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Database: PDB
Entry: 5LF0
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HEADER    HYDROLASE                               30-JUN-16   5LF0              
TITLE     HUMAN 20S PROTEASOME COMPLEX WITH EPOXOMICIN AT 2.4 ANGSTROM          
CAVEAT     5LF0    6V1 U 47 HAS WRONG CHIRALITY AT ATOM C1 IML C 2 HAS WRONG    
CAVEAT   2 5LF0    CHIRALITY AT ATOM CB IML D 2 HAS WRONG CHIRALITY AT ATOM CA  
CAVEAT   3 5LF0    IML D 2 HAS WRONG CHIRALITY AT ATOM CB IML E 2 HAS WRONG     
CAVEAT   4 5LF0    CHIRALITY AT ATOM CA IML F 2 HAS WRONG CHIRALITY AT ATOM CB  
CAVEAT   5 5LF0    IML G 2 HAS WRONG CHIRALITY AT ATOM CA IML G 2 HAS WRONG     
CAVEAT   6 5LF0    CHIRALITY AT ATOM CB IML H 2 HAS WRONG CHIRALITY AT ATOM CA  
CAVEAT   7 5LF0    IML H 2 HAS WRONG CHIRALITY AT ATOM CB                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;                           
COMPND   3 CHAIN: A, O;                                                         
COMPND   4 SYNONYM: MACROPAIN SUBUNIT C3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND   5 SUBUNIT C3,PROTEASOME COMPONENT C3;                                  
COMPND   6 EC: 3.4.25.1;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;                           
COMPND   9 CHAIN: B, P;                                                         
COMPND  10 SYNONYM: MACROPAIN SUBUNIT C9,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  11 SUBUNIT C9,PROTEASOME COMPONENT C9,PROTEASOME SUBUNIT L;             
COMPND  12 EC: 3.4.25.1;                                                        
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-7;                           
COMPND  15 CHAIN: C, Q;                                                         
COMPND  16 SYNONYM: PROTEASOME SUBUNIT RC6-1,PROTEASOME SUBUNIT XAPC7;          
COMPND  17 EC: 3.4.25.1;                                                        
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;                           
COMPND  20 CHAIN: D, R;                                                         
COMPND  21 SYNONYM: MACROPAIN ZETA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  22 ZETA CHAIN,PROTEASOME ZETA CHAIN;                                    
COMPND  23 EC: 3.4.25.1;                                                        
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;                           
COMPND  26 CHAIN: E, S;                                                         
COMPND  27 SYNONYM: 30 KDA PROSOMAL PROTEIN,PROS-30,MACROPAIN SUBUNIT C2,       
COMPND  28 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2,PROTEASOME COMPONENT 
COMPND  29 C2,PROTEASOME NU CHAIN;                                              
COMPND  30 EC: 3.4.25.1;                                                        
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;                           
COMPND  33 CHAIN: F, T;                                                         
COMPND  34 SYNONYM: MACROPAIN SUBUNIT C8,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  35 SUBUNIT C8,PROTEASOME COMPONENT C8;                                  
COMPND  36 EC: 3.4.25.1;                                                        
COMPND  37 MOL_ID: 7;                                                           
COMPND  38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;                           
COMPND  39 CHAIN: G, U;                                                         
COMPND  40 SYNONYM: 27 KDA PROSOMAL PROTEIN,P27K,MACROPAIN IOTA CHAIN,          
COMPND  41 MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN,PROTEASOME IOTA      
COMPND  42 CHAIN;                                                               
COMPND  43 EC: 3.4.25.1;                                                        
COMPND  44 MOL_ID: 8;                                                           
COMPND  45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;                            
COMPND  46 CHAIN: H, V;                                                         
COMPND  47 SYNONYM: MACROPAIN CHAIN Z,MULTICATALYTIC ENDOPEPTIDASE COMPLEX CHAIN
COMPND  48 Z,PROTEASOME SUBUNIT Z;                                              
COMPND  49 EC: 3.4.25.1;                                                        
COMPND  50 MOL_ID: 9;                                                           
COMPND  51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;                            
COMPND  52 CHAIN: I, W;                                                         
COMPND  53 SYNONYM: PROTEASOME CHAIN 13,PROTEASOME COMPONENT C10-II,PROTEASOME  
COMPND  54 THETA CHAIN;                                                         
COMPND  55 EC: 3.4.25.1;                                                        
COMPND  56 MOL_ID: 10;                                                          
COMPND  57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;                            
COMPND  58 CHAIN: J, X;                                                         
COMPND  59 SYNONYM: MACROPAIN SUBUNIT C7-I,MULTICATALYTIC ENDOPEPTIDASE COMPLEX 
COMPND  60 SUBUNIT C7-I,PROTEASOME COMPONENT C7-I;                              
COMPND  61 EC: 3.4.25.1;                                                        
COMPND  62 MOL_ID: 11;                                                          
COMPND  63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;                            
COMPND  64 CHAIN: K, Y;                                                         
COMPND  65 SYNONYM: MACROPAIN EPSILON CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND  66 EPSILON CHAIN,PROTEASOME CHAIN 6,PROTEASOME EPSILON CHAIN,PROTEASOME 
COMPND  67 SUBUNIT MB1,PROTEASOME SUBUNIT X;                                    
COMPND  68 EC: 3.4.25.1;                                                        
COMPND  69 MOL_ID: 12;                                                          
COMPND  70 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;                            
COMPND  71 CHAIN: L, Z;                                                         
COMPND  72 SYNONYM: MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX   
COMPND  73 SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN;           
COMPND  74 EC: 3.4.25.1;                                                        
COMPND  75 MOL_ID: 13;                                                          
COMPND  76 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;                            
COMPND  77 CHAIN: M, a;                                                         
COMPND  78 SYNONYM: 26 KDA PROSOMAL PROTEIN,PROS-26,MACROPAIN BETA CHAIN,       
COMPND  79 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN,PROTEASOME BETA      
COMPND  80 CHAIN,PROTEASOME CHAIN 3,HSN3;                                       
COMPND  81 EC: 3.4.25.1;                                                        
COMPND  82 MOL_ID: 14;                                                          
COMPND  83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;                            
COMPND  84 CHAIN: N, b;                                                         
COMPND  85 SYNONYM: MACROPAIN DELTA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX  
COMPND  86 DELTA CHAIN,PROTEASOME DELTA CHAIN,PROTEASOME SUBUNIT Y;             
COMPND  87 EC: 3.4.25.1;                                                        
COMPND  88 MOL_ID: 15;                                                          
COMPND  89 MOLECULE: EPOXOMICIN (PEPTIDE INHIBITOR);                            
COMPND  90 CHAIN: c, d, e, f, g, h;                                             
COMPND  91 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HELA;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: HELA;                                                     
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: HELA;                                                     
