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Database: PDB
Entry: 5L5B
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HEADER    HYDROLASE/HYDROLASE INHIBITOR           28-MAY-16   5L5B              
TITLE     YEAST 20S PROTEASOME WITH HUMAN BETA5I (1-138) AND HUMAN BETA6 (97-   
TITLE    2 111; 118-133)                                                        
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 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND  10 CHAIN: B, P;                                                         
COMPND  11 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  12 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;     
COMPND  13 EC: 3.4.25.1;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND  17 CHAIN: C, Q;                                                         
COMPND  18 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  19 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6; 
COMPND  20 EC: 3.4.25.1;                                                        
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  24 CHAIN: D, R;                                                         
COMPND  25 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  26 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2; 
COMPND  27 EC: 3.4.25.1;                                                        
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MOL_ID: 5;                                                           
COMPND  30 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  31 CHAIN: E, S;                                                         
COMPND  32 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  33 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5; 
COMPND  34 EC: 3.4.25.1;                                                        
COMPND  35 ENGINEERED: YES;                                                     
COMPND  36 MOL_ID: 6;                                                           
COMPND  37 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;                  
COMPND  38 CHAIN: F, T;                                                         
COMPND  39 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  40 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;        
COMPND  41 EC: 3.4.25.1;                                                        
COMPND  42 ENGINEERED: YES;                                                     
COMPND  43 MOL_ID: 7;                                                           
COMPND  44 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  45 CHAIN: G, U;                                                         
COMPND  46 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE     
COMPND  47 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,    
COMPND  48 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;                   
COMPND  49 EC: 3.4.25.1;                                                        
COMPND  50 ENGINEERED: YES;                                                     
COMPND  51 MOL_ID: 8;                                                           
COMPND  52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  53 CHAIN: H, V;                                                         
COMPND  54 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  55 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1; 
COMPND  56 EC: 3.4.25.1;                                                        
COMPND  57 ENGINEERED: YES;                                                     
COMPND  58 MOL_ID: 9;                                                           
COMPND  59 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  60 CHAIN: I, W;                                                         
COMPND  61 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  62 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;                              
COMPND  63 EC: 3.4.25.1;                                                        
COMPND  64 ENGINEERED: YES;                                                     
COMPND  65 MOL_ID: 10;                                                          
COMPND  66 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  67 CHAIN: J, X;                                                         
COMPND  68 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  69 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;     
COMPND  70 EC: 3.4.25.1;                                                        
COMPND  71 ENGINEERED: YES;                                                     
COMPND  72 MOL_ID: 11;                                                          
COMPND  73 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-8,PROTEASOME SUBUNIT BETA     
COMPND  74 TYPE-5;                                                              
COMPND  75 CHAIN: K, Y;                                                         
COMPND  76 SYNONYM: LOW MOLECULAR MASS PROTEIN 7,MACROPAIN SUBUNIT C13,         
COMPND  77 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C13,PROTEASOME COMPONENT
COMPND  78 C13,PROTEASOME SUBUNIT BETA-5I,REALLY INTERESTING NEW GENE 10        
COMPND  79 PROTEIN,MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  80 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2; 
COMPND  81 EC: 3.4.25.1,3.4.25.1;                                               
COMPND  82 ENGINEERED: YES;                                                     
COMPND  83 MOL_ID: 12;                                                          
COMPND  84 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6,PROTEASOME SUBUNIT BETA     
COMPND  85 TYPE-1,PROTEASOME SUBUNIT BETA TYPE-6,PROTEASOME SUBUNIT BETA TYPE-1,
COMPND  86 PROTEASOME SUBUNIT BETA TYPE-6;                                      
COMPND  87 CHAIN: L, Z;                                                         
COMPND  88 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME  
COMPND  89 COMPONENT C5,MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE       
COMPND  90 COMPLEX SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN,   
COMPND  91 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME COMPONENT 
COMPND  92 C5,MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT 
COMPND  93 C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN,MULTICATALYTIC     
COMPND  94 ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME COMPONENT C5;            
COMPND  95 EC: 3.4.25.1,3.4.25.1,3.4.25.1,3.4.25.1,3.4.25.1;                    
COMPND  96 ENGINEERED: YES;                                                     
COMPND  97 MOL_ID: 13;                                                          
COMPND  98 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  99 CHAIN: M, a;                                                         
COMPND 100 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND 101 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4; 
COMPND 102 EC: 3.4.25.1;                                                        
COMPND 103 ENGINEERED: YES;                                                     
COMPND 104 MOL_ID: 14;                                                          
COMPND 105 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND 106 CHAIN: N, b;                                                         
COMPND 107 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND 108 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3; 
COMPND 109 EC: 3.4.25.1;                                                        
COMPND 110 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 GENE: PRE8, PRS4, YML092C;                                           
SOURCE   7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE   8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  12 S288C);                                                              
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  14 ORGANISM_TAXID: 559292;                                              
SOURCE  15 GENE: PRE9, PRS5, YGR135W;                                           
SOURCE  16 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  17 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  21 S288C);                                                              
SOURCE  22 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  23 ORGANISM_TAXID: 559292;                                              
SOURCE  24 GENE: PRE6, YOL038W;                                                 
SOURCE  25 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  26 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  30 S288C);                                                              
SOURCE  31 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  32 ORGANISM_TAXID: 559292;                                              
SOURCE  33 GENE: PUP2, DOA5, YGR253C, G9155;                                    
SOURCE  34 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  35 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  36 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  37 MOL_ID: 5;                                                           
SOURCE  38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  39 S288C);                                                              
SOURCE  40 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  41 ORGANISM_TAXID: 559292;                                              
SOURCE  42 GENE: PRE5, YMR314W, YM9924.06;                                      
SOURCE  43 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  44 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  45 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  46 MOL_ID: 6;                                                           
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 GENE: PRE10, PRC1, PRS1, YOR362C, O6650;                             
SOURCE  52 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  53 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  54 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  55 MOL_ID: 7;                                                           
SOURCE  56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  57 S288C);                                                              
SOURCE  58 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  59 ORGANISM_TAXID: 559292;                                              
SOURCE  60 GENE: SCL1, PRC2, PRS2, YGL011C;                                     
SOURCE  61 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  62 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  63 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  64 MOL_ID: 8;                                                           
SOURCE  65 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  66 S288C);                                                              
SOURCE  67 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  68 ORGANISM_TAXID: 559292;                                              
SOURCE  69 GENE: PUP1, YOR157C;                                                 
SOURCE  70 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  71 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  72 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  73 MOL_ID: 9;                                                           
SOURCE  74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  75 S288C);                                                              
SOURCE  76 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  77 ORGANISM_TAXID: 559292;                                              
SOURCE  78 GENE: PUP3, YER094C;                                                 
SOURCE  79 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  80 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  81 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  82 MOL_ID: 10;                                                          
SOURCE  83 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  84 S288C);                                                              
SOURCE  85 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  86 ORGANISM_TAXID: 559292;                                              
SOURCE  87 GENE: PRE1, YER012W;                                                 
SOURCE  88 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  89 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  90 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE  91 MOL_ID: 11;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SACCHAROMYCES CEREVISIAE (STRAIN  
SOURCE  93 ATCC 204508 / S288C);                                                
SOURCE  94 ORGANISM_COMMON: HUMAN, BAKER'S YEAST;                               
SOURCE  95 ORGANISM_TAXID: 9606, 559292;                                        
SOURCE  96 GENE: PSMB8, LMP7, PSMB5I, RING10, Y2, PRE2, DOA3, PRG1, YPR103W,    
SOURCE  97 P8283.10;                                                            
SOURCE  98 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE  99 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE 100 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE 101 MOL_ID: 12;                                                          
SOURCE 102 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 103 S288C), HOMO SAPIENS, SACCHAROMYCES CEREVISIAE;                      
SOURCE 104 ORGANISM_COMMON: BAKER'S YEAST, HUMAN;                               
SOURCE 105 ORGANISM_TAXID: 559292, 9606;                                        
SOURCE 106 GENE: PRE7, PRS3, PTS1, YBL041W, YBL0407, PSMB1, PSC5;               
SOURCE 107 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE 108 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE 109 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE 110 MOL_ID: 13;                                                          
SOURCE 111 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 112 S288C);                                                              
SOURCE 113 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 114 ORGANISM_TAXID: 559292;                                              
SOURCE 115 GENE: PRE4, YFR050C;                                                 
SOURCE 116 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE 117 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE 118 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE 119 MOL_ID: 14;                                                          
SOURCE 120 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE 121 S288C);                                                              
SOURCE 122 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE 123 ORGANISM_TAXID: 559292;                                              
SOURCE 124 GENE: PRE3, YJL001W, J1407;                                          
SOURCE 125 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;                   
SOURCE 126 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE 127 EXPRESSION_SYSTEM_TAXID: 559292                                      
KEYWDS    HYDROLASE COMPLEX, PROTEASOME, MUTANT, BINDING ANALYSIS, HYDROLASE-   
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GROLL,E.M.HUBER                                                     
REVDAT   2   14-DEC-16 5L5B    1       JRNL                                     
REVDAT   1   09-NOV-16 5L5B    0                                                
JRNL        AUTH   E.M.HUBER,W.HEINEMEYER,G.DE BRUIN,H.S.OVERKLEEFT,M.GROLL     
JRNL        TITL   A HUMANIZED YEAST PROTEASOME IDENTIFIES UNIQUE BINDING MODES 
JRNL        TITL 2 OF INHIBITORS FOR THE IMMUNOSUBUNIT BETA 5I.                 
