY a    -6                                                      
REMARK 465     ALA a    -5                                                      
REMARK 465     SER a    -4                                                      
REMARK 465     PRO a    -3                                                      
REMARK 465     MET a    -2                                                      
REMARK 465     VAL a    -1                                                      
REMARK 465     ASN a     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR K     1     O    DCL d     4              2.16            
REMARK 500   OG1  THR Y     1     O    DCL g     4              2.18            
REMARK 500   OG1  THR N     1     O    DCL e     4              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO c   2   CA    PRO c   2   C      -0.133                       
REMARK 500    PRO d   2   CA    PRO d   2   C      -0.167                       
REMARK 500    PRO e   2   CA    PRO e   2   C      -0.167                       
REMARK 500    PRO f   2   CA    PRO f   2   C      -0.126                       
REMARK 500    PRO g   2   CA    PRO g   2   C      -0.170                       
REMARK 500    PRO h   2   CA    PRO h   2   C      -0.121                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO f   2   CA  -  N   -  CD  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A   2      149.97     66.40                                   
REMARK 500    ASP A   3       98.95    -57.86                                   
REMARK 500    TYR A  97      -62.87   -145.11                                   
REMARK 500    ALA A 249       53.43    -91.15                                   
REMARK 500    ARG B   8       71.26     57.39                                   
REMARK 500    THR B  10       52.25   -115.29                                   
REMARK 500    VAL B  51      105.07    -13.60                                   
REMARK 500    THR B  60       31.32    -84.74                                   
REMARK 500    GLU B  63      -38.01   -136.20                                   
REMARK 500    ALA B 219     -157.32    -83.12                                   
REMARK 500    ASP B 221      107.68     69.18                                   
REMARK 500    ARG C   4      127.77    -39.53                                   
REMARK 500    ASN C  38       21.59   -142.59                                   
REMARK 500    LEU C  52       15.06     80.22                                   
REMARK 500    PRO C 183      109.28    -40.64                                   
REMARK 500    GLN C 202     -104.53    139.01                                   
REMARK 500    ALA C 205     -120.64    -81.05                                   
REMARK 500    LYS C 206       41.83    -88.18                                   
REMARK 500    GLN C 239       82.42    -69.08                                   
REMARK 500    ARG D  45       75.46     56.38                                   
REMARK 500    SER E  39     -154.24   -109.10                                   
REMARK 500    ASP E 137     -159.84   -130.31                                   
REMARK 500    ASN E 184       89.74   -150.28                                   
REMARK 500    ASP E 202      -20.12     64.75                                   
REMARK 500    SER F   9       -4.10     83.07                                   
REMARK 500    ASP F  67     -134.20     56.66                                   
REMARK 500    LYS F 100      -55.20     75.16                                   
REMARK 500    ASP F 138     -166.21   -129.90                                   
REMARK 500    ASN F 203       40.50   -156.01                                   
REMARK 500    LYS G 165       47.50   -103.57                                   
REMARK 500    GLU G 241       36.23    -84.66                                   
REMARK 500    ASN H   9      -67.47    -28.55                                   
REMARK 500    SER H 171     -112.73     64.47                                   
REMARK 500    GLN I  31     -111.35     51.23                                   
REMARK 500    ARG I  97       47.99   -104.42                                   
REMARK 500    ASP I 134      -68.70   -104.70                                   
REMARK 500    ASP I 192       38.65   -146.44                                   
REMARK 500    GLN I 203       42.59   -108.03                                   
REMARK 500    ASP J   2      -72.62    137.01                                   
REMARK 500    VAL J   9     -164.20   -112.64                                   
REMARK 500    SER J  31       29.47   -141.78                                   
REMARK 500    LYS J  34       56.46    -91.60                                   
REMARK 500    SER K  18       24.17   -141.10                                   
REMARK 500    GLU K  72      141.05   -170.10                                   
REMARK 500    ASP L  32     -118.49     54.38                                   
REMARK 500    LYS L 100       43.15   -109.53                                   
REMARK 500    PHE L 103       69.38   -161.66                                   
REMARK 500    ASP L 200      -62.82     68.99                                   
REMARK 500    ILE M   5      -78.37   -106.83                                   
REMARK 500    THR M   9     -151.95    -89.59                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     103 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G   8   OG1                                                    
REMARK 620 2 TYR G 119   O    75.4                                              
REMARK 620 3 ARG G 122   O    75.4  68.1                                        
REMARK 620 4 MET G 125   O   148.3  74.3  84.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA I 174   O                                                      
REMARK 620 2 ASP I 177   O    67.9                                              
REMARK 620 3 SER I 180   O    91.9  81.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 204   O                                                      
REMARK 620 2 ALA Y 165   O    96.8                                              
REMARK 620 3 ASP Y 168   O   162.6  98.7                                        
REMARK 620 4 SER Y 171   O    87.7  86.0  85.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA K 165   O                                                      
REMARK 620 2 ASP K 168   O    97.4                                              
REMARK 620 3 SER K 171   O    88.3  88.6                                        
REMARK 620 4 ASP W 204   O    97.3 165.3  91.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 222   OXT                                                    
REMARK 620 2 ILE V 163   O    92.7                                              
REMARK 620 3 ASP V 166   O   139.8 122.7                                        
REMARK 620 4 SER V 169   O    82.9  90.7  78.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG N 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE N 163   O                                                      
REMARK 620 2 ASP N 166   O    71.2                                              
REMARK 620 3 SER N 169   O   101.1  74.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Z 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR Z 192   O                                                      
REMARK 620 2 HIS Z 195   O    85.4                                              
REMARK 620 3 VAL Z 198   O   105.1  84.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES K 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES Y 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL c 5 through   
REMARK 800  ALA c 3 bound to THR H 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL c 4 bound to THR H 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL d 5 through   
REMARK 800  ALA d 3 bound to THR K 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL d 4 bound to THR K 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL e 5 through   
REMARK 800  ALA e 3 bound to THR N 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL e 4 bound to THR N 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL f 5 through   
REMARK 800  ALA f 3 bound to THR V 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL f 4 bound to THR V 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL g 5 through   
REMARK 800  ALA g 3 bound to THR Y 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL g 4 bound to THR Y 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues POL h 5 through   
REMARK 800  ALA h 3 bound to THR b 1                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand DCL h 4 bound to THR b 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE c 1 and PRO c 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE d 1 and PRO d 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE e 1 and PRO e 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE f 1 and PRO f 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE g 1 and PRO g 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE h 1 and PRO h 2    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RYP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS  
REMARK 900 RESOLUTION                                                           
DBREF  4Y6Z A    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  4Y6Z B    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  4Y6Z C   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  4Y6Z D   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  4Y6Z E    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  4Y6Z F   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  4Y6Z G   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  4Y6Z H    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  4Y6Z I    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  4Y6Z J    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  4Y6Z K    1   212  UNP    P30656   PSB5_YEAST      76    287             
DBREF  4Y6Z L    1   222  UNP    P23724   PSB6_YEAST      20    241             
DBREF  4Y6Z M  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  4Y6Z N    1   196  UNP    P38624   PSB1_YEAST      20    215             
DBREF  4Y6Z O    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  4Y6Z P    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  4Y6Z Q   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  4Y6Z R   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  4Y6Z S    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  4Y6Z T   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  4Y6Z U   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  4Y6Z V    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  4Y6Z W    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  4Y6Z X    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  4Y6Z Y    1   212  UNP    P30656   PSB5_YEAST      76    287             
DBREF  4Y6Z Z    1   222  UNP    P23724   PSB6_YEAST      20    241             
DBREF  4Y6Z a  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  4Y6Z b    1   196  UNP    P38624   PSB1_YEAST      20    215             
DBREF  4Y6Z c    1     5  PDB    4Y6Z     4Y6Z             1      5             
DBREF  4Y6Z d    1     5  PDB    4Y6Z     4Y6Z             1      5             
DBREF  4Y6Z e    1     5  PDB    4Y6Z     4Y6Z             1      5             
DBREF  4Y6Z f    1     5  PDB    4Y6Z     4Y6Z             1      5             
DBREF  4Y6Z g    1     5  PDB    4Y6Z     4Y6Z             1      5             
DBREF  4Y6Z h    1     5  PDB    4Y6Z     4Y6Z             1      5             
SEQRES   1 A  250  MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER          
SEQRES   2 A  250  PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR          
SEQRES   3 A  250  ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA          
SEQRES   4 A  250  THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER          
SEQRES   5 A  250  SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER          
SEQRES   6 A  250  LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET          
SEQRES   7 A  250  GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS          
SEQRES   8 A  250  VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR          
SEQRES   9 A  250  PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE          
SEQRES  10 A  250  MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 A  250  GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN          
SEQRES  12 A  250  GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR          
SEQRES  13 A  250  PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL          
SEQRES  14 A  250  ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU          
SEQRES  15 A  250  LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR          
SEQRES  16 A  250  LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR          
SEQRES  17 A  250  ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU          
SEQRES  18 A  250  LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG          
SEQRES  19 A  250  PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU          
SEQRES  20 A  250  GLU ALA LEU                                                  
SEQRES   1 B  258  MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE          