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: HELA;                                                     
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 CELL_LINE: HELA;                                                     
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 CELL_LINE: HELA;                                                     
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 CELL_LINE: HELA;                                                     
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 CELL_LINE: HELA;                                                     
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 CELL_LINE: HELA;                                                     
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606;                                                
SOURCE  50 CELL_LINE: HELA;                                                     
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  53 ORGANISM_COMMON: HUMAN;                                              
SOURCE  54 ORGANISM_TAXID: 9606;                                                
SOURCE  55 CELL_LINE: HELA;                                                     
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  58 ORGANISM_COMMON: HUMAN;                                              
SOURCE  59 ORGANISM_TAXID: 9606;                                                
SOURCE  60 CELL_LINE: HELA;                                                     
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 CELL_LINE: HELA;                                                     
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  68 ORGANISM_COMMON: HUMAN;                                              
SOURCE  69 ORGANISM_TAXID: 9606;                                                
SOURCE  70 CELL_LINE: HELA;                                                     
SOURCE  71 MOL_ID: 15;                                                          
SOURCE  72 SYNTHETIC: YES;                                                      
SOURCE  73 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  74 ORGANISM_TAXID: 32630                                                
KEYWDS    PROTEASOME, MULTICATALYTIC PROTEINASE, NTN-HYDROLASE, HYDROLASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHRADER,F.HENNEBERG,R.MATA,K.TITTMANN,T.R.SCHNEIDER,H.STARK,       
AUTHOR   2 G.BOURENKOV,A.CHARI                                                  
REVDAT   2   06-SEP-17 5LF0    1       REMARK                                   
REVDAT   1   17-AUG-16 5LF0    0                                                
JRNL        AUTH   J.SCHRADER,F.HENNEBERG,R.A.MATA,K.TITTMANN,T.R.SCHNEIDER,    
JRNL        AUTH 2 H.STARK,G.BOURENKOV,A.CHARI                                  
JRNL        TITL   THE INHIBITION MECHANISM OF HUMAN 20S PROTEASOMES ENABLES    
JRNL        TITL 2 NEXT-GENERATION INHIBITOR DESIGN.                            
JRNL        REF    SCIENCE                       V. 353   594 2016              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   27493187                                                     
JRNL        DOI    10.1126/SCIENCE.AAF8993                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 170.23                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 262073                         
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13832                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 18302                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 997                          
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 48106                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 218                                     
REMARK   3   SOLVENT ATOMS            : 3173                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.70000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.428         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.250         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.256         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.631        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 49444 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 47096 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 66978 ; 1.522 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):108076 ; 1.177 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6301 ; 6.964 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2124 ;35.819 ;23.705       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  8266 ;15.620 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   340 ;16.753 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7587 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 56226 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 11206 ; 0.004 ; 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): 25031 ; 1.178 ; 3.545       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 25030 ; 1.178 ; 3.545       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31271 ; 1.996 ; 5.313       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 31272 ; 1.996 ; 5.313       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 24413 ; 1.455 ; 3.744       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 24413 ; 1.455 ; 3.744       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 35668 ; 2.447 ; 5.533       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 56181 ; 7.013 ;29.270       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 56182 ; 7.013 ;29.271       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 14                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     3    232       O     3    232   25966  0.07  0.05     
REMARK   3    2     B     2    249       P     2    249   27886  0.08  0.05     
REMARK   3    3     C     2    237       Q     2    237   25086  0.10  0.05     
REMARK   3    4     D     9    241       R     9    241   26296  0.08  0.05     
REMARK   3    5     E     4    236       S     4    236   27468  0.07  0.05     
REMARK   3    6     F     6    243       T     6    243   28048  0.08  0.05     
REMARK   3    7     G     2    245       U     2    245   26430  0.08  0.05     
REMARK   3    8     H     1    220       V     1    220   25348  0.08  0.05     
REMARK   3    9     I     1    204       W     1    204   25598  0.07  0.05     
REMARK   3   10     J     1    196       X     1    196   24596  0.08  0.05     
REMARK   3   11     K     1    199       Y     1    199   23480  0.09  0.05     
REMARK   3   12     L     1    213       Z     1    213   24710  0.06  0.05     
REMARK   3   13     M     1    216       a     1    216   25036  0.07  0.05     
REMARK   3   14     N     1    201       b     1    201   23676  0.08  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   232                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.7426 205.7209   1.1234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1808 T22:   0.3451                                     
REMARK   3      T33:   0.1740 T12:   0.1397                                     
REMARK   3      T13:   0.1018 T23:   0.1118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6753 L22:   2.1293                                     
REMARK   3      L33:   2.3079 L12:   0.4911                                     
REMARK   3      L13:   0.7311 L23:   0.3875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0764 S12:   0.0739 S13:   0.1172                       
REMARK   3      S21:  -0.1870 S22:  -0.0626 S23:  -0.4861                       
REMARK   3      S31:   0.1115 S32:   0.6671 S33:   0.1390                       
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     2        B   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.6909 176.8571   0.0029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6097 T22:   0.2599                                     