JRNL        REF    EMBO J.                       V.  35  2602 2016              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   27789522                                                     
JRNL        DOI    10.15252/EMBJ.201695222                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 239932                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12628                           
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17086                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 899                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 49372                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 264                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.69000                                              
REMARK   3    B22 (A**2) : -5.72000                                             
REMARK   3    B33 (A**2) : 1.13000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.16000                                             
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): 0.275         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.221         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.417        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
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): 50292 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 48035 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 68025 ; 0.887 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):110609 ; 0.687 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6314 ; 4.823 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2257 ;34.790 ;24.382       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8769 ;14.543 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   289 ;13.871 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7647 ; 0.049 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 57151 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11294 ; 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): 25343 ; 1.954 ; 4.953       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25342 ; 1.954 ; 4.953       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31628 ; 2.552 ; 7.416       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31629 ; 2.552 ; 7.416       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 24949 ; 1.958 ; 5.348       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 24949 ; 1.958 ; 5.348       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 36397 ; 2.289 ; 7.877       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 54243 ; 2.897 ;38.809       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 54222 ; 2.881 ;38.807       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 98327 ; 1.602 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   190 ;34.818 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 97516 ; 5.395 ; 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     300      1                      
REMARK   3           1     O      1       O     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3099 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3179 ; 0.000 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3449 ; 0.020 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3594 ; 0.000 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2949 ; 0.000 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3795 ; 5.120 ; 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     300      1                      
REMARK   3           1     P      1       P     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      2    B (A**2):   3756 ; 3.390 ; 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     300      1                      
REMARK   3           1     Q      1       Q     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      3    C (A**2):   3729 ; 6.140 ; 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     300      1                      
REMARK   3           1     R      1       R     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      4    D (A**2):   3578 ; 4.590 ; 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     300      1                      
REMARK   3           1     S      1       S     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      5    E (A**2):   3509 ; 4.560 ; 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     300      1                      
REMARK   3           1     T      1       T     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      6    F (A**2):   3749 ; 5.440 ; 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     300      1                      
REMARK   3           1     U      1       U     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      7    G (A**2):   3770 ; 3.540 ; 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     300      1                      
REMARK   3           1     V      1       V     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      8    H (A**2):   3403 ; 2.700 ; 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     300      1                      
REMARK   3           1     W      1       W     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      9    I (A**2):   3119 ; 2.390 ; 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     300      1                      
REMARK   3           1     X      1       X     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL     10    J (A**2):   3099 ; 3.080 ; 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     300      1                      
REMARK   3           1     Y      1       Y     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL     11    K (A**2):   3179 ; 2.370 ; 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     300      1                      
REMARK   3           1     Z      1       Z     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL     12    L (A**2):   3449 ; 2.670 ; 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     300      1                      
REMARK   3           1     a      1       a     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL     13    M (A**2):   3594 ; 2.030 ; 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     300      1                      
REMARK   3           1     b      1       b     300      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL     14    N (A**2):   2949 ; 1.750 ; 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):  66.3737 -92.3354  45.8917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0945 T22:   0.1256                                     
REMARK   3      T33:   0.1845 T12:  -0.0350                                     
REMARK   3      T13:   0.0343 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4272 L22:   0.5895                                     
REMARK   3      L33:   0.1551 L12:  -0.1635                                     
REMARK   3      L13:  -0.0553 L23:   0.0238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:   0.0030 S13:   0.0028                       
REMARK   3      S21:   0.0803 S22:   0.0406 S23:  -0.0859                       
REMARK   3      S31:  -0.0631 S32:  -0.0671 S33:  -0.0193                       
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):  58.7339 -88.1776  16.2665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1552 T22:   0.1642                                     
REMARK   3      T33:   0.1467 T12:  -0.0467                                     
REMARK   3      T13:   0.0871 T23:   0.0419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3785 L22:   0.2755                                     
REMARK   3      L33:   0.3146 L12:   0.0200                                     
REMARK   3      L13:   0.2611 L23:   0.1111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0765 S12:  -0.0296 S13:  -0.0358                       
REMARK   3      S21:  -0.1030 S22:  -0.0005 S23:   0.0302                       
REMARK   3      S31:  -0.0762 S32:   0.0813 S33:   0.0771                       
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):  31.4205 -88.0820   1.1906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2013 T22:   0.1997                                     
REMARK   3      T33:   0.1337 T12:   0.0128                                     
REMARK   3      T13:   0.0051 T23:   0.0557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6935 L22:   0.0113                                     
REMARK   3      L33:   0.0220 L12:   0.0835                                     
REMARK   3      L13:  -0.0076 L23:  -0.0033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0114 S12:   0.0833 S13:   0.0223                       
REMARK   3      S21:   0.0013 S22:   0.0009 S23:   0.0146                       
REMARK   3      S31:  -0.0056 S32:   0.0576 S33:  -0.0123                       
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):   2.2503 -90.5958  13.8557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1575 T22:   0.1337                                     
REMARK   3      T33:   0.2802 T12:   0.0551                                     
REMARK   3      T13:  -0.0732 T23:   0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0378 L22:   0.4767                                     
REMARK   3      L33:   0.2871 L12:  -0.0778                                     
REMARK   3      L13:   0.0040 L23:  -0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0050 S12:  -0.0302 S13:  -0.0212                       
REMARK   3      S21:  -0.1295 S22:   0.0126 S23:   0.1845                       
REMARK   3      S31:  -0.0450 S32:   0.0836 S33:  -0.0176                       
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):  -3.7897 -95.2323  45.8066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0708 T22:   0.1203                                     
REMARK   3      T33:   0.3885 T12:   0.0529                                     
REMARK   3      T13:   0.0469 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1552 L22:   0.3597                                     
REMARK   3      L33:   0.2018 L12:   0.1598                                     
REMARK   3      L13:   0.0865 L23:  -0.0733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0654 S12:  -0.0009 S13:   0.0770                       
REMARK   3      S21:  -0.0078 S22:   0.0583 S23:   0.1944                       
REMARK   3      S31:  -0.0723 S32:  -0.0232 S33:   0.0072                       
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):  14.7887 -95.7671  69.8927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1950 T22:   0.1280                                     
REMARK   3      T33:   0.1975 T12:   0.0140                                     
REMARK   3      T13:   0.1314 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3472 L22:   0.2100                                     
REMARK   3      L33:   0.3295 L12:   0.1761                                     
REMARK   3      L13:  -0.0828 L23:  -0.1851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0180 S12:   0.0389 S13:   0.0753                       
REMARK   3      S21:   0.0671 S22:  -0.0603 S23:   0.1006                       
REMARK   3      S31:  -0.0423 S32:   0.0230 S33:   0.0422                       
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):  47.2040 -93.7967  71.0961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2415 T22:   0.0945                                     
REMARK   3      T33:   0.0981 T12:  -0.0182                                     
REMARK   3      T13:   0.0052 T23:  -0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1243 L22:   0.1127                                     
REMARK   3      L33:   0.6639 L12:  -0.0014                                     
REMARK   3      L13:   0.0433 L23:   0.1791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.1017 S13:  -0.0021                       
REMARK   3      S21:   0.0868 S22:  -0.0100 S23:  -0.0412                       
REMARK   3      S31:  -0.0303 S32:  -0.0181 S33:   0.0214                       
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   226                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.5490-129.7359  47.4063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0503 T22:   0.1337                                     