SEQRES   2 B  258  SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU          
SEQRES   3 B  258  GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET          
SEQRES   4 B  258  ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL          
SEQRES   5 B  258  THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS          
SEQRES   6 B  258  LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA          
SEQRES   7 B  258  GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA          
SEQRES   8 B  258  ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU          
SEQRES   9 B  258  ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP          
SEQRES  10 B  258  ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO          
SEQRES  11 B  258  PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG          
SEQRES  12 B  258  TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN          
SEQRES  13 B  258  TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR          
SEQRES  14 B  258  SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP          
SEQRES  15 B  258  ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS          
SEQRES  16 B  258  THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR          
SEQRES  17 B  258  ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN          
SEQRES  18 B  258  ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU          
SEQRES  19 B  258  ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS          
SEQRES  20 B  258  ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS                  
SEQRES   1 C  254  MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO          
SEQRES   2 C  254  ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA          
SEQRES   3 C  254  VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS          
SEQRES   4 C  254  ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU          
SEQRES   5 C  254  LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER          
SEQRES   6 C  254  LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU          
SEQRES   7 C  254  ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL          
SEQRES   8 C  254  GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL          
SEQRES   9 C  254  THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN          
SEQRES  10 C  254  GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY          
SEQRES  11 C  254  VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP          
SEQRES  12 C  254  GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR          
SEQRES  13 C  254  SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS          
SEQRES  14 C  254  THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS          
SEQRES  15 C  254  GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR          
SEQRES  16 C  254  VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS          
SEQRES  17 C  254  ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE          
SEQRES  18 C  254  VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR          
SEQRES  19 C  254  GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP          
SEQRES  20 C  254  LYS LYS LYS LYS SER ASN HIS                                  
SEQRES   1 D  260  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER          
SEQRES   2 D  260  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 D  260  SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 D  260  ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS          
SEQRES   5 D  260  ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU          
SEQRES   6 D  260  LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET          
SEQRES   7 D  260  SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS          
SEQRES   8 D  260  ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP          
SEQRES   9 D  260  GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS          
SEQRES  10 D  260  ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU          
SEQRES  11 D  260  GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU          
SEQRES  12 D  260  ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE          
SEQRES  13 D  260  HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA          
SEQRES  14 D  260  LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU          
SEQRES  15 D  260  LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU          
SEQRES  16 D  260  ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET          
SEQRES  17 D  260  GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS          
SEQRES  18 D  260  ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU          
SEQRES  19 D  260  LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU          
SEQRES  20 D  260  ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER          
SEQRES   1 E  234  MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE          
SEQRES   2 E  234  SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU          
SEQRES   3 E  234  GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG          
SEQRES   4 E  234  SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN          
SEQRES   5 E  234  ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS          
SEQRES   6 E  234  CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA          
SEQRES   7 E  234  PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN          
SEQRES   8 E  234  CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA          
SEQRES   9 E  234  VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN          
SEQRES  10 E  234  LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL          
SEQRES  11 E  234  GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS          
SEQRES  12 E  234  LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU          
SEQRES  13 E  234  TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS          
SEQRES  14 E  234  THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE          
SEQRES  15 E  234  ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU          
SEQRES  16 E  234  ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL          
SEQRES  17 E  234  ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO          
SEQRES  18 E  234  PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE          
SEQRES   1 F  288  MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER          
SEQRES   2 F  288  VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR          
SEQRES   3 F  288  ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY          
SEQRES   4 F  288  ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS          
SEQRES   5 F  288  LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL          
SEQRES   6 F  288  LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR          
SEQRES   7 F  288  SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG          
SEQRES   8 F  288  GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS          
SEQRES   9 F  288  THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY          
SEQRES  10 F  288  GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG          
SEQRES  11 F  288  PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS          
SEQRES  12 F  288  ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER          
SEQRES  13 F  288  TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG          
SEQRES  14 F  288  GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS          
SEQRES  15 F  288  HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN          
SEQRES  16 F  288  ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS          
SEQRES  17 F  288  GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU          
SEQRES  18 F  288  SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP          
SEQRES  19 F  288  LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE          
SEQRES  20 F  288  ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN          
SEQRES  21 F  288  VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR          
SEQRES  22 F  288  ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS          
SEQRES  23 F  288  LEU GLU                                                      
SEQRES   1 G  252  MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP          
SEQRES   2 G  252  ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR          
SEQRES   3 G  252  GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN          
SEQRES   4 G  252  ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL          
SEQRES   5 G  252  VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP          
SEQRES   6 G  252  PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR          
SEQRES   7 G  252  ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG          
SEQRES   8 G  252  ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE          
SEQRES   9 G  252  ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU          
SEQRES  10 G  252  ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN          
SEQRES  11 G  252  ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE          
SEQRES  12 G  252  VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS          
SEQRES  13 G  252  THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR          
SEQRES  14 G  252  ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU          
SEQRES  15 G  252  GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN          
SEQRES  16 G  252  GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR          
SEQRES  17 G  252  HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN          
SEQRES  18 G  252  ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE          
SEQRES  19 G  252  THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA          
SEQRES  20 G  252  ILE ALA GLU GLN ASP                                          
SEQRES   1 H  232  THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL          
SEQRES   2 H  232  ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL          
SEQRES   3 H  232  ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO          
SEQRES   4 H  232  LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 H  232  GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU          
SEQRES   6 H  232  HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER          
SEQRES   7 H  232  ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN          
SEQRES   8 H  232  GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP          
SEQRES   9 H  232  PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY          
SEQRES  10 H  232  SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY          
SEQRES  11 H  232  SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS          
SEQRES  12 H  232  GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER          
SEQRES  13 H  232  ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER          
SEQRES  14 H  232  GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS          
SEQRES  15 H  232  ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL          
SEQRES  16 H  232  ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY          
SEQRES  17 H  232  THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS          
SEQRES  18 H  232  ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA                  
SEQRES   1 I  205  MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL          
SEQRES   2 I  205  ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP          
SEQRES   3 I  205  LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS          
SEQRES   4 I  205  PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY          
SEQRES   5 I  205  ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU          
SEQRES   6 I  205  MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU          
SEQRES   7 I  205  GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL          
SEQRES   8 I  205  SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE          
SEQRES   9 I  205  VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY          
SEQRES  10 I  205  LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE          
SEQRES  11 I  205  ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER          
SEQRES  12 I  205  ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO          
SEQRES  13 I  205  ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN          
SEQRES  14 I  205  ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY          
SEQRES  15 I  205  TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL          
SEQRES  16 I  205  VAL LYS ARG TYR LEU LYS MET ARG GLN ASP                      
SEQRES   1 J  198  MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL          
SEQRES   2 J  198  ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER          
SEQRES   3 J  198  VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER          
SEQRES   4 J  198  PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP          
SEQRES   5 J  198  THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN          
SEQRES   6 J  198  LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN          
SEQRES   7 J  198  ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER          
