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Database: PDB
Entry: 5MU8
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HEADER    CYTOKINE                                12-JAN-17   5MU8              
TITLE     HUMAN TNF-ALPHA IN COMPLEX WITH JNJ525                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A, B, C, D, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V,
COMPND   4 W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, 
COMPND   5 t, u, v, w;                                                          
COMPND   6 FRAGMENT: UNP RESIDUES 77-233;                                       
COMPND   7 SYNONYM: CACHECTIN,TNF-ALPHA,TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY
COMPND   8 MEMBER 2,TNF-A;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNF, TNFA, TNFSF2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TUMOR NECROSIS FACTOR ALPHA, PROTEROS BIOSTRUCTURES GMBH, CYTOKINE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.BLEVITT,M.D.HACK,K.L.HERMAN,P.F.JACKSON,P.J.KRAWCZUK,A.D.LEBSACK, 
AUTHOR   2 A.X.LIU,T.MIRZADEGAN,M.I.NELEN,A.P.PATRICK,S.STEINBACHER,M.E.MILLA,  
AUTHOR   3 K.J.LUMB                                                             
REVDAT   3   10-MAY-17 5MU8    1       JRNL                                     
REVDAT   2   12-APR-17 5MU8    1       JRNL                                     
REVDAT   1   29-MAR-17 5MU8    0                                                
JRNL        AUTH   J.M.BLEVITT,M.D.HACK,K.L.HERMAN,P.F.JACKSON,P.J.KRAWCZUK,    
JRNL        AUTH 2 A.D.LEBSACK,A.X.LIU,T.MIRZADEGAN,M.I.NELEN,A.N.PATRICK,      
JRNL        AUTH 3 S.STEINBACHER,M.E.MILLA,K.J.LUMB                             
JRNL        TITL   STRUCTURAL BASIS OF SMALL-MOLECULE AGGREGATE INDUCED         
JRNL        TITL 2 INHIBITION OF A PROTEIN-PROTEIN INTERACTION.                 
JRNL        REF    J. MED. CHEM.                 V.  60  3511 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28300404                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01836                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 184.24                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 158401                         
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 445                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11123                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 33                           
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 54511                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1794                                    
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 114.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.07000                                             
REMARK   3    B22 (A**2) : 4.15000                                              
REMARK   3    B33 (A**2) : -1.38000                                             
REMARK   3    B12 (A**2) : 2.12000                                              
REMARK   3    B13 (A**2) : -0.66000                                             
REMARK   3    B23 (A**2) : -1.03000                                             
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): 0.555         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.573         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 69.685        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 57790 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 54951 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 78695 ; 1.448 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):125964 ; 2.413 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6866 ; 7.644 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2540 ;37.875 ;24.535       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  9089 ;17.413 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   310 ;14.200 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  8516 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 65580 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A): 13606 ; 0.003 ; 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): 27731 ; 5.175 ; 4.558       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 27730 ; 5.175 ; 4.558       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34508 ; 8.175 ; 7.653       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 34509 ; 8.175 ; 7.653       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 30059 ; 7.798 ; 5.862       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 30059 ; 7.798 ; 5.862       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 44187 ;11.385 ; 9.572       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 61250 ;15.103 ;23.817       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 61251 ;15.103 ;23.817       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 48                                         
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     9        A   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4750  20.6820  11.1220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7688 T22:   0.2288                                     
REMARK   3      T33:   1.2185 T12:   0.0162                                     
REMARK   3      T13:  -0.3009 T23:  -0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5334 L22:   3.5637                                     
REMARK   3      L33:   6.6094 L12:   0.7153                                     
REMARK   3      L13:  -0.8169 L23:  -0.2575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0910 S12:   0.6819 S13:   0.1862                       
REMARK   3      S21:  -0.5281 S22:   0.0799 S23:   0.4596                       
REMARK   3      S31:  -0.1422 S32:  -0.4039 S33:   0.0112                       
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    10        B   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7340  19.1610  21.8570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5778 T22:   0.0473                                     
REMARK   3      T33:   0.9413 T12:  -0.0490                                     
REMARK   3      T13:  -0.2033 T23:  -0.1662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1914 L22:   3.6848                                     
REMARK   3      L33:   6.4101 L12:  -0.4069                                     
REMARK   3      L13:  -1.5903 L23:  -0.1509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0301 S12:   0.0183 S13:   0.4527                       
REMARK   3      S21:  -0.1040 S22:  -0.0356 S23:   0.1589                       
REMARK   3      S31:  -0.2127 S32:   0.0568 S33:   0.0055                       
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     8        C   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2770  -6.2500  29.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8793 T22:   0.4550                                     
REMARK   3      T33:   1.4236 T12:  -0.0522                                     
REMARK   3      T13:  -0.0653 T23:  -0.1671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1605 L22:   2.7883                                     
REMARK   3      L33:   7.1160 L12:  -0.4427                                     
REMARK   3      L13:  -1.0124 L23:  -0.7223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1928 S12:  -0.2320 S13:   0.1731                       
REMARK   3      S21:   0.1615 S22:   0.1112 S23:   0.6697                       
REMARK   3      S31:  -0.3111 S32:  -1.2837 S33:   0.0817                       
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     9        D   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.6260 -10.6970  29.8470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6443 T22:   0.0825                                     
REMARK   3      T33:   0.9071 T12:   0.0110                                     
REMARK   3      T13:  -0.0801 T23:  -0.1146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3832 L22:   2.9764                                     
REMARK   3      L33:   6.6432 L12:   0.6965                                     
REMARK   3      L13:  -0.5976 L23:  -0.7132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2063 S12:  -0.3320 S13:  -0.2800                       
REMARK   3      S21:   0.1193 S22:   0.0722 S23:   0.2858                       
REMARK   3      S31:   0.2818 S32:  -0.2736 S33:   0.1340                       
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 :   F     9        F   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.5370   5.7980  99.4960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6208 T22:   0.1739                                     
REMARK   3      T33:   0.8121 T12:   0.0109                                     
REMARK   3      T13:  -0.1841 T23:  -0.0508                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2579 L22:   3.9732                                     
REMARK   3      L33:   6.8520 L12:   0.2611                                     
REMARK   3      L13:  -2.1625 L23:  -0.3634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1327 S12:   0.6439 S13:   0.1040                       
REMARK   3      S21:  -0.4552 S22:  -0.0427 S23:   0.1855                       
REMARK   3      S31:  -0.0346 S32:  -0.1983 S33:   0.1754                       
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 :   G     9        G   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  85.3290   5.5610 110.7150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6678 T22:   0.0726                                     
REMARK   3      T33:   0.8171 T12:  -0.0628                                     
REMARK   3      T13:  -0.1347 T23:  -0.2053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5876 L22:   3.0105                                     
REMARK   3      L33:   5.0018 L12:  -0.3836                                     
REMARK   3      L13:  -1.2462 L23:   0.1901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0216 S12:   0.0693 S13:   0.3676                       
REMARK   3      S21:   0.2222 S22:  -0.0480 S23:  -0.0845                       
REMARK   3      S31:  -0.2780 S32:  -0.0336 S33:   0.0696                       
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 :   H     8        H   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.7460 -20.6040 119.4560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1245 T22:   0.4742                                     
REMARK   3      T33:   1.2549 T12:  -0.1262                                     
REMARK   3      T13:  -0.0002 T23:  -0.1215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1439 L22:   2.3007                                     
REMARK   3      L33:   6.4551 L12:  -0.4659                                     
REMARK   3      L13:  -0.5093 L23:  -0.5391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1457 S12:  -0.3522 S13:  -0.0044                       
REMARK   3      S21:   0.4172 S22:   0.1458 S23:   0.5735                       
REMARK   3      S31:  -0.5925 S32:  -1.2011 S33:  -0.0001                       
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 :   I     9        I   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  79.5020 -24.2010 119.1460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8828 T22:   0.1334                                     
REMARK   3      T33:   0.8019 T12:  -0.1455                                     
REMARK   3      T13:  -0.1020 T23:  -0.1534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8307 L22:   2.5474                                     
REMARK   3      L33:   6.0708 L12:   0.9039                                     
REMARK   3      L13:  -2.0945 L23:  -1.0352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0104 S12:  -0.2801 S13:  -0.3161                       
REMARK   3      S21:   0.2692 S22:  -0.0650 S23:   0.1202                       
REMARK   3      S31:   0.3516 S32:  -0.1595 S33:   0.0755                       
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 :   J     9        J   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2600  33.2600 132.5840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9649 T22:   0.6990                                     
REMARK   3      T33:   1.2304 T12:  -0.0171                                     
REMARK   3      T13:   0.0694 T23:  -0.0952                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8942 L22:   2.9400                                     
REMARK   3      L33:   6.6835 L12:  -0.7475                                     
REMARK   3      L13:   0.5824 L23:  -1.3065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0931 S12:  -0.6411 S13:   0.0012                       
REMARK   3      S21:   0.4792 S22:  -0.0256 S23:   0.5632                       
REMARK   3      S31:  -0.4001 S32:  -1.2660 S33:   0.1187                       
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 :   K     9        K   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3080  32.1170 128.2390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7397 T22:   0.0801                                     
REMARK   3      T33:   0.8200 T12:  -0.0182                                     
REMARK   3      T13:  -0.0406 T23:  -0.1340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8679 L22:   2.5594                                     
REMARK   3      L33:   7.5890 L12:   0.2650                                     
REMARK   3      L13:   0.1197 L23:  -0.3651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0254 S12:  -0.3279 S13:  -0.2739                       
REMARK   3      S21:   0.2573 S22:  -0.0223 S23:   0.1754                       
REMARK   3      S31:   0.2716 S32:  -0.2466 S33:  -0.0032                       
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 :   L     8        L   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3010  59.2610 111.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1556 T22:   0.7389                                     
REMARK   3      T33:   1.2696 T12:   0.2929                                     
REMARK   3      T13:  -0.1329 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3230 L22:   2.3104                                     
REMARK   3      L33:   9.0933 L12:   0.4104                                     
REMARK   3      L13:  -2.5062 L23:   0.8355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0755 S12:   0.5195 S13:  -0.2547                       
REMARK   3      S21:  -0.0680 S22:  -0.0347 S23:   0.6327                       
REMARK   3      S31:   0.0938 S32:  -1.5725 S33:   0.1102                       
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 :   M     9        M   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1450  61.9460 115.9990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9024 T22:   0.0565                                     
REMARK   3      T33:   0.8015 T12:   0.0276                                     
REMARK   3      T13:  -0.0855 T23:  -0.1580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2424 L22:   2.5401                                     
REMARK   3      L33:   7.0411 L12:  -0.0219                                     
REMARK   3      L13:   0.0227 L23:  -0.5564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0304 S12:   0.1461 S13:   0.2176                       
REMARK   3      S21:  -0.0558 S22:   0.0274 S23:   0.2260                       
REMARK   3      S31:  -0.7017 S32:  -0.2970 S33:   0.0029                       
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 :   N     9        N   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0800  64.3810 159.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0758 T22:   0.1362                                     
REMARK   3      T33:   0.6055 T12:  -0.0267                                     
REMARK   3      T13:  -0.1236 T23:  -0.2472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3395 L22:   2.9564                                     
REMARK   3      L33:   4.7995 L12:   0.2388                                     
REMARK   3      L13:  -1.2643 L23:  -0.1895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0181 S12:  -0.1519 S13:  -0.1905                       
REMARK   3      S21:   0.1862 S22:   0.0467 S23:   0.0060                       
REMARK   3      S31:  -0.0918 S32:   0.0324 S33:  -0.0286                       
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 :   O     9        O   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6320  64.1440 138.4580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0317 T22:   0.0880                                     
REMARK   3      T33:   0.5965 T12:  -0.1045                                     
REMARK   3      T13:  -0.0900 T23:  -0.1768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0730 L22:   3.1178                                     
REMARK   3      L33:   4.1611 L12:  -0.5052                                     
REMARK   3      L13:  -0.7162 L23:   0.7707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0004 S12:   0.0624 S13:   0.1396                       
REMARK   3      S21:  -0.0506 S22:   0.0733 S23:   0.0426                       
REMARK   3      S31:  -0.4550 S32:   0.0662 S33:  -0.0729                       
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 :   P     8        P   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.9110  35.9480 153.7640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3144 T22:   0.6485                                     
REMARK   3      T33:   0.9448 T12:   0.1485                                     
REMARK   3      T13:  -0.2366 T23:  -0.1499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8173 L22:   2.3792                                     
REMARK   3      L33:   5.5457 L12:   0.2341                                     
REMARK   3      L13:  -2.1322 L23:   0.9977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0234 S12:  -0.4744 S13:   0.0002                       
REMARK   3      S21:   0.3922 S22:   0.1004 S23:  -0.6715                       
REMARK   3      S31:   0.0875 S32:   0.9633 S33:  -0.0769                       
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 :   Q     9        Q   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.6480  33.3880 137.0360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0246 T22:   0.1544                                     
REMARK   3      T33:   0.7422 T12:   0.0200                                     
REMARK   3      T13:  -0.2017 T23:  -0.2536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5890 L22:   2.8373                                     
REMARK   3      L33:   4.6417 L12:  -1.4043                                     
REMARK   3      L13:  -2.0739 L23:   0.8830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0624 S12:  -0.1138 S13:  -0.4019                       
REMARK   3      S21:   0.1917 S22:   0.1975 S23:  -0.1331                       
REMARK   3      S31:   0.3319 S32:   0.5682 S33:  -0.1352                       
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 :   R     9        R   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4630  -1.4230 102.2120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8178 T22:   0.3766                                     
REMARK   3      T33:   1.0578 T12:  -0.0448                                     
REMARK   3      T13:  -0.1174 T23:  -0.2254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6455 L22:   3.1389                                     
REMARK   3      L33:   6.0484 L12:  -0.0214                                     
REMARK   3      L13:   0.6195 L23:   0.5944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:  -0.1297 S13:  -0.3216                       
REMARK   3      S21:   0.2513 S22:   0.1800 S23:  -0.5928                       
REMARK   3      S31:   0.4112 S32:   1.1024 S33:  -0.1900                       
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 :   S     9        S   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1110   2.2430 112.1680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7499 T22:   0.0956                                     
REMARK   3      T33:   0.7532 T12:  -0.0242                                     
REMARK   3      T13:  -0.1214 T23:  -0.1450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1208 L22:   3.5448                                     
REMARK   3      L33:   4.7586 L12:   0.9877                                     
REMARK   3      L13:   2.2356 L23:   0.8169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0593 S12:  -0.3560 S13:   0.2031                       
REMARK   3      S21:   0.4100 S22:  -0.1147 S23:  -0.1921                       
REMARK   3      S31:   0.0172 S32:   0.2487 S33:   0.0553                       
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 :   T     8        T   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9430 -28.3540  88.6540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0057 T22:   0.1466                                     
REMARK   3      T33:   0.8300 T12:   0.0370                                     
REMARK   3      T13:  -0.0570 T23:  -0.2632                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5576 L22:   3.6730                                     
REMARK   3      L33:   7.3811 L12:  -0.0039                                     
REMARK   3      L13:   0.9430 L23:  -0.6575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1821 S12:   0.5982 S13:   0.0049                       
REMARK   3      S21:  -0.2053 S22:   0.1069 S23:  -0.4309                       
REMARK   3      S31:   0.3741 S32:   0.3844 S33:   0.0751                       
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 :   U     9        U   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5300 -27.9350 106.5090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0479 T22:   0.0839                                     
REMARK   3      T33:   0.7756 T12:   0.0558                                     
REMARK   3      T13:  -0.0502 T23:  -0.0728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2305 L22:   3.0709                                     
REMARK   3      L33:   4.8768 L12:  -0.1029                                     
REMARK   3      L13:   0.8561 L23:   0.5180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:  -0.1576 S13:  -0.3291                       
REMARK   3      S21:   0.1528 S22:  -0.0728 S23:  -0.0422                       
REMARK   3      S31:   0.9174 S32:   0.0413 S33:   0.1086                       
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 :   V     9        V   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.0230  10.0360   9.9230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9370 T22:   0.3989                                     
REMARK   3      T33:   1.3255 T12:  -0.0874                                     
REMARK   3      T13:   0.0233 T23:  -0.1320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3551 L22:   2.8933                                     
REMARK   3      L33:   6.2343 L12:   0.0445                                     
REMARK   3      L13:  -0.6297 L23:   1.1894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0395 S12:   0.1293 S13:   0.1369                       
REMARK   3      S21:  -0.1584 S22:   0.0433 S23:  -0.8685                       
REMARK   3      S31:   0.2561 S32:   1.3425 S33:  -0.0829                       
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 :   W     9        W   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.8130  13.8710  20.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7063 T22:   0.0597                                     
REMARK   3      T33:   0.8116 T12:   0.0044                                     
REMARK   3      T13:  -0.0280 T23:  -0.1153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3744 L22:   3.1133                                     
REMARK   3      L33:   6.4986 L12:   0.2140                                     
REMARK   3      L13:   1.9793 L23:   0.2041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0049 S12:  -0.1168 S13:   0.5052                       
REMARK   3      S21:  -0.0875 S22:  -0.1330 S23:  -0.1893                       
REMARK   3      S31:   0.0518 S32:   0.3957 S33:   0.1378                       
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 :   X     8        X   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3100 -14.8050  -4.9310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1504 T22:   0.1737                                     
REMARK   3      T33:   0.7448 T12:  -0.0248                                     
REMARK   3      T13:  -0.0139 T23:  -0.2422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9577 L22:   3.0880                                     
REMARK   3      L33:   7.2302 L12:  -0.6967                                     
REMARK   3      L13:   2.2632 L23:  -1.3004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0736 S12:   0.6713 S13:   0.3888                       
REMARK   3      S21:  -0.3492 S22:  -0.0513 S23:  -0.1128                       
REMARK   3      S31:  -0.0787 S32:   0.2574 S33:   0.1249                       
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 :   Y     9        Y   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.5660 -14.8620  13.8890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9132 T22:   0.0485                                     
REMARK   3      T33:   0.6421 T12:   0.0280                                     
REMARK   3      T13:  -0.0051 T23:  -0.1279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3729 L22:   2.6397                                     
REMARK   3      L33:   4.8132 L12:   0.1600                                     
REMARK   3      L13:   1.8709 L23:  -0.1570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:   0.2148 S13:  -0.2690                       
REMARK   3      S21:  -0.1809 S22:   0.0038 S23:   0.0959                       
REMARK   3      S31:   0.4651 S32:  -0.2171 S33:   0.0834                       
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 :   Z     9        Z   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.0540  45.3480  38.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9491 T22:   0.3500                                     
REMARK   3      T33:   1.2813 T12:  -0.0524                                     
REMARK   3      T13:  -0.0307 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9443 L22:   2.1033                                     
REMARK   3      L33:   7.3966 L12:  -0.1160                                     
REMARK   3      L13:   1.7065 L23:  -0.0463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0368 S12:  -0.6716 S13:  -0.0637                       
REMARK   3      S21:   0.5564 S22:   0.0358 S23:   0.5460                       
REMARK   3      S31:  -0.1983 S32:  -0.8485 S33:   0.0009                       
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 :   a     9        a   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.9270  45.0410  34.3610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7879 T22:   0.0888                                     
REMARK   3      T33:   1.0815 T12:  -0.0286                                     