REMARK   3      T33:   0.1385 T12:   0.1943                                     
REMARK   3      T13:   0.1284 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9404 L22:   2.0044                                     
REMARK   3      L33:   1.0794 L12:  -0.0100                                     
REMARK   3      L13:   0.1861 L23:  -0.2245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0675 S12:   0.2182 S13:  -0.1818                       
REMARK   3      S21:  -0.2339 S22:  -0.0572 S23:  -0.4226                       
REMARK   3      S31:   0.4443 S32:   0.4204 S33:   0.1247                       
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     2        C   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8127 169.1653  -3.9541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7203 T22:   0.2077                                     
REMARK   3      T33:   0.2148 T12:  -0.0883                                     
REMARK   3      T13:  -0.0249 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1989 L22:   3.1853                                     
REMARK   3      L33:   1.4472 L12:   0.0521                                     
REMARK   3      L13:   0.2418 L23:  -0.2893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0165 S12:  -0.0188 S13:  -0.6620                       
REMARK   3      S21:  -0.2202 S22:   0.0257 S23:  -0.1088                       
REMARK   3      S31:   0.5981 S32:  -0.0442 S33:  -0.0422                       
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   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0897 187.9920  -7.8384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5302 T22:   0.3912                                     
REMARK   3      T33:   0.2201 T12:  -0.1683                                     
REMARK   3      T13:  -0.1547 T23:   0.0628                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6804 L22:   1.6854                                     
REMARK   3      L33:   2.4140 L12:  -0.3142                                     
REMARK   3      L13:  -1.0210 L23:  -0.1162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0630 S12:   0.1381 S13:  -0.2303                       
REMARK   3      S21:  -0.2956 S22:   0.0480 S23:   0.2005                       
REMARK   3      S31:   0.4561 S32:  -0.4878 S33:   0.0150                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     4        E   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8310 219.9040  -9.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1945 T22:   0.2953                                     
REMARK   3      T33:   0.1177 T12:  -0.0602                                     
REMARK   3      T13:  -0.0542 T23:   0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5835 L22:   1.0565                                     
REMARK   3      L33:   2.0557 L12:  -0.4420                                     
REMARK   3      L13:  -0.2393 L23:  -0.1283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:   0.2088 S13:  -0.3347                       
REMARK   3      S21:  -0.1279 S22:   0.0226 S23:   0.2926                       
REMARK   3      S31:   0.1964 S32:  -0.5861 S33:  -0.0110                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     6        F   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3940 240.1010  -7.5840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1415 T22:   0.1298                                     
REMARK   3      T33:   0.0791 T12:   0.0138                                     
REMARK   3      T13:  -0.0212 T23:   0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8014 L22:   2.3716                                     
REMARK   3      L33:   0.9746 L12:  -0.7463                                     
REMARK   3      L13:   0.0094 L23:   0.0640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:   0.1576 S13:   0.2452                       
REMARK   3      S21:  -0.1469 S22:  -0.0833 S23:   0.1495                       
REMARK   3      S31:  -0.1636 S32:  -0.1389 S33:   0.0472                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0170 233.5870  -3.6720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1341 T22:   0.2385                                     
REMARK   3      T33:   0.1327 T12:   0.0042                                     
REMARK   3      T13:   0.0552 T23:   0.1384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0298 L22:   2.9350                                     
REMARK   3      L33:   1.5325 L12:   0.3990                                     
REMARK   3      L13:   0.2334 L23:   0.6559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:   0.2156 S13:   0.2379                       
REMARK   3      S21:  -0.3233 S22:  -0.0626 S23:  -0.2735                       
REMARK   3      S31:  -0.2732 S32:   0.3521 S33:   0.0701                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   220                          
REMARK   3    RESIDUE RANGE :   c     1        c     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3520 213.9320  39.4390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0944 T22:   0.3720                                     
REMARK   3      T33:   0.0801 T12:  -0.0318                                     
REMARK   3      T13:   0.0106 T23:   0.1012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3718 L22:   1.7566                                     
REMARK   3      L33:   1.0566 L12:  -0.1017                                     
REMARK   3      L13:  -0.1755 L23:  -0.4034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:  -0.0425 S13:  -0.0962                       
REMARK   3      S21:   0.0704 S22:  -0.1586 S23:  -0.2213                       
REMARK   3      S31:   0.0081 S32:   0.4990 S33:   0.1758                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5710 186.5180  39.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2191 T22:   0.2788                                     
REMARK   3      T33:   0.0579 T12:   0.1591                                     
REMARK   3      T13:   0.0862 T23:   0.0978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7994 L22:   1.0686                                     
REMARK   3      L33:   2.3789 L12:   0.3221                                     
REMARK   3      L13:   0.5610 L23:  -0.9867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0436 S12:  -0.0040 S13:  -0.0354                       
REMARK   3      S21:  -0.0901 S22:  -0.1955 S23:  -0.1735                       
REMARK   3      S31:   0.2125 S32:   0.5381 S33:   0.2391                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1290 170.2650  36.2700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4639 T22:   0.0646                                     
REMARK   3      T33:   0.0796 T12:   0.0139                                     
REMARK   3      T13:   0.0204 T23:   0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4042 L22:   0.8780                                     
REMARK   3      L33:   3.1253 L12:   0.3396                                     
REMARK   3      L13:  -0.1625 L23:  -0.0096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:   0.0849 S13:  -0.1147                       
REMARK   3      S21:  -0.2371 S22:  -0.0088 S23:   0.1458                       
REMARK   3      S31:   0.6458 S32:  -0.0688 S33:   0.0757                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   200                          
REMARK   3    RESIDUE RANGE :   d     1        d     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0340 180.7830  32.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3062 T22:   0.3265                                     
REMARK   3      T33:   0.1112 T12:  -0.2168                                     
REMARK   3      T13:  -0.1052 T23:   0.1452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1141 L22:   1.6904                                     
REMARK   3      L33:   2.5926 L12:  -0.2537                                     