SEQRES   8 J  198  ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE          
SEQRES   9 J  198  GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR          
SEQRES  10 J  198  GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR          
SEQRES  11 J  198  GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU          
SEQRES  12 J  198  LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU          
SEQRES  13 J  198  GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU          
SEQRES  14 J  198  LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS          
SEQRES  15 J  198  ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE          
SEQRES  16 J  198  GLN ALA GLN                                                  
SEQRES   1 K  212  THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE          
SEQRES   2 K  212  VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL          
SEQRES   3 K  212  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  212  PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 K  212  GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU          
SEQRES   6 K  212  HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 K  212  ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS          
SEQRES   8 K  212  GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR          
SEQRES   9 K  212  THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER          
SEQRES  10 K  212  ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY          
SEQRES  11 K  212  SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN          
SEQRES  12 K  212  TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU          
SEQRES  13 K  212  GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA          
SEQRES  14 K  212  TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU          
SEQRES  15 K  212  ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU          
SEQRES  16 K  212  LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN          
SEQRES  17 K  212  ASN VAL ILE GLY                                              
SEQRES   1 L  222  GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU          
SEQRES   2 L  222  GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP          
SEQRES   3 L  222  THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR          
SEQRES   4 L  222  GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET          
SEQRES   5 L  222  SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL          
SEQRES   6 L  222  LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP          
SEQRES   7 L  222  HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG          
SEQRES   8 L  222  ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO          
SEQRES   9 L  222  TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP          
SEQRES  10 L  222  GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER          
SEQRES  11 L  222  TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA          
SEQRES  12 L  222  SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE          
SEQRES  13 L  222  LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS          
SEQRES  14 L  222  LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS          
SEQRES  15 L  222  LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS          
SEQRES  16 L  222  ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR          
SEQRES  17 L  222  LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG          
SEQRES  18 L  222  ASP                                                          
SEQRES   1 M  246  THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN          
SEQRES   2 M  246  THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER          
SEQRES   3 M  246  MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN          
SEQRES   4 M  246  LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL          
SEQRES   5 M  246  GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY          
SEQRES   6 M  246  ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG          
SEQRES   7 M  246  LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN          
SEQRES   8 M  246  PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR          
SEQRES   9 M  246  ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG          
SEQRES  10 M  246  SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA          
SEQRES  11 M  246  GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL          
SEQRES  12 M  246  ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA          
SEQRES  13 M  246  THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG          
SEQRES  14 M  246  LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR          
SEQRES  15 M  246  VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG          
SEQRES  16 M  246  VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE          
SEQRES  17 M  246  SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE          
SEQRES  18 M  246  LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE          
SEQRES  19 M  246  ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE              
SEQRES   1 N  196  THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE          
SEQRES   2 N  196  LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE          
SEQRES   3 N  196  ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP          
SEQRES   4 N  196  LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  196  GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU          
SEQRES   6 N  196  TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA          
SEQRES   7 N  196  ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP          
SEQRES   8 N  196  ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP          
SEQRES   9 N  196  LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY          
SEQRES  10 N  196  SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY          
SEQRES  11 N  196  SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG          
SEQRES  12 N  196  GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS          
SEQRES  13 N  196  HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER          
SEQRES  14 N  196  GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY          
SEQRES  15 N  196  VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN          
SEQRES  16 N  196  LEU                                                          
SEQRES   1 O  250  MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER          
SEQRES   2 O  250  PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR          
SEQRES   3 O  250  ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA          
SEQRES   4 O  250  THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER          
SEQRES   5 O  250  SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER          
SEQRES   6 O  250  LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET          
SEQRES   7 O  250  GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS          
SEQRES   8 O  250  VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR          
SEQRES   9 O  250  PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE          
SEQRES  10 O  250  MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 O  250  GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN          
SEQRES  12 O  250  GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR          
SEQRES  13 O  250  PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL          
SEQRES  14 O  250  ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU          
SEQRES  15 O  250  LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR          
SEQRES  16 O  250  LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR          
SEQRES  17 O  250  ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU          
SEQRES  18 O  250  LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG          
SEQRES  19 O  250  PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU          
SEQRES  20 O  250  GLU ALA LEU                                                  
SEQRES   1 P  258  MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE          
SEQRES   2 P  258  SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU          
SEQRES   3 P  258  GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET          
SEQRES   4 P  258  ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL          
SEQRES   5 P  258  THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS          
SEQRES   6 P  258  LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA          
SEQRES   7 P  258  GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA          
SEQRES   8 P  258  ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU          
SEQRES   9 P  258  ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP          
SEQRES  10 P  258  ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO          
SEQRES  11 P  258  PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG          
SEQRES  12 P  258  TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN          
SEQRES  13 P  258  TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR          
SEQRES  14 P  258  SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP          
SEQRES  15 P  258  ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS          
SEQRES  16 P  258  THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR          
SEQRES  17 P  258  ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN          
SEQRES  18 P  258  ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU          
SEQRES  19 P  258  ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS          
SEQRES  20 P  258  ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS                  
SEQRES   1 Q  254  MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO          
SEQRES   2 Q  254  ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA          
SEQRES   3 Q  254  VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS          
SEQRES   4 Q  254  ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU          
SEQRES   5 Q  254  LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER          
SEQRES   6 Q  254  LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU          
SEQRES   7 Q  254  ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL          
SEQRES   8 Q  254  GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL          
SEQRES   9 Q  254  THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN          
SEQRES  10 Q  254  GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY          
SEQRES  11 Q  254  VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP          
SEQRES  12 Q  254  GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR          
SEQRES  13 Q  254  SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS          
SEQRES  14 Q  254  THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS          
SEQRES  15 Q  254  GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR          
SEQRES  16 Q  254  VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS          
SEQRES  17 Q  254  ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE          
SEQRES  18 Q  254  VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR          
SEQRES  19 Q  254  GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP          
SEQRES  20 Q  254  LYS LYS LYS LYS SER ASN HIS                                  
SEQRES   1 R  260  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER          
SEQRES   2 R  260  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 R  260  SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 R  260  ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS          
SEQRES   5 R  260  ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU          
SEQRES   6 R  260  LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET          
SEQRES   7 R  260  SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS          
SEQRES   8 R  260  ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP          
SEQRES   9 R  260  GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS          
SEQRES  10 R  260  ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU          
SEQRES  11 R  260  GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU          
SEQRES  12 R  260  ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE          
SEQRES  13 R  260  HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA          
SEQRES  14 R  260  LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU          
SEQRES  15 R  260  LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU          
SEQRES  16 R  260  ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET          
SEQRES  17 R  260  GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS          
SEQRES  18 R  260  ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU          
SEQRES  19 R  260  LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU          
SEQRES  20 R  260  ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER          
SEQRES   1 S  234  MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE          
SEQRES   2 S  234  SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU          
SEQRES   3 S  234  GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG          