REMARK   3      T13:  -0.2110 T23:  -0.1068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1199 L22:   2.9899                                     
REMARK   3      L33:   6.2028 L12:   0.2105                                     
REMARK   3      L13:  -0.8372 L23:   0.0809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:  -0.4075 S13:  -0.4837                       
REMARK   3      S21:   0.3604 S22:   0.0047 S23:  -0.0672                       
REMARK   3      S31:   0.2916 S32:   0.1136 S33:  -0.0004                       
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 :   b     8        b   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.5120  72.3180  17.2140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8856 T22:   0.2475                                     
REMARK   3      T33:   1.1426 T12:   0.1307                                     
REMARK   3      T13:  -0.1700 T23:  -0.0707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4238 L22:   2.8913                                     
REMARK   3      L33:   9.1638 L12:   0.4294                                     
REMARK   3      L13:  -1.5970 L23:   0.3674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0500 S12:   0.3480 S13:  -0.0628                       
REMARK   3      S21:  -0.3822 S22:   0.0335 S23:   0.3762                       
REMARK   3      S31:   0.1608 S32:  -1.0057 S33:   0.0166                       
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 :   c     9        c   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.0680  75.0630  24.2330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7576 T22:   0.0385                                     
REMARK   3      T33:   0.8815 T12:   0.0038                                     
REMARK   3      T13:  -0.1227 T23:  -0.1764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7747 L22:   3.2435                                     
REMARK   3      L33:   6.5440 L12:  -0.0586                                     
REMARK   3      L13:  -0.6403 L23:  -0.2001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0496 S12:   0.0340 S13:   0.2219                       
REMARK   3      S21:  -0.1078 S22:  -0.0296 S23:   0.1286                       
REMARK   3      S31:  -0.4242 S32:  -0.0678 S33:  -0.0199                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   d     9        d   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4910  29.7460  87.1540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1731 T22:   0.3920                                     
REMARK   3      T33:   0.8571 T12:   0.0356                                     
REMARK   3      T13:   0.0201 T23:  -0.2491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8138 L22:   4.1570                                     
REMARK   3      L33:   5.0985 L12:   0.2971                                     
REMARK   3      L13:   0.3448 L23:  -0.1538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1614 S12:   0.8635 S13:   0.4806                       
REMARK   3      S21:  -0.6379 S22:  -0.0283 S23:  -0.1740                       
REMARK   3      S31:  -0.2151 S32:   0.1705 S33:  -0.1330                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   e     9        e   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8160  30.6700 107.2310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8174 T22:   0.0452                                     
REMARK   3      T33:   0.7194 T12:   0.0400                                     
REMARK   3      T13:  -0.0814 T23:  -0.1605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7262 L22:   3.0338                                     
REMARK   3      L33:   4.4275 L12:   0.5318                                     
REMARK   3      L13:   1.4189 L23:   1.0287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1342 S12:   0.1165 S13:  -0.0305                       
REMARK   3      S21:   0.0511 S22:   0.0613 S23:   0.0577                       
REMARK   3      S31:   0.2542 S32:   0.2377 S33:  -0.1954                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   f     8        f   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.6500  59.0960  93.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3912 T22:   0.8797                                     
REMARK   3      T33:   1.1624 T12:  -0.1749                                     
REMARK   3      T13:   0.1867 T23:  -0.1506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2261 L22:   3.1477                                     
REMARK   3      L33:   6.4574 L12:   0.3153                                     
REMARK   3      L13:   1.5611 L23:   1.1711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0854 S12:   0.8749 S13:  -0.0379                       
REMARK   3      S21:  -0.4649 S22:  -0.0726 S23:  -0.6459                       
REMARK   3      S31:   0.3395 S32:   1.3787 S33:  -0.0128                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   g     9        g   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7590  61.5750 108.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9543 T22:   0.1761                                     
REMARK   3      T33:   0.7171 T12:  -0.1802                                     
REMARK   3      T13:   0.0517 T23:  -0.1918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1955 L22:   3.7445                                     
REMARK   3      L33:   5.7904 L12:   1.3111                                     
REMARK   3      L13:   2.8269 L23:   1.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0284 S12:   0.1054 S13:   0.3769                       
REMARK   3      S21:  -0.1976 S22:   0.0953 S23:  -0.1756                       
REMARK   3      S31:  -0.5089 S32:   0.7111 S33:  -0.0669                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   h     9        h   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.8720  14.6550  68.9770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3340 T22:   0.4816                                     
REMARK   3      T33:   0.7648 T12:   0.0055                                     
REMARK   3      T13:  -0.1336 T23:  -0.3399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6410 L22:   3.8372                                     
REMARK   3      L33:   5.2110 L12:  -1.5755                                     
REMARK   3      L13:   0.1187 L23:  -0.9742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1568 S12:  -0.9268 S13:  -0.2317                       
REMARK   3      S21:   0.7240 S22:   0.1486 S23:   0.2360                       
REMARK   3      S31:  -0.1300 S32:  -0.3222 S33:   0.0081                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   i     9        i   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1130  15.7840  47.7360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8866 T22:   0.1334                                     
REMARK   3      T33:   0.7051 T12:  -0.0346                                     
REMARK   3      T13:  -0.1625 T23:  -0.2523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8286 L22:   3.1937                                     
REMARK   3      L33:   3.9878 L12:  -1.4896                                     
REMARK   3      L13:  -0.9388 L23:   0.1989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:  -0.2961 S13:   0.3727                       
REMARK   3      S21:   0.2695 S22:  -0.1073 S23:   0.1264                       
REMARK   3      S31:  -0.2773 S32:  -0.1064 S33:   0.0806                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   j     8        j   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.2600 -16.2840  63.5230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2955 T22:   0.6271                                     
REMARK   3      T33:   0.9728 T12:  -0.0128                                     
REMARK   3      T13:  -0.1883 T23:  -0.0618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8771 L22:   3.5505                                     
REMARK   3      L33:   4.8480 L12:  -0.4232                                     
REMARK   3      L13:  -0.7155 L23:   0.5153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2399 S12:  -1.0120 S13:   0.1826                       
REMARK   3      S21:   0.4910 S22:  -0.1044 S23:  -0.5578                       
REMARK   3      S31:  -0.2560 S32:   0.7080 S33:  -0.1355                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   k     9        k   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1430 -15.0820  45.1440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8579 T22:   0.1409                                     
REMARK   3      T33:   0.6058 T12:  -0.0339                                     
REMARK   3      T13:  -0.1216 T23:  -0.0888                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9360 L22:   4.4533                                     
REMARK   3      L33:   3.3295 L12:  -1.9792                                     
REMARK   3      L13:  -0.7118 L23:   0.4430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0115 S12:  -0.2385 S13:  -0.3632                       
REMARK   3      S21:   0.2871 S22:  -0.0640 S23:   0.1117                       
REMARK   3      S31:   0.2592 S32:  -0.0068 S33:   0.0754                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   l     9        l   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3390  77.6300  68.5670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0765 T22:   0.2541                                     
REMARK   3      T33:   0.8425 T12:  -0.0458                                     
REMARK   3      T13:  -0.1009 T23:  -0.2881                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6429 L22:   2.4639                                     
REMARK   3      L33:   4.9751 L12:   0.0243                                     
REMARK   3      L13:  -1.2456 L23:  -0.6301                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0639 S12:  -0.2210 S13:  -0.4305                       
REMARK   3      S21:   0.5072 S22:   0.0186 S23:   0.1065                       
REMARK   3      S31:   0.1459 S32:   0.0342 S33:   0.0454                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   m     9        m   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9750  77.5780  47.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9247 T22:   0.2376                                     
REMARK   3      T33:   0.7692 T12:  -0.1285                                     
REMARK   3      T13:  -0.1471 T23:  -0.2246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9903 L22:   2.3566                                     
REMARK   3      L33:   3.5337 L12:  -0.0965                                     
REMARK   3      L13:  -1.4792 L23:  -0.0541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2616 S12:  -0.0871 S13:   0.1608                       
REMARK   3      S21:   0.0355 S22:  -0.1338 S23:   0.1093                       
REMARK   3      S31:  -0.2144 S32:  -0.0372 S33:  -0.1278                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   n     8        n   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0610  50.6650  62.6060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4169 T22:   0.9865                                     
REMARK   3      T33:   1.3346 T12:   0.2707                                     
REMARK   3      T13:  -0.3314 T23:  -0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2265 L22:   2.0979                                     
REMARK   3      L33:   5.4407 L12:   0.8970                                     
REMARK   3      L13:  -2.3716 L23:   1.1185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1090 S12:  -0.6328 S13:  -0.1547                       
REMARK   3      S21:   0.4151 S22:   0.1638 S23:  -0.4757                       
REMARK   3      S31:   0.1759 S32:   0.9417 S33:  -0.2727                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   o     9        o   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4700  47.3280  45.5250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0090 T22:   0.3788                                     
REMARK   3      T33:   0.9768 T12:   0.0334                                     
REMARK   3      T13:  -0.3047 T23:  -0.1331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3977 L22:   2.8982                                     
REMARK   3      L33:   3.5346 L12:  -1.1508                                     
REMARK   3      L13:  -2.7549 L23:   0.1033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0942 S12:  -0.5251 S13:  -0.4623                       
REMARK   3      S21:   0.1780 S22:   0.1314 S23:  -0.2482                       
REMARK   3      S31:   0.5453 S32:   0.5673 S33:  -0.0373                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   p     9        p   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8730  45.2850  -4.3540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3704 T22:   0.7385                                     
REMARK   3      T33:   1.2744 T12:  -0.1292                                     
REMARK   3      T13:  -0.0255 T23:  -0.5981                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7142 L22:   2.3494                                     
REMARK   3      L33:   4.7238 L12:   0.1311                                     
REMARK   3      L13:   0.1533 L23:  -1.0966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1011 S12:   1.5316 S13:  -0.1620                       
REMARK   3      S21:  -0.6308 S22:   0.1964 S23:  -0.1617                       
REMARK   3      S31:   0.0449 S32:   0.3723 S33:  -0.0954                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   q     9        q   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7000  45.2350  15.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9213 T22:   0.1130                                     
REMARK   3      T33:   1.0788 T12:   0.0672                                     
REMARK   3      T13:  -0.1300 T23:  -0.2852                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3169 L22:   1.7206                                     
REMARK   3      L33:   4.1094 L12:   0.9963                                     
REMARK   3      L13:   1.5689 L23:   0.0467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0178 S12:   0.2144 S13:  -0.4600                       
REMARK   3      S21:   0.0098 S22:   0.1248 S23:  -0.1071                       
REMARK   3      S31:   0.3166 S32:   0.1492 S33:  -0.1069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   r     8        r   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8310  75.1270   3.7730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2978 T22:   0.8691                                     
REMARK   3      T33:   1.2753 T12:  -0.0697                                     
REMARK   3      T13:   0.1107 T23:  -0.3961                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8723 L22:   3.3697                                     
REMARK   3      L33:   5.8225 L12:   0.0919                                     
REMARK   3      L13:   1.1183 L23:   1.2442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0787 S12:   0.9220 S13:  -0.1526                       
REMARK   3      S21:  -0.5681 S22:   0.0142 S23:  -0.6496                       
REMARK   3      S31:   0.1802 S32:   1.0667 S33:  -0.0930                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   s     9        s   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5220  76.6040  18.4220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9274 T22:   0.1509                                     
REMARK   3      T33:   0.8604 T12:  -0.0334                                     
REMARK   3      T13:   0.0073 T23:  -0.2857                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6900 L22:   3.8045                                     
REMARK   3      L33:   3.6740 L12:   1.4750                                     
REMARK   3      L13:   2.6435 L23:   1.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0514 S12:   0.0069 S13:   0.1764                       
REMARK   3      S21:  -0.2938 S22:  -0.0039 S23:  -0.1480                       
REMARK   3      S31:  -0.1074 S32:   0.3954 S33:  -0.0476                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   t     9        t   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7020   4.5950 159.2220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3469 T22:   0.5821                                     
REMARK   3      T33:   0.8480 T12:  -0.1099                                     
REMARK   3      T13:  -0.1542 T23:  -0.2500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6533 L22:   2.5107                                     
REMARK   3      L33:   3.7097 L12:  -1.2195                                     
REMARK   3      L13:  -1.0772 L23:  -0.6663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:  -0.8021 S13:  -0.3259                       
REMARK   3      S21:   0.4870 S22:   0.0796 S23:   0.2925                       
REMARK   3      S31:  -0.1233 S32:  -0.1674 S33:  -0.1026                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   u     9        u   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0710   4.5580 138.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0813 T22:   0.3088                                     
REMARK   3      T33:   0.6719 T12:  -0.1481                                     
REMARK   3      T13:  -0.1867 T23:  -0.1767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1093 L22:   2.4903                                     
REMARK   3      L33:   3.5518 L12:  -0.3485                                     
REMARK   3      L13:  -1.5635 L23:   0.6088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2009 S12:  -0.0863 S13:   0.4041                       
REMARK   3      S21:   0.1531 S22:  -0.1569 S23:  -0.0637                       
REMARK   3      S31:  -0.3564 S32:  -0.1231 S33:  -0.0441                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   v     8        v   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5830 -25.4110 157.1710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8950 T22:   1.0420                                     
REMARK   3      T33:   1.2065 T12:   0.1012                                     
REMARK   3      T13:  -0.3374 T23:   0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1864 L22:   2.2359                                     
REMARK   3      L33:   4.9032 L12:   0.5779                                     
REMARK   3      L13:  -3.2881 L23:   1.9973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2415 S12:  -0.9901 S13:   0.3484                       
REMARK   3      S21:   0.4727 S22:   0.0545 S23:  -0.4023                       
REMARK   3      S31:   0.0488 S32:   0.7709 S33:  -0.2960                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   w     9        w   157                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3510 -26.4160 137.4780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2115 T22:   0.3622                                     
REMARK   3      T33:   0.7558 T12:  -0.0238                                     
REMARK   3      T13:  -0.2383 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6779 L22:   3.0965                                     
REMARK   3      L33:   3.9675 L12:  -1.4455                                     
REMARK   3      L13:  -2.4274 L23:   0.3823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0886 S12:  -0.4765 S13:  -0.5932                       
REMARK   3      S21:   0.2517 S22:  -0.0337 S23:  -0.0495                       
REMARK   3      S31:   0.7038 S32:   0.3947 S33:   0.1224                       
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 5MU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003026.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SI (111) MONOCHROMATOR FOLLOWED    
REMARK 200                                   BY A TOROIDAL FOCUSING MIRROR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 158847                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 184.240                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,      
REMARK 300              16, 17, 18, 19, 20, 21, 22, 23, 24                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, U                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, W                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 13                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z, a                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 14                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: b, c                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 15                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: d, e                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 16                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: f, g                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 17                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: h, i                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 18                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: j, k                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 19                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: l, m                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 20                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: n, o                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 21                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: p, q                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 22                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: r, s                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 23                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: t, u                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 24                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: v, w                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     ARG A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     ALA C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     ALA D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ALA F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     PRO F     8                                                      
REMARK 465     ASN F    30                                                      
REMARK 465     ARG F    31                                                      
REMARK 465     ARG F    32                                                      
REMARK 465     ALA F    33                                                      
REMARK 465     ASN F    34                                                      
REMARK 465     ALA F    35                                                      
REMARK 465     GLU F   107                                                      
REMARK 465     GLY F   108                                                      
REMARK 465     ALA F   109                                                      
REMARK 465     ALA G    -1                                                      
REMARK 465     MET G     0                                                      
REMARK 465     VAL G     1                                                      
REMARK 465     ARG G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     SER G     5                                                      
REMARK 465     ARG G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     PRO G     8                                                      
REMARK 465     ALA H    -1                                                      
REMARK 465     MET H     0                                                      
REMARK 465     VAL H     1                                                      
REMARK 465     ARG H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     ARG H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     ALA I    -1                                                      
REMARK 465     MET I     0                                                      
REMARK 465     VAL I     1                                                      
REMARK 465     ARG I     2                                                      
REMARK 465     SER I     3                                                      
REMARK 465     SER I     4                                                      
REMARK 465     SER I     5                                                      
REMARK 465     ARG I     6                                                      
REMARK 465     THR I     7                                                      
REMARK 465     PRO I     8                                                      
REMARK 465     ARG I   103                                                      
REMARK 465     GLU I   104                                                      
REMARK 465     THR I   105                                                      
REMARK 465     PRO I   106                                                      
REMARK 465     GLU I   107                                                      
REMARK 465     GLY I   108                                                      
REMARK 465     ALA I   109                                                      
REMARK 465     GLU I   110                                                      
REMARK 465     ALA J    -1                                                      
REMARK 465     MET J     0                                                      
REMARK 465     VAL J     1                                                      
REMARK 465     ARG J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     SER J     4                                                      
REMARK 465     SER J     5                                                      
REMARK 465     ARG J     6                                                      
REMARK 465     THR J     7                                                      
REMARK 465     PRO J     8                                                      
REMARK 465     ASN J    30                                                      
REMARK 465     ARG J    31                                                      
REMARK 465     ARG J    32                                                      
REMARK 465     ALA J    33                                                      
REMARK 465     ASN J    34                                                      
REMARK 465     ALA J    35                                                      
REMARK 465     GLU J   107                                                      
REMARK 465     GLY J   108                                                      
REMARK 465     ALA J   109                                                      
REMARK 465     GLU J   110                                                      
REMARK 465     ALA J   111                                                      
REMARK 465     ALA K    -1                                                      
REMARK 465     MET K     0                                                      