REMARK   3      L13:  -0.6306 L23:   0.3085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0043 S12:   0.1463 S13:  -0.1227                       
REMARK   3      S21:  -0.2671 S22:   0.0648 S23:   0.1773                       
REMARK   3      S31:   0.4610 S32:  -0.5497 S33:  -0.0605                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5750 210.2690  30.8530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1183 T22:   0.4843                                     
REMARK   3      T33:   0.1525 T12:  -0.0188                                     
REMARK   3      T13:  -0.0223 T23:   0.1940                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1987 L22:   1.3927                                     
REMARK   3      L33:   1.4805 L12:   0.1983                                     
REMARK   3      L13:  -0.2673 L23:   0.1446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0005 S12:   0.0304 S13:  -0.0024                       
REMARK   3      S21:  -0.1120 S22:   0.1387 S23:   0.3624                       
REMARK   3      S31:  -0.0324 S32:  -0.6235 S33:  -0.1381                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3020 237.9210  33.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2707 T22:   0.2029                                     
REMARK   3      T33:   0.0781 T12:   0.1353                                     
REMARK   3      T13:   0.0756 T23:   0.0828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1026 L22:   1.2366                                     
REMARK   3      L33:   2.2572 L12:   0.2583                                     
REMARK   3      L13:   0.1756 L23:   0.4352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0206 S12:   0.0053 S13:   0.1913                       
REMARK   3      S21:   0.1253 S22:   0.0966 S23:   0.1838                       
REMARK   3      S31:  -0.5334 S32:  -0.3703 S33:  -0.0760                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   202                          
REMARK   3    RESIDUE RANGE :   e     1        e     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7740 241.4350  35.6530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2933 T22:   0.0933                                     
REMARK   3      T33:   0.0195 T12:  -0.0773                                     
REMARK   3      T13:  -0.0016 T23:   0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7132 L22:   1.4149                                     
REMARK   3      L33:   2.3532 L12:  -0.2208                                     
REMARK   3      L13:   0.1565 L23:  -0.1651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0242 S12:  -0.0517 S13:   0.1214                       
REMARK   3      S21:   0.1214 S22:  -0.0791 S23:  -0.0291                       
REMARK   3      S31:  -0.5354 S32:   0.1216 S33:   0.0549                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     3        O   232                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2410 225.9840 103.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5539 T22:   0.6830                                     
REMARK   3      T33:   0.3325 T12:   0.3243                                     
REMARK   3      T13:   0.2337 T23:   0.1022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5479 L22:   2.0577                                     
REMARK   3      L33:   1.9260 L12:  -0.0951                                     
REMARK   3      L13:   0.5642 L23:  -0.4960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0323 S12:  -0.1096 S13:   0.3551                       
REMARK   3      S21:   0.2639 S22:   0.0580 S23:   0.5867                       
REMARK   3      S31:  -0.5533 S32:  -0.5897 S33:  -0.0256                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     2        P   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3567 194.1928 104.7678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2948 T22:   0.7481                                     
REMARK   3      T33:   0.2414 T12:   0.0726                                     
REMARK   3      T13:   0.1687 T23:   0.2293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1059 L22:   1.8179                                     
REMARK   3      L33:   1.5573 L12:   0.4759                                     
REMARK   3      L13:   0.3084 L23:   0.4150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.2458 S13:   0.0374                       
REMARK   3      S21:   0.2858 S22:   0.0741 S23:   0.5170                       
REMARK   3      S31:  -0.1130 S32:  -0.8080 S33:  -0.0685                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     2        Q   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2599 173.9302 109.3716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4441 T22:   0.4104                                     
REMARK   3      T33:   0.3140 T12:  -0.0170                                     
REMARK   3      T13:   0.0204 T23:   0.1317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2080 L22:   2.8038                                     
REMARK   3      L33:   2.6669 L12:   0.7149                                     
REMARK   3      L13:   0.1222 L23:   0.3914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1098 S12:  -0.0972 S13:  -0.7369                       
REMARK   3      S21:   0.1853 S22:  -0.0096 S23:   0.3857                       
REMARK   3      S31:   0.6349 S32:  -0.4686 S33:  -0.1002                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     9        R   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3622 180.4972 112.7604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2747 T22:   0.3394                                     
REMARK   3      T33:   0.1012 T12:  -0.0030                                     
REMARK   3      T13:   0.0417 T23:   0.0855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0632 L22:   1.0005                                     
REMARK   3      L33:   2.8606 L12:   0.0716                                     
REMARK   3      L13:  -0.4834 L23:   0.1479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:  -0.1743 S13:  -0.2594                       
REMARK   3      S21:   0.0612 S22:   0.0368 S23:   0.1444                       
REMARK   3      S31:   0.2996 S32:   0.1438 S33:   0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     2        S   239                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6017 208.8297 113.8660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4530 T22:   0.4160                                     
REMARK   3      T33:   0.0499 T12:  -0.1445                                     
REMARK   3      T13:  -0.0288 T23:   0.0419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4697 L22:   1.1218                                     
REMARK   3      L33:   2.0800 L12:  -0.2013                                     
REMARK   3      L13:  -0.1027 L23:  -0.0595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0675 S12:  -0.3581 S13:  -0.1411                       
REMARK   3      S21:   0.3068 S22:  -0.0236 S23:  -0.1922                       
REMARK   3      S31:  -0.0814 S32:   0.5751 S33:   0.0911                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     5        T   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1779 236.6674 111.7070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9524 T22:   0.3210                                     
REMARK   3      T33:   0.0727 T12:  -0.1729                                     
REMARK   3      T13:  -0.0021 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0714 L22:   2.1492                                     
REMARK   3      L33:   0.5862 L12:   0.7768                                     
REMARK   3      L13:  -0.3858 L23:   0.2283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1648 S12:  -0.4641 S13:   0.1503                       
REMARK   3      S21:   0.1952 S22:  -0.0974 S23:  -0.3044                       