SEQRES   4 S  234  SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN          
SEQRES   5 S  234  ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS          
SEQRES   6 S  234  CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA          
SEQRES   7 S  234  PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN          
SEQRES   8 S  234  CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA          
SEQRES   9 S  234  VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN          
SEQRES  10 S  234  LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL          
SEQRES  11 S  234  GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS          
SEQRES  12 S  234  LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU          
SEQRES  13 S  234  TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS          
SEQRES  14 S  234  THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE          
SEQRES  15 S  234  ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU          
SEQRES  16 S  234  ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL          
SEQRES  17 S  234  ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO          
SEQRES  18 S  234  PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE          
SEQRES   1 T  288  MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER          
SEQRES   2 T  288  VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR          
SEQRES   3 T  288  ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY          
SEQRES   4 T  288  ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS          
SEQRES   5 T  288  LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL          
SEQRES   6 T  288  LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR          
SEQRES   7 T  288  SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG          
SEQRES   8 T  288  GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS          
SEQRES   9 T  288  THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY          
SEQRES  10 T  288  GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG          
SEQRES  11 T  288  PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS          
SEQRES  12 T  288  ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER          
SEQRES  13 T  288  TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG          
SEQRES  14 T  288  GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS          
SEQRES  15 T  288  HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN          
SEQRES  16 T  288  ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS          
SEQRES  17 T  288  GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU          
SEQRES  18 T  288  SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP          
SEQRES  19 T  288  LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE          
SEQRES  20 T  288  ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN          
SEQRES  21 T  288  VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR          
SEQRES  22 T  288  ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS          
SEQRES  23 T  288  LEU GLU                                                      
SEQRES   1 U  252  MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP          
SEQRES   2 U  252  ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR          
SEQRES   3 U  252  GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN          
SEQRES   4 U  252  ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL          
SEQRES   5 U  252  VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP          
SEQRES   6 U  252  PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR          
SEQRES   7 U  252  ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG          
SEQRES   8 U  252  ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE          
SEQRES   9 U  252  ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU          
SEQRES  10 U  252  ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN          
SEQRES  11 U  252  ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE          
SEQRES  12 U  252  VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS          
SEQRES  13 U  252  THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR          
SEQRES  14 U  252  ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU          
SEQRES  15 U  252  GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN          
SEQRES  16 U  252  GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR          
SEQRES  17 U  252  HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN          
SEQRES  18 U  252  ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE          
SEQRES  19 U  252  THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA          
SEQRES  20 U  252  ILE ALA GLU GLN ASP                                          
SEQRES   1 V  232  THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL          
SEQRES   2 V  232  ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL          
SEQRES   3 V  232  ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO          
SEQRES   4 V  232  LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 V  232  GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU          
SEQRES   6 V  232  HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER          
SEQRES   7 V  232  ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN          
SEQRES   8 V  232  GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP          
SEQRES   9 V  232  PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY          
SEQRES  10 V  232  SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY          
SEQRES  11 V  232  SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS          
SEQRES  12 V  232  GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER          
SEQRES  13 V  232  ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER          
SEQRES  14 V  232  GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS          
SEQRES  15 V  232  ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL          
SEQRES  16 V  232  ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY          
SEQRES  17 V  232  THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS          
SEQRES  18 V  232  ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA                  
SEQRES   1 W  205  MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL          
SEQRES   2 W  205  ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP          
SEQRES   3 W  205  LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS          
SEQRES   4 W  205  PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY          
SEQRES   5 W  205  ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU          
SEQRES   6 W  205  MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU          
SEQRES   7 W  205  GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL          
SEQRES   8 W  205  SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE          
SEQRES   9 W  205  VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY          
SEQRES  10 W  205  LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE          
SEQRES  11 W  205  ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER          
SEQRES  12 W  205  ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO          
SEQRES  13 W  205  ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN          
SEQRES  14 W  205  ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY          
SEQRES  15 W  205  TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL          
SEQRES  16 W  205  VAL LYS ARG TYR LEU LYS MET ARG GLN ASP                      
SEQRES   1 X  198  MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL          
SEQRES   2 X  198  ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER          
SEQRES   3 X  198  VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER          
SEQRES   4 X  198  PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP          
SEQRES   5 X  198  THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN          
SEQRES   6 X  198  LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN          
SEQRES   7 X  198  ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER          
SEQRES   8 X  198  ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE          
SEQRES   9 X  198  GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR          
SEQRES  10 X  198  GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR          
SEQRES  11 X  198  GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU          
SEQRES  12 X  198  LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU          
SEQRES  13 X  198  GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU          
SEQRES  14 X  198  LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS          
SEQRES  15 X  198  ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE          
SEQRES  16 X  198  GLN ALA GLN                                                  
SEQRES   1 Y  212  THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE          
SEQRES   2 Y  212  VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL          
SEQRES   3 Y  212  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  212  PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  212  GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU          
SEQRES   6 Y  212  HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  212  ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS          
SEQRES   8 Y  212  GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR          
SEQRES   9 Y  212  THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER          
SEQRES  10 Y  212  ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY          
SEQRES  11 Y  212  SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN          
SEQRES  12 Y  212  TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU          
SEQRES  13 Y  212  GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA          
SEQRES  14 Y  212  TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU          
SEQRES  15 Y  212  ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU          
SEQRES  16 Y  212  LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN          
SEQRES  17 Y  212  ASN VAL ILE GLY                                              
SEQRES   1 Z  222  GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  222  GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP          
SEQRES   3 Z  222  THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR          
SEQRES   4 Z  222  GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET          
SEQRES   5 Z  222  SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL          
SEQRES   6 Z  222  LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP          
SEQRES   7 Z  222  HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG          
SEQRES   8 Z  222  ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO          
SEQRES   9 Z  222  TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP          
SEQRES  10 Z  222  GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER          
SEQRES  11 Z  222  TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA          
SEQRES  12 Z  222  SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE          
SEQRES  13 Z  222  LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS          
SEQRES  14 Z  222  LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS          
SEQRES  15 Z  222  LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS          
SEQRES  16 Z  222  ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR          
SEQRES  17 Z  222  LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG          
SEQRES  18 Z  222  ASP                                                          
SEQRES   1 a  246  THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN          
SEQRES   2 a  246  THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER          
SEQRES   3 a  246  MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN          
SEQRES   4 a  246  LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL          
SEQRES   5 a  246  GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY          
SEQRES   6 a  246  ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG          
SEQRES   7 a  246  LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN          
SEQRES   8 a  246  PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR          
SEQRES   9 a  246  ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG          
SEQRES  10 a  246  SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA          
SEQRES  11 a  246  GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL          
SEQRES  12 a  246  ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA          
SEQRES  13 a  246  THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG          
SEQRES  14 a  246  LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR          
SEQRES  15 a  246  VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG          
SEQRES  16 a  246  VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE          
SEQRES  17 a  246  SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE          
SEQRES  18 a  246  LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE          
SEQRES  19 a  246  ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE              