REMARK   3      T33:   0.1536 T12:   0.0096                                     
REMARK   3      T13:  -0.0271 T23:  -0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0163 L22:   0.3918                                     
REMARK   3      L33:   0.1737 L12:  -0.0071                                     
REMARK   3      L13:  -0.0390 L23:   0.1495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0166 S12:   0.0333 S13:   0.0120                       
REMARK   3      S21:   0.0828 S22:   0.0049 S23:  -0.1339                       
REMARK   3      S31:  -0.0204 S32:  -0.0805 S33:  -0.0215                       
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):  68.1264-127.5743  20.7397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0632 T22:   0.1912                                     
REMARK   3      T33:   0.1676 T12:  -0.0006                                     
REMARK   3      T13:   0.0958 T23:  -0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0893 L22:   0.9069                                     
REMARK   3      L33:   0.1072 L12:  -0.0705                                     
REMARK   3      L13:  -0.0811 L23:  -0.0764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0030 S12:   0.0318 S13:  -0.0097                       
REMARK   3      S21:  -0.0366 S22:   0.0039 S23:  -0.0588                       
REMARK   3      S31:   0.0052 S32:  -0.0239 S33:  -0.0009                       
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):  44.1143-127.1921  -0.4829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2619 T22:   0.1578                                     
REMARK   3      T33:   0.0806 T12:  -0.0085                                     
REMARK   3      T13:   0.0529 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2907 L22:   0.6206                                     
REMARK   3      L33:   0.2111 L12:   0.0049                                     
REMARK   3      L13:   0.1224 L23:   0.3105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0547 S12:  -0.0871 S13:  -0.0099                       
REMARK   3      S21:  -0.1943 S22:  -0.0465 S23:   0.0443                       
REMARK   3      S31:  -0.0566 S32:  -0.0556 S33:  -0.0082                       
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   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3001-131.5416   2.8355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1409 T22:   0.1594                                     
REMARK   3      T33:   0.1763 T12:   0.0079                                     
REMARK   3      T13:  -0.1227 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0449 L22:   0.5280                                     
REMARK   3      L33:   0.0233 L12:   0.1240                                     
REMARK   3      L13:  -0.0275 L23:  -0.1038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0177 S12:  -0.0531 S13:   0.0131                       
REMARK   3      S21:   0.0352 S22:  -0.0048 S23:   0.0738                       
REMARK   3      S31:   0.0101 S32:   0.0145 S33:  -0.0129                       
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):  -4.6742-135.2606  28.5498              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0243 T22:   0.1546                                     
REMARK   3      T33:   0.2569 T12:  -0.0040                                     
REMARK   3      T13:  -0.0049 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0197 L22:   0.0707                                     
REMARK   3      L33:   0.1546 L12:   0.0358                                     
REMARK   3      L13:   0.0429 L23:   0.0623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0051 S12:   0.0081 S13:   0.0302                       
REMARK   3      S21:   0.0140 S22:  -0.0160 S23:   0.0804                       
REMARK   3      S31:   0.0079 S32:   0.1086 S33:   0.0210                       
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   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6503-138.7312  60.3921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0796 T22:   0.1561                                     
REMARK   3      T33:   0.1528 T12:  -0.0101                                     
REMARK   3      T13:   0.0977 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1458 L22:   0.4534                                     
REMARK   3      L33:   0.2029 L12:  -0.1377                                     
REMARK   3      L13:   0.0333 L23:   0.0175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:   0.0220 S13:   0.0435                       
REMARK   3      S21:   0.1163 S22:  -0.0239 S23:   0.0580                       
REMARK   3      S31:   0.0381 S32:   0.0129 S33:   0.0215                       
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):  39.7045-134.6129  70.8853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2153 T22:   0.1438                                     
REMARK   3      T33:   0.0302 T12:  -0.0076                                     
REMARK   3      T13:  -0.0029 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2640 L22:   0.5499                                     
REMARK   3      L33:   0.1785 L12:  -0.1448                                     
REMARK   3      L13:  -0.2095 L23:   0.0680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:   0.0508 S13:   0.0493                       
REMARK   3      S21:   0.1698 S22:  -0.0030 S23:  -0.0499                       
REMARK   3      S31:  -0.0095 S32:  -0.0234 S33:  -0.0266                       
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):   2.2350-207.6769  36.9522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1629 T22:   0.0823                                     
REMARK   3      T33:   0.1925 T12:  -0.0628                                     
REMARK   3      T13:  -0.0344 T23:   0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3639 L22:   0.5409                                     
REMARK   3      L33:   0.2056 L12:  -0.1452                                     
REMARK   3      L13:  -0.0534 L23:   0.1666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:  -0.0028 S13:   0.0527                       
REMARK   3      S21:   0.0600 S22:  -0.0047 S23:   0.1046                       
REMARK   3      S31:   0.1182 S32:   0.0300 S33:   0.0003                       
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):   8.8564-206.6919   6.8104              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2001 T22:   0.0886                                     
REMARK   3      T33:   0.1479 T12:  -0.0316                                     
REMARK   3      T13:  -0.1052 T23:  -0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4161 L22:   0.3798                                     
REMARK   3      L33:   0.1306 L12:   0.1105                                     
REMARK   3      L13:  -0.0025 L23:   0.1166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0190 S12:  -0.0249 S13:   0.0361                       
REMARK   3      S21:  -0.0884 S22:  -0.0196 S23:   0.0445                       
REMARK   3      S31:   0.0541 S32:  -0.0031 S33:   0.0005                       
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):  35.8000-204.3188  -8.8502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2954 T22:   0.0978                                     
REMARK   3      T33:   0.0925 T12:   0.0489                                     
REMARK   3      T13:  -0.0691 T23:  -0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4634 L22:   0.0557                                     
REMARK   3      L33:   0.4994 L12:   0.1143                                     
REMARK   3      L13:   0.2206 L23:  -0.0332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0999 S12:   0.0249 S13:   0.0313                       
REMARK   3      S21:  -0.0332 S22:   0.0025 S23:   0.0458                       
REMARK   3      S31:   0.0841 S32:   0.0358 S33:  -0.1025                       
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):  65.3396-203.8858   3.2386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2785 T22:   0.1231                                     
REMARK   3      T33:   0.1896 T12:   0.0860                                     
REMARK   3      T13:   0.1564 T23:  -0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5208 L22:   0.2060                                     
REMARK   3      L33:   0.2274 L12:   0.1543                                     
REMARK   3      L13:   0.0958 L23:   0.1723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0669 S12:   0.0028 S13:   0.0137                       
REMARK   3      S21:  -0.1647 S22:  -0.0584 S23:  -0.1091                       
REMARK   3      S31:  -0.0950 S32:  -0.1123 S33:  -0.0085                       
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):  72.3904-204.6491  35.2831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0949 T22:   0.0906                                     
REMARK   3      T33:   0.3223 T12:   0.0790                                     
REMARK   3      T13:  -0.0348 T23:  -0.0717                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2923 L22:   0.3050                                     
REMARK   3      L33:   0.4667 L12:   0.2857                                     
REMARK   3      L13:   0.0039 L23:   0.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.0402 S13:  -0.0444                       
REMARK   3      S21:   0.0215 S22:   0.0710 S23:  -0.1319                       
REMARK   3      S31:   0.1227 S32:   0.0389 S33:  -0.0791                       
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):  54.5092-208.2956  59.6139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2667 T22:   0.0506                                     
REMARK   3      T33:   0.1856 T12:   0.0563                                     
REMARK   3      T13:  -0.1383 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3247 L22:   0.1252                                     
REMARK   3      L33:   0.1884 L12:   0.1948                                     
REMARK   3      L13:  -0.2219 L23:  -0.1186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0220 S12:  -0.0330 S13:  -0.1010                       
REMARK   3      S21:   0.0434 S22:  -0.0285 S23:  -0.0965                       
REMARK   3      S31:  -0.0092 S32:  -0.0112 S33:   0.0065                       
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):  22.1572-210.6274  61.3385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3014 T22:   0.0461                                     
REMARK   3      T33:   0.0844 T12:  -0.0126                                     
REMARK   3      T13:  -0.0131 T23:   0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1737 L22:   0.2600                                     
REMARK   3      L33:   0.2551 L12:  -0.1640                                     
REMARK   3      L13:  -0.0293 L23:  -0.0698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0213 S12:   0.0033 S13:  -0.0177                       
REMARK   3      S21:   0.0941 S22:   0.0263 S23:   0.0725                       
REMARK   3      S31:   0.0397 S32:   0.0167 S33:  -0.0051                       
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   226                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2714-171.0820  44.8676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0666 T22:   0.1185                                     
REMARK   3      T33:   0.1770 T12:  -0.0232                                     
REMARK   3      T13:   0.0317 T23:   0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1720 L22:   0.3427                                     
REMARK   3      L33:   0.1149 L12:  -0.0982                                     
REMARK   3      L13:   0.1341 L23:  -0.1212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0604 S12:   0.0703 S13:  -0.0082                       
REMARK   3      S21:   0.0085 S22:  -0.0464 S23:   0.1273                       
REMARK   3      S31:   0.0332 S32:   0.0728 S33:  -0.0140                       
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):  -0.1463-168.7012  18.2100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0579 T22:   0.1446                                     
REMARK   3      T33:   0.1972 T12:  -0.0153                                     