REMARK   3      S31:  -0.5603 S32:   0.3162 S33:  -0.0674                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     2        U   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6438 244.0769 107.4817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9974 T22:   0.3784                                     
REMARK   3      T33:   0.2125 T12:   0.2487                                     
REMARK   3      T13:   0.1555 T23:  -0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9092 L22:   1.6572                                     
REMARK   3      L33:   1.0127 L12:   0.4795                                     
REMARK   3      L13:  -0.1834 L23:  -0.2538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0093 S12:  -0.2441 S13:   0.5296                       
REMARK   3      S21:   0.3265 S22:   0.0361 S23:   0.1383                       
REMARK   3      S31:  -0.7009 S32:  -0.1299 S33:  -0.0268                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V     1        V   220                          
REMARK   3    RESIDUE RANGE :   f     1        f     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6347 229.6817  65.1496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3635 T22:   0.4672                                     
REMARK   3      T33:   0.1318 T12:   0.2472                                     
REMARK   3      T13:   0.1659 T23:   0.1269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0493 L22:   1.4838                                     
REMARK   3      L33:   0.9539 L12:   0.6923                                     
REMARK   3      L13:   0.1335 L23:  -0.1490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0020 S12:  -0.0771 S13:  -0.0180                       
REMARK   3      S21:   0.1924 S22:   0.1305 S23:   0.2914                       
REMARK   3      S31:  -0.3165 S32:  -0.5880 S33:  -0.1284                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2296 202.4531  65.1724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1154 T22:   0.6439                                     
REMARK   3      T33:   0.2108 T12:   0.0273                                     
REMARK   3      T13:   0.0955 T23:   0.2546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4350 L22:   0.9801                                     
REMARK   3      L33:   2.6955 L12:   0.0057                                     
REMARK   3      L13:   0.5471 L23:   0.4777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0133 S12:  -0.0101 S13:   0.0855                       
REMARK   3      S21:   0.1104 S22:   0.1613 S23:   0.2899                       
REMARK   3      S31:  -0.1496 S32:  -0.7983 S33:  -0.1480                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2566 175.9988  68.5067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2650 T22:   0.2726                                     
REMARK   3      T33:   0.1043 T12:  -0.1372                                     
REMARK   3      T13:  -0.0042 T23:   0.1337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2066 L22:   1.1261                                     
REMARK   3      L33:   2.2192 L12:  -0.1173                                     
REMARK   3      L13:  -0.1870 L23:   0.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:  -0.0995 S13:  -0.1428                       
REMARK   3      S21:   0.0465 S22:   0.1236 S23:   0.0008                       
REMARK   3      S31:   0.4395 S32:  -0.2892 S33:  -0.0824                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     1        Y   201                          
REMARK   3    RESIDUE RANGE :   g     1        g     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7160 172.2722  72.6770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2333 T22:   0.1505                                     
REMARK   3      T33:   0.0350 T12:   0.0440                                     
REMARK   3      T13:   0.0270 T23:   0.0678                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5939 L22:   1.5554                                     
REMARK   3      L33:   2.8567 L12:   0.4800                                     
REMARK   3      L13:  -0.7873 L23:   0.1526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0875 S12:  -0.1883 S13:  -0.1010                       
REMARK   3      S21:   0.0757 S22:  -0.0549 S23:  -0.0587                       
REMARK   3      S31:   0.5293 S32:   0.1226 S33:   0.1424                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     1        Z   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.3256 194.7534  73.8627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0935 T22:   0.3510                                     
REMARK   3      T33:   0.0614 T12:  -0.0043                                     
REMARK   3      T13:   0.0019 T23:   0.1138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9119 L22:   1.4029                                     
REMARK   3      L33:   2.0913 L12:   0.1598                                     
REMARK   3      L13:  -0.4400 L23:  -0.1349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0082 S12:  -0.1228 S13:  -0.0257                       
REMARK   3      S21:   0.1609 S22:  -0.1776 S23:  -0.2075                       
REMARK   3      S31:   0.0789 S32:   0.5722 S33:   0.1859                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   a     1        a   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6327 227.4608  70.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3523 T22:   0.2197                                     
REMARK   3      T33:   0.0335 T12:  -0.1608                                     
REMARK   3      T13:  -0.0301 T23:   0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3792 L22:   1.1796                                     
REMARK   3      L33:   2.1984 L12:  -0.0709                                     
REMARK   3      L13:  -0.2217 L23:  -0.6004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0228 S12:  -0.1171 S13:   0.0981                       
REMARK   3      S21:   0.2031 S22:  -0.1143 S23:  -0.1777                       
REMARK   3      S31:  -0.4998 S32:   0.3945 S33:   0.0916                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   b     1        b   203                          
REMARK   3    RESIDUE RANGE :   h     1        h     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8775 244.5273  67.9061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6302 T22:   0.0963                                     
REMARK   3      T33:   0.0189 T12:   0.0507                                     
REMARK   3      T13:   0.0632 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0388 L22:   1.4285                                     
REMARK   3      L33:   2.2755 L12:  -0.0612                                     
REMARK   3      L13:   0.2779 L23:  -0.1597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0126 S12:  -0.0336 S13:   0.1175                       
REMARK   3      S21:   0.2927 S22:   0.0102 S23:   0.0615                       
REMARK   3      S31:  -0.6888 S32:   0.0047 S33:  -0.0228                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5LF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000621.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : CRL TRANSFOCATOR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 262073                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 170.230                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.830                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 5LE5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.2 M MAGNESIUM          