REMARK 465     VAL K     1                                                      
REMARK 465     ARG K     2                                                      
REMARK 465     SER K     3                                                      
REMARK 465     SER K     4                                                      
REMARK 465     SER K     5                                                      
REMARK 465     ARG K     6                                                      
REMARK 465     THR K     7                                                      
REMARK 465     PRO K     8                                                      
REMARK 465     ALA L    -1                                                      
REMARK 465     MET L     0                                                      
REMARK 465     VAL L     1                                                      
REMARK 465     ARG L     2                                                      
REMARK 465     SER L     3                                                      
REMARK 465     SER L     4                                                      
REMARK 465     SER L     5                                                      
REMARK 465     ARG L     6                                                      
REMARK 465     THR L     7                                                      
REMARK 465     ARG L   103                                                      
REMARK 465     GLU L   104                                                      
REMARK 465     THR L   105                                                      
REMARK 465     PRO L   106                                                      
REMARK 465     GLU L   107                                                      
REMARK 465     GLY L   108                                                      
REMARK 465     ALA L   109                                                      
REMARK 465     GLU L   110                                                      
REMARK 465     ALA M    -1                                                      
REMARK 465     MET M     0                                                      
REMARK 465     VAL M     1                                                      
REMARK 465     ARG M     2                                                      
REMARK 465     SER M     3                                                      
REMARK 465     SER M     4                                                      
REMARK 465     SER M     5                                                      
REMARK 465     ARG M     6                                                      
REMARK 465     THR M     7                                                      
REMARK 465     PRO M     8                                                      
REMARK 465     ALA N    -1                                                      
REMARK 465     MET N     0                                                      
REMARK 465     VAL N     1                                                      
REMARK 465     ARG N     2                                                      
REMARK 465     SER N     3                                                      
REMARK 465     SER N     4                                                      
REMARK 465     SER N     5                                                      
REMARK 465     ARG N     6                                                      
REMARK 465     THR N     7                                                      
REMARK 465     PRO N     8                                                      
REMARK 465     ASN N    30                                                      
REMARK 465     ARG N    31                                                      
REMARK 465     ARG N    32                                                      
REMARK 465     ALA N    33                                                      
REMARK 465     ASN N    34                                                      
REMARK 465     ALA N    35                                                      
REMARK 465     ALA O    -1                                                      
REMARK 465     MET O     0                                                      
REMARK 465     VAL O     1                                                      
REMARK 465     ARG O     2                                                      
REMARK 465     SER O     3                                                      
REMARK 465     SER O     4                                                      
REMARK 465     SER O     5                                                      
REMARK 465     ARG O     6                                                      
REMARK 465     THR O     7                                                      
REMARK 465     PRO O     8                                                      
REMARK 465     PRO O   106                                                      
REMARK 465     GLU O   107                                                      
REMARK 465     GLY O   108                                                      
REMARK 465     ALA O   109                                                      
REMARK 465     ALA P    -1                                                      
REMARK 465     MET P     0                                                      
REMARK 465     VAL P     1                                                      
REMARK 465     ARG P     2                                                      
REMARK 465     SER P     3                                                      
REMARK 465     SER P     4                                                      
REMARK 465     SER P     5                                                      
REMARK 465     ARG P     6                                                      
REMARK 465     THR P     7                                                      
REMARK 465     GLY P   108                                                      
REMARK 465     ALA P   109                                                      
REMARK 465     GLU P   110                                                      
REMARK 465     ALA P   111                                                      
REMARK 465     LYS P   112                                                      
REMARK 465     ALA Q    -1                                                      
REMARK 465     MET Q     0                                                      
REMARK 465     VAL Q     1                                                      
REMARK 465     ARG Q     2                                                      
REMARK 465     SER Q     3                                                      
REMARK 465     SER Q     4                                                      
REMARK 465     SER Q     5                                                      
REMARK 465     ARG Q     6                                                      
REMARK 465     THR Q     7                                                      
REMARK 465     PRO Q     8                                                      
REMARK 465     ALA R    -1                                                      
REMARK 465     MET R     0                                                      
REMARK 465     VAL R     1                                                      
REMARK 465     ARG R     2                                                      
REMARK 465     SER R     3                                                      
REMARK 465     SER R     4                                                      
REMARK 465     SER R     5                                                      
REMARK 465     ARG R     6                                                      
REMARK 465     THR R     7                                                      
REMARK 465     PRO R     8                                                      
REMARK 465     ASN R    30                                                      
REMARK 465     ARG R    31                                                      
REMARK 465     ARG R    32                                                      
REMARK 465     ALA R    33                                                      
REMARK 465     ASN R    34                                                      
REMARK 465     ALA R    35                                                      
REMARK 465     PRO R   106                                                      
REMARK 465     GLU R   107                                                      
REMARK 465     GLY R   108                                                      
REMARK 465     ALA R   109                                                      
REMARK 465     GLU R   110                                                      
REMARK 465     ALA S    -1                                                      
REMARK 465     MET S     0                                                      
REMARK 465     VAL S     1                                                      
REMARK 465     ARG S     2                                                      
REMARK 465     SER S     3                                                      
REMARK 465     SER S     4                                                      
REMARK 465     SER S     5                                                      
REMARK 465     ARG S     6                                                      
REMARK 465     THR S     7                                                      
REMARK 465     PRO S     8                                                      
REMARK 465     ALA T    -1                                                      
REMARK 465     MET T     0                                                      
REMARK 465     VAL T     1                                                      
REMARK 465     ARG T     2                                                      
REMARK 465     SER T     3                                                      
REMARK 465     SER T     4                                                      
REMARK 465     SER T     5                                                      
REMARK 465     ARG T     6                                                      
REMARK 465     THR T     7                                                      
REMARK 465     GLU T   107                                                      
REMARK 465     GLY T   108                                                      
REMARK 465     ALA T   109                                                      
REMARK 465     GLU T   110                                                      
REMARK 465     ALA U    -1                                                      
REMARK 465     MET U     0                                                      
REMARK 465     VAL U     1                                                      
REMARK 465     ARG U     2                                                      
REMARK 465     SER U     3                                                      
REMARK 465     SER U     4                                                      
REMARK 465     SER U     5                                                      
REMARK 465     ARG U     6                                                      
REMARK 465     THR U     7                                                      
REMARK 465     PRO U     8                                                      
REMARK 465     ALA V    -1                                                      
REMARK 465     MET V     0                                                      
REMARK 465     VAL V     1                                                      
REMARK 465     ARG V     2                                                      
REMARK 465     SER V     3                                                      
REMARK 465     SER V     4                                                      
REMARK 465     SER V     5                                                      
REMARK 465     ARG V     6                                                      
REMARK 465     THR V     7                                                      
REMARK 465     PRO V     8                                                      
REMARK 465     ASN V    30                                                      
REMARK 465     ARG V    31                                                      
REMARK 465     ARG V    32                                                      
REMARK 465     ALA V    33                                                      
REMARK 465     ASN V    34                                                      
REMARK 465     ALA V    35                                                      
REMARK 465     GLU V   107                                                      
REMARK 465     GLY V   108                                                      
REMARK 465     ALA V   109                                                      
REMARK 465     GLU V   110                                                      
REMARK 465     ALA V   111                                                      
REMARK 465     ALA W    -1                                                      
REMARK 465     MET W     0                                                      
REMARK 465     VAL W     1                                                      
REMARK 465     ARG W     2                                                      
REMARK 465     SER W     3                                                      
REMARK 465     SER W     4                                                      
REMARK 465     SER W     5                                                      
REMARK 465     ARG W     6                                                      
REMARK 465     THR W     7                                                      
REMARK 465     PRO W     8                                                      
REMARK 465     PRO W   106                                                      
REMARK 465     GLU W   107                                                      
REMARK 465     GLY W   108                                                      
REMARK 465     ALA W   109                                                      
REMARK 465     GLU W   110                                                      
REMARK 465     ALA W   111                                                      
REMARK 465     ALA X    -1                                                      
REMARK 465     MET X     0                                                      
REMARK 465     VAL X     1                                                      
REMARK 465     ARG X     2                                                      
REMARK 465     SER X     3                                                      
REMARK 465     SER X     4                                                      
REMARK 465     SER X     5                                                      
REMARK 465     ARG X     6                                                      
REMARK 465     THR X     7                                                      
REMARK 465     ALA Y    -1                                                      
REMARK 465     MET Y     0                                                      
REMARK 465     VAL Y     1                                                      
REMARK 465     ARG Y     2                                                      
REMARK 465     SER Y     3                                                      
REMARK 465     SER Y     4                                                      
REMARK 465     SER Y     5                                                      
REMARK 465     ARG Y     6                                                      
REMARK 465     THR Y     7                                                      
REMARK 465     PRO Y     8                                                      
REMARK 465     ALA Z    -1                                                      
REMARK 465     MET Z     0                                                      
REMARK 465     VAL Z     1                                                      
REMARK 465     ARG Z     2                                                      
REMARK 465     SER Z     3                                                      
REMARK 465     SER Z     4                                                      
REMARK 465     SER Z     5                                                      
REMARK 465     ARG Z     6                                                      
REMARK 465     THR Z     7                                                      
REMARK 465     PRO Z     8                                                      
REMARK 465     ASN Z    30                                                      
REMARK 465     ARG Z    31                                                      
REMARK 465     ARG Z    32                                                      
REMARK 465     ALA Z    33                                                      
REMARK 465     ASN Z    34                                                      
REMARK 465     ALA Z    35                                                      
REMARK 465     ALA a    -1                                                      
REMARK 465     MET a     0                                                      
REMARK 465     VAL a     1                                                      
REMARK 465     ARG a     2                                                      
REMARK 465     SER a     3                                                      
REMARK 465     SER a     4                                                      
REMARK 465     SER a     5                                                      
REMARK 465     ARG a     6                                                      
REMARK 465     THR a     7                                                      
REMARK 465     PRO a     8                                                      
REMARK 465     ALA b    -1                                                      
REMARK 465     MET b     0                                                      
REMARK 465     VAL b     1                                                      
REMARK 465     ARG b     2                                                      
REMARK 465     SER b     3                                                      
REMARK 465     SER b     4                                                      
REMARK 465     SER b     5                                                      
REMARK 465     ARG b     6                                                      
REMARK 465     THR b     7                                                      
REMARK 465     PRO b   106                                                      
REMARK 465     GLU b   107                                                      
REMARK 465     GLY b   108                                                      
REMARK 465     ALA b   109                                                      
REMARK 465     GLU b   110                                                      
REMARK 465     ALA b   111                                                      
REMARK 465     ALA c    -1                                                      
REMARK 465     MET c     0                                                      
REMARK 465     VAL c     1                                                      
REMARK 465     ARG c     2                                                      
REMARK 465     SER c     3                                                      
REMARK 465     SER c     4                                                      
REMARK 465     SER c     5                                                      
REMARK 465     ARG c     6                                                      
REMARK 465     THR c     7                                                      
REMARK 465     PRO c     8                                                      
REMARK 465     PRO c   106                                                      
REMARK 465     GLU c   107                                                      
REMARK 465     GLY c   108                                                      
REMARK 465     ALA c   109                                                      
REMARK 465     ALA d    -1                                                      
REMARK 465     MET d     0                                                      
REMARK 465     VAL d     1                                                      
REMARK 465     ARG d     2                                                      
REMARK 465     SER d     3                                                      
REMARK 465     SER d     4                                                      
REMARK 465     SER d     5                                                      
REMARK 465     ARG d     6                                                      
REMARK 465     THR d     7                                                      
REMARK 465     PRO d     8                                                      
REMARK 465     ASN d    30                                                      
REMARK 465     ARG d    31                                                      
REMARK 465     ARG d    32                                                      
REMARK 465     ALA d    33                                                      
REMARK 465     ASN d    34                                                      
REMARK 465     ALA d    35                                                      
REMARK 465     GLU d   107                                                      
REMARK 465     GLY d   108                                                      
REMARK 465     ALA d   109                                                      
REMARK 465     GLU d   110                                                      
REMARK 465     ALA d   111                                                      
REMARK 465     ALA e    -1                                                      
REMARK 465     MET e     0                                                      
REMARK 465     VAL e     1                                                      
REMARK 465     ARG e     2                                                      
REMARK 465     SER e     3                                                      
REMARK 465     SER e     4                                                      
REMARK 465     SER e     5                                                      
REMARK 465     ARG e     6                                                      
REMARK 465     THR e     7                                                      
REMARK 465     PRO e     8                                                      
REMARK 465     ALA f    -1                                                      
REMARK 465     MET f     0                                                      
REMARK 465     VAL f     1                                                      
REMARK 465     ARG f     2                                                      
REMARK 465     SER f     3                                                      
REMARK 465     SER f     4                                                      
REMARK 465     SER f     5                                                      
REMARK 465     ARG f     6                                                      
REMARK 465     THR f     7                                                      
REMARK 465     PRO f   106                                                      
REMARK 465     GLU f   107                                                      
REMARK 465     GLY f   108                                                      
REMARK 465     ALA f   109                                                      
REMARK 465     GLU f   110                                                      
REMARK 465     ALA f   111                                                      
REMARK 465     LYS f   112                                                      
REMARK 465     ALA g    -1                                                      
REMARK 465     MET g     0                                                      
REMARK 465     VAL g     1                                                      
REMARK 465     ARG g     2                                                      
REMARK 465     SER g     3                                                      
REMARK 465     SER g     4                                                      
REMARK 465     SER g     5                                                      
REMARK 465     ARG g     6                                                      
REMARK 465     THR g     7                                                      
REMARK 465     PRO g     8                                                      
REMARK 465     GLU g   107                                                      
REMARK 465     GLY g   108                                                      
REMARK 465     ALA g   109                                                      
REMARK 465     GLU g   110                                                      
REMARK 465     ALA h    -1                                                      
REMARK 465     MET h     0                                                      
REMARK 465     VAL h     1                                                      
REMARK 465     ARG h     2                                                      
REMARK 465     SER h     3                                                      
REMARK 465     SER h     4                                                      
REMARK 465     SER h     5                                                      
REMARK 465     ARG h     6                                                      
REMARK 465     THR h     7                                                      
REMARK 465     PRO h     8                                                      
REMARK 465     ASN h    30                                                      
REMARK 465     ARG h    31                                                      
REMARK 465     ARG h    32                                                      
REMARK 465     ALA h    33                                                      
REMARK 465     ASN h    34                                                      
REMARK 465     ALA h    35                                                      
REMARK 465     PRO h   106                                                      
REMARK 465     GLU h   107                                                      
REMARK 465     GLY h   108                                                      
REMARK 465     ALA h   109                                                      
REMARK 465     GLU h   110                                                      
REMARK 465     ALA h   111                                                      
REMARK 465     ALA i    -1                                                      
REMARK 465     MET i     0                                                      
REMARK 465     VAL i     1                                                      