SEQRES   1 b  196  THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE          
SEQRES   2 b  196  LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE          
SEQRES   3 b  196  ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP          
SEQRES   4 b  196  LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  196  GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU          
SEQRES   6 b  196  TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA          
SEQRES   7 b  196  ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP          
SEQRES   8 b  196  ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP          
SEQRES   9 b  196  LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY          
SEQRES  10 b  196  SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY          
SEQRES  11 b  196  SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG          
SEQRES  12 b  196  GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS          
SEQRES  13 b  196  HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER          
SEQRES  14 b  196  GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY          
SEQRES  15 b  196  VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN          
SEQRES  16 b  196  LEU                                                          
SEQRES   1 c    5  ACE PRO ALA DCL POL                                          
SEQRES   1 d    5  ACE PRO ALA DCL POL                                          
SEQRES   1 e    5  ACE PRO ALA DCL POL                                          
SEQRES   1 f    5  ACE PRO ALA DCL POL                                          
SEQRES   1 g    5  ACE PRO ALA DCL POL                                          
SEQRES   1 h    5  ACE PRO ALA DCL POL                                          
HET    ACE  c   1       3                                                       
HET    DCL  c   4       8                                                       
HET    POL  c   5       4                                                       
HET    ACE  d   1       3                                                       
HET    DCL  d   4       8                                                       
HET    POL  d   5       4                                                       
HET    ACE  e   1       3                                                       
HET    DCL  e   4       8                                                       
HET    POL  e   5       4                                                       
HET    ACE  f   1       3                                                       
HET    DCL  f   4       8                                                       
HET    POL  f   5       4                                                       
HET    ACE  g   1       3                                                       
HET    DCL  g   4       8                                                       
HET    POL  g   5       4                                                       
HET    ACE  h   1       3                                                       
HET    DCL  h   4       8                                                       
HET    POL  h   5       4                                                       
HET     MG  G 301       1                                                       
HET     CL  G 302       1                                                       
HET     MG  I 301       1                                                       
HET     MG  I 302       1                                                       
HET     MG  K 301       1                                                       
HET    MES  K 302      12                                                       
HET     MG  L 301       1                                                       
HET     MG  N 201       1                                                       
HET     CL  N 202       1                                                       
HET     CL  U 301       1                                                       
HET    MES  Y 301      12                                                       
HET     MG  Z 301       1                                                       
HET     CL  b 201       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     DCL 2-AMINO-4-METHYL-PENTAN-1-OL                                     
HETNAM     POL N-PROPANOL                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     DCL LEUCINOL                                                         
HETSYN     POL 1-PROPONOL                                                       
FORMUL  29  ACE    6(C2 H4 O)                                                   
FORMUL  29  DCL    6(C6 H15 N O)                                                
FORMUL  29  POL    6(C3 H8 O)                                                   
FORMUL  35   MG    7(MG 2+)                                                     
FORMUL  36   CL    4(CL 1-)                                                     
FORMUL  40  MES    2(C6 H13 N O4 S)                                             
FORMUL  48  HOH   *427(H2 O)                                                    
HELIX    1 AA1 LEU A   18  GLY A   31  1                                  14    
HELIX    2 AA2 MET A   78  SER A   96  1                                  19    
HELIX    3 AA3 TYR A   97  GLY A  102  1                                   6    
HELIX    4 AA4 PRO A  106  ALA A  121  1                                  16    
HELIX    5 AA5 GLY A  167  TRP A  179  1                                  13    
HELIX    6 AA6 GLU A  184  VAL A  200  1                                  17    
HELIX    7 AA7 ASN A  218  LEU A  222  5                                   5    
HELIX    8 AA8 THR A  239  ALA A  249  1                                  11    
HELIX    9 AA9 GLY B    1  ASP B    6  5                                   6    
HELIX   10 AB1 LEU B   18  SER B   29  1                                  12    
HELIX   11 AB2 LEU B   79  ASN B  102  1                                  24    
HELIX   12 AB3 PRO B  106  HIS B  124  1                                  19    
HELIX   13 AB4 ASN B  167  TYR B  179  1                                  13    
HELIX   14 AB5 LYS B  184  THR B  200  1                                  17    
HELIX   15 AB6 THR B  206  ASP B  208  5                                   3    
HELIX   16 AB7 LYS B  230  THR B  241  1                                  12    
HELIX   17 AB8 ILE C   15  GLY C   28  1                                  14    
HELIX   18 AB9 LEU C   76  GLU C   99  1                                  24    
HELIX   19 AC1 THR C  103  TYR C  118  1                                  16    
HELIX   20 AC2 ASN C  165  TYR C  177  1                                  13    
HELIX   21 AC3 THR C  185  GLU C  199  1                                  15    
HELIX   22 AC4 SER C  223  GLN C  239  1                                  17    
HELIX   23 AC5 LEU D   13  LEU D   25  1                                  13    
HELIX   24 AC6 GLU D   52  ILE D   56  5                                   5    
HELIX   25 AC7 ASP D   76  ASP D   96  1                                  21    
HELIX   26 AC8 ASN D  100  LEU D  113  1                                  14    
HELIX   27 AC9 GLY D  167  TRP D  179  1                                  13    
HELIX   28 AD1 THR D  184  MET D  200  1                                  17    
HELIX   29 AD2 ASP D  224  ALA D  241  1                                  18    
HELIX   30 AD3 LEU E   18  GLN E   30  1                                  13    
HELIX   31 AD4 LEU E   76  ASN E   99  1                                  24    
HELIX   32 AD5 ALA E  103  ASN E  118  1                                  16    
HELIX   33 AD6 ARG E  163  ILE E  179  1                                  17    
HELIX   34 AD7 ASN E  184  SER E  197  1                                  14    
HELIX   35 AD8 GLN E  198  LEU E  200  5                                   3    
HELIX   36 AD9 ASP E  225  ILE E  233  5                                   9    
HELIX   37 AE1 ASN F   17  ASN F   29  1                                  13    
HELIX   38 AE2 LEU F   77  LYS F  100  1                                  24    
HELIX   39 AE3 PRO F  104  HIS F  119  1                                  16    
HELIX   40 AE4 GLY F  164  HIS F  179  1                                  16    
HELIX   41 AE5 SER F  184  HIS F  200  1                                  17    
HELIX   42 AE6 GLU F  201  LYS F  204  5                                   4    
HELIX   43 AE7 LYS F  228  ASN F  244  1                                  17    
HELIX   44 AE8 GLY G    2  HIS G    6  5                                   5    
HELIX   45 AE9 LEU G   16  THR G   26  1                                  11    
HELIX   46 AF1 ASP G   56  VAL G   60  5                                   5    
HELIX   47 AF2 PRO G   77  GLY G  100  1                                  24    
HELIX   48 AF3 PRO G  104  ARG G  122  1                                  19    
HELIX   49 AF4 LYS G  165  LYS G  181  1                                  17    
HELIX   50 AF5 SER G  189  GLY G  206  1                                  18    
HELIX   51 AF6 SER G  228  GLU G  241  1                                  14    
HELIX   52 AF7 THR H   48  SER H   71  1                                  24    
HELIX   53 AF8 ARG H   75  TYR H   90  1                                  16    
HELIX   54 AF9 GLY H  130  TRP H  142  1                                  13    
HELIX   55 AG1 THR H  147  ASP H  166  1                                  20    
HELIX   56 AG2 ASP I    2  ILE I    6  5                                   5    
HELIX   57 AG3 LEU I   55  GLU I   78  1                                  24    
HELIX   58 AG4 GLU I   82  GLU I   96  1                                  15    
HELIX   59 AG5 ALA I  141  TYR I  153  1                                  13    
HELIX   60 AG6 GLU I  158  ASP I  175  1                                  18    
HELIX   61 AG7 GLY J   51  ASP J   72  1                                  22    
HELIX   62 AG8 SER J   76  ILE J   92  1                                  17    
HELIX   63 AG9 SER J  136  TYR J  148  1                                  13    
HELIX   64 AH1 THR J  153  MET J  172  1                                  20    
HELIX   65 AH2 GLY K   48  LYS K   71  1                                  24    
HELIX   66 AH3 SER K   75  TYR K   90  1                                  16    
HELIX   67 AH4 GLY K  132  SER K  142  1                                  11    
HELIX   68 AH5 SER K  149  ASP K  168  1                                  20    
HELIX   69 AH6 VAL K  193  GLY K  205  1                                  13    
HELIX   70 AH7 PHE L   57  HIS L   79  1                                  23    
HELIX   71 AH8 SER L   85  GLY L   99  1                                  15    
HELIX   72 AH9 ALA L  142  VAL L  154  1                                  13    
HELIX   73 AI1 SER L  176  HIS L  195  1                                  20    
HELIX   74 AI2 ILE M   57  TYR M   76  1                                  20    
HELIX   75 AI3 GLU M   88  LYS M  106  1                                  19    
HELIX   76 AI4 GLY M  145  ARG M  156  1                                  12    
HELIX   77 AI5 ARG M  161  ILE M  165  5                                   5    
HELIX   78 AI6 THR M  169  ASP M  188  1                                  20    
HELIX   79 AI7 TRP M  219  ILE M  225  5                                   7    
HELIX   80 AI8 SER N   48  GLY N   71  1                                  24    
HELIX   81 AI9 SER N   74  ASN N   89  1                                  16    
HELIX   82 AJ1 LYS N   90  LEU N   93  5                                   4    
HELIX   83 AJ2 GLY N  128  PHE N  133  5                                   6    
HELIX   84 AJ3 ILE N  134  PHE N  142  1                                   9    
HELIX   85 AJ4 SER N  147  ASP N  166  1                                  20    
HELIX   86 AJ5 TYR N  189  GLU N  194  1                                   6    
HELIX   87 AJ6 LEU O   18  GLY O   31  1                                  14    
HELIX   88 AJ7 MET O   78  SER O   96  1                                  19    
HELIX   89 AJ8 TYR O   97  GLY O  102  1                                   6    
HELIX   90 AJ9 PRO O  106  ALA O  121  1                                  16    
HELIX   91 AK1 GLY O  167  TRP O  179  1                                  13    
HELIX   92 AK2 GLU O  184  VAL O  200  1                                  17    
HELIX   93 AK3 ASN O  218  LEU O  222  5                                   5    
HELIX   94 AK4 THR O  239  ALA O  249  1                                  11    
HELIX   95 AK5 GLY P    1  ASP P    6  5                                   6    
HELIX   96 AK6 LEU P   18  SER P   29  1                                  12    
HELIX   97 AK7 LEU P   79  ASN P  102  1                                  24    
HELIX   98 AK8 PRO P  106  HIS P  124  1                                  19    
HELIX   99 AK9 ASN P  167  TYR P  179  1                                  13    
HELIX  100 AL1 LYS P  184  THR P  200  1                                  17    
HELIX  101 AL2 THR P  206  ASP P  208  5                                   3    
HELIX  102 AL3 LYS P  230  THR P  241  1                                  12    
HELIX  103 AL4 ILE Q   15  GLY Q   28  1                                  14    