REMARK   3      T13:  -0.1048 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3858 L22:   0.5865                                     
REMARK   3      L33:   0.2235 L12:  -0.1463                                     
REMARK   3      L13:   0.1348 L23:  -0.1492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:   0.0086 S13:   0.0366                       
REMARK   3      S21:  -0.0774 S22:   0.0136 S23:   0.0885                       
REMARK   3      S31:   0.0058 S32:   0.0303 S33:  -0.0040                       
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):  23.2011-165.4229  -3.4788              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2400 T22:   0.1319                                     
REMARK   3      T33:   0.0760 T12:  -0.0118                                     
REMARK   3      T13:  -0.0489 T23:  -0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0956 L22:   0.7796                                     
REMARK   3      L33:   0.0623 L12:   0.1284                                     
REMARK   3      L13:  -0.0003 L23:  -0.1510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0123 S12:  -0.0546 S13:  -0.0428                       
REMARK   3      S21:  -0.1633 S22:  -0.0054 S23:  -0.0241                       
REMARK   3      S31:  -0.0176 S32:  -0.0005 S33:  -0.0069                       
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   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.1033-161.6278  -0.4444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1429 T22:   0.1767                                     
REMARK   3      T33:   0.1240 T12:   0.0024                                     
REMARK   3      T13:   0.0970 T23:  -0.0384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0121 L22:   0.1957                                     
REMARK   3      L33:   0.0261 L12:   0.0248                                     
REMARK   3      L13:  -0.0090 L23:  -0.0688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0254 S12:  -0.0392 S13:   0.0076                       
REMARK   3      S21:   0.0051 S22:  -0.0237 S23:   0.0061                       
REMARK   3      S31:  -0.0086 S32:   0.0190 S33:  -0.0016                       
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):  72.8796-162.3046  25.0731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0242 T22:   0.1466                                     
REMARK   3      T33:   0.1877 T12:   0.0438                                     
REMARK   3      T13:   0.0249 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0510 L22:   0.0785                                     
REMARK   3      L33:   0.2012 L12:   0.0604                                     
REMARK   3      L13:  -0.0977 L23:  -0.1103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0185 S12:   0.0250 S13:  -0.0141                       
REMARK   3      S21:  -0.0170 S22:   0.0108 S23:  -0.0492                       
REMARK   3      S31:  -0.0050 S32:  -0.0883 S33:   0.0077                       
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   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.5225-164.3021  57.3965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1482 T22:   0.1048                                     
REMARK   3      T33:   0.1351 T12:   0.0356                                     
REMARK   3      T13:  -0.1016 T23:  -0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1137 L22:   0.4123                                     
REMARK   3      L33:   0.0564 L12:  -0.0206                                     
REMARK   3      L13:  -0.0663 L23:  -0.0642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.0720 S13:  -0.0259                       
REMARK   3      S21:   0.1008 S22:  -0.0153 S23:  -0.0808                       
REMARK   3      S31:  -0.0007 S32:  -0.0446 S33:   0.0177                       
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):  29.7991-170.2018  68.0008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2330 T22:   0.1132                                     
REMARK   3      T33:   0.0341 T12:  -0.0147                                     
REMARK   3      T13:   0.0145 T23:   0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2537 L22:   0.4782                                     
REMARK   3      L33:   0.0955 L12:   0.0031                                     
REMARK   3      L13:   0.0895 L23:   0.1349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0603 S12:   0.0676 S13:   0.0157                       
REMARK   3      S21:   0.1931 S22:  -0.0477 S23:   0.0243                       
REMARK   3      S31:   0.0609 S32:  -0.0358 S33:  -0.0126                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5L5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000156.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-15                          
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   : 252560                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: 5CZ4                                                 
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      150.95000            
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: 28-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             
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     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     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   OD1  ASP J    52     NH1  ARG K    91              2.15            
REMARK 500   O    ILE J    25     OH   TYR X   139              2.19            
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    ARG J  95   CD  -  NE  -  CZ  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG J  95   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG J  95   NE  -  CZ  -  NH2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG J 149   CD  -  NE  -  CZ  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG J 149   NE  -  CZ  -  NH1 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ARG J 149   NE  -  CZ  -  NH2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG X  95   CD  -  NE  -  CZ  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    ARG X  95   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG X  95   NE  -  CZ  -  NH2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG X 149   CD  -  NE  -  CZ  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ARG X 149   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG X 149   NE  -  CZ  -  NH2 ANGL. DEV. = -10.0 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      138.93     56.43                                   
REMARK 500    TYR A  97      -65.07   -152.20                                   
REMARK 500    ALA A 249       40.79    -93.02                                   
REMARK 500    ARG B   8       78.48     59.88                                   
REMARK 500    THR B  10       58.42   -113.98                                   
REMARK 500    VAL B  51       93.18    -15.15                                   
REMARK 500    ASN B 220      101.58    -52.84                                   
REMARK 500    ASP B 221     -179.84     72.26                                   
REMARK 500    GLN C 120       35.91   -140.64                                   
REMARK 500    PRO C 183      106.24    -43.20                                   
REMARK 500    GLN C 202     -100.03    112.00                                   
REMARK 500    ALA C 205     -105.68    -82.81                                   
REMARK 500    ARG D   2      152.39    179.77                                   
REMARK 500    SER E  39     -157.28   -111.96                                   
REMARK 500    ASP E 137     -159.28   -126.00                                   
REMARK 500    ASP E 202      -49.38     67.82                                   
REMARK 500    ASP F  67     -131.45     56.27                                   
REMARK 500    LYS F 100      -54.86     74.79                                   
REMARK 500    ASP F 138     -167.58   -127.42                                   
REMARK 500    SER H 171     -113.72     67.66                                   
REMARK 500    GLN I  31     -106.95     60.92                                   
REMARK 500    ASP I 134      -72.00    -90.97                                   
REMARK 500    ASP I 192       36.25   -147.50                                   
REMARK 500    GLN I 203       48.55   -107.99                                   
REMARK 500    VAL J   9     -164.92   -102.53                                   
REMARK 500    SER J  31       28.19   -146.30                                   
REMARK 500    LYS J  34       59.12    -90.85                                   
REMARK 500    HIS K  10       42.53   -103.74                                   
REMARK 500    SER K  18       10.31   -141.59                                   
REMARK 500    ASP K 105     -158.97   -133.64                                   
REMARK 500    ASP L  32     -115.09     56.24                                   
REMARK 500    PHE L 103       62.38   -165.91                                   
REMARK 500    ASN L 165       70.19     55.75                                   
REMARK 500    ASP L 200      -61.97     71.25                                   
REMARK 500    ILE M   5      -73.11   -107.95                                   
REMARK 500    THR M   9     -154.58    -83.99                                   
REMARK 500    ALA M  83     -114.66   -146.83                                   
REMARK 500    LYS N 107     -149.08     69.10                                   
REMARK 500    THR O   2      139.23     56.16                                   
REMARK 500    TYR O  97      -65.11   -152.01                                   
REMARK 500    ALA O 249       40.91    -92.90                                   
REMARK 500    ARG P   8       78.52     59.84                                   
REMARK 500    THR P  10       58.40   -113.71                                   
REMARK 500    VAL P  51       93.10    -15.29                                   
REMARK 500    LYS P  64      -53.00   -120.14                                   
REMARK 500    ASN P 220      101.57    -52.89                                   
REMARK 500    ASP P 221     -179.77     72.40                                   
REMARK 500    GLN Q 120       35.92   -140.45                                   
REMARK 500    PRO Q 183      105.96    -43.09                                   
REMARK 500    GLN Q 202     -100.07    111.98                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG J  95         0.11    SIDE CHAIN                              
REMARK 500    ARG J 149         0.08    SIDE CHAIN                              
REMARK 500    ARG X  95         0.07    SIDE CHAIN                              
REMARK 500    ARG X 149         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH P 310        DISTANCE =  5.84 ANGSTROMS                       
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    83.4                                              
REMARK 620 3 ARG G 122   O    84.0  81.6                                        
REMARK 620 4 MET G 125   O   168.1  85.2  91.1                                  
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 ASP I 177   O                                                      
REMARK 620 2 SER I 180   O    82.3                                              
REMARK 620 N                    1                                               
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 164   O   100.0                                              
REMARK 620 3 ASP Y 167   O   164.3  95.6                                        
REMARK 620 4 SER Y 170   O    98.0  80.8  85.7                                  
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 164   O                                                      
REMARK 620 2 ASP K 167   O    96.1                                              
REMARK 620 3 SER K 170   O    83.1  87.5                                        
REMARK 620 4 ASP W 204   O   102.6 160.5 100.2                                  
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   102.8                                              
REMARK 620 3 ASP V 166   O   139.9 117.2                                        