REMARK 465     ARG i     2                                                      
REMARK 465     SER i     3                                                      
REMARK 465     SER i     4                                                      
REMARK 465     SER i     5                                                      
REMARK 465     ARG i     6                                                      
REMARK 465     THR i     7                                                      
REMARK 465     PRO i     8                                                      
REMARK 465     GLU i   107                                                      
REMARK 465     GLY i   108                                                      
REMARK 465     ALA i   109                                                      
REMARK 465     GLU i   110                                                      
REMARK 465     ALA j    -1                                                      
REMARK 465     MET j     0                                                      
REMARK 465     VAL j     1                                                      
REMARK 465     ARG j     2                                                      
REMARK 465     SER j     3                                                      
REMARK 465     SER j     4                                                      
REMARK 465     SER j     5                                                      
REMARK 465     ARG j     6                                                      
REMARK 465     THR j     7                                                      
REMARK 465     ALA k    -1                                                      
REMARK 465     MET k     0                                                      
REMARK 465     VAL k     1                                                      
REMARK 465     ARG k     2                                                      
REMARK 465     SER k     3                                                      
REMARK 465     SER k     4                                                      
REMARK 465     SER k     5                                                      
REMARK 465     ARG k     6                                                      
REMARK 465     THR k     7                                                      
REMARK 465     PRO k     8                                                      
REMARK 465     THR k   105                                                      
REMARK 465     PRO k   106                                                      
REMARK 465     GLU k   107                                                      
REMARK 465     GLY k   108                                                      
REMARK 465     ALA k   109                                                      
REMARK 465     GLU k   110                                                      
REMARK 465     ALA k   111                                                      
REMARK 465     ALA l    -1                                                      
REMARK 465     MET l     0                                                      
REMARK 465     VAL l     1                                                      
REMARK 465     ARG l     2                                                      
REMARK 465     SER l     3                                                      
REMARK 465     SER l     4                                                      
REMARK 465     SER l     5                                                      
REMARK 465     ARG l     6                                                      
REMARK 465     THR l     7                                                      
REMARK 465     PRO l     8                                                      
REMARK 465     ASN l    30                                                      
REMARK 465     ARG l    31                                                      
REMARK 465     ARG l    32                                                      
REMARK 465     ALA l    33                                                      
REMARK 465     ASN l    34                                                      
REMARK 465     ALA l    35                                                      
REMARK 465     ALA m    -1                                                      
REMARK 465     MET m     0                                                      
REMARK 465     VAL m     1                                                      
REMARK 465     ARG m     2                                                      
REMARK 465     SER m     3                                                      
REMARK 465     SER m     4                                                      
REMARK 465     SER m     5                                                      
REMARK 465     ARG m     6                                                      
REMARK 465     THR m     7                                                      
REMARK 465     PRO m     8                                                      
REMARK 465     GLU m   107                                                      
REMARK 465     GLY m   108                                                      
REMARK 465     ALA n    -1                                                      
REMARK 465     MET n     0                                                      
REMARK 465     VAL n     1                                                      
REMARK 465     ARG n     2                                                      
REMARK 465     SER n     3                                                      
REMARK 465     SER n     4                                                      
REMARK 465     SER n     5                                                      
REMARK 465     ARG n     6                                                      
REMARK 465     THR n     7                                                      
REMARK 465     GLY n   108                                                      
REMARK 465     ALA n   109                                                      
REMARK 465     GLU n   110                                                      
REMARK 465     ALA o    -1                                                      
REMARK 465     MET o     0                                                      
REMARK 465     VAL o     1                                                      
REMARK 465     ARG o     2                                                      
REMARK 465     SER o     3                                                      
REMARK 465     SER o     4                                                      
REMARK 465     SER o     5                                                      
REMARK 465     ARG o     6                                                      
REMARK 465     THR o     7                                                      
REMARK 465     PRO o     8                                                      
REMARK 465     GLU o   110                                                      
REMARK 465     ALA o   111                                                      
REMARK 465     ALA p    -1                                                      
REMARK 465     MET p     0                                                      
REMARK 465     VAL p     1                                                      
REMARK 465     ARG p     2                                                      
REMARK 465     SER p     3                                                      
REMARK 465     SER p     4                                                      
REMARK 465     SER p     5                                                      
REMARK 465     ARG p     6                                                      
REMARK 465     THR p     7                                                      
REMARK 465     PRO p     8                                                      
REMARK 465     ASN p    30                                                      
REMARK 465     ARG p    31                                                      
REMARK 465     ARG p    32                                                      
REMARK 465     ALA p    33                                                      
REMARK 465     ASN p    34                                                      
REMARK 465     ALA p    35                                                      
REMARK 465     GLU p   107                                                      
REMARK 465     GLY p   108                                                      
REMARK 465     ALA p   109                                                      
REMARK 465     GLU p   110                                                      
REMARK 465     ALA q    -1                                                      
REMARK 465     MET q     0                                                      
REMARK 465     VAL q     1                                                      
REMARK 465     ARG q     2                                                      
REMARK 465     SER q     3                                                      
REMARK 465     SER q     4                                                      
REMARK 465     SER q     5                                                      
REMARK 465     ARG q     6                                                      
REMARK 465     THR q     7                                                      
REMARK 465     PRO q     8                                                      
REMARK 465     ALA r    -1                                                      
REMARK 465     MET r     0                                                      
REMARK 465     VAL r     1                                                      
REMARK 465     ARG r     2                                                      
REMARK 465     SER r     3                                                      
REMARK 465     SER r     4                                                      
REMARK 465     SER r     5                                                      
REMARK 465     ARG r     6                                                      
REMARK 465     THR r     7                                                      
REMARK 465     GLU r   107                                                      
REMARK 465     GLY r   108                                                      
REMARK 465     ALA r   109                                                      
REMARK 465     GLU r   110                                                      
REMARK 465     ALA r   111                                                      
REMARK 465     LYS r   112                                                      
REMARK 465     ALA s    -1                                                      
REMARK 465     MET s     0                                                      
REMARK 465     VAL s     1                                                      
REMARK 465     ARG s     2                                                      
REMARK 465     SER s     3                                                      
REMARK 465     SER s     4                                                      
REMARK 465     SER s     5                                                      
REMARK 465     ARG s     6                                                      
REMARK 465     THR s     7                                                      
REMARK 465     PRO s     8                                                      
REMARK 465     ALA t    -1                                                      
REMARK 465     MET t     0                                                      
REMARK 465     VAL t     1                                                      
REMARK 465     ARG t     2                                                      
REMARK 465     SER t     3                                                      
REMARK 465     SER t     4                                                      
REMARK 465     SER t     5                                                      
REMARK 465     ARG t     6                                                      
REMARK 465     THR t     7                                                      
REMARK 465     PRO t     8                                                      
REMARK 465     ASN t    30                                                      
REMARK 465     ARG t    31                                                      
REMARK 465     ARG t    32                                                      
REMARK 465     ALA t    33                                                      
REMARK 465     ASN t    34                                                      
REMARK 465     ALA t    35                                                      
REMARK 465     ALA u    -1                                                      
REMARK 465     MET u     0                                                      
REMARK 465     VAL u     1                                                      
REMARK 465     ARG u     2                                                      
REMARK 465     SER u     3                                                      
REMARK 465     SER u     4                                                      
REMARK 465     SER u     5                                                      
REMARK 465     ARG u     6                                                      
REMARK 465     THR u     7                                                      
REMARK 465     PRO u     8                                                      
REMARK 465     GLU u   107                                                      
REMARK 465     GLY u   108                                                      
REMARK 465     ALA u   109                                                      
REMARK 465     GLU u   110                                                      
REMARK 465     ALA v    -1                                                      
REMARK 465     MET v     0                                                      
REMARK 465     VAL v     1                                                      
REMARK 465     ARG v     2                                                      
REMARK 465     SER v     3                                                      
REMARK 465     SER v     4                                                      
REMARK 465     SER v     5                                                      
REMARK 465     ARG v     6                                                      
REMARK 465     THR v     7                                                      
REMARK 465     GLU v   107                                                      
REMARK 465     GLY v   108                                                      
REMARK 465     ALA v   109                                                      
REMARK 465     GLU v   110                                                      
REMARK 465     ALA v   111                                                      
REMARK 465     LYS v   112                                                      
REMARK 465     ALA w    -1                                                      
REMARK 465     MET w     0                                                      
REMARK 465     VAL w     1                                                      
REMARK 465     ARG w     2                                                      
REMARK 465     SER w     3                                                      
REMARK 465     SER w     4                                                      
REMARK 465     SER w     5                                                      
REMARK 465     ARG w     6                                                      
REMARK 465     THR w     7                                                      
REMARK 465     PRO w     8                                                      
REMARK 465     GLU w   107                                                      
REMARK 465     GLY w   108                                                      
REMARK 465     ALA w   109                                                      
REMARK 465     GLU w   110                                                      
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   ND2  ASN B    92     O    SER W    86              1.87            
REMARK 500   OG1  THR B   105     O    ALA B   111              2.12            
REMARK 500   O    TYR R    87     N    THR R    89              2.13            
REMARK 500   OE1  GLN B    61     OH   TYR B   151              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CZ   ARG D    32     OE1  GLU s    23     1545     1.78            
REMARK 500   NH1  ARG D    32     OE1  GLU s    23     1545     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  22      105.91    -55.19                                   
REMARK 500    GLU A  23       88.30    -60.94                                   
REMARK 500    GLN A  61      141.69   -172.95                                   
REMARK 500    CYS A  69      112.55   -168.38                                   
REMARK 500    SER A  99       75.93   -114.69                                   
REMARK 500    ALA A 111       41.01   -161.07                                   
REMARK 500    LYS A 128      105.78    -55.18                                   
REMARK 500    ASP A 143       76.35   -118.33                                   
REMARK 500    GLN A 149       56.10   -103.70                                   
REMARK 500    ALA B  14      147.15   -179.65                                   
REMARK 500    GLU B  23      -75.67    -75.53                                   
REMARK 500    GLN B  88      -18.73     81.41                                   
REMARK 500    LYS B 112       95.49     70.66                                   
REMARK 500    GLU B 116       93.03   -169.34                                   
REMARK 500    PHE B 152      114.75   -174.77                                   
REMARK 500    GLN C  25     -152.30   -155.25                                   
REMARK 500    LEU C  26       49.24   -151.22                                   
REMARK 500    ARG C  32     -167.60   -125.16                                   
REMARK 500    GLN C  88       33.30     75.99                                   
REMARK 500    ASP C 143       76.56   -107.77                                   
REMARK 500    PHE C 144       83.99    -56.23                                   
REMARK 500    GLU C 146      113.94     62.74                                   
REMARK 500    LYS D  11       73.11     62.61                                   
REMARK 500    PRO D  12      128.64    -39.15                                   
REMARK 500    HIS D  15      113.29   -163.76                                   
REMARK 500    GLN D  21      -53.63    -23.89                                   
REMARK 500    ALA D  22       78.01    -69.19                                   
REMARK 500    ASN D  34       -7.27     82.49                                   
REMARK 500    ASP D  45       44.01     38.15                                   
REMARK 500    SER D  60      143.72   -175.38                                   
REMARK 500    VAL D  85      -71.95    -58.02                                   
REMARK 500    GLN D  88      -25.44     78.37                                   
REMARK 500    LEU D  93      -58.29   -120.40                                   
REMARK 500    SER D  95      140.24   -174.30                                   
REMARK 500    THR D 105      123.66     70.69                                   
REMARK 500    PRO D 106        0.30    -66.92                                   
REMARK 500    GLU D 107       86.70     62.62                                   
REMARK 500    ALA D 109      168.85     65.71                                   
REMARK 500    GLU D 110       77.60      1.14                                   
REMARK 500    SER D 133       96.90   -165.45                                   
REMARK 500    PHE D 152      106.12   -167.99                                   
REMARK 500    ASN F  39       47.94     39.14                                   
REMARK 500    VAL F  50      124.05    -38.88                                   
REMARK 500    GLN F  88       -3.01     59.17                                   
REMARK 500    ALA F 111       97.68   -162.87                                   
REMARK 500    ARG F 138       76.31   -118.31                                   
REMARK 500    SER F 147       12.02     57.33                                   
REMARK 500    GLN F 149       44.60    -90.59                                   
REMARK 500    ALA G  14      147.68   -170.21                                   
REMARK 500    GLU G  23      -65.57    -90.75                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     352 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO W  100     CYS W  101                 -149.41                    
REMARK 500 PRO e  100     CYS e  101                 -145.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI J 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI J 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI L 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI M 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI N 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI P 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI P 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI Q 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI R 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI U 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI X 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI X 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI Z 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI Z 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI b 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI b 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI d 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI f 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI f 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI h 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI h 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI j 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI j 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI l 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI n 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI n 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI o 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI p 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI p 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI r 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI r 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI t 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI t 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JNI v 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU s 23 and ARG D     
REMARK 800  32                                                                  
DBREF  5MU8 A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 D    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 F    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 G    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 H    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 I    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 J    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 K    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 L    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 M    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 N    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 O    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 P    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 Q    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 R    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 S    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 T    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 U    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 V    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 W    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 X    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 Y    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 Z    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 a    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 b    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 c    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 d    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 e    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 f    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 g    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 h    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 i    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 j    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 k    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 l    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 m    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 n    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 o    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 p    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 q    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 r    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 s    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 t    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 u    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 v    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  5MU8 w    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQADV 5MU8 ALA A   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET A    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA B   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET B    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA C   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET C    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA D   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET D    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA F   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET F    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA G   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET G    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA H   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET H    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA I   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET I    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA J   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET J    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA K   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET K    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA L   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET L    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA M   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET M    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA N   