HELIX  104 AL5 LEU Q   76  GLU Q   99  1                                  24    
HELIX  105 AL6 THR Q  103  TYR Q  118  1                                  16    
HELIX  106 AL7 ASN Q  165  TYR Q  177  1                                  13    
HELIX  107 AL8 THR Q  185  GLU Q  199  1                                  15    
HELIX  108 AL9 SER Q  223  GLN Q  239  1                                  17    
HELIX  109 AM1 LEU R   13  LEU R   25  1                                  13    
HELIX  110 AM2 GLU R   52  ILE R   56  5                                   5    
HELIX  111 AM3 ASP R   76  ASP R   96  1                                  21    
HELIX  112 AM4 ASN R  100  LEU R  113  1                                  14    
HELIX  113 AM5 GLY R  167  TRP R  179  1                                  13    
HELIX  114 AM6 THR R  184  MET R  200  1                                  17    
HELIX  115 AM7 ASP R  224  ALA R  241  1                                  18    
HELIX  116 AM8 LEU S   18  GLN S   30  1                                  13    
HELIX  117 AM9 LEU S   76  ASN S   99  1                                  24    
HELIX  118 AN1 ALA S  103  ASN S  118  1                                  16    
HELIX  119 AN2 ARG S  163  ILE S  179  1                                  17    
HELIX  120 AN3 ASN S  184  SER S  197  1                                  14    
HELIX  121 AN4 GLN S  198  LEU S  200  5                                   3    
HELIX  122 AN5 ASP S  225  ILE S  233  5                                   9    
HELIX  123 AN6 ASN T   17  ASN T   29  1                                  13    
HELIX  124 AN7 LEU T   77  LYS T  100  1                                  24    
HELIX  125 AN8 PRO T  104  HIS T  119  1                                  16    
HELIX  126 AN9 GLY T  164  HIS T  179  1                                  16    
HELIX  127 AO1 SER T  184  HIS T  200  1                                  17    
HELIX  128 AO2 GLU T  201  LYS T  204  5                                   4    
HELIX  129 AO3 LYS T  228  ASN T  244  1                                  17    
HELIX  130 AO4 GLY U    2  HIS U    6  5                                   5    
HELIX  131 AO5 LEU U   16  THR U   26  1                                  11    
HELIX  132 AO6 ASP U   56  VAL U   60  5                                   5    
HELIX  133 AO7 PRO U   77  GLY U  100  1                                  24    
HELIX  134 AO8 PRO U  104  ARG U  122  1                                  19    
HELIX  135 AO9 LYS U  165  LYS U  181  1                                  17    
HELIX  136 AP1 SER U  189  GLY U  206  1                                  18    
HELIX  137 AP2 SER U  228  GLU U  241  1                                  14    
HELIX  138 AP3 THR V   48  SER V   71  1                                  24    
HELIX  139 AP4 ARG V   75  TYR V   90  1                                  16    
HELIX  140 AP5 GLY V  130  TRP V  142  1                                  13    
HELIX  141 AP6 THR V  147  ASP V  166  1                                  20    
HELIX  142 AP7 ASP W    2  ILE W    6  5                                   5    
HELIX  143 AP8 LEU W   55  GLU W   78  1                                  24    
HELIX  144 AP9 GLU W   82  GLU W   96  1                                  15    
HELIX  145 AQ1 ALA W  141  TYR W  153  1                                  13    
HELIX  146 AQ2 GLU W  158  ASP W  175  1                                  18    
HELIX  147 AQ3 GLY X   51  ASP X   72  1                                  22    
HELIX  148 AQ4 SER X   76  ILE X   92  1                                  17    
HELIX  149 AQ5 SER X  136  TYR X  148  1                                  13    
HELIX  150 AQ6 THR X  153  MET X  172  1                                  20    
HELIX  151 AQ7 GLY Y   48  LYS Y   71  1                                  24    
HELIX  152 AQ8 SER Y   75  TYR Y   90  1                                  16    
HELIX  153 AQ9 GLY Y  132  SER Y  142  1                                  11    
HELIX  154 AR1 SER Y  149  ASP Y  168  1                                  20    
HELIX  155 AR2 VAL Y  193  GLY Y  205  1                                  13    
HELIX  156 AR3 PHE Z   57  HIS Z   79  1                                  23    
HELIX  157 AR4 SER Z   85  GLY Z   99  1                                  15    
HELIX  158 AR5 ALA Z  142  VAL Z  154  1                                  13    
HELIX  159 AR6 SER Z  176  HIS Z  195  1                                  20    
HELIX  160 AR7 ILE a   57  TYR a   76  1                                  20    
HELIX  161 AR8 GLU a   88  LYS a  106  1                                  19    
HELIX  162 AR9 GLY a  145  ARG a  156  1                                  12    
HELIX  163 AS1 ARG a  161  ILE a  165  5                                   5    
HELIX  164 AS2 THR a  169  ASP a  188  1                                  20    
HELIX  165 AS3 TRP a  219  ILE a  225  5                                   7    
HELIX  166 AS4 SER b   48  GLY b   71  1                                  24    
HELIX  167 AS5 SER b   74  ASN b   89  1                                  16    
HELIX  168 AS6 LYS b   90  LEU b   93  5                                   4    
HELIX  169 AS7 GLY b  128  PHE b  133  5                                   6    
HELIX  170 AS8 ILE b  134  PHE b  142  1                                   9    
HELIX  171 AS9 SER b  147  ASP b  166  1                                  20    
HELIX  172 AT1 TYR b  189  GLU b  194  1                                   6    
SHEET    1 AA1 5 ALA A 161  ILE A 164  0                                        
SHEET    2 AA1 5 SER A  34  LYS A  38 -1  N  SER A  34   O  ILE A 164           
SHEET    3 AA1 5 VAL A  43  GLU A  48 -1  O  VAL A  44   N  ILE A  37           
SHEET    4 AA1 5 ILE A 209  ILE A 214 -1  O  GLU A 210   N  THR A  47           
SHEET    5 AA1 5 PHE A 235  LYS A 237 -1  O  ARG A 236   N  ILE A 213           
SHEET    1 AA2 6 ALA A  56  MET A  57  0                                        
SHEET    2 AA2 6 TYR G 154  TYR G 157 -1  O  GLY G 156   N  MET A  57           
SHEET    3 AA2 6 GLY G 142  THR G 148 -1  N  ILE G 145   O  TYR G 157           
SHEET    4 AA2 6 ILE G 131  ASP G 138 -1  N  PHE G 134   O  TYR G 146           
SHEET    5 AA2 6 GLY G  71  ASN G  75 -1  N  GLY G  71   O  VAL G 135           
SHEET    6 AA2 6 ILE G  63  CYS G  65 -1  N  PHE G  64   O  MET G  72           
SHEET    1 AA3 5 SER A  65  THR A  68  0                                        
SHEET    2 AA3 5 ILE A  71  GLY A  77 -1  O  ILE A  71   N  LEU A  67           
SHEET    3 AA3 5 VAL A 132  ASP A 140 -1  O  ALA A 137   N  GLY A  72           
SHEET    4 AA3 5 GLY A 144  VAL A 150 -1  O  TYR A 148   N  ILE A 136           
SHEET    5 AA3 5 TYR A 156  PRO A 158 -1  O  PHE A 157   N  GLN A 149           
SHEET    1 AA4 6 TYR A 224  THR A 225  0                                        
SHEET    2 AA4 6 ALA H 184  LEU H 191  1  O  TYR H 186   N  THR A 225           
SHEET    3 AA4 6 VAL H 173  GLU H 179 -1  N  VAL H 175   O  LEU H 187           
SHEET    4 AA4 6 GLY H  11  ALA H  16 -1  N  VAL H  12   O  MET H 178           
SHEET    5 AA4 6 ILE H   3  PHE H   8 -1  N  VAL H   6   O  VAL H  13           
SHEET    6 AA4 6 TYR H 124  LEU H 127 -1  O  LEU H 125   N  GLY H   5           
SHEET    1 AA5 5 ALA B 161  VAL B 164  0                                        
SHEET    2 AA5 5 ALA B  34  ALA B  39 -1  N  GLY B  36   O  ILE B 162           
SHEET    3 AA5 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  ILE B  35           
SHEET    4 AA5 5 LEU B 210  ARG B 216 -1  O  ALA B 213   N  LEU B  45           
SHEET    5 AA5 5 TYR B 225  ILE B 228 -1  O  LYS B 227   N  THR B 214           
SHEET    1 AA6 5 LEU B  65  LYS B  67  0                                        
SHEET    2 AA6 5 ILE B  72  GLY B  78 -1  O  VAL B  74   N  TYR B  66           
SHEET    3 AA6 5 VAL B 132  ASP B 140 -1  O  ALA B 137   N  ALA B  73           
SHEET    4 AA6 5 GLY B 144  SER B 150 -1  O  TYR B 148   N  TYR B 136           
SHEET    5 AA6 5 TYR B 156  TRP B 159 -1  O  TRP B 159   N  LEU B 147           
SHEET    1 AA7 5 ALA C 159  ILE C 162  0                                        
SHEET    2 AA7 5 ALA C  31  LYS C  35 -1  N  GLY C  33   O  GLN C 160           
SHEET    3 AA7 5 VAL C  40  GLU C  45 -1  O  GLY C  43   N  VAL C  32           
SHEET    4 AA7 5 ILE C 208  LYS C 214 -1  O  THR C 211   N  LEU C  42           
SHEET    5 AA7 5 ASP C 218  ALA C 221 -1  O  ASP C 218   N  LYS C 214           
SHEET    1 AA8 5 SER C  63  LYS C  64  0                                        
SHEET    2 AA8 5 VAL C  69  GLY C  75 -1  O  LEU C  71   N  SER C  63           
SHEET    3 AA8 5 VAL C 129  GLY C 135 -1  O  ALA C 134   N  VAL C  70           
SHEET    4 AA8 5 LYS C 144  THR C 148 -1  O  TYR C 146   N  ILE C 133           
SHEET    5 AA8 5 TYR C 154  SER C 156 -1  O  SER C 155   N  GLN C 147           
SHEET    1 AA9 5 ALA D 161  ILE D 164  0                                        
SHEET    2 AA9 5 ALA D  29  ALA D  33 -1  N  ALA D  29   O  ILE D 164           
SHEET    3 AA9 5 VAL D  38  GLU D  43 -1  O  GLY D  41   N  ILE D  30           
SHEET    4 AA9 5 ALA D 209  THR D 215 -1  O  SER D 212   N  LEU D  40           
SHEET    5 AA9 5 GLY D 219  ILE D 222 -1  O  LYS D 221   N  CYS D 213           
SHEET    1 AB1 5 ILE D  59  ASP D  63  0                                        
SHEET    2 AB1 5 ILE D  66  GLY D  72 -1  O  CYS D  68   N  VAL D  60           
SHEET    3 AB1 5 VAL D 132  ASP D 140 -1  O  ALA D 137   N  GLY D  67           
SHEET    4 AB1 5 GLY D 144  ALA D 150 -1  O  PHE D 148   N  ILE D 136           
SHEET    5 AB1 5 PHE D 156  ARG D 158 -1  O  TYR D 157   N  HIS D 149           
SHEET    1 AB2 5 GLY E 157  ILE E 160  0                                        
SHEET    2 AB2 5 THR E  34  ARG E  38 -1  N  GLY E  36   O  THR E 158           
SHEET    3 AB2 5 HIS E  42  LEU E  48 -1  O  VAL E  46   N  VAL E  35           
SHEET    4 AB2 5 LEU E 210  GLY E 216 -1  O  SER E 211   N  ALA E  47           
SHEET    5 AB2 5 THR E 219  TYR E 224 -1  O  TYR E 224   N  ILE E 212           
SHEET    1 AB3 5 ILE E  62  LYS E  64  0                                        
SHEET    2 AB3 5 MET E  69  GLY E  75 -1  O  LEU E  71   N  ILE E  63           
SHEET    3 AB3 5 VAL E 129  ASP E 137 -1  O  ILE E 134   N  GLY E  70           
SHEET    4 AB3 5 GLY E 140  PHE E 146 -1  O  PHE E 146   N  LEU E 131           
SHEET    5 AB3 5 VAL E 152  GLU E 154 -1  O  THR E 153   N  GLU E 145           
SHEET    1 AB4 5 GLY F 158  THR F 161  0                                        
SHEET    2 AB4 5 SER F  33  CYS F  38 -1  N  GLY F  35   O  ALA F 159           
SHEET    3 AB4 5 GLY F  41  LEU F  49 -1  O  GLY F  41   N  CYS F  38           
SHEET    4 AB4 5 PHE F 208  SER F 216 -1  O  SER F 213   N  PHE F  44           
SHEET    5 AB4 5 LYS F 225  PHE F 226 -1  O  LYS F 225   N  TRP F 214           
SHEET    1 AB5 5 GLN F  64  VAL F  66  0                                        
SHEET    2 AB5 5 ILE F  70  GLY F  76 -1  O  CYS F  72   N  GLN F  64           
SHEET    3 AB5 5 VAL F 130  ASP F 138 -1  O  ILE F 133   N  VAL F  73           
SHEET    4 AB5 5 GLY F 141  LEU F 147 -1  O  TYR F 145   N  PHE F 134           
SHEET    5 AB5 5 TYR F 153  GLY F 155 -1  O  TRP F 154   N  MET F 146           
SHEET    1 AB6 5 THR G 160  THR G 162  0                                        
SHEET    2 AB6 5 SER G  33  ARG G  37 -1  N  SER G  33   O  THR G 162           
SHEET    3 AB6 5 THR G  42  GLN G  47 -1  O  ILE G  45   N  LEU G  34           
SHEET    4 AB6 5 LEU G 214  THR G 220 -1  O  GLY G 217   N  VAL G  44           
SHEET    5 AB6 5 LYS G 223  THR G 226 -1  O  PHE G 225   N  VAL G 218           
SHEET    1 AB7 2 SER H  20  GLN H  22  0                                        
SHEET    2 AB7 2 ILE H  25  ASP H  28 -1  O  ILE H  25   N  GLN H  22           
SHEET    1 AB8 5 LEU H  34  SER H  38  0                                        
SHEET    2 AB8 5 ILE H  41  GLY H  47 -1  O  CYS H  43   N  HIS H  35           
SHEET    3 AB8 5 ALA H  96  ASP H 104 -1  O  TYR H  97   N  ALA H  46           
SHEET    4 AB8 5 GLY H 107  ILE H 113 -1  O  PHE H 111   N  VAL H 100           
SHEET    5 AB8 5 THR H 119  VAL H 121 -1  O  ASP H 120   N  SER H 112           
SHEET    1 AB9 6 VAL H 212  VAL H 218  0                                        
SHEET    2 AB9 6 GLU I 193  LEU I 199 -1  O  VAL I 194   N  VAL H 218           
SHEET    3 AB9 6 ALA I 184  LYS I 190 -1  N  ILE I 188   O  VAL I 195           
SHEET    4 AB9 6 CYS I  19  ASP I  25 -1  N  VAL I  20   O  ILE I 189           
SHEET    5 AB9 6 ILE I  10  GLY I  16 -1  N  VAL I  12   O  ALA I  23           
SHEET    6 AB9 6 PHE I 135  GLY I 139 -1  O  ILE I 136   N  ALA I  13           
SHEET    1 AC1 2 LEU I  28  SER I  30  0                                        
SHEET    2 AC1 2 LEU I  33  SER I  36 -1  O  LEU I  33   N  SER I  30           
SHEET    1 AC2 5 ILE I  42  TYR I  45  0                                        
SHEET    2 AC2 5 VAL I  48  GLY I  54 -1  O  LEU I  50   N  PHE I  43           
SHEET    3 AC2 5 VAL I 104  ILE I 111 -1  O  VAL I 107   N  GLY I  51           
SHEET    4 AC2 5 PRO I 118  PHE I 123 -1  O  PHE I 119   N  GLY I 110           
SHEET    5 AC2 5 ILE I 129  GLU I 131 -1  O  ASP I 130   N  GLY I 122           
SHEET    1 AC3 5 TYR J 130  HIS J 133  0                                        
SHEET    2 AC3 5 ILE J   4  ARG J   8 -1  N  GLY J   6   O  GLY J 131           