REMARK 620 4 SER V 169   O    95.9  97.7  82.6                                  
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    69.6                                              
REMARK 620 3 SER N 169   O    97.6  66.5                                        
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    79.4                                              
REMARK 620 3 VAL Z 198   O    93.5  72.7                                        
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 CL G 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CZ4   RELATED DB: PDB                                   
REMARK 900 YEAST 20S PROTEASOME AT 2.3 A RESOLUTION                             
DBREF  5L5B A    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  5L5B B    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  5L5B C   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  5L5B D   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  5L5B E    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  5L5B F   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  5L5B G   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  5L5B H    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  5L5B I    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  5L5B J    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  5L5B K    1   138  UNP    P28062   PSB8_HUMAN      73    210             
DBREF  5L5B K  139   211  UNP    P30656   PSB5_YEAST     215    287             
DBREF  5L5B L    1    96  UNP    P23724   PSB6_YEAST      20    115             
DBREF  5L5B L   97   111  UNP    P20618   PSB1_HUMAN     124    138             
DBREF  5L5B L  112   117  UNP    P23724   PSB6_YEAST     131    136             
DBREF  5L5B L  118   133  UNP    P20618   PSB1_HUMAN     145    160             
DBREF  5L5B L  134   222  UNP    P23724   PSB6_YEAST     153    241             
DBREF  5L5B M  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  5L5B N    1   196  UNP    P38624   PSB1_YEAST      20    215             
DBREF  5L5B O    1   250  UNP    P23639   PSA2_YEAST       1    250             
DBREF  5L5B P    0   257  UNP    P23638   PSA3_YEAST       1    258             
DBREF  5L5B Q   -1   252  UNP    P40303   PSA4_YEAST       1    254             
DBREF  5L5B R   -7   252  UNP    P32379   PSA5_YEAST       1    260             
DBREF  5L5B S    0   233  UNP    P40302   PSA6_YEAST       1    234             
DBREF  5L5B T   -3   284  UNP    P21242   PSA7_YEAST       1    288             
DBREF  5L5B U   -8   243  UNP    P21243   PSA1_YEAST       1    252             
DBREF  5L5B V    1   232  UNP    P25043   PSB2_YEAST      30    261             
DBREF  5L5B W    0   204  UNP    P25451   PSB3_YEAST       1    205             
DBREF  5L5B X    1   198  UNP    P22141   PSB4_YEAST       1    198             
DBREF  5L5B Y    1   138  UNP    P28062   PSB8_HUMAN      73    210             
DBREF  5L5B Y  139   211  UNP    P30656   PSB5_YEAST     215    287             
DBREF  5L5B Z    1    96  UNP    P23724   PSB6_YEAST      20    115             
DBREF  5L5B Z   97   111  UNP    P20618   PSB1_HUMAN     124    138             
DBREF  5L5B Z  112   117  UNP    P23724   PSB6_YEAST     131    136             
DBREF  5L5B Z  118   133  UNP    P20618   PSB1_HUMAN     145    160             
DBREF  5L5B Z  134   222  UNP    P23724   PSB6_YEAST     153    241             
DBREF  5L5B a  -12   233  UNP    P30657   PSB7_YEAST      21    266             
DBREF  5L5B b    1   196  UNP    P38624   PSB1_YEAST      20    215             
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  211  THR THR THR LEU ALA PHE LYS PHE GLN HIS GLY VAL ILE          
SEQRES   2 K  211  ALA ALA VAL ASP SER ARG ALA SER ALA GLY SER TYR ILE          
SEQRES   3 K  211  SER ALA LEU ARG VAL ASN LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  211  TYR LEU LEU GLY THR MET SER GLY CYS ALA ALA ASP CYS          
SEQRES   5 K  211  GLN TYR TRP GLU ARG LEU LEU ALA LYS GLU CYS ARG LEU          
SEQRES   6 K  211  TYR TYR LEU ARG ASN GLY GLU ARG ILE SER VAL SER ALA          
SEQRES   7 K  211  ALA SER LYS LEU LEU SER ASN MET MET CYS GLN TYR ARG          
SEQRES   8 K  211  GLY MET GLY LEU SER MET GLY SER MET ILE CYS GLY TRP          
SEQRES   9 K  211  ASP LYS LYS GLY PRO GLY LEU TYR TYR VAL ASP GLU HIS          
SEQRES  10 K  211  GLY THR ARG LEU SER GLY ASN MET PHE SER THR GLY SER          
SEQRES  11 K  211  GLY ASN THR TYR ALA TYR GLY VAL LEU ASP SER ASN TYR          
SEQRES  12 K  211  LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY          
SEQRES  13 K  211  LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR          
SEQRES  14 K  211  SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP          
SEQRES  15 K  211  GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU          
SEQRES  16 K  211  PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN          
SEQRES  17 K  211  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 SER ARG ARG PHE PHE PRO          
SEQRES   9 L  222  TYR TYR VAL TYR ASN 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 GLN 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  211  THR THR THR LEU ALA PHE LYS PHE GLN HIS GLY VAL ILE          
SEQRES   2 Y  211  ALA ALA VAL ASP SER ARG ALA SER ALA GLY SER TYR ILE          
SEQRES   3 Y  211  SER ALA LEU ARG VAL ASN LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  211  TYR LEU LEU GLY THR MET SER GLY CYS ALA ALA ASP CYS          
SEQRES   5 Y  211  GLN TYR TRP GLU ARG LEU LEU ALA LYS GLU CYS ARG LEU          
SEQRES   6 Y  211  TYR TYR LEU ARG ASN GLY GLU ARG ILE SER VAL SER ALA          
SEQRES   7 Y  211  ALA SER LYS LEU LEU SER ASN MET MET CYS GLN TYR ARG          
SEQRES   8 Y  211  GLY MET GLY LEU SER MET GLY SER MET ILE CYS GLY TRP          
SEQRES   9 Y  211  ASP LYS LYS GLY PRO GLY LEU TYR TYR VAL ASP GLU HIS          
SEQRES  10 Y  211  GLY THR ARG LEU SER GLY ASN MET PHE SER THR GLY SER          
SEQRES  11 Y  211  GLY ASN THR TYR ALA TYR GLY VAL LEU ASP SER ASN TYR          
SEQRES  12 Y  211  LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY          
SEQRES  13 Y  211  LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR          
SEQRES  14 Y  211  SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP          
SEQRES  15 Y  211  GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU          
SEQRES  16 Y  211  PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN          
SEQRES  17 Y  211  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 SER ARG ARG PHE PHE PRO          
SEQRES   9 Z  222  TYR TYR VAL TYR ASN 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 GLN 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                                                          
HET     MG  G 301       1                                                       
HET     CL  G 302       1                                                       
HET     CL  G 303       1                                                       
HET     MG  H 301       1                                                       
HET     MG  I 301       1                                                       
HET     MG  I 302       1                                                       
HET     MG  J 201       1                                                       
HET     MG  K 301       1                                                       
HET     MG  L 301       1                                                       
HET     MG  N 201       1                                                       
HET     CL  U 301       1                                                       
HET     CL  U 302       1                                                       
HET     MG  Z 301       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL  29   MG    9(MG 2+)                                                     
FORMUL  30   CL    4(CL 1-)                                                     
FORMUL  42  HOH   *264(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 GLU B   57  SER B   61  5                                   5    
HELIX   12 AB3 LEU B   79  ASN B  102  1                                  24    
HELIX   13 AB4 PRO B  106  HIS B  124  1                                  19    
HELIX   14 AB5 ASN B  167  TYR B  179  1                                  13    
HELIX   15 AB6 LYS B  184  THR B  200  1                                  17    
HELIX   16 AB7 THR B  206  ASP B  208  5                                   3    
HELIX   17 AB8 LYS B  230  THR B  241  1                                  12    
HELIX   18 AB9 ILE C   15  GLY C   28  1                                  14    
HELIX   19 AC1 LEU C   76  GLU C   99  1                                  24    
HELIX   20 AC2 THR C  103  TYR C  118  1                                  16    
HELIX   21 AC3 ASN C  165  TYR C  177  1                                  13    
HELIX   22 AC4 THR C  185  GLU C  199  1                                  15    
HELIX   23 AC5 SER C  223  GLN C  239  1                                  17    
HELIX   24 AC6 LEU D   13  LEU D   25  1                                  13    
HELIX   25 AC7 GLU D   52  ILE D   56  5                                   5    
HELIX   26 AC8 ASP D   76  ASP D   96  1                                  21    
HELIX   27 AC9 ASN D  100  LEU D  113  1                                  14    
HELIX   28 AD1 GLY D  167  TRP D  179  1                                  13    
HELIX   29 AD2 THR D  184  MET D  200  1                                  17    
HELIX   30 AD3 ASP D  224  ALA D  241  1                                  18    
HELIX   31 AD4 LEU E   18  GLY E   31  1                                  14    
HELIX   32 AD5 LEU E   76  ASN E   99  1                                  24    
HELIX   33 AD6 ALA E  103  SER E  121  1                                  19    
HELIX   34 AD7 ARG E  163  ILE E  179  1                                  17    
HELIX   35 AD8 ASN E  184  SER E  197  1                                  14    
HELIX   36 AD9 GLN E  198  LEU E  200  5                                   3    
HELIX   37 AE1 ASP E  225  ILE E  233  5                                   9    
HELIX   38 AE2 ASN F   17  GLY F   30  1                                  14    
HELIX   39 AE3 LEU F   77  LYS F  100  1                                  24    
HELIX   40 AE4 PRO F  104  HIS F  119  1                                  16    
HELIX   41 AE5 GLY F  164  HIS F  179  1                                  16    
HELIX   42 AE6 SER F  184  HIS F  200  1                                  17    
HELIX   43 AE7 GLU F  201  LYS F  204  5                                   4    
HELIX   44 AE8 LYS F  228  ASN F  244  1                                  17    
HELIX   45 AE9 GLY G    2  HIS G    6  5                                   5    
HELIX   46 AF1 LEU G   16  THR G   26  1                                  11    
HELIX   47 AF2 ASP G   56  VAL G   60  5                                   5    
HELIX   48 AF3 PRO G   77  GLY G  100  1                                  24    
HELIX   49 AF4 PRO G  104  ARG G  122  1                                  19    
HELIX   50 AF5 LYS G  165  LYS G  181  1                                  17    
HELIX   51 AF6 SER G  189  GLY G  206  1                                  18    
HELIX   52 AF7 SER G  228  GLU G  241  1                                  14    
HELIX   53 AF8 THR H   48  SER H   71  1                                  24    
HELIX   54 AF9 ARG H   75  TYR H   90  1                                  16    
HELIX   55 AG1 GLY H  130  TRP H  142  1                                  13    
HELIX   56 AG2 THR H  147  ASP H  166  1                                  20    
HELIX   57 AG3 ASP I    2  ILE I    6  5                                   5    
HELIX   58 AG4 LEU I   55  GLU I   78  1                                  24    
HELIX   59 AG5 GLU I   82  GLU I   96  1                                  15    
HELIX   60 AG6 ALA I  141  TYR I  153  1                                  13    
HELIX   61 AG7 GLU I  158  ASP I  175  1                                  18    
HELIX   62 AG8 GLY J   51  ASP J   72  1                                  22    
HELIX   63 AG9 SER J   76  ARG J   93  1                                  18    