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET N    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA O   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET O    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA P   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET P    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA Q   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET Q    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA R   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET R    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA S   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET S    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA T   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET T    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA U   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET U    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA V   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET V    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA W   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET W    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA X   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET X    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA Y   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET Y    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA Z   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET Z    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA a   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET a    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA b   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET b    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA c   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET c    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA d   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET d    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA e   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET e    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA f   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET f    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA g   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET g    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA h   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET h    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA i   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET i    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA j   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET j    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA k   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET k    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA l   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET l    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA m   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET m    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA n   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET n    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA o   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET o    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA p   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET p    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA q   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET q    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA r   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET r    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA s   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET s    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA t   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET t    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA u   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET u    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA v   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET v    0  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 ALA w   -1  UNP  P01375              EXPRESSION TAG                 
SEQADV 5MU8 MET w    0  UNP  P01375              EXPRESSION TAG                 
SEQRES   1 A  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 A  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 A  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 A  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 A  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 A  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 A  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 A  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 A  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 A  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 A  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 A  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 A  159  ILE ALA LEU                                                  
SEQRES   1 B  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 B  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 B  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 B  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 B  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 B  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 B  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 B  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 B  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 B  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 B  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 B  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 B  159  ILE ALA LEU                                                  
SEQRES   1 C  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 C  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 C  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 C  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 C  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 C  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 C  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 C  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 C  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 C  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 C  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 C  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 C  159  ILE ALA LEU                                                  
SEQRES   1 D  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 D  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 D  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 D  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 D  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 D  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 D  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 D  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 D  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 D  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 D  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 D  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 D  159  ILE ALA LEU                                                  
SEQRES   1 F  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 F  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 F  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 F  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 F  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 F  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 F  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 F  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 F  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 F  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 F  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 F  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 F  159  ILE ALA LEU                                                  
SEQRES   1 G  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 G  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 G  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 G  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 G  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 G  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 G  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 G  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 G  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 G  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 G  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 G  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 G  159  ILE ALA LEU                                                  
SEQRES   1 H  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 H  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 H  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 H  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 H  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 H  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 H  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 H  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 H  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 H  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 H  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 H  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 H  159  ILE ALA LEU                                                  
SEQRES   1 I  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 I  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 I  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 I  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 I  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 I  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 I  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 I  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 I  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 I  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 I  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 I  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 I  159  ILE ALA LEU                                                  
SEQRES   1 J  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 J  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 J  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 J  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 J  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 J  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 J  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 J  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 J  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 J  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 J  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 J  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 J  159  ILE ALA LEU                                                  
SEQRES   1 K  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 K  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 K  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 K  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 K  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 K  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 K  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 K  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 K  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 K  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 K  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 K  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 K  159  ILE ALA LEU                                                  
SEQRES   1 L  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 L  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 L  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 L  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 L  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 L  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 L  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 L  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 L  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 L  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 L  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 L  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 L  159  ILE ALA LEU                                                  
SEQRES   1 M  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 M  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 M  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 M  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 M  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 M  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 M  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 M  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 M  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 M  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 M  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 M  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 M  159  ILE ALA LEU                                                  
SEQRES   1 N  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 N  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 N  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 N  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 N  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 N  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 N  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 N  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 N  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 N  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 N  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 N  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 N  159  ILE ALA LEU                                                  
SEQRES   1 O  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 O  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 O  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 O  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 O  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 O  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 O  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 O  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 O  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 O  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 O  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 O  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 O  159  ILE ALA LEU                                                  
SEQRES   1 P  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 P  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 P  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 P  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 P  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 P  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 P  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 P  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 P  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 P  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 P  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 P  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 P  159  ILE ALA LEU                                                  
SEQRES   1 Q  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 Q  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 Q  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 Q  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 Q  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 Q  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 Q  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 Q  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 Q  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 Q  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 Q  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 Q  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 Q  159  ILE ALA LEU                                                  
SEQRES   1 R  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 R  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 R  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 R  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 R  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 R  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 R  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 R  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 R  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 R  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 R  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 R  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 R  159  ILE ALA LEU                                                  
SEQRES   1 S  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 S  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 S  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 S  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 S  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 S  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 S  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 S  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 S  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 S  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 S  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 S  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 S  159  ILE ALA LEU                                                  
SEQRES   1 T  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 T  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 T  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 T  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 T  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 T  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 T  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 T  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 T  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 T  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 T  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 T  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 T  159  ILE ALA LEU                                                  
SEQRES   1 U  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 U  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 U  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 U  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 U  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 U  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 U  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 U  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 U  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 U  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 U  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 U  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 U  159  ILE ALA LEU                                                  
SEQRES   1 V  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 V  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 V  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 V  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 V  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 V  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 V  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 V  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 V  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 V  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 V  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 V  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 V  159  ILE ALA LEU                                                  
SEQRES   1 W  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 W  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 W  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 W  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 W  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 W  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 W  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 W  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 W  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 W  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 W  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 W  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 W  159  ILE ALA LEU                                                  
SEQRES   1 X  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 X  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 X  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 X  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 X  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 X  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 X  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 X  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 X  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 X  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 X  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 X  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 X  159  ILE ALA LEU                                                  
SEQRES   1 Y  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 Y  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 Y  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 Y  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 Y  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 Y  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 Y  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 Y  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 Y  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 Y  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 Y  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 Y  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 Y  159  ILE ALA LEU                                                  
SEQRES   1 Z  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 Z  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 Z  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 Z  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 Z  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 Z  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 Z  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 Z  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 Z  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 Z  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 Z  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 Z  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 Z  159  ILE ALA LEU                                                  
SEQRES   1 a  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 a  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 a  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 a  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 a  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 a  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 a  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 a  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 a  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 a  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 a  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 a  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 a  159  ILE ALA LEU                                                  
SEQRES   1 b  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 b  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 b  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 b  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 b  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 b  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 b  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 b  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 b  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 b  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 b  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 b  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 b  159  ILE ALA LEU                                                  
SEQRES   1 c  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 c  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 c  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 c  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 c  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 c  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 c  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 c  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 c  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 c  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 c  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 c  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 c  159  ILE ALA LEU                                                  
SEQRES   1 d  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 d  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 d  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 d  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 d  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 d  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 d  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 d  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 d  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 d  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 d  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 d  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 d  159  ILE ALA LEU                                                  
SEQRES   1 e  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 e  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 e  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 e  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 e  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 e  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 e  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 e  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 e  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 e  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 e  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 e  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 e  159  ILE ALA LEU                                                  