SHEET    3 AC3 5 VAL J  13  SER J  18 -1  O  ALA J  16   N  LEU J   5           
SHEET    4 AC3 5 VAL J 179  ASP J 185 -1  O  VAL J 184   N  VAL J  13           
SHEET    5 AC3 5 GLY J 188  VAL J 192 -1  O  ARG J 190   N  ILE J 183           
SHEET    1 AC4 2 VAL J  21  ARG J  23  0                                        
SHEET    2 AC4 2 SER J  26  LYS J  29 -1  O  SER J  26   N  ARG J  23           
SHEET    1 AC5 5 THR J  35  SER J  39  0                                        
SHEET    2 AC5 5 THR J  42  GLY J  48 -1  O  MET J  44   N  ARG J  36           
SHEET    3 AC5 5 VAL J 100  ASP J 108 -1  O  ASN J 101   N  ALA J  47           
SHEET    4 AC5 5 LYS J 113  ILE J 119 -1  O  ILE J 119   N  VAL J 102           
SHEET    5 AC5 5 LYS J 125  GLU J 127 -1  O  VAL J 126   N  GLN J 118           
SHEET    1 AC6 5 ILE K 126  VAL K 129  0                                        
SHEET    2 AC6 5 THR K   3  PHE K   8 -1  N  THR K   3   O  VAL K 129           
SHEET    3 AC6 5 GLY K  11  VAL K  16 -1  O  ALA K  15   N  LEU K   4           
SHEET    4 AC6 5 SER K 174  THR K 181 -1  O  VAL K 180   N  ILE K  12           
SHEET    5 AC6 5 GLY K 184  ASP K 192 -1  O  HIS K 191   N  VAL K 175           
SHEET    1 AC7 2 ALA K  20  ALA K  22  0                                        
SHEET    2 AC7 2 TRP K  25  SER K  28 -1  O  SER K  28   N  ALA K  20           
SHEET    1 AC8 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AC8 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC8 5 GLY K  98  THR K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC8 5 GLY K 109  ASP K 116 -1  O  VAL K 115   N  THR K  99           
SHEET    5 AC8 5 ARG K 121  LYS K 123 -1  O  LEU K 122   N  TYR K 114           
SHEET    1 AC9 5 CYS L 136  GLY L 140  0                                        
SHEET    2 AC9 5 THR L  11  ALA L  16 -1  N  ILE L  12   O  GLY L 139           
SHEET    3 AC9 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AC9 5 GLY L 201  THR L 208 -1  O  VAL L 207   N  ALA L  21           
SHEET    5 AC9 5 GLY L 211  GLU L 218 -1  O  TYR L 217   N  LEU L 202           
SHEET    1 AD1 2 ASN L  29  THR L  31  0                                        
SHEET    2 AD1 2 SER L  34  SER L  37 -1  O  ASN L  36   N  ASN L  29           
SHEET    1 AD2 5 PHE L  44  ASP L  45  0                                        
SHEET    2 AD2 5 VAL L  51  GLY L  56 -1  O  MET L  52   N  PHE L  44           
SHEET    3 AD2 5 VAL L 107  LEU L 114 -1  O  HIS L 108   N  ASN L  55           
SHEET    4 AD2 5 GLY L 120  PHE L 125 -1  O  PHE L 125   N  THR L 109           
SHEET    5 AD2 5 TYR L 131  GLU L 134 -1  O  GLU L 134   N  VAL L 122           
SHEET    1 AD3 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AD3 5 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD3 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD3 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD3 5 LEU M  42  VAL M  45 -1  N  ILE M  43   O  VAL M  51           
SHEET    1 AD4 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AD4 7 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD4 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD4 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD4 7 ASN M 112  VAL M 119 -1  O  ALA M 117   N  VAL M  50           
SHEET    6 AD4 7 GLN M 125  ASN M 131 -1  O  VAL M 130   N  ILE M 114           
SHEET    7 AD4 7 THR M 136  TYR M 137 -1  O  TYR M 137   N  TYR M 129           
SHEET    1 AD5 5 THR M 141  ALA M 143  0                                        
SHEET    2 AD5 5 VAL M  11  LYS M  15 -1  N  SER M  13   O  LEU M 142           
SHEET    3 AD5 5 GLY M  19  ASP M  25 -1  O  ALA M  23   N  ILE M  12           
SHEET    4 AD5 5 ASN M 194  ASP M 201 -1  O  ALA M 198   N  ILE M  22           
SHEET    5 AD5 5 GLY M 205  GLN M 213 -1  O  LYS M 209   N  LEU M 197           
SHEET    1 AD6 5 TYR N 124  ALA N 127  0                                        
SHEET    2 AD6 5 ILE N   3  THR N   7 -1  N  ILE N   3   O  ALA N 127           
SHEET    3 AD6 5 GLY N  11  ALA N  16 -1  O  GLY N  15   N  MET N   4           
SHEET    4 AD6 5 ILE N 173  THR N 179 -1  O  LEU N 178   N  VAL N  12           
SHEET    5 AD6 5 VAL N 183  PHE N 188 -1  O  GLU N 184   N  VAL N 177           
SHEET    1 AD7 2 THR N  20  THR N  22  0                                        
SHEET    2 AD7 2 TYR N  25  ASN N  28 -1  O  TYR N  25   N  THR N  22           
SHEET    1 AD8 5 LEU N  34  HIS N  38  0                                        
SHEET    2 AD8 5 ILE N  41  GLY N  47 -1  O  CYS N  43   N  THR N  35           
SHEET    3 AD8 5 ALA N  95  TYR N 102 -1  O  ALA N 100   N  TRP N  42           
SHEET    4 AD8 5 GLY N 108  ILE N 113 -1  O  TYR N 111   N  VAL N  99           
SHEET    5 AD8 5 HIS N 120  LEU N 122 -1  O  HIS N 120   N  THR N 112           
SHEET    1 AD9 5 ALA O 161  ILE O 164  0                                        
SHEET    2 AD9 5 SER O  34  LYS O  38 -1  N  SER O  34   O  ILE O 164           
SHEET    3 AD9 5 VAL O  43  GLU O  48 -1  O  VAL O  44   N  ILE O  37           
SHEET    4 AD9 5 ILE O 209  ILE O 214 -1  O  GLU O 210   N  THR O  47           
SHEET    5 AD9 5 PHE O 235  LYS O 237 -1  O  ARG O 236   N  ILE O 213           
SHEET    1 AE1 6 ALA O  56  MET O  57  0                                        
SHEET    2 AE1 6 TYR U 154  TYR U 157 -1  O  GLY U 156   N  MET O  57           
SHEET    3 AE1 6 GLY U 142  THR U 148 -1  N  ILE U 145   O  TYR U 157           
SHEET    4 AE1 6 ILE U 131  ASP U 138 -1  N  PHE U 134   O  TYR U 146           
SHEET    5 AE1 6 GLY U  71  ASN U  75 -1  N  GLY U  71   O  VAL U 135           
SHEET    6 AE1 6 ILE U  63  CYS U  65 -1  N  PHE U  64   O  MET U  72           
SHEET    1 AE2 5 SER O  65  THR O  68  0                                        
SHEET    2 AE2 5 ILE O  71  GLY O  77 -1  O  ILE O  71   N  LEU O  67           
SHEET    3 AE2 5 VAL O 132  ASP O 140 -1  O  ALA O 137   N  GLY O  72           
SHEET    4 AE2 5 GLY O 144  VAL O 150 -1  O  TYR O 148   N  ILE O 136           
SHEET    5 AE2 5 TYR O 156  PRO O 158 -1  O  PHE O 157   N  GLN O 149           
SHEET    1 AE3 6 TYR O 224  THR O 225  0                                        
SHEET    2 AE3 6 ALA V 184  LEU V 191  1  O  TYR V 186   N  THR O 225           
SHEET    3 AE3 6 VAL V 173  GLU V 179 -1  N  VAL V 175   O  LEU V 187           
SHEET    4 AE3 6 GLY V  11  ALA V  16 -1  N  VAL V  12   O  MET V 178           
SHEET    5 AE3 6 ILE V   3  PHE V   8 -1  N  VAL V   6   O  VAL V  13           
SHEET    6 AE3 6 TYR V 124  LEU V 127 -1  O  LEU V 125   N  GLY V   5           
SHEET    1 AE4 5 ALA P 161  VAL P 164  0                                        
SHEET    2 AE4 5 ALA P  34  ALA P  39 -1  N  GLY P  36   O  ILE P 162           
SHEET    3 AE4 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  ILE P  35           
SHEET    4 AE4 5 LEU P 210  ARG P 216 -1  O  ALA P 213   N  LEU P  45           
SHEET    5 AE4 5 TYR P 225  ILE P 228 -1  O  LYS P 227   N  THR P 214           
SHEET    1 AE5 5 LEU P  65  LYS P  67  0                                        
SHEET    2 AE5 5 ILE P  72  GLY P  78 -1  O  VAL P  74   N  TYR P  66           
SHEET    3 AE5 5 VAL P 132  ASP P 140 -1  O  ALA P 137   N  ALA P  73           
SHEET    4 AE5 5 GLY P 144  SER P 150 -1  O  TYR P 148   N  TYR P 136           
SHEET    5 AE5 5 TYR P 156  TRP P 159 -1  O  TRP P 159   N  LEU P 147           
SHEET    1 AE6 5 ALA Q 159  ILE Q 162  0                                        
SHEET    2 AE6 5 ALA Q  31  LYS Q  35 -1  N  GLY Q  33   O  GLN Q 160           
SHEET    3 AE6 5 VAL Q  40  GLU Q  45 -1  O  VAL Q  41   N  VAL Q  34           
SHEET    4 AE6 5 ILE Q 208  LYS Q 214 -1  O  THR Q 211   N  LEU Q  42           
SHEET    5 AE6 5 ASP Q 218  ALA Q 221 -1  O  ASP Q 218   N  LYS Q 214           
SHEET    1 AE7 5 SER Q  63  LYS Q  64  0                                        
SHEET    2 AE7 5 VAL Q  69  GLY Q  75 -1  O  LEU Q  71   N  SER Q  63           
SHEET    3 AE7 5 VAL Q 129  GLY Q 135 -1  O  ALA Q 134   N  VAL Q  70           
SHEET    4 AE7 5 LYS Q 144  THR Q 148 -1  O  TYR Q 146   N  ILE Q 133           
SHEET    5 AE7 5 TYR Q 154  SER Q 156 -1  O  SER Q 155   N  GLN Q 147           
SHEET    1 AE8 5 ALA R 161  ILE R 164  0                                        
SHEET    2 AE8 5 ALA R  29  ALA R  33 -1  N  ALA R  29   O  ILE R 164           
SHEET    3 AE8 5 VAL R  38  GLU R  43 -1  O  GLY R  41   N  ILE R  30           
SHEET    4 AE8 5 ALA R 209  THR R 215 -1  O  SER R 212   N  LEU R  40           
SHEET    5 AE8 5 GLY R 219  ILE R 222 -1  O  LYS R 221   N  CYS R 213           
SHEET    1 AE9 5 ILE R  59  ASP R  63  0                                        
SHEET    2 AE9 5 ILE R  66  GLY R  72 -1  O  CYS R  68   N  VAL R  60           
SHEET    3 AE9 5 VAL R 132  ASP R 140 -1  O  ALA R 137   N  GLY R  67           
SHEET    4 AE9 5 GLY R 144  ALA R 150 -1  O  PHE R 148   N  ILE R 136           
SHEET    5 AE9 5 PHE R 156  ARG R 158 -1  O  TYR R 157   N  HIS R 149           
SHEET    1 AF1 5 GLY S 157  ILE S 160  0                                        
SHEET    2 AF1 5 THR S  34  ARG S  38 -1  N  GLY S  36   O  THR S 158           
SHEET    3 AF1 5 HIS S  42  LEU S  48 -1  O  VAL S  46   N  VAL S  35           
SHEET    4 AF1 5 LEU S 210  GLY S 216 -1  O  SER S 211   N  ALA S  47           
SHEET    5 AF1 5 THR S 219  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF2 5 ILE S  62  LYS S  64  0                                        
SHEET    2 AF2 5 MET S  69  GLY S  75 -1  O  LEU S  71   N  ILE S  63           
SHEET    3 AF2 5 VAL S 129  ASP S 137 -1  O  ILE S 134   N  GLY S  70           
SHEET    4 AF2 5 GLY S 140  PHE S 146 -1  O  PHE S 146   N  LEU S 131           
SHEET    5 AF2 5 VAL S 152  GLU S 154 -1  O  THR S 153   N  GLU S 145           
SHEET    1 AF3 5 GLY T 158  THR T 161  0                                        
SHEET    2 AF3 5 SER T  33  CYS T  38 -1  N  GLY T  35   O  ALA T 159           
SHEET    3 AF3 5 GLY T  41  LEU T  49 -1  O  GLY T  41   N  CYS T  38           
SHEET    4 AF3 5 PHE T 208  SER T 216 -1  O  SER T 213   N  PHE T  44           
SHEET    5 AF3 5 LYS T 225  PHE T 226 -1  O  LYS T 225   N  TRP T 214           
SHEET    1 AF4 5 GLN T  64  VAL T  66  0                                        
SHEET    2 AF4 5 ILE T  70  GLY T  76 -1  O  CYS T  72   N  GLN T  64           
SHEET    3 AF4 5 VAL T 130  ASP T 138 -1  O  ILE T 133   N  VAL T  73           
SHEET    4 AF4 5 GLY T 141  LEU T 147 -1  O  TYR T 145   N  PHE T 134           
SHEET    5 AF4 5 TYR T 153  GLY T 155 -1  O  TRP T 154   N  MET T 146           
SHEET    1 AF5 5 THR U 160  THR U 162  0                                        
SHEET    2 AF5 5 SER U  33  ARG U  37 -1  N  SER U  33   O  THR U 162           
SHEET    3 AF5 5 THR U  42  GLN U  47 -1  O  ILE U  45   N  LEU U  34           
SHEET    4 AF5 5 LEU U 214  THR U 220 -1  O  GLY U 217   N  VAL U  44           
SHEET    5 AF5 5 LYS U 223  THR U 226 -1  O  PHE U 225   N  VAL U 218           
SHEET    1 AF6 2 SER V  20  GLN V  22  0                                        
SHEET    2 AF6 2 ILE V  25  ASP V  28 -1  O  ILE V  25   N  GLN V  22           
SHEET    1 AF7 5 LEU V  34  SER V  38  0                                        
SHEET    2 AF7 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF7 5 ALA V  96  ASP V 104 -1  O  TYR V  97   N  ALA V  46           
SHEET    4 AF7 5 GLY V 107  ILE V 113 -1  O  PHE V 111   N  VAL V 100           
SHEET    5 AF7 5 THR V 119  VAL V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AF8 6 VAL V 212  VAL V 218  0                                        
SHEET    2 AF8 6 GLU W 193  LEU W 199 -1  O  VAL W 194   N  VAL V 218           
SHEET    3 AF8 6 ALA W 184  LYS W 190 -1  N  ILE W 188   O  VAL W 195           
SHEET    4 AF8 6 CYS W  19  ASP W  25 -1  N  VAL W  20   O  ILE W 189           
SHEET    5 AF8 6 ILE W  10  GLY W  16 -1  N  VAL W  12   O  ALA W  23           
SHEET    6 AF8 6 PHE W 135  GLY W 139 -1  O  ILE W 136   N  ALA W  13           
SHEET    1 AF9 2 LEU W  28  SER W  30  0                                        
SHEET    2 AF9 2 LEU W  33  SER W  36 -1  O  LEU W  33   N  SER W  30           
SHEET    1 AG1 5 ILE W  42  TYR W  45  0                                        
SHEET    2 AG1 5 VAL W  48  GLY W  54 -1  O  LEU W  50   N  PHE W  43           
SHEET    3 AG1 5 VAL W 104  ILE W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG1 5 PRO W 118  PHE W 123 -1  O  PHE W 119   N  GLY W 110           
SHEET    5 AG1 5 ILE W 129  GLU W 131 -1  O  ASP W 130   N  GLY W 122           
SHEET    1 AG2 5 TYR X 130  HIS X 133  0                                        
SHEET    2 AG2 5 ILE X   4  ARG X   8 -1  N  GLY X   6   O  GLY X 131           
SHEET    3 AG2 5 VAL X  13  SER X  18 -1  O  ALA X  16   N  LEU X   5           
SHEET    4 AG2 5 VAL X 179  ASP X 185 -1  O  VAL X 184   N  VAL X  13           
SHEET    5 AG2 5 GLY X 188  VAL X 192 -1  O  ARG X 190   N  ILE X 183           
SHEET    1 AG3 2 VAL X  21  ARG X  23  0                                        
SHEET    2 AG3 2 SER X  26  LYS X  29 -1  O  SER X  26   N  ARG X  23           
SHEET    1 AG4 5 THR X  35  SER X  39  0                                        
SHEET    2 AG4 5 THR X  42  GLY X  48 -1  O  MET X  44   N  ARG X  36           
SHEET    3 AG4 5 VAL X 100  ASP X 108 -1  O  ASN X 101   N  ALA X  47           
SHEET    4 AG4 5 LYS X 113  ILE X 119 -1  O  ILE X 119   N  VAL X 102           
SHEET    5 AG4 5 LYS X 125  GLU X 127 -1  O  VAL X 126   N  GLN X 118           