HELIX   64 AH1 TYR J  135  TYR J  148  1                                  14    
HELIX   65 AH2 THR J  153  MET J  172  1                                  20    
HELIX   66 AH3 CYS K   48  GLY K   71  1                                  24    
HELIX   67 AH4 SER K   75  CYS K   88  1                                  14    
HELIX   68 AH5 GLY K  131  TYR K  143  1                                  13    
HELIX   69 AH6 SER K  148  ASP K  167  1                                  20    
HELIX   70 AH7 VAL K  192  GLY K  204  1                                  13    
HELIX   71 AH8 PHE L   57  HIS L   79  1                                  23    
HELIX   72 AH9 SER L   85  SER L   99  1                                  15    
HELIX   73 AI1 ALA L  142  VAL L  154  1                                  13    
HELIX   74 AI2 SER L  176  HIS L  195  1                                  20    
HELIX   75 AI3 ILE M   57  TYR M   76  1                                  20    
HELIX   76 AI4 GLU M   88  LYS M  106  1                                  19    
HELIX   77 AI5 GLY M  145  ARG M  156  1                                  12    
HELIX   78 AI6 ARG M  161  ILE M  165  5                                   5    
HELIX   79 AI7 THR M  169  ASP M  188  1                                  20    
HELIX   80 AI8 TRP M  219  ILE M  225  5                                   7    
HELIX   81 AI9 SER N   48  GLY N   71  1                                  24    
HELIX   82 AJ1 SER N   74  ASN N   89  1                                  16    
HELIX   83 AJ2 LYS N   90  LEU N   93  5                                   4    
HELIX   84 AJ3 GLY N  128  PHE N  133  5                                   6    
HELIX   85 AJ4 ILE N  134  PHE N  142  1                                   9    
HELIX   86 AJ5 SER N  147  ASP N  166  1                                  20    
HELIX   87 AJ6 TYR N  189  GLU N  194  1                                   6    
HELIX   88 AJ7 LEU O   18  GLY O   31  1                                  14    
HELIX   89 AJ8 MET O   78  SER O   96  1                                  19    
HELIX   90 AJ9 TYR O   97  GLY O  102  1                                   6    
HELIX   91 AK1 PRO O  106  ALA O  121  1                                  16    
HELIX   92 AK2 GLY O  167  TRP O  179  1                                  13    
HELIX   93 AK3 GLU O  184  VAL O  200  1                                  17    
HELIX   94 AK4 ASN O  218  LEU O  222  5                                   5    
HELIX   95 AK5 THR O  239  ALA O  249  1                                  11    
HELIX   96 AK6 GLY P    1  ASP P    6  5                                   6    
HELIX   97 AK7 LEU P   18  SER P   29  1                                  12    
HELIX   98 AK8 GLU P   57  SER P   61  5                                   5    
HELIX   99 AK9 LEU P   79  ASN P  102  1                                  24    
HELIX  100 AL1 PRO P  106  HIS P  124  1                                  19    
HELIX  101 AL2 ASN P  167  TYR P  179  1                                  13    
HELIX  102 AL3 LYS P  184  THR P  200  1                                  17    
HELIX  103 AL4 THR P  206  ASP P  208  5                                   3    
HELIX  104 AL5 LYS P  230  THR P  241  1                                  12    
HELIX  105 AL6 ILE Q   15  GLY Q   28  1                                  14    
HELIX  106 AL7 LEU Q   76  GLU Q   99  1                                  24    
HELIX  107 AL8 THR Q  103  TYR Q  118  1                                  16    
HELIX  108 AL9 ASN Q  165  TYR Q  177  1                                  13    
HELIX  109 AM1 THR Q  185  GLU Q  199  1                                  15    
HELIX  110 AM2 SER Q  223  GLN Q  239  1                                  17    
HELIX  111 AM3 LEU R   13  LEU R   25  1                                  13    
HELIX  112 AM4 GLU R   52  ILE R   56  5                                   5    
HELIX  113 AM5 ASP R   76  ASP R   96  1                                  21    
HELIX  114 AM6 ASN R  100  LEU R  113  1                                  14    
HELIX  115 AM7 GLY R  167  TRP R  179  1                                  13    
HELIX  116 AM8 THR R  184  MET R  200  1                                  17    
HELIX  117 AM9 ASP R  224  ALA R  241  1                                  18    
HELIX  118 AN1 LEU S   18  GLY S   31  1                                  14    
HELIX  119 AN2 LEU S   76  ASN S   99  1                                  24    
HELIX  120 AN3 ALA S  103  SER S  121  1                                  19    
HELIX  121 AN4 ARG S  163  ILE S  179  1                                  17    
HELIX  122 AN5 ASN S  184  SER S  197  1                                  14    
HELIX  123 AN6 GLN S  198  LEU S  200  5                                   3    
HELIX  124 AN7 ASP S  225  ILE S  233  5                                   9    
HELIX  125 AN8 ASN T   17  GLY T   30  1                                  14    
HELIX  126 AN9 LEU T   77  LYS T  100  1                                  24    
HELIX  127 AO1 PRO T  104  HIS T  119  1                                  16    
HELIX  128 AO2 GLY T  164  HIS T  179  1                                  16    
HELIX  129 AO3 SER T  184  HIS T  200  1                                  17    
HELIX  130 AO4 GLU T  201  LYS T  204  5                                   4    
HELIX  131 AO5 LYS T  228  ASN T  244  1                                  17    
HELIX  132 AO6 GLY U    2  HIS U    6  5                                   5    
HELIX  133 AO7 LEU U   16  THR U   26  1                                  11    
HELIX  134 AO8 ASP U   56  VAL U   60  5                                   5    
HELIX  135 AO9 PRO U   77  GLY U  100  1                                  24    
HELIX  136 AP1 PRO U  104  ARG U  122  1                                  19    
HELIX  137 AP2 LYS U  165  LYS U  181  1                                  17    
HELIX  138 AP3 SER U  189  GLY U  206  1                                  18    
HELIX  139 AP4 SER U  228  GLU U  241  1                                  14    
HELIX  140 AP5 THR V   48  SER V   71  1                                  24    
HELIX  141 AP6 ARG V   75  TYR V   90  1                                  16    
HELIX  142 AP7 GLY V  130  TRP V  142  1                                  13    
HELIX  143 AP8 THR V  147  ASP V  166  1                                  20    
HELIX  144 AP9 ASP W    2  ILE W    6  5                                   5    
HELIX  145 AQ1 LEU W   55  GLU W   78  1                                  24    
HELIX  146 AQ2 GLU W   82  GLU W   96  1                                  15    
HELIX  147 AQ3 ALA W  141  TYR W  153  1                                  13    
HELIX  148 AQ4 GLU W  158  ASP W  175  1                                  18    
HELIX  149 AQ5 GLY X   51  ASP X   72  1                                  22    
HELIX  150 AQ6 SER X   76  ARG X   93  1                                  18    
HELIX  151 AQ7 TYR X  135  TYR X  148  1                                  14    
HELIX  152 AQ8 THR X  153  MET X  172  1                                  20    
HELIX  153 AQ9 CYS Y   48  GLY Y   71  1                                  24    
HELIX  154 AR1 SER Y   75  CYS Y   88  1                                  14    
HELIX  155 AR2 GLY Y  131  TYR Y  143  1                                  13    
HELIX  156 AR3 SER Y  148  ASP Y  167  1                                  20    
HELIX  157 AR4 VAL Y  192  GLY Y  204  1                                  13    
HELIX  158 AR5 PHE Z   57  HIS Z   79  1                                  23    
HELIX  159 AR6 SER Z   85  SER Z   99  1                                  15    
HELIX  160 AR7 ALA Z  142  VAL Z  154  1                                  13    
HELIX  161 AR8 SER Z  176  HIS Z  195  1                                  20    
HELIX  162 AR9 ILE a   57  TYR a   76  1                                  20    
HELIX  163 AS1 GLU a   88  LYS a  106  1                                  19    
HELIX  164 AS2 GLY a  145  ARG a  156  1                                  12    
HELIX  165 AS3 ARG a  161  ILE a  165  5                                   5    
HELIX  166 AS4 THR a  169  ASP a  188  1                                  20    
HELIX  167 AS5 TRP a  219  ILE a  225  5                                   7    
HELIX  168 AS6 SER b   48  GLY b   71  1                                  24    
HELIX  169 AS7 SER b   74  ASN b   89  1                                  16    
HELIX  170 AS8 LYS b   90  LEU b   93  5                                   4    
HELIX  171 AS9 GLY b  128  PHE b  133  5                                   6    
HELIX  172 AT1 ILE b  134  PHE b  142  1                                   9    
HELIX  173 AT2 SER b  147  ASP b  166  1                                  20    
HELIX  174 AT3 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  ALA A  39 -1  N  SER A  34   O  ILE A 164           
SHEET    3 AA1 5 GLY A  42  GLU A  48 -1  O  GLY A  42   N  ALA A  39           
SHEET    4 AA1 5 ILE A 209  ILE A 214 -1  O  ILE A 214   N  VAL A  43           
SHEET    5 AA1 5 PHE A 235  LYS A 237 -1  O  ARG A 236   N  ILE A 213           
SHEET    1 AA2 5 SER A  65  THR A  68  0                                        
SHEET    2 AA2 5 ILE A  71  GLY A  77 -1  O  ILE A  71   N  LEU A  67           
SHEET    3 AA2 5 VAL A 132  ASP A 140 -1  O  ALA A 137   N  GLY A  72           
SHEET    4 AA2 5 GLY A 144  VAL A 150 -1  O  TYR A 148   N  ILE A 136           
SHEET    5 AA2 5 TYR A 156  PRO A 158 -1  O  PHE A 157   N  GLN A 149           
SHEET    1 AA3 6 TYR A 224  THR A 225  0                                        
SHEET    2 AA3 6 ALA H 184  LEU H 191  1  O  TYR H 186   N  THR A 225           
SHEET    3 AA3 6 VAL H 173  GLU H 179 -1  N  VAL H 175   O  LEU H 187           
SHEET    4 AA3 6 GLY H  11  ASP H  17 -1  N  ALA H  16   O  ASP H 174           
SHEET    5 AA3 6 ILE H   3  PHE H   8 -1  N  VAL H   6   O  VAL H  13           
SHEET    6 AA3 6 TYR H 124  LEU H 127 -1  O  LEU H 127   N  ILE H   3           
SHEET    1 AA4 5 ALA B 161  VAL B 164  0                                        
SHEET    2 AA4 5 ALA B  34  ALA B  39 -1  N  GLY B  36   O  ILE B 162           
SHEET    3 AA4 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  ILE B  35           
SHEET    4 AA4 5 LEU B 210  ARG B 216 -1  O  ALA B 213   N  LEU B  45           
SHEET    5 AA4 5 TYR B 225  ILE B 228 -1  O  TYR B 225   N  ARG B 216           
SHEET    1 AA5 5 LEU B  65  LYS B  67  0                                        
SHEET    2 AA5 5 ILE B  72  GLY B  78 -1  O  VAL B  74   N  TYR B  66           
SHEET    3 AA5 5 VAL B 132  ASP B 140 -1  O  ALA B 137   N  ALA B  73           
SHEET    4 AA5 5 GLY B 144  SER B 150 -1  O  TYR B 148   N  TYR B 136           
SHEET    5 AA5 5 TYR B 156  TRP B 159 -1  O  TRP B 159   N  LEU B 147           
SHEET    1 AA6 5 ALA C 159  ILE C 162  0                                        
SHEET    2 AA6 5 ALA C  31  LYS C  35 -1  N  GLY C  33   O  GLN C 160           
SHEET    3 AA6 5 VAL C  40  GLU C  45 -1  O  VAL C  41   N  VAL C  34           
SHEET    4 AA6 5 ILE C 208  LYS C 214 -1  O  VAL C 213   N  VAL C  40           
SHEET    5 AA6 5 ASP C 218  ALA C 221 -1  O  ASP C 218   N  LYS C 214           
SHEET    1 AA7 5 SER C  63  LYS C  64  0                                        
SHEET    2 AA7 5 VAL C  69  GLY C  75 -1  O  LEU C  71   N  SER C  63           
SHEET    3 AA7 5 VAL C 129  GLY C 135 -1  O  ALA C 134   N  VAL C  70           
SHEET    4 AA7 5 LYS C 144  THR C 148 -1  O  TYR C 146   N  ILE C 133           
SHEET    5 AA7 5 TYR C 154  SER C 156 -1  O  SER C 155   N  GLN C 147           
SHEET    1 AA8 5 ALA D 161  ILE D 164  0                                        
SHEET    2 AA8 5 ALA D  29  ALA D  33 -1  N  GLY D  31   O  LYS D 162           
SHEET    3 AA8 5 VAL D  38  GLU D  43 -1  O  GLY D  41   N  ILE D  30           
SHEET    4 AA8 5 ALA D 209  THR D 215 -1  O  SER D 212   N  LEU D  40           
SHEET    5 AA8 5 GLY D 219  ILE D 222 -1  O  LYS D 221   N  CYS D 213           
SHEET    1 AA9 5 ILE D  59  ASP D  63  0                                        
SHEET    2 AA9 5 ILE D  66  GLY D  72 -1  O  CYS D  68   N  VAL D  60           