SEQRES   1 f  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 f  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 f  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 f  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 f  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 f  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 f  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 f  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 f  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 f  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 f  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 f  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 f  159  ILE ALA LEU                                                  
SEQRES   1 g  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 g  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 g  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 g  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 g  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 g  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 g  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 g  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 g  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 g  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 g  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 g  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 g  159  ILE ALA LEU                                                  
SEQRES   1 h  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 h  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 h  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 h  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 h  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 h  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 h  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 h  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 h  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 h  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 h  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 h  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 h  159  ILE ALA LEU                                                  
SEQRES   1 i  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 i  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 i  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 i  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 i  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 i  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 i  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 i  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 i  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 i  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 i  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 i  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 i  159  ILE ALA LEU                                                  
SEQRES   1 j  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 j  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 j  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 j  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 j  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 j  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 j  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 j  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 j  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 j  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 j  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 j  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 j  159  ILE ALA LEU                                                  
SEQRES   1 k  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 k  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 k  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 k  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 k  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 k  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 k  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 k  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 k  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 k  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 k  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 k  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 k  159  ILE ALA LEU                                                  
SEQRES   1 l  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 l  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 l  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 l  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 l  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 l  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 l  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 l  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 l  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 l  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 l  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 l  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 l  159  ILE ALA LEU                                                  
SEQRES   1 m  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 m  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 m  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 m  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 m  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 m  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 m  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 m  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 m  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 m  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 m  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 m  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 m  159  ILE ALA LEU                                                  
SEQRES   1 n  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 n  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 n  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 n  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 n  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 n  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 n  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 n  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 n  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 n  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 n  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 n  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 n  159  ILE ALA LEU                                                  
SEQRES   1 o  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 o  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 o  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 o  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 o  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 o  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 o  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 o  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 o  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 o  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 o  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 o  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 o  159  ILE ALA LEU                                                  
SEQRES   1 p  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 p  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 p  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 p  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 p  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 p  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 p  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 p  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 p  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 p  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 p  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 p  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 p  159  ILE ALA LEU                                                  
SEQRES   1 q  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 q  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 q  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 q  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 q  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 q  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 q  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 q  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 q  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 q  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 q  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 q  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 q  159  ILE ALA LEU                                                  
SEQRES   1 r  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 r  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 r  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 r  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 r  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 r  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 r  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 r  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 r  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 r  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 r  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 r  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 r  159  ILE ALA LEU                                                  
SEQRES   1 s  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 s  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 s  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 s  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 s  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 s  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 s  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 s  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 s  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 s  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 s  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 s  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 s  159  ILE ALA LEU                                                  
SEQRES   1 t  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 t  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 t  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 t  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 t  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 t  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 t  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 t  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 t  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 t  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 t  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 t  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 t  159  ILE ALA LEU                                                  
SEQRES   1 u  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 u  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 u  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 u  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 u  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 u  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 u  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 u  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 u  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 u  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 u  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 u  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 u  159  ILE ALA LEU                                                  
SEQRES   1 v  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 v  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 v  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 v  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 v  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 v  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 v  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 v  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 v  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 v  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 v  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 v  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 v  159  ILE ALA LEU                                                  
SEQRES   1 w  159  ALA MET VAL ARG SER SER SER ARG THR PRO SER ASP LYS          
SEQRES   2 w  159  PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY          
SEQRES   3 w  159  GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU          
SEQRES   4 w  159  ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL          
SEQRES   5 w  159  PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU          
SEQRES   6 w  159  PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU          
SEQRES   7 w  159  THR HIS THR ILE SER ARG ILE ALA VAL SER TYR GLN THR          
SEQRES   8 w  159  LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN          
SEQRES   9 w  159  ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR          
SEQRES  10 w  159  GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS          
SEQRES  11 w  159  GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR          
SEQRES  12 w  159  LEU ASP PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE          
SEQRES  13 w  159  ILE ALA LEU                                                  
HET    JNI  A 201      39                                                       
HET    JNI  A 202      39                                                       
HET    JNI  C 201      39                                                       
HET    JNI  C 202      39                                                       
HET    JNI  D 201      39                                                       
HET    JNI  F 201      39                                                       
HET    JNI  F 202      39                                                       
HET    JNI  H 201      39                                                       
HET    JNI  H 202      39                                                       
HET    JNI  J 201      39                                                       
HET    JNI  J 202      39                                                       
HET    JNI  L 201      39                                                       
HET    JNI  M 201      39                                                       
HET    JNI  N 201      39                                                       
HET    JNI  P 201      39                                                       
HET    JNI  P 202      39                                                       
HET    JNI  Q 201      39                                                       
HET    JNI  R 201      39                                                       
HET    JNI  U 201      39                                                       
HET    JNI  V 201      39                                                       
HET    JNI  V 202      39                                                       
HET    JNI  X 201      39                                                       
HET    JNI  X 202      39                                                       
HET    JNI  Z 201      39                                                       
HET    JNI  Z 202      39                                                       
HET    JNI  b 201      39                                                       
HET    JNI  b 202      39                                                       
HET    JNI  d 201      39                                                       
HET    JNI  f 201      39                                                       
HET    JNI  f 202      39                                                       
HET    JNI  h 201      39                                                       
HET    JNI  h 202      39                                                       
HET    JNI  j 201      39                                                       
HET    JNI  j 202      39                                                       
HET    JNI  l 201      39                                                       
HET    JNI  n 201      39                                                       
HET    JNI  n 202      39                                                       
HET    JNI  o 201      39                                                       
HET    JNI  p 201      39                                                       
HET    JNI  p 202      39                                                       
HET    JNI  r 201      39                                                       
HET    JNI  r 202      39                                                       
HET    JNI  t 201      39                                                       
HET    JNI  t 202      39                                                       
HET    JNI  v 201      39                                                       
HET    JNI  v 202      39                                                       
HETNAM     JNI ~{N}4-(PHENYLMETHYL)-~{N}4-[2-[3-(2-PIPERAZIN-1-                 
HETNAM   2 JNI  YLPYRIMIDIN-5-YL)PHENYL]PHENYL]PYRIMIDINE-2,4-DIAMINE           
FORMUL  49  JNI    46(C31 H30 N8)                                               
HELIX    1 AA1 ARG A  138  LEU A  142  5                                   5    
HELIX    2 AA2 ARG B  138  LEU B  142  5                                   5    
HELIX    3 AA3 ARG C  138  LEU C  142  5                                   5    
HELIX    4 AA4 ARG F  138  LEU F  142  5                                   5    
HELIX    5 AA5 ARG G  138  LEU G  142  5                                   5    
HELIX    6 AA6 ARG H  138  LEU H  142  5                                   5    
HELIX    7 AA7 ARG I  138  LEU I  142  5                                   5    
HELIX    8 AA8 ARG L  138  LEU L  142  5                                   5    
HELIX    9 AA9 ARG M  138  LEU M  142  5                                   5    
HELIX   10 AB1 ARG N  138  LEU N  142  5                                   5    
HELIX   11 AB2 ARG O  138  LEU O  142  5                                   5    
HELIX   12 AB3 ARG P  138  LEU P  142  5                                   5    
HELIX   13 AB4 ARG Q  138  LEU Q  142  5                                   5    
HELIX   14 AB5 ARG R  138  LEU R  142  5                                   5    
HELIX   15 AB6 ARG S  138  LEU S  142  5                                   5    
HELIX   16 AB7 ARG U  138  LEU U  142  5                                   5    
HELIX   17 AB8 ARG V  138  LEU V  142  5                                   5    
HELIX   18 AB9 ARG W  138  LEU W  142  5                                   5    
HELIX   19 AC1 ARG X  138  LEU X  142  5                                   5    
HELIX   20 AC2 ARG Y  138  LEU Y  142  5                                   5    
HELIX   21 AC3 ARG Z  138  LEU Z  142  5                                   5    
HELIX   22 AC4 ARG a  138  LEU a  142  5                                   5    
HELIX   23 AC5 ARG b  138  LEU b  142  5                                   5    
HELIX   24 AC6 ARG c  138  LEU c  142  5                                   5    
HELIX   25 AC7 ARG d  138  LEU d  142  5                                   5    
HELIX   26 AC8 ARG e  138  LEU e  142  5                                   5    
HELIX   27 AC9 ARG f  138  LEU f  142  5                                   5    
HELIX   28 AD1 ARG g  138  LEU g  142  5                                   5    
HELIX   29 AD2 ARG h  138  LEU h  142  5                                   5    
HELIX   30 AD3 ARG i  138  LEU i  142  5                                   5    
HELIX   31 AD4 ARG j  138  LEU j  142  5                                   5    
HELIX   32 AD5 ARG k  138  LEU k  142  5                                   5    
HELIX   33 AD6 ARG l  138  LEU l  142  5                                   5    
HELIX   34 AD7 ARG m  138  LEU m  142  5                                   5    
HELIX   35 AD8 ARG n  138  LEU n  142  5                                   5    
HELIX   36 AD9 ARG p  138  LEU p  142  5                                   5    
HELIX   37 AE1 ARG q  138  LEU q  142  5                                   5    
HELIX   38 AE2 ARG r  138  LEU r  142  5                                   5    
HELIX   39 AE3 ARG s  138  LEU s  142  5                                   5    
HELIX   40 AE4 ARG t  138  LEU t  142  5                                   5    
HELIX   41 AE5 ARG u  138  LEU u  142  5                                   5    
HELIX   42 AE6 ARG v  138  LEU v  142  5                                   5    
HELIX   43 AE7 ASN w   39  VAL w   41  5                                   3    
HELIX   44 AE8 ARG w  138  LEU w  142  5                                   5    
SHEET    1 AA1 3 LEU A  29  LEU A  29  0                                        
SHEET    2 AA1 3 VAL A  13  VAL A  17 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA1 3 ALA A  35  ALA A  38 -1  O  ALA A  38   N  VAL A  13           
SHEET    1 AA2 5 LEU A  29  LEU A  29  0                                        
SHEET    2 AA2 5 VAL A  13  VAL A  17 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA2 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16           
SHEET    4 AA2 5 GLY A  54  GLY A  66 -1  N  TYR A  59   O  GLY A 153           
SHEET    5 AA2 5 TRP A 114  LEU A 126 -1  O  ILE A 118   N  VAL A  62           
SHEET    1 AA3 5 GLU A  42  ARG A  44  0                                        
SHEET    2 AA3 5 GLN A  47  VAL A  49 -1  O  VAL A  49   N  GLU A  42           
SHEET    3 AA3 5 ARG A 131  GLU A 135 -1  O  LEU A 132   N  LEU A  48           
SHEET    4 AA3 5 LEU A  76  ILE A  83 -1  N  ILE A  83   O  ARG A 131           
SHEET    5 AA3 5 LYS A  90  LYS A  98 -1  O  VAL A  91   N  ARG A  82           
SHEET    1 AA4 3 TRP B  28  LEU B  29  0                                        
SHEET    2 AA4 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3 AA4 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15           
SHEET    1 AA5 5 TRP B  28  LEU B  29  0                                        
SHEET    2 AA5 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29           
SHEET    3 AA5 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16           
SHEET    4 AA5 5 GLY B  54  LEU B  63 -1  N  LEU B  57   O  ILE B 155           
SHEET    5 AA5 5 PRO B 117  LEU B 126 -1  O  PHE B 124   N  TYR B  56           
SHEET    1 AA6 5 GLU B  42  ARG B  44  0                                        
SHEET    2 AA6 5 GLN B  47  VAL B  49 -1  O  GLN B  47   N  ARG B  44           
SHEET    3 AA6 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48           
SHEET    4 AA6 5 LEU B  76  ILE B  83 -1  N  THR B  79   O  GLU B 135           
SHEET    5 AA6 5 LYS B  90  LYS B  98 -1  O  LYS B  98   N  LEU B  76           
SHEET    1 AA7 3 TRP C  28  LEU C  29  0                                        
SHEET    2 AA7 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3 AA7 3 LEU C  36  ALA C  38 -1  O  LEU C  36   N  HIS C  15           
SHEET    1 AA8 5 TRP C  28  LEU C  29  0                                        
SHEET    2 AA8 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3 AA8 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16           
SHEET    4 AA8 5 GLY C  54  GLN C  67 -1  N  LEU C  57   O  ILE C 155           
SHEET    5 AA8 5 PRO C 113  LEU C 126 -1  O  LEU C 126   N  GLY C  54           
SHEET    1 AA9 5 GLU C  42  ARG C  44  0                                        
SHEET    2 AA9 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42           
SHEET    3 AA9 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48           
SHEET    4 AA9 5 LEU C  76  ILE C  83 -1  N  THR C  79   O  GLU C 135           
SHEET    5 AA9 5 LYS C  90  LYS C  98 -1  O  VAL C  91   N  ARG C  82           
SHEET    1 AB1 3 TRP D  28  LEU D  29  0                                        
SHEET    2 AB1 3 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3 AB1 3 LEU D  36  ALA D  38 -1  O  LEU D  36   N  HIS D  15           
SHEET    1 AB2 5 TRP D  28  LEU D  29  0                                        
SHEET    2 AB2 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3 AB2 5 VAL D 150  ALA D 156 -1  O  ILE D 154   N  ALA D  14           
SHEET    4 AB2 5 GLY D  54  GLY D  66 -1  N  LEU D  57   O  ILE D 155           
SHEET    5 AB2 5 TRP D 114  LEU D 126 -1  O  GLY D 122   N  ILE D  58           
SHEET    1 AB3 2 GLU D  42  ARG D  44  0                                        
SHEET    2 AB3 2 GLN D  47  VAL D  49 -1  O  GLN D  47   N  ARG D  44           
SHEET    1 AB4 3 VAL D  91  LYS D  98  0                                        
SHEET    2 AB4 3 LEU D  76  ILE D  83 -1  N  LEU D  76   O  LYS D  98           
SHEET    3 AB4 3 ARG D 131  ILE D 136 -1  O  ARG D 131   N  ILE D  83           
SHEET    1 AB5 5 LEU F  37  ALA F  38  0                                        
SHEET    2 AB5 5 VAL F  13  VAL F  17 -1  N  VAL F  13   O  ALA F  38           
SHEET    3 AB5 5 TYR F 151  ALA F 156 -1  O  PHE F 152   N  VAL F  16           
SHEET    4 AB5 5 GLY F  54  GLY F  66 -1  N  LEU F  57   O  ILE F 155           
SHEET    5 AB5 5 TRP F 114  LEU F 126 -1  O  GLY F 122   N  ILE F  58           
SHEET    1 AB6 5 GLU F  42  ARG F  44  0                                        
SHEET    2 AB6 5 GLN F  47  VAL F  49 -1  O  GLN F  47   N  ARG F  44           
SHEET    3 AB6 5 ARG F 131  ILE F 136 -1  O  LEU F 132   N  LEU F  48           
SHEET    4 AB6 5 LEU F  76  ILE F  83 -1  N  THR F  79   O  GLU F 135           
SHEET    5 AB6 5 LYS F  90  LYS F  98 -1  O  LEU F  94   N  ILE F  80           
SHEET    1 AB7 3 TRP G  28  LEU G  29  0                                        
SHEET    2 AB7 3 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29           
SHEET    3 AB7 3 LEU G  36  ALA G  38 -1  O  LEU G  36   N  HIS G  15           
SHEET    1 AB8 5 TRP G  28  LEU G  29  0                                        
SHEET    2 AB8 5 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29           
SHEET    3 AB8 5 TYR G 151  ALA G 156 -1  O  PHE G 152   N  VAL G  16           
SHEET    4 AB8 5 GLY G  54  GLN G  67 -1  N  LEU G  57   O  ILE G 155           
SHEET    5 AB8 5 PRO G 113  LEU G 126 -1  O  PHE G 124   N  TYR G  56           
SHEET    1 AB9 5 GLU G  42  ARG G  44  0                                        
SHEET    2 AB9 5 GLN G  47  VAL G  49 -1  O  GLN G  47   N  ARG G  44           
SHEET    3 AB9 5 ARG G 131  ILE G 136 -1  O  LEU G 132   N  LEU G  48           
SHEET    4 AB9 5 LEU G  76  ILE G  83 -1  N  THR G  79   O  GLU G 135           
SHEET    5 AB9 5 LYS G  90  LYS G  98 -1  O  LYS G  98   N  LEU G  76           
SHEET    1 AC1 3 TRP H  28  LEU H  29  0                                        
SHEET    2 AC1 3 VAL H  13  ALA H  18 -1  N  VAL H  17   O  LEU H  29           
SHEET    3 AC1 3 LEU H  36  ALA H  38 -1  O  ALA H  38   N  VAL H  13           