REMARK 280  CHLORIDE, 10 % PEG3350, PH 6.5, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       56.53500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      157.39500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      157.39500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.53500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.18500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 34-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 34-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 134310 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 207690 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1198.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,         
REMARK 350                    AND CHAINS: d, e, f, g, h                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     LYS B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     LYS B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     GLN B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C   239                                                      
REMARK 465     GLU C   240                                                      
REMARK 465     LYS C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     GLN C   244                                                      
REMARK 465     LYS C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     ALA C   247                                                      
REMARK 465     SER C   248                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PHE D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PHE E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     GLU E   238                                                      
REMARK 465     ARG E   239                                                      
REMARK 465     PRO E   240                                                      
REMARK 465     GLN E   241                                                      
REMARK 465     ARG E   242                                                      
REMARK 465     LYS E   243                                                      
REMARK 465     ALA E   244                                                      
REMARK 465     GLN E   245                                                      
REMARK 465     PRO E   246                                                      
REMARK 465     ALA E   247                                                      
REMARK 465     GLN E   248                                                      
REMARK 465     PRO E   249                                                      
REMARK 465     ALA E   250                                                      
REMARK 465     ASP E   251                                                      
REMARK 465     GLU E   252                                                      
REMARK 465     PRO E   253                                                      
REMARK 465     ALA E   254                                                      
REMARK 465     GLU E   255                                                      
REMARK 465     LYS E   256                                                      
REMARK 465     ALA E   257                                                      
REMARK 465     ASP E   258                                                      
REMARK 465     GLU E   259                                                      
REMARK 465     PRO E   260                                                      
REMARK 465     MET E   261                                                      
REMARK 465     GLU E   262                                                      
REMARK 465     HIS E   263                                                      
REMARK 465     MET F     0                                                      
REMARK 465     SER F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ILE F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F   245                                                      
REMARK 465     GLU F   246                                                      
REMARK 465     ASP F   247                                                      
REMARK 465     GLU F   248                                                      
REMARK 465     SER F   249                                                      
REMARK 465     ASP F   250                                                      
REMARK 465     ASP F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     ASN F   253                                                      
REMARK 465     MET F   254                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ASP G   246                                                      
REMARK 465     ILE H   221                                                      
REMARK 465     GLU H   222                                                      
REMARK 465     VAL H   223                                                      
REMARK 465     LEU H   224                                                      
REMARK 465     GLU H   225                                                      
REMARK 465     GLU H   226                                                      
REMARK 465     THR H   227                                                      
REMARK 465     VAL H   228                                                      
REMARK 465     GLN H   229                                                      
REMARK 465     THR H   230                                                      
REMARK 465     MET H   231                                                      
REMARK 465     ASP H   232                                                      
REMARK 465     THR H   233                                                      
REMARK 465     SER H   234                                                      
REMARK 465     MET I     0                                                      
REMARK 465     PRO J   197                                                      
REMARK 465     LYS J   198                                                      
REMARK 465     GLN J   199                                                      
REMARK 465     GLY J   200                                                      
REMARK 465     SER J   201                                                      
REMARK 465     GLY K   201                                                      
REMARK 465     SER K   202                                                      
REMARK 465     THR K   203                                                      
REMARK 465     PRO K   204                                                      
REMARK 465     GLY M   217                                                      
REMARK 465     PHE M   218                                                      
REMARK 465     GLU M   219                                                      
REMARK 465     PRO N   203                                                      
REMARK 465     PRO N   204                                                      
REMARK 465     ALA N   205                                                      
REMARK 465     MET O     0                                                      
REMARK 465     ALA O     1                                                      
REMARK 465     GLU O     2                                                      
REMARK 465     ALA O   233                                                      
REMARK 465     MET P     1                                                      
REMARK 465     GLU P   250                                                      
REMARK 465     LYS P   251                                                      
REMARK 465     LYS P   252                                                      
REMARK 465     GLU P   253                                                      
REMARK 465     LYS P   254                                                      
REMARK 465     GLU P   255                                                      
REMARK 465     GLN P   256                                                      
REMARK 465     LYS P   257                                                      
REMARK 465     GLU P   258                                                      
REMARK 465     LYS P   259                                                      