SHEET    3 AA9 5 VAL D 132  ASP D 140 -1  O  ALA D 137   N  GLY D  67           
SHEET    4 AA9 5 GLY D 144  ALA D 150 -1  O  PHE D 148   N  ILE D 136           
SHEET    5 AA9 5 PHE D 156  ARG D 158 -1  O  TYR D 157   N  HIS D 149           
SHEET    1 AB1 5 GLY E 157  ILE E 160  0                                        
SHEET    2 AB1 5 THR E  34  ARG E  38 -1  N  GLY E  36   O  THR E 158           
SHEET    3 AB1 5 HIS E  42  LEU E  48 -1  O  VAL E  46   N  VAL E  35           
SHEET    4 AB1 5 LEU E 210  GLY E 216 -1  O  SER E 211   N  ALA E  47           
SHEET    5 AB1 5 THR E 219  TYR E 224 -1  O  TYR E 224   N  ILE E 212           
SHEET    1 AB2 5 ILE E  62  ASP E  66  0                                        
SHEET    2 AB2 5 MET E  69  GLY E  75 -1  O  LEU E  71   N  ILE E  63           
SHEET    3 AB2 5 VAL E 129  ASP E 137 -1  O  ILE E 134   N  GLY E  70           
SHEET    4 AB2 5 GLY E 140  PHE E 146 -1  O  PHE E 146   N  LEU E 131           
SHEET    5 AB2 5 VAL E 152  GLU E 154 -1  O  THR E 153   N  GLU E 145           
SHEET    1 AB3 5 GLY F 158  THR F 161  0                                        
SHEET    2 AB3 5 SER F  33  LYS F  37 -1  N  GLY F  35   O  ALA F 159           
SHEET    3 AB3 5 GLY F  41  LEU F  49 -1  O  VAL F  43   N  ILE F  36           
SHEET    4 AB3 5 PHE F 208  SER F 216 -1  O  SER F 213   N  PHE F  44           
SHEET    5 AB3 5 HIS F 224  PHE F 226 -1  O  LYS F 225   N  TRP F 214           
SHEET    1 AB4 5 GLN F  64  VAL F  66  0                                        
SHEET    2 AB4 5 ILE F  70  GLY F  76 -1  O  CYS F  72   N  GLN F  64           
SHEET    3 AB4 5 VAL F 130  ASP F 138 -1  O  ILE F 133   N  VAL F  73           
SHEET    4 AB4 5 GLY F 141  LEU F 147 -1  O  TYR F 145   N  PHE F 134           
SHEET    5 AB4 5 TYR F 153  GLY F 155 -1  O  TRP F 154   N  MET F 146           
SHEET    1 AB5 5 ALA G 159  THR G 162  0                                        
SHEET    2 AB5 5 SER G  33  ARG G  37 -1  N  SER G  33   O  THR G 162           
SHEET    3 AB5 5 THR G  42  GLN G  47 -1  O  ILE G  45   N  LEU G  34           
SHEET    4 AB5 5 LEU G 214  THR G 220 -1  O  GLY G 217   N  VAL G  44           
SHEET    5 AB5 5 LYS G 223  THR G 226 -1  O  PHE G 225   N  VAL G 218           
SHEET    1 AB6 5 ILE G  63  CYS G  65  0                                        
SHEET    2 AB6 5 GLY G  71  ASN G  75 -1  O  MET G  72   N  PHE G  64           
SHEET    3 AB6 5 ILE G 131  ASP G 138 -1  O  VAL G 135   N  GLY G  71           
SHEET    4 AB6 5 GLY G 142  THR G 148 -1  O  TYR G 146   N  PHE G 134           
SHEET    5 AB6 5 TYR G 154  GLY G 156 -1  O  VAL G 155   N  LYS G 147           
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  ILE H 217  0                                        
SHEET    2 AB9 6 GLU I 193  LEU I 199 -1  O  TYR I 198   N  LEU H 213           
SHEET    3 AB9 6 ALA I 184  LYS I 190 -1  N  VAL I 186   O  ARG I 197           
SHEET    4 AB9 6 CYS I  19  ASP I  25 -1  N  ILE I  22   O  TYR I 187           
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  VAL I  35   N  LEU I  28           
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  ALA I 121   N  VAL I 108           
SHEET    5 AC2 5 ILE I 129  ASP I 130 -1  O  ASP I 130   N  GLY I 122           
SHEET    1 AC3 5 TYR J 130  ALA J 132  0                                        
SHEET    2 AC3 5 ILE J   4  ARG J   8 -1  N  GLY J   6   O  GLY J 131           
SHEET    3 AC3 5 SER J  12  SER J  18 -1  O  ALA J  16   N  LEU J   5           
SHEET    4 AC3 5 VAL J 179  ASP J 185 -1  O  ILE J 180   N  SER J  17           
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 MET K 125  THR K 128  0                                        
SHEET    2 AC6 5 THR K   3  PHE K   8 -1  N  ALA K   5   O  PHE K 126           
SHEET    3 AC6 5 GLY K  11  VAL K  16 -1  O  GLY K  11   N  PHE K   8           
SHEET    4 AC6 5 SER K 173  THR K 180 -1  O  VAL K 179   N  VAL K  12           
SHEET    5 AC6 5 GLY K 183  ASP K 191 -1  O  ILE K 185   N  HIS K 178           
SHEET    1 AC7 2 ALA K  20  ALA K  22  0                                        
SHEET    2 AC7 2 TYR K  25  ALA K  28 -1  O  TYR K  25   N  ALA K  22           
SHEET    1 AC8 4 VAL K  34  ASN K  38  0                                        
SHEET    2 AC8 4 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC8 4 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC8 4 SER K  46  GLY K  47 -1  N  SER K  46   O  GLY K  98           
SHEET    1 AC9 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AC9 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC9 5 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC9 5 GLY K 108  ASP K 115 -1  O  GLY K 110   N  GLY K 103           
SHEET    5 AC9 5 ARG K 120  SER K 122 -1  O  LEU K 121   N  TYR K 113           
SHEET    1 AD1 5 CYS L 136  GLY L 140  0                                        
SHEET    2 AD1 5 THR L  11  ALA L  16 -1  N  ILE L  12   O  GLY L 139           
SHEET    3 AD1 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AD1 5 GLY L 201  THR L 208 -1  O  VAL L 207   N  ALA L  21           
SHEET    5 AD1 5 GLY L 211  GLU L 218 -1  O  GLU L 215   N  ILE L 204           
SHEET    1 AD2 2 ASN L  29  THR L  31  0                                        
SHEET    2 AD2 2 SER L  34  SER L  37 -1  O  ASN L  36   N  ASN L  29           
SHEET    1 AD3 5 VAL L  43  GLY L  47  0                                        
SHEET    2 AD3 5 ILE L  50  GLY L  56 -1  O  MET L  52   N  PHE L  44           
SHEET    3 AD3 5 VAL L 107  LEU L 114 -1  O  TYR L 108   N  ASN L  55           
SHEET    4 AD3 5 GLY L 120  PHE L 125 -1  O  PHE L 125   N  ASN L 109           
SHEET    5 AD3 5 TYR L 131  GLU L 134 -1  O  GLU L 134   N  VAL L 122           
SHEET    1 AD4 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AD4 5 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD4 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD4 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD4 5 LEU M  42  VAL M  45 -1  N  ILE M  43   O  VAL M  51           
SHEET    1 AD5 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AD5 7 GLY M  28  TYR M  30 -1  N  TYR M  30   O  LEU M  33           
SHEET    3 AD5 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD5 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD5 7 ASN M 112  VAL M 119 -1  O  ALA M 117   N  VAL M  50           
SHEET    6 AD5 7 GLN M 125  ASN M 131 -1  O  VAL M 130   N  ILE M 114           
SHEET    7 AD5 7 THR M 136  SER M 138 -1  O  TYR M 137   N  TYR M 129           
SHEET    1 AD6 5 THR M 141  ALA M 143  0                                        
SHEET    2 AD6 5 VAL M  11  TYR M  16 -1  N  SER M  13   O  LEU M 142           
SHEET    3 AD6 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  TYR M  16           
SHEET    4 AD6 5 ASN M 194  ASP M 201 -1  O  ALA M 198   N  ILE M  22           
SHEET    5 AD6 5 GLY M 205  GLN M 213 -1  O  LYS M 209   N  LEU M 197           
SHEET    1 AD7 5 TYR N 124  ALA N 127  0                                        
SHEET    2 AD7 5 ILE N   3  THR N   7 -1  N  ILE N   3   O  ALA N 127           
SHEET    3 AD7 5 GLY N  11  ALA N  16 -1  O  GLY N  15   N  MET N   4           
SHEET    4 AD7 5 ILE N 173  THR N 179 -1  O  LEU N 178   N  VAL N  12           
SHEET    5 AD7 5 GLY N 182  PHE N 188 -1  O  GLU N 184   N  VAL N 177           
SHEET    1 AD8 2 THR N  20  THR N  22  0                                        
SHEET    2 AD8 2 TYR N  25  ASN N  28 -1  O  TYR N  25   N  THR N  22           
SHEET    1 AD9 5 LEU N  34  HIS N  38  0                                        
SHEET    2 AD9 5 ILE N  41  GLY N  47 -1  O  CYS N  43   N  THR N  35           
SHEET    3 AD9 5 ALA N  95  TYR N 102 -1  O  GLY N  96   N  SER N  46           
SHEET    4 AD9 5 GLY N 108  ILE N 113 -1  O  TYR N 111   N  VAL N  99           
SHEET    5 AD9 5 HIS N 120  LEU N 122 -1  O  LEU N 122   N  VAL N 110           
SHEET    1 AE1 5 ALA O 161  ILE O 164  0                                        
SHEET    2 AE1 5 SER O  34  ALA O  39 -1  N  SER O  34   O  ILE O 164           
SHEET    3 AE1 5 GLY O  42  GLU O  48 -1  O  GLY O  42   N  ALA O  39           
SHEET    4 AE1 5 ILE O 209  ILE O 214 -1  O  ILE O 214   N  VAL O  43           
SHEET    5 AE1 5 PHE O 235  LYS O 237 -1  O  ARG O 236   N  ILE O 213           
SHEET    1 AE2 6 ALA O  56  MET O  57  0                                        
SHEET    2 AE2 6 TYR U 154  TYR U 157 -1  O  GLY U 156   N  MET O  57           
SHEET    3 AE2 6 GLY U 142  THR U 148 -1  N  ILE U 145   O  TYR U 157           
SHEET    4 AE2 6 ILE U 131  ASP U 138 -1  N  PHE U 134   O  TYR U 146           
SHEET    5 AE2 6 GLY U  71  ASN U  75 -1  N  GLY U  71   O  VAL U 135           
SHEET    6 AE2 6 ILE U  63  CYS U  65 -1  N  PHE U  64   O  MET U  72           
SHEET    1 AE3 5 SER O  65  THR O  68  0                                        
SHEET    2 AE3 5 ILE O  71  GLY O  77 -1  O  ILE O  71   N  LEU O  67           
SHEET    3 AE3 5 VAL O 132  ASP O 140 -1  O  ALA O 137   N  GLY O  72           
SHEET    4 AE3 5 GLY O 144  VAL O 150 -1  O  TYR O 148   N  ILE O 136           
SHEET    5 AE3 5 TYR O 156  PRO O 158 -1  O  PHE O 157   N  GLN O 149           
SHEET    1 AE4 6 TYR O 224  THR O 225  0                                        
SHEET    2 AE4 6 ALA V 184  LEU V 191  1  O  TYR V 186   N  THR O 225           
SHEET    3 AE4 6 VAL V 173  GLU V 179 -1  N  VAL V 175   O  LEU V 187           
SHEET    4 AE4 6 GLY V  11  ASP V  17 -1  N  ALA V  16   O  ASP V 174           
SHEET    5 AE4 6 ILE V   3  PHE V   8 -1  N  VAL V   6   O  VAL V  13           
SHEET    6 AE4 6 TYR V 124  LEU V 127 -1  O  LEU V 127   N  ILE V   3           
SHEET    1 AE5 5 ALA P 161  VAL P 164  0                                        
SHEET    2 AE5 5 ALA P  34  ALA P  39 -1  N  GLY P  36   O  ILE P 162           
SHEET    3 AE5 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  ILE P  35           
SHEET    4 AE5 5 LEU P 210  ARG P 216 -1  O  ALA P 213   N  LEU P  45           
SHEET    5 AE5 5 TYR P 225  ILE P 228 -1  O  TYR P 225   N  ARG P 216           
SHEET    1 AE6 5 LEU P  65  LYS P  67  0                                        
SHEET    2 AE6 5 ILE P  72  GLY P  78 -1  O  VAL P  74   N  TYR P  66           
SHEET    3 AE6 5 VAL P 132  ASP P 140 -1  O  ALA P 137   N  ALA P  73           
SHEET    4 AE6 5 GLY P 144  SER P 150 -1  O  TYR P 148   N  TYR P 136           
SHEET    5 AE6 5 TYR P 156  TRP P 159 -1  O  TRP P 159   N  LEU P 147           
SHEET    1 AE7 5 ALA Q 159  ILE Q 162  0                                        
SHEET    2 AE7 5 ALA Q  31  LYS Q  35 -1  N  GLY Q  33   O  GLN Q 160           
SHEET    3 AE7 5 VAL Q  40  GLU Q  45 -1  O  VAL Q  41   N  VAL Q  34           
SHEET    4 AE7 5 ILE Q 208  LYS Q 214 -1  O  VAL Q 213   N  VAL Q  40           
SHEET    5 AE7 5 ASP Q 218  ALA Q 221 -1  O  ASP Q 218   N  LYS Q 214           
SHEET    1 AE8 5 SER Q  63  ASP Q  66  0                                        
SHEET    2 AE8 5 VAL Q  69  GLY Q  75 -1  O  LEU Q  71   N  SER Q  63           
SHEET    3 AE8 5 VAL Q 129  GLY Q 135 -1  O  ALA Q 134   N  VAL Q  70           
SHEET    4 AE8 5 LYS Q 144  THR Q 148 -1  O  TYR Q 146   N  ILE Q 133           
SHEET    5 AE8 5 TYR Q 154  SER Q 156 -1  O  SER Q 155   N  GLN Q 147           
SHEET    1 AE9 5 ALA R 161  ILE R 164  0                                        
SHEET    2 AE9 5 ALA R  29  ALA R  33 -1  N  GLY R  31   O  LYS R 162           
SHEET    3 AE9 5 VAL R  38  GLU R  43 -1  O  GLY R  41   N  ILE R  30           
SHEET    4 AE9 5 ALA R 209  THR R 215 -1  O  SER R 212   N  LEU R  40           
SHEET    5 AE9 5 GLY R 219  ILE R 222 -1  O  LYS R 221   N  CYS R 213           
SHEET    1 AF1 5 ILE R  59  ASP R  63  0                                        
SHEET    2 AF1 5 ILE R  66  GLY R  72 -1  O  CYS R  68   N  VAL R  60           
SHEET    3 AF1 5 VAL R 132  ASP R 140 -1  O  ALA R 137   N  GLY R  67           
SHEET    4 AF1 5 GLY R 144  ALA R 150 -1  O  PHE R 148   N  ILE R 136           
SHEET    5 AF1 5 PHE R 156  ARG R 158 -1  O  TYR R 157   N  HIS R 149           
SHEET    1 AF2 5 GLY S 157  ILE S 160  0                                        
SHEET    2 AF2 5 THR S  34  ARG S  38 -1  N  GLY S  36   O  THR S 158           
SHEET    3 AF2 5 HIS S  42  LEU S  48 -1  O  VAL S  46   N  VAL S  35           