SHEET    1 AC2 5 TRP H  28  LEU H  29  0                                        
SHEET    2 AC2 5 VAL H  13  ALA H  18 -1  N  VAL H  17   O  LEU H  29           
SHEET    3 AC2 5 TYR H 151  ALA H 156 -1  O  ILE H 154   N  ALA H  14           
SHEET    4 AC2 5 GLY H  54  GLN H  67 -1  N  LEU H  57   O  ILE H 155           
SHEET    5 AC2 5 PRO H 113  LEU H 126 -1  O  GLY H 122   N  ILE H  58           
SHEET    1 AC3 5 GLU H  42  ARG H  44  0                                        
SHEET    2 AC3 5 GLN H  47  VAL H  49 -1  O  GLN H  47   N  ARG H  44           
SHEET    3 AC3 5 ARG H 131  ILE H 136 -1  O  LEU H 132   N  LEU H  48           
SHEET    4 AC3 5 LEU H  76  ILE H  83 -1  N  THR H  79   O  GLU H 135           
SHEET    5 AC3 5 LYS H  90  LYS H  98 -1  O  LYS H  98   N  LEU H  76           
SHEET    1 AC4 3 TRP I  28  LEU I  29  0                                        
SHEET    2 AC4 3 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29           
SHEET    3 AC4 3 LEU I  36  ALA I  38 -1  O  LEU I  36   N  HIS I  15           
SHEET    1 AC5 5 TRP I  28  LEU I  29  0                                        
SHEET    2 AC5 5 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29           
SHEET    3 AC5 5 TYR I 151  ALA I 156 -1  O  ILE I 154   N  ALA I  14           
SHEET    4 AC5 5 GLY I  54  GLY I  66 -1  N  LEU I  57   O  ILE I 155           
SHEET    5 AC5 5 TRP I 114  LEU I 126 -1  O  PHE I 124   N  TYR I  56           
SHEET    1 AC6 5 GLU I  42  ARG I  44  0                                        
SHEET    2 AC6 5 GLN I  47  VAL I  49 -1  O  GLN I  47   N  ARG I  44           
SHEET    3 AC6 5 ARG I 131  ILE I 136 -1  O  LEU I 132   N  LEU I  48           
SHEET    4 AC6 5 LEU I  76  ILE I  83 -1  N  ILE I  83   O  ARG I 131           
SHEET    5 AC6 5 LYS I  90  LYS I  98 -1  O  LYS I  98   N  LEU I  76           
SHEET    1 AC7 5 LEU J  37  ALA J  38  0                                        
SHEET    2 AC7 5 VAL J  13  VAL J  17 -1  N  VAL J  13   O  ALA J  38           
SHEET    3 AC7 5 TYR J 151  ALA J 156 -1  O  ILE J 154   N  ALA J  14           
SHEET    4 AC7 5 GLY J  54  GLY J  66 -1  N  LEU J  57   O  ILE J 155           
SHEET    5 AC7 5 TRP J 114  LEU J 126 -1  O  GLY J 122   N  ILE J  58           
SHEET    1 AC8 5 GLU J  42  ARG J  44  0                                        
SHEET    2 AC8 5 GLN J  47  VAL J  49 -1  O  VAL J  49   N  GLU J  42           
SHEET    3 AC8 5 ARG J 131  ILE J 136 -1  O  LEU J 132   N  LEU J  48           
SHEET    4 AC8 5 LEU J  76  ILE J  83 -1  N  ILE J  83   O  ARG J 131           
SHEET    5 AC8 5 LYS J  90  LYS J  98 -1  O  LYS J  98   N  LEU J  76           
SHEET    1 AC9 3 TRP K  28  LEU K  29  0                                        
SHEET    2 AC9 3 VAL K  13  ALA K  18 -1  N  VAL K  17   O  LEU K  29           
SHEET    3 AC9 3 LEU K  36  ALA K  38 -1  O  LEU K  36   N  HIS K  15           
SHEET    1 AD1 5 TRP K  28  LEU K  29  0                                        
SHEET    2 AD1 5 VAL K  13  ALA K  18 -1  N  VAL K  17   O  LEU K  29           
SHEET    3 AD1 5 TYR K 151  ALA K 156 -1  O  ILE K 154   N  ALA K  14           
SHEET    4 AD1 5 GLY K  54  GLY K  66 -1  N  LEU K  57   O  ILE K 155           
SHEET    5 AD1 5 TRP K 114  LEU K 126 -1  O  PHE K 124   N  TYR K  56           
SHEET    1 AD2 5 GLU K  42  ARG K  44  0                                        
SHEET    2 AD2 5 GLN K  47  VAL K  49 -1  O  GLN K  47   N  ARG K  44           
SHEET    3 AD2 5 ARG K 131  ILE K 136 -1  O  LEU K 132   N  LEU K  48           
SHEET    4 AD2 5 LEU K  76  ILE K  83 -1  N  SER K  81   O  SER K 133           
SHEET    5 AD2 5 LEU K  94  LYS K  98 -1  O  LYS K  98   N  LEU K  76           
SHEET    1 AD3 3 TRP L  28  LEU L  29  0                                        
SHEET    2 AD3 3 VAL L  13  ALA L  18 -1  N  VAL L  17   O  LEU L  29           
SHEET    3 AD3 3 LEU L  36  ALA L  38 -1  O  LEU L  36   N  HIS L  15           
SHEET    1 AD4 5 TRP L  28  LEU L  29  0                                        
SHEET    2 AD4 5 VAL L  13  ALA L  18 -1  N  VAL L  17   O  LEU L  29           
SHEET    3 AD4 5 TYR L 151  ALA L 156 -1  O  PHE L 152   N  VAL L  16           
SHEET    4 AD4 5 GLY L  54  GLN L  67 -1  N  LEU L  57   O  ILE L 155           
SHEET    5 AD4 5 PRO L 113  LEU L 126 -1  O  GLY L 122   N  ILE L  58           
SHEET    1 AD5 5 GLU L  42  ARG L  44  0                                        
SHEET    2 AD5 5 GLN L  47  VAL L  49 -1  O  GLN L  47   N  ARG L  44           
SHEET    3 AD5 5 ARG L 131  LEU L 132 -1  O  LEU L 132   N  LEU L  48           
SHEET    4 AD5 5 LEU L  76  ILE L  83 -1  N  ILE L  83   O  ARG L 131           
SHEET    5 AD5 5 LYS L  90  LYS L  98 -1  O  LEU L  94   N  ILE L  80           
SHEET    1 AD6 5 GLU L  42  ARG L  44  0                                        
SHEET    2 AD6 5 GLN L  47  VAL L  49 -1  O  GLN L  47   N  ARG L  44           
SHEET    3 AD6 5 ARG L 131  LEU L 132 -1  O  LEU L 132   N  LEU L  48           
SHEET    4 AD6 5 LEU L  76  ILE L  83 -1  N  ILE L  83   O  ARG L 131           
SHEET    5 AD6 5 GLU L 135  ILE L 136 -1  O  GLU L 135   N  THR L  79           
SHEET    1 AD7 3 TRP M  28  LEU M  29  0                                        
SHEET    2 AD7 3 VAL M  13  ALA M  18 -1  N  VAL M  17   O  LEU M  29           
SHEET    3 AD7 3 LEU M  36  ALA M  38 -1  O  LEU M  36   N  HIS M  15           
SHEET    1 AD8 5 TRP M  28  LEU M  29  0                                        
SHEET    2 AD8 5 VAL M  13  ALA M  18 -1  N  VAL M  17   O  LEU M  29           
SHEET    3 AD8 5 TYR M 151  ALA M 156 -1  O  ILE M 154   N  ALA M  14           
SHEET    4 AD8 5 GLY M  54  GLN M  67 -1  N  LEU M  57   O  ILE M 155           
SHEET    5 AD8 5 PRO M 113  LEU M 126 -1  O  GLY M 122   N  ILE M  58           
SHEET    1 AD9 5 GLU M  42  ARG M  44  0                                        
SHEET    2 AD9 5 GLN M  47  VAL M  49 -1  O  GLN M  47   N  ARG M  44           
SHEET    3 AD9 5 ARG M 131  GLU M 135 -1  O  LEU M 132   N  LEU M  48           
SHEET    4 AD9 5 LEU M  76  ILE M  83 -1  N  THR M  79   O  GLU M 135           
SHEET    5 AD9 5 VAL M  91  LYS M  98 -1  O  LYS M  98   N  LEU M  76           
SHEET    1 AE1 5 LEU N  37  ALA N  38  0                                        
SHEET    2 AE1 5 VAL N  13  VAL N  17 -1  N  VAL N  13   O  ALA N  38           
SHEET    3 AE1 5 TYR N 151  ALA N 156 -1  O  PHE N 152   N  VAL N  16           
SHEET    4 AE1 5 GLY N  54  GLY N  66 -1  N  TYR N  59   O  GLY N 153           
SHEET    5 AE1 5 TRP N 114  LEU N 126 -1  O  LEU N 126   N  GLY N  54           
SHEET    1 AE2 5 GLU N  42  ARG N  44  0                                        
SHEET    2 AE2 5 GLN N  47  VAL N  49 -1  O  GLN N  47   N  ARG N  44           
SHEET    3 AE2 5 ARG N 131  ILE N 136 -1  O  LEU N 132   N  LEU N  48           
SHEET    4 AE2 5 LEU N  76  ILE N  83 -1  N  THR N  79   O  GLU N 135           
SHEET    5 AE2 5 VAL N  91  LYS N  98 -1  O  LYS N  98   N  LEU N  76           
SHEET    1 AE3 3 TRP O  28  LEU O  29  0                                        
SHEET    2 AE3 3 VAL O  13  ALA O  18 -1  N  VAL O  17   O  LEU O  29           
SHEET    3 AE3 3 LEU O  36  ALA O  38 -1  O  LEU O  36   N  HIS O  15           
SHEET    1 AE4 5 TRP O  28  LEU O  29  0                                        
SHEET    2 AE4 5 VAL O  13  ALA O  18 -1  N  VAL O  17   O  LEU O  29           
SHEET    3 AE4 5 TYR O 151  ALA O 156 -1  O  ILE O 154   N  ALA O  14           
SHEET    4 AE4 5 GLY O  54  GLY O  66 -1  N  GLN O  61   O  TYR O 151           
SHEET    5 AE4 5 TRP O 114  LEU O 126 -1  O  LEU O 120   N  SER O  60           
SHEET    1 AE5 5 GLU O  42  ARG O  44  0                                        
SHEET    2 AE5 5 GLN O  47  VAL O  49 -1  O  GLN O  47   N  ARG O  44           
SHEET    3 AE5 5 ARG O 131  ILE O 136 -1  O  LEU O 132   N  LEU O  48           
SHEET    4 AE5 5 LEU O  76  ILE O  83 -1  N  THR O  79   O  GLU O 135           
SHEET    5 AE5 5 LYS O  90  LYS O  98 -1  O  LYS O  98   N  LEU O  76           
SHEET    1 AE6 3 TRP P  28  LEU P  29  0                                        
SHEET    2 AE6 3 VAL P  13  ALA P  18 -1  N  VAL P  17   O  LEU P  29           
SHEET    3 AE6 3 LEU P  36  ALA P  38 -1  O  LEU P  36   N  HIS P  15           
SHEET    1 AE7 5 TRP P  28  LEU P  29  0                                        
SHEET    2 AE7 5 VAL P  13  ALA P  18 -1  N  VAL P  17   O  LEU P  29           
SHEET    3 AE7 5 TYR P 151  ALA P 156 -1  O  PHE P 152   N  VAL P  16           
SHEET    4 AE7 5 GLY P  54  GLY P  66 -1  N  TYR P  59   O  GLY P 153           
SHEET    5 AE7 5 TRP P 114  LEU P 126 -1  O  LEU P 126   N  GLY P  54           
SHEET    1 AE8 2 GLU P  42  ARG P  44  0                                        
SHEET    2 AE8 2 GLN P  47  VAL P  49 -1  O  GLN P  47   N  ARG P  44           
SHEET    1 AE9 3 LYS P  90  LYS P  98  0                                        
SHEET    2 AE9 3 LEU P  76  ILE P  83 -1  N  ILE P  80   O  LEU P  93           
SHEET    3 AE9 3 ALA P 134  ILE P 136 -1  O  GLU P 135   N  THR P  79           
SHEET    1 AF1 3 TRP Q  28  LEU Q  29  0                                        
SHEET    2 AF1 3 VAL Q  13  ALA Q  18 -1  N  VAL Q  17   O  LEU Q  29           
SHEET    3 AF1 3 LEU Q  36  ALA Q  38 -1  O  ALA Q  38   N  VAL Q  13           
SHEET    1 AF2 5 TRP Q  28  LEU Q  29  0                                        
SHEET    2 AF2 5 VAL Q  13  ALA Q  18 -1  N  VAL Q  17   O  LEU Q  29           
SHEET    3 AF2 5 TYR Q 151  ALA Q 156 -1  O  ILE Q 154   N  ALA Q  14           
SHEET    4 AF2 5 GLY Q  54  GLN Q  67 -1  N  GLN Q  61   O  TYR Q 151           
SHEET    5 AF2 5 PRO Q 113  LEU Q 126 -1  O  LEU Q 126   N  GLY Q  54           
SHEET    1 AF3 5 GLU Q  42  ARG Q  44  0                                        
SHEET    2 AF3 5 GLN Q  47  VAL Q  49 -1  O  GLN Q  47   N  ARG Q  44           
SHEET    3 AF3 5 ARG Q 131  ILE Q 136 -1  O  LEU Q 132   N  LEU Q  48           
SHEET    4 AF3 5 LEU Q  76  ILE Q  83 -1  N  THR Q  79   O  GLU Q 135           
SHEET    5 AF3 5 LYS Q  90  LYS Q  98 -1  O  VAL Q  91   N  ARG Q  82           
SHEET    1 AF4 3 TRP R  28  LEU R  29  0                                        
SHEET    2 AF4 3 VAL R  13  ALA R  18 -1  N  VAL R  17   O  LEU R  29           
SHEET    3 AF4 3 LEU R  37  ALA R  38 -1  O  ALA R  38   N  VAL R  13           
SHEET    1 AF5 5 TRP R  28  LEU R  29  0                                        
SHEET    2 AF5 5 VAL R  13  ALA R  18 -1  N  VAL R  17   O  LEU R  29           
SHEET    3 AF5 5 TYR R 151  ILE R 155 -1  O  PHE R 152   N  VAL R  16           
SHEET    4 AF5 5 GLY R  54  GLN R  67 -1  N  TYR R  59   O  GLY R 153           
SHEET    5 AF5 5 PRO R 113  LEU R 126 -1  O  ILE R 118   N  VAL R  62           
SHEET    1 AF6 5 GLU R  42  ARG R  44  0                                        
SHEET    2 AF6 5 GLN R  47  VAL R  49 -1  O  GLN R  47   N  ARG R  44           
SHEET    3 AF6 5 ARG R 131  ILE R 136 -1  O  LEU R 132   N  LEU R  48           
SHEET    4 AF6 5 LEU R  76  ILE R  83 -1  N  SER R  81   O  SER R 133           
SHEET    5 AF6 5 LYS R  90  LYS R  98 -1  O  LYS R  98   N  LEU R  76           
SHEET    1 AF7 3 TRP S  28  LEU S  29  0                                        
SHEET    2 AF7 3 VAL S  13  ALA S  18 -1  N  VAL S  17   O  LEU S  29           
SHEET    3 AF7 3 LEU S  36  ALA S  38 -1  O  LEU S  36   N  HIS S  15           
SHEET    1 AF8 5 TRP S  28  LEU S  29  0                                        
SHEET    2 AF8 5 VAL S  13  ALA S  18 -1  N  VAL S  17   O  LEU S  29           
SHEET    3 AF8 5 TYR S 151  ALA S 156 -1  O  PHE S 152   N  VAL S  16           
SHEET    4 AF8 5 GLY S  54  GLY S  66 -1  N  GLN S  61   O  TYR S 151           
SHEET    5 AF8 5 TRP S 114  LEU S 126 -1  O  LEU S 126   N  GLY S  54           
SHEET    1 AF9 5 GLU S  42  ARG S  44  0                                        
SHEET    2 AF9 5 GLN S  47  VAL S  49 -1  O  VAL S  49   N  GLU S  42           
SHEET    3 AF9 5 ARG S 131  ILE S 136 -1  O  LEU S 132   N  LEU S  48           
SHEET    4 AF9 5 LEU S  76  ILE S  83 -1  N  THR S  79   O  GLU S 135           
SHEET    5 AF9 5 VAL S  91  LYS S  98 -1  O  VAL S  91   N  ARG S  82           
SHEET    1 AG1 3 TRP T  28  LEU T  29  0                                        
SHEET    2 AG1 3 VAL T  13  ALA T  18 -1  N  VAL T  17   O  LEU T  29           
SHEET    3 AG1 3 LEU T  36  ALA T  38 -1  O  LEU T  36   N  HIS T  15           
SHEET    1 AG2 5 TRP T  28  LEU T  29  0                                        
SHEET    2 AG2 5 VAL T  13  ALA T  18 -1  N  VAL T  17   O  LEU T  29           
SHEET    3 AG2 5 TYR T 151  ALA T 156 -1  O  PHE T 152   N  VAL T  16           
SHEET    4 AG2 5 GLY T  54  GLY T  66 -1  N  LEU T  57   O  ILE T 155           
SHEET    5 AG2 5 TRP T 114  LEU T 126 -1  O  TRP T 114   N  GLY T  66           
SHEET    1 AG3 5 GLU T  42  ARG T  44  0                                        
SHEET    2 AG3 5 GLN T  47  VAL T  49 -1  O  VAL T  49   N  GLU T  42           
SHEET    3 AG3 5 ARG T 131  ILE T 136 -1  O  LEU T 132   N  LEU T  48           
SHEET    4 AG3 5 LEU T  76  ILE T  83 -1  N  ILE T  83   O  ARG T 131           
SHEET    5 AG3 5 LYS T  90  LYS T  98 -1  O  LEU T  94   N  ILE T  80           
SHEET    1 AG4 5 LEU U  36  ALA U  38  0                                        
SHEET    2 AG4 5 VAL U  13  VAL U  17 -1  N  VAL U  13   O  ALA U  38           
SHEET    3 AG4 5 TYR U 151  ILE U 155 -1  O  PHE U 152   N  VAL U  16           
SHEET    4 AG4 5 GLY U  54  GLN U  67 -1  N  GLN U  61   O  TYR U 151           
SHEET    5 AG4 5 PRO U 113  LEU U 126 -1  O  LEU U 120   N  SER U  60           
SHEET    1 AG5 5 GLU U  42  ARG U  44  0                                        
SHEET    2 AG5 5 GLN U  47  VAL U  49 -1  O  GLN U  47   N  ARG U  44           
SHEET    3 AG5 5 ARG U 131  ILE U 136 -1  O  LEU U 132   N  LEU U  48           
SHEET    4 AG5 5 LEU U  76  ILE U  83 -1  N  THR U  79   O  GLU U 135           
SHEET    5 AG5 5 VAL U  91  LYS U  98 -1  O  LYS U  98   N  LEU U  76           
SHEET    1 AG6 5 LEU V  37  ALA V  38  0                                        
SHEET    2 AG6 5 VAL V  13  VAL V  17 -1  N  VAL V  13   O  ALA V  38           
SHEET    3 AG6 5 TYR V 151  ALA V 156 -1  O  PHE V 152   N  VAL V  16           
SHEET    4 AG6 5 GLY V  54  GLY V  66 -1  N  TYR V  59   O  GLY V 153           
SHEET    5 AG6 5 TRP V 114  LEU V 126 -1  O  LEU V 120   N  SER V  60           
SHEET    1 AG7 5 LEU V  43  ARG V  44  0                                        
SHEET    2 AG7 5 GLN V  47  VAL V  49 -1  O  GLN V  47   N  ARG V  44           
SHEET    3 AG7 5 ARG V 131  GLU V 135 -1  O  LEU V 132   N  LEU V  48           
SHEET    4 AG7 5 LEU V  76  ILE V  83 -1  N  ILE V  83   O  ARG V 131           
SHEET    5 AG7 5 LYS V  90  LYS V  98 -1  O  LYS V  98   N  LEU V  76           
SHEET    1 AG8 3 TRP W  28  LEU W  29  0                                        
SHEET    2 AG8 3 VAL W  13  ALA W  18 -1  N  VAL W  17   O  LEU W  29           
SHEET    3 AG8 3 LEU W  36  ALA W  38 -1  O  LEU W  36   N  HIS W  15           
SHEET    1 AG9 5 TRP W  28  LEU W  29  0                                        
SHEET    2 AG9 5 VAL W  13  ALA W  18 -1  N  VAL W  17   O  LEU W  29           
SHEET    3 AG9 5 TYR W 151  ALA W 156 -1  O  PHE W 152   N  VAL W  16           
SHEET    4 AG9 5 GLY W  54  GLY W  66 -1  N  LEU W  57   O  ILE W 155           
SHEET    5 AG9 5 TRP W 114  LEU W 126 -1  O  GLY W 122   N  ILE W  58           
SHEET    1 AH1 5 GLU W  42  ARG W  44  0                                        
SHEET    2 AH1 5 GLN W  47  VAL W  49 -1  O  VAL W  49   N  GLU W  42           
SHEET    3 AH1 5 ARG W 131  ILE W 136 -1  O  LEU W 132   N  LEU W  48           
SHEET    4 AH1 5 LEU W  76  ILE W  83 -1  N  ILE W  83   O  ARG W 131           
SHEET    5 AH1 5 LYS W  90  LYS W  98 -1  O  VAL W  91   N  ARG W  82           
SHEET    1 AH2 3 TRP X  28  LEU X  29  0                                        
SHEET    2 AH2 3 VAL X  13  ALA X  18 -1  N  VAL X  17   O  LEU X  29           
SHEET    3 AH2 3 LEU X  36  ALA X  38 -1  O  LEU X  36   N  HIS X  15           
SHEET    1 AH3 5 TRP X  28  LEU X  29  0                                        
SHEET    2 AH3 5 VAL X  13  ALA X  18 -1  N  VAL X  17   O  LEU X  29           
SHEET    3 AH3 5 TYR X 151  ALA X 156 -1  O  PHE X 152   N  VAL X  16           
SHEET    4 AH3 5 GLY X  54  GLY X  66 -1  N  LEU X  57   O  ILE X 155           
SHEET    5 AH3 5 TRP X 114  LEU X 126 -1  O  ILE X 118   N  VAL X  62           
SHEET    1 AH4 5 GLU X  42  LEU X  43  0                                        
SHEET    2 AH4 5 LEU X  48  VAL X  49 -1  O  VAL X  49   N  GLU X  42           
SHEET    3 AH4 5 ARG X 131  LEU X 132 -1  O  LEU X 132   N  LEU X  48           
SHEET    4 AH4 5 LEU X  76  ILE X  83 -1  N  ILE X  83   O  ARG X 131           
SHEET    5 AH4 5 LYS X  90  LYS X  98 -1  O  LYS X  98   N  LEU X  76           
SHEET    1 AH5 5 GLU X  42  LEU X  43  0                                        
SHEET    2 AH5 5 LEU X  48  VAL X  49 -1  O  VAL X  49   N  GLU X  42           
SHEET    3 AH5 5 ARG X 131  LEU X 132 -1  O  LEU X 132   N  LEU X  48           
SHEET    4 AH5 5 LEU X  76  ILE X  83 -1  N  ILE X  83   O  ARG X 131           
SHEET    5 AH5 5 GLU X 135  ILE X 136 -1  O  GLU X 135   N  THR X  79           
SHEET    1 AH6 3 TRP Y  28  LEU Y  29  0                                        
SHEET    2 AH6 3 VAL Y  13  ALA Y  18 -1  N  VAL Y  17   O  LEU Y  29           
SHEET    3 AH6 3 LEU Y  36  ALA Y  38 -1  O  ALA Y  38   N  VAL Y  13           
SHEET    1 AH7 5 TRP Y  28  LEU Y  29  0                                        
SHEET    2 AH7 5 VAL Y  13  ALA Y  18 -1  N  VAL Y  17   O  LEU Y  29           
SHEET    3 AH7 5 TYR Y 151  ALA Y 156 -1  O  PHE Y 152   N  VAL Y  16           
SHEET    4 AH7 5 GLY Y  54  GLN Y  67 -1  N  LEU Y  57   O  ILE Y 155           
SHEET    5 AH7 5 PRO Y 113  LEU Y 126 -1  O  LEU Y 126   N  GLY Y  54           
SHEET    1 AH8 2 GLU Y  42  ARG Y  44  0                                        
SHEET    2 AH8 2 GLN Y  47  VAL Y  49 -1  O  GLN Y  47   N  ARG Y  44           
SHEET    1 AH9 3 LYS Y  90  LYS Y  98  0                                        
SHEET    2 AH9 3 LEU Y  76  ILE Y  83 -1  N  ARG Y  82   O  VAL Y  91           
SHEET    3 AH9 3 ARG Y 131  ILE Y 136 -1  O  GLU Y 135   N  THR Y  79           
SHEET    1 AI1 5 LEU Z  37  ALA Z  38  0                                        
SHEET    2 AI1 5 VAL Z  13  VAL Z  17 -1  N  VAL Z  13   O  ALA Z  38           
SHEET    3 AI1 5 TYR Z 151  ALA Z 156 -1  O  ILE Z 154   N  ALA Z  14           
SHEET    4 AI1 5 GLY Z  54  GLY Z  66 -1  N  LEU Z  57   O  ILE Z 155           
SHEET    5 AI1 5 TRP Z 114  LEU Z 126 -1  O  GLU Z 116   N  PHE Z  64           
SHEET    1 AI2 5 GLU Z  42  ARG Z  44  0                                        
SHEET    2 AI2 5 GLN Z  47  VAL Z  49 -1  O  GLN Z  47   N  ARG Z  44           
SHEET    3 AI2 5 ARG Z 131  ILE Z 136 -1  O  LEU Z 132   N  LEU Z  48           
SHEET    4 AI2 5 LEU Z  76  ILE Z  83 -1  N  THR Z  79   O  GLU Z 135           
SHEET    5 AI2 5 LYS Z  90  LYS Z  98 -1  O  LYS Z  98   N  LEU Z  76           
SHEET    1 AI3 3 TRP a  28  LEU a  29  0                                        
SHEET    2 AI3 3 VAL a  13  ALA a  18 -1  N  VAL a  17   O  LEU a  29           
SHEET    3 AI3 3 LEU a  36  ALA a  38 -1  O  ALA a  38   N  VAL a  13           
SHEET    1 AI4 5 TRP a  28  LEU a  29  0                                        
SHEET    2 AI4 5 VAL a  13  ALA a  18 -1  N  VAL a  17   O  LEU a  29           
SHEET    3 AI4 5 TYR a 151  ALA a 156 -1  O  PHE a 152   N  VAL a  16           
SHEET    4 AI4 5 GLY a  54  GLN a  67 -1  N  GLN a  61   O  TYR a 151           
SHEET    5 AI4 5 PRO a 113  LEU a 126 -1  O  LEU a 126   N  GLY a  54           
SHEET    1 AI5 5 GLU a  42  ARG a  44  0                                        
SHEET    2 AI5 5 GLN a  47  VAL a  49 -1  O  GLN a  47   N  ARG a  44           
SHEET    3 AI5 5 ARG a 131  ILE a 136 -1  O  LEU a 132   N  LEU a  48           
SHEET    4 AI5 5 LEU a  76  ILE a  83 -1  N  ILE a  83   O  ARG a 131           
SHEET    5 AI5 5 VAL a  91  LYS a  98 -1  O  LYS a  98   N  LEU a  76           
SHEET    1 AI6 5 LEU b  36  ALA b  38  0                                        
SHEET    2 AI6 5 VAL b  13  VAL b  17 -1  N  HIS b  15   O  LEU b  36           
SHEET    3 AI6 5 TYR b 151  ALA b 156 -1  O  PHE b 152   N  VAL b  16           
SHEET    4 AI6 5 GLY b  54  GLY b  66 -1  N  LEU b  57   O  ILE b 155           
SHEET    5 AI6 5 TRP b 114  LEU b 126 -1  O  LEU b 126   N  GLY b  54           
SHEET    1 AI7 5 GLU b  42  ARG b  44  0                                        
SHEET    2 AI7 5 GLN b  47  VAL b  49 -1  O  VAL b  49   N  GLU b  42           
SHEET    3 AI7 5 ARG b 131  ILE b 136 -1  O  LEU b 132   N  LEU b  48           
SHEET    4 AI7 5 LEU b  76  ILE b  83 -1  N  THR b  79   O  GLU b 135           
SHEET    5 AI7 5 LYS b  90  LYS b  98 -1  O  VAL b  91   N  ARG b  82           
SHEET    1 AI8 3 TRP c  28  LEU c  29  0                                        
SHEET    2 AI8 3 VAL c  13  ALA c  18 -1  N  VAL c  17   O  LEU c  29           
SHEET    3 AI8 3 LEU c  36  LEU c  37 -1  O  LEU c  36   N  HIS c  15           
SHEET    1 AI9 5 TRP c  28  LEU c  29  0                                        
SHEET    2 AI9 5 VAL c  13  ALA c  18 -1  N  VAL c  17   O  LEU c  29           
SHEET    3 AI9 5 TYR c 151  ALA c 156 -1  O  ILE c 154   N  ALA c  14           
SHEET    4 AI9 5 GLY c  54  GLN c  67 -1  N  LEU c  57   O  ILE c 155           
SHEET    5 AI9 5 PRO c 113  LEU c 126 -1  O  LEU c 126   N  GLY c  54           
SHEET    1 AJ1 5 GLU c  42  ARG c  44  0                                        
SHEET    2 AJ1 5 GLN c  47  VAL c  49 -1  O  VAL c  49   N  GLU c  42           
SHEET    3 AJ1 5 ARG c 131  ILE c 136 -1  O  LEU c 132   N  LEU c  48           
SHEET    4 AJ1 5 LEU c  76  ILE c  83 -1  N  THR c  79   O  GLU c 135           
SHEET    5 AJ1 5 LYS c  90  LYS c  98 -1  O  LYS c  98   N  LEU c  76           
SHEET    1 AJ2 5 LEU d  37  ALA d  38  0                                        
SHEET    2 AJ2 5 VAL d  13  VAL d  17 -1  N  VAL d  13   O  ALA d  38           
SHEET    3 AJ2 5 TYR d 151  LEU d 157 -1  O  PHE d 152   N  VAL d  16           
SHEET    4 AJ2 5 GLY d  54  GLY d  66 -1  N  LEU d  55   O  LEU d 157           
SHEET    5 AJ2 5 TRP d 114  LEU d 126 -1  O  GLY d 122   N  ILE d  58           
SHEET    1 AJ3 5 GLU d  42  ARG d  44  0                                        
SHEET    2 AJ3 5 GLN d  47  VAL d  49 -1  O  VAL d  49   N  GLU d  42           
SHEET    3 AJ3 5 ARG d 131  ILE d 136 -1  O  LEU d 132   N  LEU d  48           
SHEET    4 AJ3 5 LEU d  76  ILE d  83 -1  N  THR d  79   O  GLU d 135           
SHEET    5 AJ3 5 LYS d  90  LYS d  98 -1  O  LEU d  94   N  ILE d  80           
SHEET    1 AJ4 3 TRP e  28  LEU e  29  0                                        
SHEET    2 AJ4 3 VAL e  13  ALA e  18 -1  N  VAL e  17   O  LEU e  29           
SHEET    3 AJ4 3 LEU e  36  ALA e  38 -1  O  ALA e  38   N  VAL e  13           
SHEET    1 AJ5 5 TRP e  28  LEU e  29  0                                        
SHEET    2 AJ5 5 VAL e  13  ALA e  18 -1  N  VAL e  17   O  LEU e  29           
SHEET    3 AJ5 5 TYR e 151  ALA e 156 -1  O  PHE e 152   N  VAL e  16           
SHEET    4 AJ5 5 GLY e  54  GLN e  67 -1  N  LEU e  57   O  ILE e 155           
SHEET    5 AJ5 5 PRO e 113  LEU e 126 -1  O  ILE e 118   N  VAL e  62           
SHEET    1 AJ6 5 GLU e  42  ARG e  44  0                                        
SHEET    2 AJ6 5 GLN e  47  VAL e  49 -1  O  VAL e  49   N  GLU e  42           
SHEET    3 AJ6 5 ARG e 131  ILE e 136 -1  O  LEU e 132   N  LEU e  48           
SHEET    4 AJ6 5 LEU e  76  ILE e  83 -1  N  ILE e  83   O  ARG e 131           
SHEET    5 AJ6 5 VAL e  91  LYS e  98 -1  O  VAL e  91   N  ARG e  82           
SHEET    1 AJ7 3 TRP f  28  LEU f  29  0                                        
SHEET    2 AJ7 3 VAL f  13  ALA f  18 -1  N  VAL f  17   O  LEU f  29           
SHEET    3 AJ7 3 LEU f  36  ALA f  38 -1  O  LEU f  36   N  HIS f  15           
SHEET    1 AJ8 5 TRP f  28  LEU f  29  0                                        
SHEET    2 AJ8 5 VAL f  13  ALA f  18 -1  N  VAL f  17   O  LEU f  29           
SHEET    3 AJ8 5 TYR f 151  ALA f 156 -1  O  PHE f 152   N  VAL f  16           
SHEET    4 AJ8 5 GLY f  54  GLY f  66 -1  N  TYR f  59   O  GLY f 153           
SHEET    5 AJ8 5 TRP f 114  LEU f 126 -1  O  LEU f 120   N  SER f  60           
SHEET    1 AJ9 4 LEU f  48  VAL f  49  0                                        
SHEET    2 AJ9 4 ARG f 131  ILE f 136 -1  O  LEU f 132   N  LEU f  48           
SHEET    3 AJ9 4 LEU f  76  ILE f  83 -1  N  ILE f  83   O  ARG f 131           
SHEET    4 AJ9 4 VAL f  91  LYS f  98 -1  O  VAL f  91   N  ARG f  82           
SHEET    1 AK1 3 TRP g  28  LEU g  29  0                                        
SHEET    2 AK1 3 VAL g  13  ALA g  18 -1  N  VAL g  17   O  LEU g  29           
SHEET    3 AK1 3 LEU g  36  ALA g  38 -1  O  LEU g  36   N  HIS g  15           
SHEET    1 AK2 5 TRP g  28  LEU g  29  0                                        
SHEET    2 AK2 5 VAL g  13  ALA g  18 -1  N  VAL g  17   O  LEU g  29           
SHEET    3 AK2 5 TYR g 151  ALA g 156 -1  O  PHE g 152   N  VAL g  16           
SHEET    4 AK2 5 GLY g  54  GLY g  66 -1  N  GLN g  61   O  TYR g 151           
SHEET    5 AK2 5 TRP g 114  LEU g 126 -1  O  PHE g 124   N  TYR g  56           
SHEET    1 AK3 5 GLU g  42  ARG g  44  0                                        
SHEET    2 AK3 5 GLN g  47  VAL g  49 -1  O  VAL g  49   N  GLU g  42           
SHEET    3 AK3 5 ARG g 131  ILE g 136 -1  O  LEU g 132   N  LEU g  48           
SHEET    4 AK3 5 LEU g  76  ILE g  83 -1  N  THR g  79   O  GLU g 135           
SHEET    5 AK3 5 LYS g  90  LYS g  98 -1  O  LYS g  98   N  LEU g  76           
SHEET    1 AK4 5 LEU h  37  ALA h  38  0                                        
SHEET    2 AK4 5 VAL h  13  VAL h  17 -1  N  VAL h  13   O  ALA h  38           
SHEET    3 AK4 5 TYR h 151  ALA h 156 -1  O  PHE h 152   N  VAL h  16           
SHEET    4 AK4 5 GLY h  54  GLY h  66 -1  N  LEU h  57   O  ILE h 155           
SHEET    5 AK4 5 TRP h 114  LEU h 126 -1  O  LEU h 126   N  GLY h  54           
SHEET    1 AK5 5 GLU h  42  LEU h  43  0                                        
SHEET    2 AK5 5 LEU h  48  VAL h  49 -1  O  VAL h  49   N  GLU h  42           
SHEET    3 AK5 5 ARG h 131  ILE h 136 -1  O  LEU h 132   N  LEU h  48           
SHEET    4 AK5 5 LEU h  76  ILE h  83 -1  N  THR h  79   O  GLU h 135           
SHEET    5 AK5 5 VAL h  91  LYS h  98 -1  O  VAL h  91   N  ARG h  82           
SHEET    1 AK6 3 TRP i  28  LEU i  29  0                                        
SHEET    2 AK6 3 VAL i  13  ALA i  18 -1  N  VAL i  17   O  LEU i  29           
SHEET    3 AK6 3 LEU i  36  ALA i  38 -1  O  ALA i  38   N  VAL i  13           
SHEET    1 AK7 5 TRP i  28  LEU i  29  0                                        
SHEET    2 AK7 5 VAL i  13  ALA i  18 -1  N  VAL i  17   O  LEU i  29           
SHEET    3 AK7 5 TYR i 151  ALA i 156 -1  O  PHE i 152   N  VAL i  16           
SHEET    4 AK7 5 GLY i  54  GLY i  66 -1  N  LEU i  57   O  ILE i 155           
SHEET    5 AK7 5 TRP i 114  LEU i 126 -1  O  LEU i 120   N  SER i  60           