REMARK 465     ASP P   260                                                      
REMARK 465     LYS P   261                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     LYS Q   241                                                      
REMARK 465     LYS Q   242                                                      
REMARK 465     LYS Q   243                                                      
REMARK 465     GLN Q   244                                                      
REMARK 465     LYS Q   245                                                      
REMARK 465     LYS Q   246                                                      
REMARK 465     ALA Q   247                                                      
REMARK 465     SER Q   248                                                      
REMARK 465     MET R     1                                                      
REMARK 465     PHE R     2                                                      
REMARK 465     LEU R     3                                                      
REMARK 465     THR R     4                                                      
REMARK 465     ARG R     5                                                      
REMARK 465     SER R     6                                                      
REMARK 465     GLU R     7                                                      
REMARK 465     TYR R     8                                                      
REMARK 465     MET S     1                                                      
REMARK 465     PRO S   240                                                      
REMARK 465     GLN S   241                                                      
REMARK 465     ARG S   242                                                      
REMARK 465     LYS S   243                                                      
REMARK 465     ALA S   244                                                      
REMARK 465     GLN S   245                                                      
REMARK 465     PRO S   246                                                      
REMARK 465     ALA S   247                                                      
REMARK 465     GLN S   248                                                      
REMARK 465     PRO S   249                                                      
REMARK 465     ALA S   250                                                      
REMARK 465     ASP S   251                                                      
REMARK 465     GLU S   252                                                      
REMARK 465     PRO S   253                                                      
REMARK 465     ALA S   254                                                      
REMARK 465     GLU S   255                                                      
REMARK 465     LYS S   256                                                      
REMARK 465     ALA S   257                                                      
REMARK 465     ASP S   258                                                      
REMARK 465     GLU S   259                                                      
REMARK 465     PRO S   260                                                      
REMARK 465     MET S   261                                                      
REMARK 465     GLU S   262                                                      
REMARK 465     HIS S   263                                                      
REMARK 465     MET T     0                                                      
REMARK 465     SER T     1                                                      
REMARK 465     SER T     2                                                      
REMARK 465     ILE T     3                                                      
REMARK 465     GLY T     4                                                      
REMARK 465     GLU T   245                                                      
REMARK 465     GLU T   246                                                      
REMARK 465     ASP T   247                                                      
REMARK 465     GLU T   248                                                      
REMARK 465     SER T   249                                                      
REMARK 465     ASP T   250                                                      
REMARK 465     ASP T   251                                                      
REMARK 465     ASP T   252                                                      
REMARK 465     ASN T   253                                                      
REMARK 465     MET T   254                                                      
REMARK 465     MET U     1                                                      
REMARK 465     PHE U   187                                                      
REMARK 465     ASP U   188                                                      
REMARK 465     TRP U   189                                                      
REMARK 465     THR U   190                                                      
REMARK 465     PHE U   191                                                      
REMARK 465     GLU U   192                                                      
REMARK 465     ASP U   246                                                      
REMARK 465     ILE V   221                                                      
REMARK 465     GLU V   222                                                      
REMARK 465     VAL V   223                                                      
REMARK 465     LEU V   224                                                      
REMARK 465     GLU V   225                                                      
REMARK 465     GLU V   226                                                      
REMARK 465     THR V   227                                                      
REMARK 465     VAL V   228                                                      
REMARK 465     GLN V   229                                                      
REMARK 465     THR V   230                                                      
REMARK 465     MET V   231                                                      
REMARK 465     ASP V   232                                                      
REMARK 465     THR V   233                                                      
REMARK 465     SER V   234                                                      
REMARK 465     MET W     0                                                      
REMARK 465     PRO X   197                                                      
REMARK 465     LYS X   198                                                      
REMARK 465     GLN X   199                                                      
REMARK 465     GLY X   200                                                      
REMARK 465     SER X   201                                                      
REMARK 465     SER Y   202                                                      
REMARK 465     THR Y   203                                                      
REMARK 465     PRO Y   204                                                      
REMARK 465     GLY a   217                                                      
REMARK 465     PHE a   218                                                      
REMARK 465     GLU a   219                                                      
REMARK 465     PRO b   204                                                      
REMARK 465     ALA b   205                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     ARG A  59    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 140    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  15    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     GLU B 181    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 183    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 199    CG   CD   CE   NZ                                   