SHEET    1 AG5 5 ILE Y 126  VAL Y 129  0                                        
SHEET    2 AG5 5 THR Y   3  PHE Y   8 -1  N  THR Y   3   O  VAL Y 129           
SHEET    3 AG5 5 GLY Y  11  VAL Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4 AG5 5 SER Y 174  THR Y 181 -1  O  VAL Y 180   N  ILE Y  12           
SHEET    5 AG5 5 GLY Y 184  ASP Y 192 -1  O  HIS Y 191   N  VAL Y 175           
SHEET    1 AG6 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG6 2 TRP Y  25  SER Y  28 -1  O  SER Y  28   N  ALA Y  20           
SHEET    1 AG7 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AG7 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AG7 5 GLY Y  98  THR Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AG7 5 GLY Y 109  ASP Y 116 -1  O  VAL Y 115   N  THR Y  99           
SHEET    5 AG7 5 ARG Y 121  LYS Y 123 -1  O  LEU Y 122   N  TYR Y 114           
SHEET    1 AG8 5 CYS Z 136  GLY Z 140  0                                        
SHEET    2 AG8 5 THR Z  11  ALA Z  16 -1  N  ILE Z  12   O  GLY Z 139           
SHEET    3 AG8 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AG8 5 GLY Z 201  THR Z 208 -1  O  VAL Z 207   N  ALA Z  21           
SHEET    5 AG8 5 GLY Z 211  GLU Z 218 -1  O  TYR Z 217   N  LEU Z 202           
SHEET    1 AG9 2 ASN Z  29  THR Z  31  0                                        
SHEET    2 AG9 2 SER Z  34  SER Z  37 -1  O  ASN Z  36   N  ASN Z  29           
SHEET    1 AH1 5 PHE Z  44  ASP Z  45  0                                        
SHEET    2 AH1 5 VAL Z  51  GLY Z  56 -1  O  MET Z  52   N  PHE Z  44           
SHEET    3 AH1 5 VAL Z 107  LEU Z 114 -1  O  HIS Z 108   N  ASN Z  55           
SHEET    4 AH1 5 GLY Z 120  PHE Z 125 -1  O  PHE Z 125   N  THR Z 109           
SHEET    5 AH1 5 TYR Z 131  GLU Z 134 -1  O  GLU Z 134   N  VAL Z 122           
SHEET    1 AH2 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH2 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH2 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH2 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH2 5 LEU a  42  VAL a  45 -1  N  ILE a  43   O  VAL a  51           
SHEET    1 AH3 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH3 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH3 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH3 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH3 7 ASN a 112  VAL a 119 -1  O  ALA a 117   N  VAL a  50           
SHEET    6 AH3 7 GLN a 125  ASN a 131 -1  O  VAL a 130   N  ILE a 114           
SHEET    7 AH3 7 THR a 136  SER a 138 -1  O  TYR a 137   N  TYR a 129           
SHEET    1 AH4 5 THR a 141  ALA a 143  0                                        
SHEET    2 AH4 5 VAL a  11  LYS a  15 -1  N  SER a  13   O  LEU a 142           
SHEET    3 AH4 5 GLY a  19  ASP a  25 -1  O  ALA a  23   N  ILE a  12           
SHEET    4 AH4 5 ASN a 194  ASP a 201 -1  O  ALA a 198   N  ILE a  22           
SHEET    5 AH4 5 GLY a 205  GLN a 213 -1  O  LYS a 209   N  LEU a 197           
SHEET    1 AH5 5 TYR b 124  ALA b 127  0                                        
SHEET    2 AH5 5 ILE b   3  PHE b   8 -1  N  ILE b   3   O  ALA b 127           
SHEET    3 AH5 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4 AH5 5 ILE b 173  THR b 179 -1  O  LEU b 178   N  VAL b  12           
SHEET    5 AH5 5 VAL b 183  PHE b 188 -1  O  GLU b 184   N  VAL b 177           
SHEET    1 AH6 2 THR b  20  THR b  22  0                                        
SHEET    2 AH6 2 TYR b  25  ASN b  28 -1  O  TYR b  25   N  THR b  22           
SHEET    1 AH7 5 LEU b  34  HIS b  38  0                                        
SHEET    2 AH7 5 ILE b  41  GLY b  47 -1  O  CYS b  43   N  THR b  35           
SHEET    3 AH7 5 ALA b  95  TYR b 102 -1  O  ALA b 100   N  TRP b  42           
SHEET    4 AH7 5 GLY b 108  ILE b 113 -1  O  TYR b 111   N  VAL b  99           
SHEET    5 AH7 5 HIS b 120  LEU b 122 -1  O  HIS b 120   N  THR b 112           
LINK         OG1 THR H   1                 C   DCL c   4     1555   1555  1.40  
LINK         N   THR H   1                 C2  POL c   5     1555   1555  1.50  
LINK         OG1 THR K   1                 C   DCL d   4     1555   1555  1.38  
LINK         N   THR K   1                 C2  POL d   5     1555   1555  1.48  
LINK         OG1 THR N   1                 C   DCL e   4     1555   1555  1.39  
LINK         N   THR N   1                 C2  POL e   5     1555   1555  1.51  
LINK         OG1 THR V   1                 C   DCL f   4     1555   1555  1.39  
LINK         N   THR V   1                 C2  POL f   5     1555   1555  1.49  
LINK         OG1 THR Y   1                 C   DCL g   4     1555   1555  1.38  
LINK         N   THR Y   1                 C2  POL g   5     1555   1555  1.49  
LINK         OG1 THR b   1                 C   DCL h   4     1555   1555  1.45  
LINK         N   THR b   1                 C2  POL h   5     1555   1555  1.50  
LINK         C   ACE c   1                 N   PRO c   2     1555   1555  1.32  
LINK         C   ALA c   3                 N   DCL c   4     1555   1555  1.33  
LINK         C   DCL c   4                 C2  POL c   5     1555   1555  1.58  
LINK         C   ACE d   1                 N   PRO d   2     1555   1555  1.31  
LINK         C   ALA d   3                 N   DCL d   4     1555   1555  1.32  
LINK         C   DCL d   4                 C2  POL d   5     1555   1555  1.59  
LINK         C   ACE e   1                 N   PRO e   2     1555   1555  1.33  
LINK         C   ALA e   3                 N   DCL e   4     1555   1555  1.32  
LINK         C   DCL e   4                 C2  POL e   5     1555   1555  1.57  
LINK         C   ACE f   1                 N   PRO f   2     1555   1555  1.34  
LINK         C   ALA f   3                 N   DCL f   4     1555   1555  1.33  
LINK         C   DCL f   4                 C2  POL f   5     1555   1555  1.57  
LINK         C   ACE g   1                 N   PRO g   2     1555   1555  1.32  
LINK         C   ALA g   3                 N   DCL g   4     1555   1555  1.31  
LINK         C   DCL g   4                 C2  POL g   5     1555   1555  1.57  
LINK         C   ACE h   1                 N   PRO h   2     1555   1555  1.35  
LINK         C   ALA h   3                 N   DCL h   4     1555   1555  1.35  
LINK         C   DCL h   4                 C2  POL h   5     1555   1555  1.60  
LINK         OG1 THR G   8                MG    MG G 301     1555   1555  2.65  
LINK         O   TYR G 119                MG    MG G 301     1555   1555  2.99  
LINK         O   ARG G 122                MG    MG G 301     1555   1555  2.72  
LINK         O   MET G 125                MG    MG G 301     1555   1555  2.38  
LINK         O   ALA I 174                MG    MG I 301     1555   1555  2.50  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.70  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.27  
LINK         O   ASP I 204                MG    MG I 302     1555   1555  2.34  
LINK        MG    MG I 302                 O   ALA Y 165     1555   1555  2.40  
LINK        MG    MG I 302                 O   ASP Y 168     1555   1555  2.12  
LINK        MG    MG I 302                 O   SER Y 171     1555   1555  2.62  
LINK         O   ALA K 165                MG    MG K 301     1555   1555  2.42  
LINK         O   ASP K 168                MG    MG K 301     1555   1555  2.15  
LINK         O   SER K 171                MG    MG K 301     1555   1555  2.51  
LINK        MG    MG K 301                 O   ASP W 204     1555   1555  2.26  
LINK         OXT ASP L 222                MG    MG L 301     1555   1555  2.28  
LINK        MG    MG L 301                 O   ILE V 163     1555   1555  2.21  
LINK        MG    MG L 301                 O   ASP V 166     1555   1555  2.08  
LINK        MG    MG L 301                 O   SER V 169     1555   1555  2.50  
LINK         O   ILE N 163                MG    MG N 201     1555   1555  2.65  
LINK         O   ASP N 166                MG    MG N 201     1555   1555  2.80  
LINK         O   SER N 169                MG    MG N 201     1555   1555  2.48  
LINK         O   THR Z 192                MG    MG Z 301     1555   1555  2.61  
LINK         O   HIS Z 195                MG    MG Z 301     1555   1555  2.69  
LINK         O   VAL Z 198                MG    MG Z 301     1555   1555  2.36  
SITE     1 AC1  5 THR G   8  TYR G 119  ARG G 122  ALA G 123                    
SITE     2 AC1  5 MET G 125                                                     
SITE     1 AC2  3 ARG G 111  ASN G 114  TYR H  69                               
SITE     1 AC3  3 ALA I 174  ASP I 177  SER I 180                               
SITE     1 AC4  5 ASP I 204  ALA Y 165  ASP Y 168  ALA Y 169                    
SITE     2 AC4  5 SER Y 171                                                     
SITE     1 AC5  5 ALA K 165  ASP K 168  ALA K 169  SER K 171                    
SITE     2 AC5  5 ASP W 204                                                     
SITE     1 AC6  7 THR K   1  GLY K  47  MET K  97  GLY K 130                    
SITE     2 AC6  7 SER K 131  DCL d   4  POL d   5                               
SITE     1 AC7  4 ASP L 222  ILE V 163  ASP V 166  SER V 169                    
SITE     1 AC8  5 ARG N  19  ILE N 163  ASP N 166  SER N 169                    
SITE     2 AC8  5 LEU a  34                                                     
SITE     1 AC9  2 ARG N  45  GLN N  53                                          
SITE     1 AD1  3 ARG U 111  ASN U 114  TYR V  69                               
SITE     1 AD2  7 GLY Y  47  MET Y  97  SER Y 117  GLY Y 130                    
SITE     2 AD2  7 SER Y 131  DCL g   4  POL g   5                               
SITE     1 AD3  3 THR Z 192  HIS Z 195  VAL Z 198                               
SITE     1 AD4  2 ARG b  45  GLN b  53                                          
SITE     1 AD5 10 THR H   1  ARG H  19  SER H  20  THR H  21                    
SITE     2 AD5 10 GLY H  47  ALA H  49  GLY H 168  ACE c   1                    
SITE     3 AD5 10 PRO c   2  HOH c 101                                          
SITE     1 AD6  7 THR H   1  SER H  20  GLY H  47  ALA H  49                    
SITE     2 AD6  7 ALA c   3  POL c   5  HOH c 101                               
SITE     1 AD7  9 THR K   1  ARG K  19  ALA K  20  THR K  21                    
SITE     2 AD7  9 GLY K  47  TYR K 170  MES K 302  ACE d   1                    
SITE     3 AD7  9 PRO d   2                                                     
SITE     1 AD8  5 THR K   1  GLY K  47  MES K 302  ALA d   3                    
SITE     2 AD8  5 POL d   5                                                     
SITE     1 AD9 12 THR N   1  ARG N  19  THR N  20  THR N  21                    
SITE     2 AD9 12 LYS N  33  ARG N  45  GLY N  47  ALA N  49                    
SITE     3 AD9 12 SER N 168  ACE e   1  PRO e   2  HOH e 301                    
SITE     1 AE1  8 THR N   1  THR N  20  ARG N  45  GLY N  47                    
SITE     2 AE1  8 ALA N  49  ALA e   3  POL e   5  HOH e 301                    
SITE     1 AE2  9 THR V   1  ARG V  19  SER V  20  THR V  21                    
SITE     2 AE2  9 LYS V  33  GLY V  47  GLY V 168  PRO f   2                    
SITE     3 AE2  9 HOH f 101                                                     
SITE     1 AE3  5 THR V   1  GLY V  47  ALA f   3  POL f   5                    
SITE     2 AE3  5 HOH f 101                                                     
SITE     1 AE4 10 THR Y   1  ARG Y  19  ALA Y  20  THR Y  21                    
SITE     2 AE4 10 GLY Y  47  ALA Y  49  SER Y 131  TYR Y 170                    
SITE     3 AE4 10 MES Y 301  PRO g   2                                          
SITE     1 AE5  6 THR Y   1  GLY Y  47  ALA Y  49  MES Y 301                    
SITE     2 AE5  6 ALA g   3  POL g   5                                          
SITE     1 AE6 12 THR b   1  ARG b  19  THR b  20  THR b  21                    
SITE     2 AE6 12 LYS b  33  ARG b  45  GLY b  47  THR b  52                    
SITE     3 AE6 12 SER b 168  ACE h   1  PRO h   2  HOH h 102                    
SITE     1 AE7  8 THR b   1  THR b  20  ARG b  45  GLY b  47                    
SITE     2 AE7  8 THR b  52  ALA h   3  POL h   5  HOH h 102                    
SITE     1 AE8  4 THR H  21  GLN H  22  ALA H  49  ALA c   3                    
SITE     1 AE9  4 THR K  21  ALA K  49  ASP L 126  ALA d   3                    
SITE     1 AF1  4 THR N  21  THR N  22  ALA N  49  ALA e   3                    
SITE     1 AF2  3 THR V  21  ALA V  49  ALA f   3                               
SITE     1 AF3  3 THR Y  21  ALA Y  49  ALA g   3                               
SITE     1 AF4  6 HIS V 114  HIS V 116  THR b  21  ALA b  49                    
SITE     2 AF4  6 ALA h   3  HOH h 101                                          
CRYST1  136.580  301.570  146.350  90.00 113.25  90.00 P 1 21 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007322  0.000000  0.003146        0.00000                         
SCALE2      0.000000  0.003316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007437        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 -0.999891  0.000391  0.014736       68.58237    1                    
MTRIX2   2 -0.002891 -0.985429 -0.170061     -290.68451    1                    
MTRIX3   2  0.014454 -0.170085  0.985323      -25.24635    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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