SHEET    1 AK8 5 GLU i  42  ARG i  44  0                                        
SHEET    2 AK8 5 GLN i  47  VAL i  49 -1  O  GLN i  47   N  ARG i  44           
SHEET    3 AK8 5 ARG i 131  ILE i 136 -1  O  LEU i 132   N  LEU i  48           
SHEET    4 AK8 5 LEU i  76  ILE i  83 -1  N  THR i  79   O  GLU i 135           
SHEET    5 AK8 5 VAL i  91  LYS i  98 -1  O  LYS i  98   N  LEU i  76           
SHEET    1 AK9 3 TRP j  28  LEU j  29  0                                        
SHEET    2 AK9 3 VAL j  13  ALA j  18 -1  N  VAL j  17   O  LEU j  29           
SHEET    3 AK9 3 LEU j  36  ALA j  38 -1  O  LEU j  36   N  HIS j  15           
SHEET    1 AL1 5 TRP j  28  LEU j  29  0                                        
SHEET    2 AL1 5 VAL j  13  ALA j  18 -1  N  VAL j  17   O  LEU j  29           
SHEET    3 AL1 5 TYR j 151  ALA j 156 -1  O  PHE j 152   N  VAL j  16           
SHEET    4 AL1 5 GLY j  54  GLY j  66 -1  N  LEU j  57   O  ILE j 155           
SHEET    5 AL1 5 TRP j 114  LEU j 126 -1  O  PHE j 124   N  TYR j  56           
SHEET    1 AL2 5 LEU j  43  ARG j  44  0                                        
SHEET    2 AL2 5 GLN j  47  VAL j  49 -1  O  GLN j  47   N  ARG j  44           
SHEET    3 AL2 5 ARG j 131  ILE j 136 -1  O  LEU j 132   N  LEU j  48           
SHEET    4 AL2 5 LEU j  76  ILE j  83 -1  N  THR j  79   O  GLU j 135           
SHEET    5 AL2 5 LYS j  90  LYS j  98 -1  O  LYS j  98   N  LEU j  76           
SHEET    1 AL3 3 TRP k  28  LEU k  29  0                                        
SHEET    2 AL3 3 VAL k  13  ALA k  18 -1  N  VAL k  17   O  LEU k  29           
SHEET    3 AL3 3 LEU k  36  ALA k  38 -1  O  LEU k  36   N  HIS k  15           
SHEET    1 AL4 5 TRP k  28  LEU k  29  0                                        
SHEET    2 AL4 5 VAL k  13  ALA k  18 -1  N  VAL k  17   O  LEU k  29           
SHEET    3 AL4 5 TYR k 151  ALA k 156 -1  O  PHE k 152   N  VAL k  16           
SHEET    4 AL4 5 GLY k  54  GLN k  67 -1  N  LEU k  57   O  ILE k 155           
SHEET    5 AL4 5 PRO k 113  LEU k 126 -1  O  GLU k 116   N  PHE k  64           
SHEET    1 AL5 5 GLU k  42  ARG k  44  0                                        
SHEET    2 AL5 5 GLN k  47  VAL k  49 -1  O  VAL k  49   N  GLU k  42           
SHEET    3 AL5 5 ARG k 131  ILE k 136 -1  O  LEU k 132   N  LEU k  48           
SHEET    4 AL5 5 LEU k  76  ILE k  83 -1  N  THR k  79   O  GLU k 135           
SHEET    5 AL5 5 LYS k  90  LYS k  98 -1  O  LYS k  98   N  LEU k  76           
SHEET    1 AL6 5 LEU l  37  ALA l  38  0                                        
SHEET    2 AL6 5 VAL l  13  VAL l  17 -1  N  VAL l  13   O  ALA l  38           
SHEET    3 AL6 5 TYR l 151  ALA l 156 -1  O  PHE l 152   N  VAL l  16           
SHEET    4 AL6 5 GLY l  54  GLY l  66 -1  N  LEU l  57   O  ILE l 155           
SHEET    5 AL6 5 TRP l 114  LEU l 126 -1  O  LEU l 126   N  GLY l  54           
SHEET    1 AL7 3 GLU l  42  ARG l  44  0                                        
SHEET    2 AL7 3 GLN l  47  VAL l  49 -1  O  VAL l  49   N  GLU l  42           
SHEET    3 AL7 3 ARG l 131  LEU l 132 -1  O  LEU l 132   N  LEU l  48           
SHEET    1 AL8 3 LYS l  90  LYS l  98  0                                        
SHEET    2 AL8 3 LEU l  76  ILE l  83 -1  N  ILE l  80   O  LEU l  93           
SHEET    3 AL8 3 ALA l 134  ILE l 136 -1  O  GLU l 135   N  THR l  79           
SHEET    1 AL9 3 TRP m  28  LEU m  29  0                                        
SHEET    2 AL9 3 VAL m  13  ALA m  18 -1  N  VAL m  17   O  LEU m  29           
SHEET    3 AL9 3 LEU m  36  ALA m  38 -1  O  LEU m  36   N  HIS m  15           
SHEET    1 AM1 5 TRP m  28  LEU m  29  0                                        
SHEET    2 AM1 5 VAL m  13  ALA m  18 -1  N  VAL m  17   O  LEU m  29           
SHEET    3 AM1 5 TYR m 151  ALA m 156 -1  O  PHE m 152   N  VAL m  16           
SHEET    4 AM1 5 GLY m  54  GLN m  67 -1  N  LEU m  57   O  ILE m 155           
SHEET    5 AM1 5 PRO m 113  LEU m 126 -1  O  ILE m 118   N  VAL m  62           
SHEET    1 AM2 5 GLU m  42  ARG m  44  0                                        
SHEET    2 AM2 5 GLN m  47  VAL m  49 -1  O  GLN m  47   N  ARG m  44           
SHEET    3 AM2 5 ARG m 131  ILE m 136 -1  O  LEU m 132   N  LEU m  48           
SHEET    4 AM2 5 LEU m  76  ILE m  83 -1  N  THR m  79   O  GLU m 135           
SHEET    5 AM2 5 VAL m  91  LYS m  98 -1  O  LYS m  98   N  LEU m  76           
SHEET    1 AM3 3 TRP n  28  LEU n  29  0                                        
SHEET    2 AM3 3 VAL n  13  ALA n  18 -1  N  VAL n  17   O  LEU n  29           
SHEET    3 AM3 3 LEU n  36  ALA n  38 -1  O  ALA n  38   N  VAL n  13           
SHEET    1 AM4 5 TRP n  28  LEU n  29  0                                        
SHEET    2 AM4 5 VAL n  13  ALA n  18 -1  N  VAL n  17   O  LEU n  29           
SHEET    3 AM4 5 TYR n 151  ALA n 156 -1  O  PHE n 152   N  VAL n  16           
SHEET    4 AM4 5 GLY n  54  GLY n  66 -1  N  GLN n  61   O  TYR n 151           
SHEET    5 AM4 5 TRP n 114  LEU n 126 -1  O  GLU n 116   N  PHE n  64           
SHEET    1 AM5 4 LEU n  48  VAL n  49  0                                        
SHEET    2 AM5 4 ARG n 131  LEU n 132 -1  O  LEU n 132   N  LEU n  48           
SHEET    3 AM5 4 LEU n  76  ILE n  83 -1  N  ILE n  83   O  ARG n 131           
SHEET    4 AM5 4 LYS n  90  LYS n  98 -1  O  VAL n  91   N  ARG n  82           
SHEET    1 AM6 3 TRP o  28  LEU o  29  0                                        
SHEET    2 AM6 3 VAL o  13  ALA o  18 -1  N  VAL o  17   O  LEU o  29           
SHEET    3 AM6 3 LEU o  36  ALA o  38 -1  O  LEU o  36   N  HIS o  15           
SHEET    1 AM7 5 TRP o  28  LEU o  29  0                                        
SHEET    2 AM7 5 VAL o  13  ALA o  18 -1  N  VAL o  17   O  LEU o  29           
SHEET    3 AM7 5 TYR o 151  ALA o 156 -1  O  ILE o 154   N  ALA o  14           
SHEET    4 AM7 5 GLY o  54  VAL o  62 -1  N  GLN o  61   O  TYR o 151           
SHEET    5 AM7 5 ILE o 118  LEU o 126 -1  O  PHE o 124   N  TYR o  56           
SHEET    1 AM8 5 GLU o  42  ARG o  44  0                                        
SHEET    2 AM8 5 GLN o  47  VAL o  49 -1  O  GLN o  47   N  ARG o  44           
SHEET    3 AM8 5 ARG o 131  ILE o 136 -1  O  LEU o 132   N  LEU o  48           
SHEET    4 AM8 5 LEU o  76  ILE o  83 -1  N  ILE o  83   O  ARG o 131           
SHEET    5 AM8 5 LYS o  90  LYS o  98 -1  O  VAL o  91   N  ARG o  82           
SHEET    1 AM9 2 LYS o  65  GLN o  67  0                                        
SHEET    2 AM9 2 PRO o 113  TYR o 115 -1  O  TRP o 114   N  GLY o  66           
SHEET    1 AN1 5 LEU p  37  ALA p  38  0                                        
SHEET    2 AN1 5 VAL p  13  VAL p  17 -1  N  VAL p  13   O  ALA p  38           
SHEET    3 AN1 5 TYR p 151  ALA p 156 -1  O  PHE p 152   N  VAL p  16           
SHEET    4 AN1 5 GLY p  54  GLY p  66 -1  N  LEU p  57   O  ILE p 155           
SHEET    5 AN1 5 TRP p 114  LEU p 126 -1  O  GLY p 122   N  ILE p  58           
SHEET    1 AN2 5 GLU p  42  LEU p  43  0                                        
SHEET    2 AN2 5 LEU p  48  VAL p  49 -1  O  VAL p  49   N  GLU p  42           
SHEET    3 AN2 5 ARG p 131  ILE p 136 -1  O  LEU p 132   N  LEU p  48           
SHEET    4 AN2 5 LEU p  76  ILE p  83 -1  N  THR p  79   O  GLU p 135           
SHEET    5 AN2 5 LYS p  90  LYS p  98 -1  O  LEU p  94   N  ILE p  80           
SHEET    1 AN3 3 TRP q  28  LEU q  29  0                                        
SHEET    2 AN3 3 VAL q  13  ALA q  18 -1  N  VAL q  17   O  LEU q  29           
SHEET    3 AN3 3 LEU q  36  ALA q  38 -1  O  LEU q  36   N  HIS q  15           
SHEET    1 AN4 5 TRP q  28  LEU q  29  0                                        
SHEET    2 AN4 5 VAL q  13  ALA q  18 -1  N  VAL q  17   O  LEU q  29           
SHEET    3 AN4 5 TYR q 151  ALA q 156 -1  O  PHE q 152   N  VAL q  16           
SHEET    4 AN4 5 GLY q  54  GLN q  67 -1  N  LEU q  57   O  ILE q 155           
SHEET    5 AN4 5 PRO q 113  LEU q 126 -1  O  GLY q 122   N  ILE q  58           
SHEET    1 AN5 5 GLU q  42  ARG q  44  0                                        
SHEET    2 AN5 5 GLN q  47  VAL q  49 -1  O  GLN q  47   N  ARG q  44           
SHEET    3 AN5 5 ARG q 131  SER q 133 -1  O  LEU q 132   N  LEU q  48           
SHEET    4 AN5 5 LEU q  76  ILE q  83 -1  N  SER q  81   O  SER q 133           
SHEET    5 AN5 5 VAL q  91  LYS q  98 -1  O  VAL q  91   N  ARG q  82           
SHEET    1 AN6 5 LEU r  37  ALA r  38  0                                        
SHEET    2 AN6 5 VAL r  13  ALA r  14 -1  N  VAL r  13   O  ALA r  38           
SHEET    3 AN6 5 ILE r 154  LEU r 157 -1  O  ILE r 154   N  ALA r  14           
SHEET    4 AN6 5 GLY r  54  GLY r  66 -1  N  LEU r  57   O  ILE r 155           
SHEET    5 AN6 5 TRP r 114  LEU r 126 -1  O  GLY r 122   N  ILE r  58           
SHEET    1 AN7 2 VAL r  17  ALA r  18  0                                        
SHEET    2 AN7 2 TRP r  28  LEU r  29 -1  O  LEU r  29   N  VAL r  17           
SHEET    1 AN8 3 VAL r  91  LYS r  98  0                                        
SHEET    2 AN8 3 LEU r  76  ILE r  83 -1  N  ARG r  82   O  VAL r  91           
SHEET    3 AN8 3 ARG r 131  ILE r 136 -1  O  GLU r 135   N  THR r  79           
SHEET    1 AN9 3 TRP s  28  LEU s  29  0                                        
SHEET    2 AN9 3 VAL s  13  ALA s  18 -1  N  VAL s  17   O  LEU s  29           
SHEET    3 AN9 3 LEU s  36  ALA s  38 -1  O  LEU s  36   N  HIS s  15           
SHEET    1 AO1 5 TRP s  28  LEU s  29  0                                        
SHEET    2 AO1 5 VAL s  13  ALA s  18 -1  N  VAL s  17   O  LEU s  29           
SHEET    3 AO1 5 TYR s 151  ALA s 156 -1  O  PHE s 152   N  VAL s  16           
SHEET    4 AO1 5 GLY s  54  LEU s  63 -1  N  LEU s  57   O  ILE s 155           
SHEET    5 AO1 5 PRO s 117  LEU s 126 -1  O  PHE s 124   N  TYR s  56           
SHEET    1 AO2 5 GLU s  42  ARG s  44  0                                        
SHEET    2 AO2 5 GLN s  47  VAL s  49 -1  O  VAL s  49   N  GLU s  42           
SHEET    3 AO2 5 ARG s 131  ILE s 136 -1  O  LEU s 132   N  LEU s  48           
SHEET    4 AO2 5 LEU s  76  ILE s  83 -1  N  THR s  79   O  GLU s 135           
SHEET    5 AO2 5 LYS s  90  LYS s  98 -1  O  VAL s  91   N  ARG s  82           
SHEET    1 AO3 2 GLY s  66  GLN s  67  0                                        
SHEET    2 AO3 2 PRO s 113  TRP s 114 -1  O  TRP s 114   N  GLY s  66           
SHEET    1 AO4 5 LEU t  37  ALA t  38  0                                        
SHEET    2 AO4 5 VAL t  13  VAL t  17 -1  N  VAL t  13   O  ALA t  38           
SHEET    3 AO4 5 TYR t 151  ALA t 156 -1  O  ILE t 154   N  ALA t  14           
SHEET    4 AO4 5 LEU t  55  GLY t  66 -1  N  GLN t  61   O  TYR t 151           
SHEET    5 AO4 5 TRP t 114  GLN t 125 -1  O  ILE t 118   N  VAL t  62           
SHEET    1 AO5 5 LEU t  43  ARG t  44  0                                        
SHEET    2 AO5 5 GLN t  47  VAL t  49 -1  O  GLN t  47   N  ARG t  44           
SHEET    3 AO5 5 ARG t 131  ILE t 136 -1  O  LEU t 132   N  LEU t  48           
SHEET    4 AO5 5 LEU t  76  ILE t  83 -1  N  THR t  79   O  GLU t 135           
SHEET    5 AO5 5 LYS t  90  LYS t  98 -1  O  VAL t  91   N  ARG t  82           
SHEET    1 AO6 3 TRP u  28  LEU u  29  0                                        
SHEET    2 AO6 3 VAL u  13  ALA u  18 -1  N  VAL u  17   O  LEU u  29           
SHEET    3 AO6 3 LEU u  36  ALA u  38 -1  O  LEU u  36   N  HIS u  15           
SHEET    1 AO7 5 TRP u  28  LEU u  29  0                                        
SHEET    2 AO7 5 VAL u  13  ALA u  18 -1  N  VAL u  17   O  LEU u  29           
SHEET    3 AO7 5 TYR u 151  ALA u 156 -1  O  PHE u 152   N  VAL u  16           
SHEET    4 AO7 5 GLY u  54  GLN u  67 -1  N  TYR u  59   O  GLY u 153           
SHEET    5 AO7 5 PRO u 113  LEU u 126 -1  O  PHE u 124   N  TYR u  56           
SHEET    1 AO8 5 GLU u  42  ARG u  44  0                                        
SHEET    2 AO8 5 GLN u  47  VAL u  49 -1  O  GLN u  47   N  ARG u  44           
SHEET    3 AO8 5 ARG u 131  ILE u 136 -1  O  LEU u 132   N  LEU u  48           
SHEET    4 AO8 5 LEU u  76  ILE u  83 -1  N  THR u  79   O  GLU u 135           
SHEET    5 AO8 5 LYS u  90  LYS u  98 -1  O  VAL u  91   N  ARG u  82           
SHEET    1 AO9 3 TRP v  28  LEU v  29  0                                        
SHEET    2 AO9 3 ALA v  14  ALA v  18 -1  N  VAL v  17   O  LEU v  29           
SHEET    3 AO9 3 LEU v  36  LEU v  37 -1  O  LEU v  36   N  HIS v  15           
SHEET    1 AP1 5 TRP v  28  LEU v  29  0                                        
SHEET    2 AP1 5 ALA v  14  ALA v  18 -1  N  VAL v  17   O  LEU v  29           
SHEET    3 AP1 5 TYR v 151  LEU v 157 -1  O  PHE v 152   N  VAL v  16           
SHEET    4 AP1 5 GLY v  54  GLY v  66 -1  N  LEU v  57   O  ILE v 155           
SHEET    5 AP1 5 TRP v 114  LEU v 126 -1  O  TRP v 114   N  GLY v  66           
SHEET    1 AP2 3 GLU v  42  LEU v  43  0                                        
SHEET    2 AP2 3 LEU v  48  VAL v  49 -1  O  VAL v  49   N  GLU v  42           
SHEET    3 AP2 3 ARG v 131  LEU v 132 -1  O  LEU v 132   N  LEU v  48           
SHEET    1 AP3 3 LYS v  90  LYS v  98  0                                        
SHEET    2 AP3 3 LEU v  76  ILE v  83 -1  N  ILE v  80   O  LEU v  93           
SHEET    3 AP3 3 ALA v 134  ILE v 136 -1  O  GLU v 135   N  THR v  79           
SHEET    1 AP4 3 TRP w  28  LEU w  29  0                                        
SHEET    2 AP4 3 VAL w  13  ALA w  18 -1  N  VAL w  17   O  LEU w  29           
SHEET    3 AP4 3 LEU w  36  ALA w  38 -1  O  LEU w  36   N  HIS w  15           
SHEET    1 AP5 5 TRP w  28  LEU w  29  0                                        
SHEET    2 AP5 5 VAL w  13  ALA w  18 -1  N  VAL w  17   O  LEU w  29           
SHEET    3 AP5 5 TYR w 151  ALA w 156 -1  O  ILE w 154   N  ALA w  14           
SHEET    4 AP5 5 GLY w  54  GLN w  67 -1  N  LEU w  57   O  ILE w 155           
SHEET    5 AP5 5 PRO w 113  LEU w 126 -1  O  GLY w 122   N  ILE w  58           
SHEET    1 AP6 5 GLU w  42  ARG w  44  0                                        
SHEET    2 AP6 5 GLN w  47  VAL w  49 -1  O  VAL w  49   N  GLU w  42           
SHEET    3 AP6 5 ARG w 131  ILE w 136 -1  O  LEU w 132   N  LEU w  48           
SHEET    4 AP6 5 LEU w  76  ILE w  83 -1  N  THR w  79   O  GLU w 135           
SHEET    5 AP6 5 LYS w  90  LYS w  98 -1  O  VAL w  91   N  ARG w  82           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.03  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.01  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.03  
SSBOND   5 CYS F   69    CYS F  101                          1555   1555  2.02  
SSBOND   6 CYS G   69    CYS G  101                          1555   1555  1.99  
SSBOND   7 CYS H   69    CYS H  101                          1555   1555  2.02  
SSBOND   8 CYS I   69    CYS I  101                          1555   1555  2.03  
SSBOND   9 CYS J   69    CYS J  101                          1555   1555  2.03  
SSBOND  10 CYS K   69    CYS K  101                          1555   1555  2.03  
SSBOND  11 CYS L   69    CYS L  101                          1555   1555  2.03  
SSBOND  12 CYS M   69    CYS M  101                          1555   1555  2.04  
SSBOND  13 CYS N   69    CYS N  101                          1555   1555  2.02  
SSBOND  14 CYS O   69    CYS O  101                          1555   1555  2.01  
SSBOND  15 CYS P   69    CYS P  101                          1555   1555  2.04  
SSBOND  16 CYS Q   69    CYS Q  101                          1555   1555  2.03  
SSBOND  17 CYS R   69    CYS R  101                          1555   1555  2.03  
SSBOND  18 CYS S   69    CYS S  101                          1555   1555  2.03  
SSBOND  19 CYS T   69    CYS T  101                          1555   1555  2.01  
SSBOND  20 CYS U   69    CYS U  101                          1555   1555  2.05  
SSBOND  21 CYS V   69    CYS V  101                          1555   1555  2.03  
SSBOND  22 CYS W   69    CYS W  101                          1555   1555  2.03  
SSBOND  23 CYS X   69    CYS X  101                          1555   1555  2.03  
SSBOND  24 CYS Y   69    CYS Y  101                          1555   1555  2.03  
SSBOND  25 CYS Z   69    CYS Z  101                          1555   1555  2.03  
SSBOND  26 CYS a   69    CYS a  101                          1555   1555  2.01  
SSBOND  27 CYS b   69    CYS b  101                          1555   1555  2.03  
SSBOND  28 CYS c   69    CYS c  101                          1555   1555  2.03  
SSBOND  29 CYS d   69    CYS d  101                          1555   1555  2.03  
SSBOND  30 CYS e   69    CYS e  101                          1555   1555  2.05  
SSBOND  31 CYS f   69    CYS f  101                          1555   1555  2.03  
SSBOND  32 CYS g   69    CYS g  101                          1555   1555  2.02  
SSBOND  33 CYS h   69    CYS h  101                          1555   1555  2.03  
SSBOND  34 CYS i   69    CYS i  101                          1555   1555  2.01  
SSBOND  35 CYS j   69    CYS j  101                          1555   1555  2.03  
SSBOND  36 CYS k   69    CYS k  101                          1555   1555  2.04  
SSBOND  37 CYS l   69    CYS l  101                          1555   1555  2.02  
SSBOND  38 CYS m   69    CYS m  101                          1555   1555  2.02  
SSBOND  39 CYS n   69    CYS n  101                          1555   1555  2.03  
SSBOND  40 CYS o   69    CYS o  101                          1555   1555  2.03  
SSBOND  41 CYS p   69    CYS p  101                          1555   1555  2.04  
SSBOND  42 CYS q   69    CYS q  101                          1555   1555  2.01  
SSBOND  43 CYS r   69    CYS r  101                          1555   1555  2.03  
SSBOND  44 CYS s   69    CYS s  101                          1555   1555  2.04  
SSBOND  45 CYS t   69    CYS t  101                          1555   1555  2.03  
SSBOND  46 CYS u   69    CYS u  101                          1555   1555  2.01  
SSBOND  47 CYS v   69    CYS v  101                          1555   1555  2.03  
SSBOND  48 CYS w   69    CYS w  101                          1555   1555  2.04  
LINK         NH2 ARG D  32                 OE1 GLU s  23     1555   1545  1.43  
SITE     1 AC1 14 LEU A  57  SER A  60  TYR A 119  LEU A 120                    
SITE     2 AC1 14 GLY A 121  GLY A 122  TYR A 151  ILE A 155                    
SITE     3 AC1 14 JNI A 202  LEU B  57  TYR B 119  GLY B 121                    
SITE     4 AC1 14 GLY B 122  JNI C 201                                          
SITE     1 AC2  5 HIS A  15  JNI A 201  JNI C 201  JNI C 202                    
SITE     2 AC2  5 JNI D 201                                                     
SITE     1 AC3  8 JNI A 201  JNI A 202  LEU B  55  LEU B 157                    
SITE     2 AC3  8 TYR C 119  SER D  60  GLY D 121  JNI D 201                    
SITE     1 AC4  8 SER A   9  LEU A  36  JNI A 202  HIS C  15                    
SITE     2 AC4  8 ASN C  34  LEU C  36  TYR C  59  SER C 147                    
SITE     1 AC5  4 JNI A 202  JNI C 201  LEU D  57  ALA D 156                    
SITE     1 AC6 13 LEU F  57  SER F  60  GLN F  61  TYR F 119                    
SITE     2 AC6 13 LEU F 120  GLY F 121  GLY F 122  TYR F 151                    
SITE     3 AC6 13 JNI F 202  TYR G 119  GLY G 121  JNI H 202                    
SITE     4 AC6 13 LEU I 157                                                     
SITE     1 AC7  4 HIS F  15  JNI F 201  JNI H 201  JNI H 202                    
SITE     1 AC8  5 JNI F 202  TYR H 151  ILE H 155  JNI H 202                    
SITE     2 AC8  5 TYR I  59                                                     
SITE     1 AC9  8 JNI F 201  JNI F 202  LEU G  55  LEU G 157                    
SITE     2 AC9  8 TYR H 119  JNI H 201  TYR I 119  GLY I 121                    
SITE     1 AD1 15 LEU J  57  ILE J  58  TYR J  59  SER J  60                    
SITE     2 AD1 15 GLN J  61  TYR J 119  LEU J 120  GLY J 121                    
SITE     3 AD1 15 GLY J 122  TYR J 151  JNI J 202  LEU K  57                    
SITE     4 AD1 15 TYR K 119  GLY K 121  JNI L 201                               
SITE     1 AD2  3 HIS J  15  JNI J 201  JNI L 201                               
SITE     1 AD3 10 JNI J 201  JNI J 202  TYR L 119  LEU L 120                    
SITE     2 AD3 10 GLY L 121  TYR M  59  TYR M 119  LEU M 120                    
SITE     3 AD3 10 GLY M 121  JNI M 201                                          
SITE     1 AD4  6 GLY L 121  TYR L 151  JNI L 201  LYS M  11                    
SITE     2 AD4  6 LEU M  57  LEU M 157                                          
SITE     1 AD5 14 LEU N  57  TYR N  59  SER N  60  GLN N  61                    
SITE     2 AD5 14 TYR N 119  LEU N 120  GLY N 121  GLY N 122                    
SITE     3 AD5 14 TYR N 151  LEU O  57  TYR O 119  GLY O 121                    
SITE     4 AD5 14 GLY O 122  JNI P 201                                          
SITE     1 AD6  4 JNI N 201  ILE P 155  JNI P 202  JNI Q 201                    
SITE     1 AD7  7 LEU O 157  TYR P 119  JNI P 201  TYR Q 119                    
SITE     2 AD7  7 LEU Q 120  GLY Q 121  JNI Q 201                               
SITE     1 AD8  7 LEU P  57  LEU P 157  JNI P 201  JNI P 202                    
SITE     2 AD8  7 LYS Q  11  LEU Q  57  ALA Q 156                               
SITE     1 AD9  8 LEU R  57  SER R  60  GLN R  61  TYR R 119                    
SITE     2 AD9  8 GLY R 121  TYR R 151  TYR S 119  GLY S 121                    
SITE     1 AE1  6 GLY T 121  TYR T 151  LYS U  11  LEU U  57                    
SITE     2 AE1  6 TYR U  59  ALA U 156                                          
SITE     1 AE2 10 LEU V  57  SER V  60  GLN V  61  TYR V 119                    
SITE     2 AE2 10 LEU V 120  TYR V 151  JNI V 202  TYR W 119                    
SITE     3 AE2 10 GLY W 121  JNI X 202                                          
SITE     1 AE3  4 HIS V  15  JNI V 201  JNI X 201  JNI X 202                    
SITE     1 AE4  9 JNI V 202  LEU X  57  GLY X 121  TYR X 151                    
SITE     2 AE4  9 JNI X 202  LYS Y  11  LEU Y  57  TYR Y  59                    
SITE     3 AE4  9 LEU Y 157                                                     
SITE     1 AE5  8 JNI V 201  JNI V 202  LEU W  55  LEU W 157                    
SITE     2 AE5  8 TYR X 119  JNI X 201  TYR Y 119  GLY Y 121                    
SITE     1 AE6 13 LEU Z  57  SER Z  60  GLN Z  61  TYR Z 119                    
SITE     2 AE6 13 LEU Z 120  GLY Z 121  TYR Z 151  JNI Z 202                    
SITE     3 AE6 13 LEU a  57  TYR a 119  GLY a 121  GLY a 122                    
SITE     4 AE6 13 JNI b 202                                                     
SITE     1 AE7  2 JNI Z 201  JNI b 201                                          
SITE     1 AE8 10 JNI Z 202  LEU b  57  GLY b 121  TYR b 151                    
SITE     2 AE8 10 JNI b 202  LYS c  11  LEU c  57  TYR c  59                    
SITE     3 AE8 10 ALA c 156  LEU c 157                                          
SITE     1 AE9  6 JNI Z 201  LEU a  55  LEU a 157  TYR b 119                    
SITE     2 AE9  6 JNI b 201  TYR c 119                                          
SITE     1 AF1 10 LEU d  57  TYR d  59  SER d  60  GLN d  61                    
SITE     2 AF1 10 TYR d 119  LEU d 120  TYR d 151  TYR e 119                    
SITE     3 AF1 10 GLY e 121  JNI f 201                                          
SITE     1 AF2  4 HIS d  15  JNI d 201  ILE f 155  JNI f 202                    
SITE     1 AF3 11 SER d   9  ASP d  10  VAL d  13  ASN d  39                    
SITE     2 AF3 11 ILE d 155  PRO f   8  SER f   9  HIS f  15                    
SITE     3 AF3 11 ALA f  33  ASN f  34  JNI f 201                               
SITE     1 AF4 10 LEU h  57  SER h  60  TYR h 119  LEU h 120                    
SITE     2 AF4 10 TYR h 151  LEU i  57  TYR i 119  GLY i 121                    
SITE     3 AF4 10 JNI j 202  LYS k  11                                          
SITE     1 AF5  1 JNI j 201                                                     
SITE     1 AF6  6 JNI h 202  GLY j 121  TYR j 151  JNI j 202                    
SITE     2 AF6  6 LEU k  57  LEU k 157                                          
SITE     1 AF7  6 JNI h 201  LEU i  55  LEU i 157  TYR j 119                    
SITE     2 AF7  6 JNI j 201  TYR k 119                                          
SITE     1 AF8 11 LEU l  57  SER l  60  GLN l  61  PRO l 117                    
SITE     2 AF8 11 TYR l 119  LEU l 120  TYR l 151  TYR m 119                    
SITE     3 AF8 11 GLY m 121  JNI n 201  JNI n 202                               
SITE     1 AF9  2 JNI l 201  JNI o 201                                          
SITE     1 AG1  6 JNI l 201  LEU m  55  LEU m 157  TYR n 119                    
SITE     2 AG1  6 TYR o 119  JNI o 201                                          
SITE     1 AG2  8 TYR n  59  GLY n 121  JNI n 201  JNI n 202                    
SITE     2 AG2  8 LYS o  11  LEU o  57  ALA o 156  LEU o 157                    
SITE     1 AG3 10 LEU p  57  TYR p  59  GLN p  61  TYR p 119                    
SITE     2 AG3 10 LEU p 120  TYR p 151  JNI p 202  TYR q 119                    
SITE     3 AG3 10 GLY q 121  JNI r 202                                          
SITE     1 AG4  8 HIS p  15  JNI p 201  SER r   9  VAL r  13                    
SITE     2 AG4  8 HIS r  15  ILE r 155  JNI r 201  JNI r 202                    
SITE     1 AG5  7 JNI p 202  SER r  60  GLY r 121  TYR r 151                    
SITE     2 AG5  7 ILE r 155  JNI r 202  TYR s  59                               
SITE     1 AG6  7 JNI p 201  JNI p 202  LEU q  55  LEU q 157                    
SITE     2 AG6  7 TYR r 119  JNI r 201  TYR s 119                               
SITE     1 AG7 12 LEU t  57  SER t  60  TYR t 119  LEU t 120                    
SITE     2 AG7 12 GLY t 121  GLY t 122  TYR t 151  JNI t 202                    
SITE     3 AG7 12 LEU u  57  TYR u 119  GLY u 121  LEU w 157                    
SITE     1 AG8  5 HIS t  15  JNI t 201  SER v   9  JNI v 201                    
SITE     2 AG8  5 JNI v 202                                                     
SITE     1 AG9  7 JNI t 202  TYR v 119  GLY v 121  TYR v 151                    
SITE     2 AG9  7 JNI v 202  LEU w  57  TYR w  59                               
SITE     1 AH1  6 JNI t 202  LEU u  55  LEU u 157  TYR v 119                    
SITE     2 AH1  6 JNI v 201  TYR w 119                                          
SITE     1 AH2 20 VAL C  91  GLN D  21  ALA D  22  GLY D  24                    
SITE     2 AH2 20 GLN D  25  ASN D  30  ARG D  31  ALA D  33                    
SITE     3 AH2 20 ASN D  34  ALA D  35  SER D 147  PRO s  20                    
SITE     4 AH2 20 ALA s  22  GLY s  24  GLN s  25  ASN s  30                    
SITE     5 AH2 20 ARG s  31  ALA s  33  ASN s  34  ALA s  35                    
CRYST1  104.888  118.348  186.747  97.57  94.31  98.75 P 1          48          
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      0.009534  0.001468  0.000942        0.00000                         
SCALE2      0.000000  0.008549  0.001255        0.00000                         
SCALE3      0.000000  0.000000  0.005428        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system