SHEET    4 AF2 5 LEU S 210  GLY S 216 -1  O  SER S 211   N  ALA S  47           
SHEET    5 AF2 5 THR S 219  TYR S 224 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF3 5 ILE S  62  ASP S  66  0                                        
SHEET    2 AF3 5 MET S  69  GLY S  75 -1  O  LEU S  71   N  ILE S  63           
SHEET    3 AF3 5 VAL S 129  ASP S 137 -1  O  ILE S 134   N  GLY S  70           
SHEET    4 AF3 5 GLY S 140  PHE S 146 -1  O  PHE S 146   N  LEU S 131           
SHEET    5 AF3 5 VAL S 152  GLU S 154 -1  O  THR S 153   N  GLU S 145           
SHEET    1 AF4 5 GLY T 158  THR T 161  0                                        
SHEET    2 AF4 5 SER T  33  LYS T  37 -1  N  GLY T  35   O  ALA T 159           
SHEET    3 AF4 5 GLY T  41  LEU T  49 -1  O  VAL T  43   N  ILE T  36           
SHEET    4 AF4 5 PHE T 208  SER T 216 -1  O  SER T 213   N  PHE T  44           
SHEET    5 AF4 5 HIS T 224  PHE T 226 -1  O  LYS T 225   N  TRP T 214           
SHEET    1 AF5 5 GLN T  64  VAL T  66  0                                        
SHEET    2 AF5 5 ILE T  70  GLY T  76 -1  O  CYS T  72   N  GLN T  64           
SHEET    3 AF5 5 VAL T 130  ASP T 138 -1  O  ILE T 133   N  VAL T  73           
SHEET    4 AF5 5 GLY T 141  LEU T 147 -1  O  TYR T 145   N  PHE T 134           
SHEET    5 AF5 5 TYR T 153  GLY T 155 -1  O  TRP T 154   N  MET T 146           
SHEET    1 AF6 5 ALA U 159  THR U 162  0                                        
SHEET    2 AF6 5 SER U  33  ARG U  37 -1  N  SER U  33   O  THR U 162           
SHEET    3 AF6 5 THR U  42  GLN U  47 -1  O  ILE U  45   N  LEU U  34           
SHEET    4 AF6 5 LEU U 214  THR U 220 -1  O  GLY U 217   N  VAL U  44           
SHEET    5 AF6 5 LYS U 223  THR U 226 -1  O  PHE U 225   N  VAL U 218           
SHEET    1 AF7 2 SER V  20  GLN V  22  0                                        
SHEET    2 AF7 2 ILE V  25  ASP V  28 -1  O  ILE V  25   N  GLN V  22           
SHEET    1 AF8 5 LEU V  34  SER V  38  0                                        
SHEET    2 AF8 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF8 5 ALA V  96  ASP V 104 -1  O  TYR V  97   N  ALA V  46           
SHEET    4 AF8 5 GLY V 107  ILE V 113 -1  O  PHE V 111   N  VAL V 100           
SHEET    5 AF8 5 THR V 119  VAL V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AF9 6 VAL V 212  ILE V 217  0                                        
SHEET    2 AF9 6 GLU W 193  LEU W 199 -1  O  TYR W 198   N  LEU V 213           
SHEET    3 AF9 6 ALA W 184  LYS W 190 -1  N  VAL W 186   O  ARG W 197           
SHEET    4 AF9 6 CYS W  19  ASP W  25 -1  N  ILE W  22   O  TYR W 187           
SHEET    5 AF9 6 ILE W  10  GLY W  16 -1  N  VAL W  12   O  ALA W  23           
SHEET    6 AF9 6 PHE W 135  GLY W 139 -1  O  ILE W 136   N  ALA W  13           
SHEET    1 AG1 2 LEU W  28  SER W  30  0                                        
SHEET    2 AG1 2 LEU W  33  SER W  36 -1  O  VAL W  35   N  LEU W  28           
SHEET    1 AG2 5 ILE W  42  TYR W  45  0                                        
SHEET    2 AG2 5 VAL W  48  GLY W  54 -1  O  LEU W  50   N  PHE W  43           
SHEET    3 AG2 5 VAL W 104  ILE W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG2 5 PRO W 118  PHE W 123 -1  O  ALA W 121   N  VAL W 108           
SHEET    5 AG2 5 ILE W 129  ASP W 130 -1  O  ASP W 130   N  GLY W 122           
SHEET    1 AG3 5 TYR X 130  ALA X 132  0                                        
SHEET    2 AG3 5 ILE X   4  ARG X   8 -1  N  GLY X   6   O  GLY X 131           
SHEET    3 AG3 5 SER X  12  SER X  18 -1  O  ALA X  16   N  LEU X   5           
SHEET    4 AG3 5 VAL X 179  ASP X 185 -1  O  ILE X 180   N  SER X  17           
SHEET    5 AG3 5 GLY X 188  VAL X 192 -1  O  ARG X 190   N  ILE X 183           
SHEET    1 AG4 2 VAL X  21  ARG X  23  0                                        
SHEET    2 AG4 2 SER X  26  LYS X  29 -1  O  SER X  26   N  ARG X  23           
SHEET    1 AG5 5 THR X  35  SER X  39  0                                        
SHEET    2 AG5 5 THR X  42  GLY X  48 -1  O  MET X  44   N  ARG X  36           
SHEET    3 AG5 5 VAL X 100  ASP X 108 -1  O  GLY X 105   N  LEU X  43           
SHEET    4 AG5 5 LYS X 113  ILE X 119 -1  O  ILE X 119   N  VAL X 102           
SHEET    5 AG5 5 LYS X 125  GLU X 127 -1  O  VAL X 126   N  GLN X 118           
SHEET    1 AG6 5 MET Y 125  THR Y 128  0                                        
SHEET    2 AG6 5 THR Y   3  PHE Y   8 -1  N  ALA Y   5   O  PHE Y 126           
SHEET    3 AG6 5 GLY Y  11  VAL Y  16 -1  O  GLY Y  11   N  PHE Y   8           
SHEET    4 AG6 5 SER Y 173  THR Y 180 -1  O  VAL Y 179   N  VAL Y  12           
SHEET    5 AG6 5 GLY Y 183  ASP Y 191 -1  O  ILE Y 185   N  HIS Y 178           
SHEET    1 AG7 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG7 2 TYR Y  25  ALA Y  28 -1  O  TYR Y  25   N  ALA Y  22           
SHEET    1 AG8 4 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AG8 4 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AG8 4 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AG8 4 SER Y  46  GLY Y  47 -1  N  SER Y  46   O  GLY Y  98           
SHEET    1 AG9 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AG9 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AG9 5 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AG9 5 GLY Y 108  ASP Y 115 -1  O  GLY Y 110   N  GLY Y 103           
SHEET    5 AG9 5 ARG Y 120  SER Y 122 -1  O  LEU Y 121   N  TYR Y 113           
SHEET    1 AH1 5 CYS Z 136  GLY Z 140  0                                        
SHEET    2 AH1 5 THR Z  11  ALA Z  16 -1  N  ILE Z  12   O  GLY Z 139           
SHEET    3 AH1 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AH1 5 GLY Z 201  THR Z 208 -1  O  VAL Z 207   N  ALA Z  21           
SHEET    5 AH1 5 GLY Z 211  GLU Z 218 -1  O  GLU Z 215   N  ILE Z 204           
SHEET    1 AH2 2 ASN Z  29  THR Z  31  0                                        
SHEET    2 AH2 2 SER Z  34  SER Z  37 -1  O  ASN Z  36   N  ASN Z  29           
SHEET    1 AH3 5 VAL Z  43  GLY Z  47  0                                        
SHEET    2 AH3 5 ILE Z  50  GLY Z  56 -1  O  MET Z  52   N  PHE Z  44           
SHEET    3 AH3 5 VAL Z 107  LEU Z 114 -1  O  TYR Z 108   N  ASN Z  55           
SHEET    4 AH3 5 GLY Z 120  PHE Z 125 -1  O  PHE Z 125   N  ASN Z 109           
SHEET    5 AH3 5 TYR Z 131  GLU Z 134 -1  O  GLU Z 134   N  VAL Z 122           
SHEET    1 AH4 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH4 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH4 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH4 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH4 5 LEU a  42  VAL a  45 -1  N  ILE a  43   O  VAL a  51           
SHEET    1 AH5 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH5 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH5 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH5 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH5 7 ASN a 112  VAL a 119 -1  O  ALA a 117   N  VAL a  50           
SHEET    6 AH5 7 GLN a 125  ASN a 131 -1  O  VAL a 130   N  ILE a 114           
SHEET    7 AH5 7 THR a 136  SER a 138 -1  O  TYR a 137   N  TYR a 129           
SHEET    1 AH6 5 THR a 141  ALA a 143  0                                        
SHEET    2 AH6 5 VAL a  11  TYR a  16 -1  N  SER a  13   O  LEU a 142           
SHEET    3 AH6 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  TYR a  16           
SHEET    4 AH6 5 ASN a 194  ASP a 201 -1  O  ALA a 198   N  ILE a  22           
SHEET    5 AH6 5 GLY a 205  GLN a 213 -1  O  LYS a 209   N  LEU a 197           
SHEET    1 AH7 5 TYR b 124  ALA b 127  0                                        
SHEET    2 AH7 5 ILE b   3  THR b   7 -1  N  ILE b   3   O  ALA b 127           
SHEET    3 AH7 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4 AH7 5 ILE b 173  THR b 179 -1  O  LEU b 178   N  VAL b  12           
SHEET    5 AH7 5 GLY b 182  PHE b 188 -1  O  GLU b 184   N  VAL b 177           
SHEET    1 AH8 2 THR b  20  THR b  22  0                                        
SHEET    2 AH8 2 TYR b  25  ASN b  28 -1  O  TYR b  25   N  THR b  22           
SHEET    1 AH9 5 LEU b  34  HIS b  38  0                                        
SHEET    2 AH9 5 ILE b  41  GLY b  47 -1  O  CYS b  43   N  THR b  35           
SHEET    3 AH9 5 ALA b  95  TYR b 102 -1  O  GLY b  96   N  SER b  46           
SHEET    4 AH9 5 GLY b 108  ILE b 113 -1  O  TYR b 111   N  VAL b  99           
SHEET    5 AH9 5 HIS b 120  LEU b 122 -1  O  HIS b 120   N  THR b 112           
LINK         OG1 THR G   8                MG    MG G 301     1555   1555  2.61  
LINK         O   TYR G 119                MG    MG G 301     1555   1555  2.60  
LINK         O   ARG G 122                MG    MG G 301     1555   1555  2.39  
LINK         O   MET G 125                MG    MG G 301     1555   1555  2.14  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.32  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.61  
LINK         O   ASP I 204                MG    MG I 302     1555   1555  2.45  
LINK         O   THR J 124                MG    MG J 201     1555   1555  2.95  
LINK         O   ALA K 164                MG    MG K 301     1555   1555  2.32  
LINK         O   ASP K 167                MG    MG K 301     1555   1555  2.14  
LINK         O   SER K 170                MG    MG K 301     1555   1555  2.43  
LINK         OXT ASP L 222                MG    MG L 301     1555   1555  1.99  
LINK         O   ILE N 163                MG    MG N 201     1555   1555  2.69  
LINK         O   ASP N 166                MG    MG N 201     1555   1555  2.95  
LINK         O   SER N 169                MG    MG N 201     1555   1555  2.65  
LINK         O   ILE V 163                MG    MG L 301     1555   1555  2.14  
LINK         O   ASP V 166                MG    MG L 301     1555   1555  2.07  
LINK         O   SER V 169                MG    MG L 301     1555   1555  2.28  
LINK         O   ASP W 204                MG    MG K 301     1555   1555  2.39  
LINK         O   ALA Y 164                MG    MG I 302     1555   1555  2.34  
LINK         O   ASP Y 167                MG    MG I 302     1555   1555  2.10  
LINK         O   SER Y 170                MG    MG I 302     1555   1555  2.52  
LINK         O   THR Z 192                MG    MG Z 301     1555   1555  2.72  
LINK         O   HIS Z 195                MG    MG Z 301     1555   1555  2.86  
LINK         O   VAL Z 198                MG    MG Z 301     1555   1555  2.68  
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  1 CYS G  65                                                     
SITE     1 AC4  2 GLN H  91  ASP N  51                                          
SITE     1 AC5  4 ALA I 174  ASP I 177  SER I 180  ASP I 204                    
SITE     1 AC6  6 ASP I 204  ARG Y  19  ALA Y 164  ASP Y 167                    
SITE     2 AC6  6 ALA Y 168  SER Y 170                                          
SITE     1 AC7  3 GLN J 118  ASP J 120  THR J 124                               
SITE     1 AC8  6 ARG K  19  ALA K 164  ASP K 167  ALA K 168                    
SITE     2 AC8  6 SER K 170  ASP W 204                                          
SITE     1 AC9  4 ASP L 222  ILE V 163  ASP V 166  SER V 169                    
SITE     1 AD1  5 ARG N  19  ILE N 163  ASP N 166  SER N 169                    
SITE     2 AD1  5 LEU a  34                                                     
SITE     1 AD2  3 ARG U 111  ASN U 114  TYR V  69                               
SITE     1 AD3  1 CYS U  65                                                     
SITE     1 AD4  4 THR Z 192  HIS Z 195  VAL Z 198  ASP Z 222                    
CRYST1  134.050  301.900  144.450  90.00 112.61  90.00 P 1 21 1      4          
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      0.007460  0.000000  0.003107        0.00000                         
SCALE2      0.000000  0.003312  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007499        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 -0.999418 -0.003146  0.033970       66.69798    1                    
MTRIX2   2 -0.002742 -0.985107 -0.171918     -290.56039    1                    
MTRIX3   2  0.034005 -0.171912  0.984525      -26.26646    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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