REMARK 470     ASP B 202    CG   OD1  OD2                                       
REMARK 470     VAL B 203    CG1  CG2                                            
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 470     GLU B 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  47    CG   CD   CE   NZ                                   
REMARK 470     LYS C  48    CG   CD   CE   NZ                                   
REMARK 470     SER C  49    OG                                                  
REMARK 470     VAL C  50    CG1  CG2                                            
REMARK 470     LYS C  52    CG   CD   CE   NZ                                   
REMARK 470     PHE C 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 166    CG   CD   CE   NZ                                   
REMARK 470     GLU C 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 174    CG   CD   CE   NZ                                   
REMARK 470     LYS C 189    CG   CD   CE   NZ                                   
REMARK 470     LYS C 193    CG   CD   CE   NZ                                   
REMARK 470     LEU C 196    CG   CD1  CD2                                       
REMARK 470     VAL C 199    CG1  CG2                                            
REMARK 470     GLN C 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 204    CG   CD   CE   NZ                                   
REMARK 470     ILE C 206    CG1  CG2  CD1                                       
REMARK 470     GLU C 207    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 215    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 218    CG   CD   CE   NZ                                   
REMARK 470     GLU C 223    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 224    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 232    CG1  CG2  CD1                                       
REMARK 470     ASP D 129    CG   OD1  OD2                                       
REMARK 470     LYS D 149    CG   CD   CE   NZ                                   
REMARK 470     SER D 172    OG                                                  
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     LYS D 192    CG   CD   CE   NZ                                   
REMARK 470     LYS D 196    CG   CD   CE   NZ                                   
REMARK 470     LYS D 209    CG   CD   CE   NZ                                   
REMARK 470     LYS E  41    CG   CD   CE   NZ                                   
REMARK 470     ARG E  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E  53    CG   CD   OE1  NE2                                  
REMARK 470     SER E  54    OG                                                  
REMARK 470     GLU E  55    CG   CD   OE1  OE2                                  
REMARK 470     HIS E  59    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E 208    CG   CD   CE   NZ                                   
REMARK 470     GLU E 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU F  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 205    CG   CD   CE   NZ                                   
REMARK 470     LYS G  45    CG   CD   CE   NZ                                   
REMARK 470     GLU G 145    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 146    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 181    CG   CD   CE   NZ                                   
REMARK 470     GLU G 196    CG   CD   OE1  OE2                                  
REMARK 470     LYS H   9    CG   CD   CE   NZ                                   
REMARK 470     LYS H 180    CG   CD   CE   NZ                                   
REMARK 470     ASN J  24    CG   OD1  ND2                                       
REMARK 470     GLU J 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 154    CG   CD   OE1  OE2                                  
REMARK 470     ARG K   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 106    CG   CD   CE   NZ                                   
REMARK 470     ARG L   1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 162    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 173    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 200    CG   CD   CE   NZ                                   
REMARK 470     ARG O   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O  17    CG   CD   CE   NZ                                   
REMARK 470     LYS O  50    CG   CD   CE   NZ                                   
REMARK 470     GLN O  51    CG   CD   OE1  NE2                                  
REMARK 470     LYS O  52    CG   CD   CE   NZ                                   
REMARK 470     ILE O  54    CG1  CG2  CD1                                       
REMARK 470     LYS O  69    CG   CD   CE   NZ                                   
REMARK 470     LYS O 164    CG   CD   CE   NZ                                   
REMARK 470     GLU O 174    CG   CD   OE1  OE2                                  
REMARK 470     LYS O 175    CG   CD   CE   NZ                                   
REMARK 470     TYR O 177    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU O 179    CG   CD   OE1  OE2                                  
REMARK 470     HIS O 188    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU P  15    CG   CD   OE1  OE2                                  
REMARK 470     ASN P  51    CG   OD1  ND2                                       
REMARK 470     ILE P  52    CG1  CG2  CD1                                       
REMARK 470     LYS P 199    CG   CD   CE   NZ                                   
REMARK 470     LYS P 205    CG   CD   CE   NZ                                   
REMARK 470     GLU P 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 210    CG   CD   CE   NZ                                   
REMARK 470     ARG P 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS P 229    CG   CD   CE   NZ                                   
REMARK 470     LYS P 231    CG   CD   CE   NZ                                   
REMARK 470     GLU P 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 238    CG   CD   CE   NZ                                   
REMARK 470     LYS P 239    CG   CD   CE   NZ                                   
REMARK 470     ARG Q  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Q  47    CG   CD   CE   NZ                                   
REMARK 470     LYS Q  48    CG   CD   CE   NZ                                   
REMARK 470     SER Q  49    OG                                                  
REMARK 470     VAL Q  50    CG1  CG2                                            
REMARK 470     LYS Q  52    CG   CD   CE   NZ                                   
REMARK 470     LYS Q  61    CG   CD   CE   NZ                                   
REMARK 470     PHE Q 138    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS Q 166    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 174    CG   CD   CE   NZ                                   
REMARK 470     GLU Q 182    CG   CD   OE1  OE2                                  
REMARK 470     LYS Q 189    CG   CD   CE   NZ                                   
REMARK 470     LYS Q 193    CG   CD   CE   NZ                                   
REMARK 470     GLN Q 200    CG   CD   OE1  NE2                                  
REMARK 470     LYS Q 204    CG   CD   CE   NZ                                   
REMARK 470     GLU Q 207    CG   CD   OE1  OE2                                  
REMARK 470     GLN Q 215    CG   CD   OE1  NE2                                  
REMARK 470     LYS Q 218    CG   CD   CE   NZ                                   
REMARK 470     GLU R 126    CG   CD   OE1  OE2                                  
REMARK 470     ASP R 127    CG   OD1  OD2                                       
REMARK 470     ASP R 129    CG   OD1  OD2                                       
REMARK 470     LYS R 149    CG   CD   CE   NZ                                   
REMARK 470     GLU R 175    CG   CD   OE1  OE2                                  
REMARK 470     GLU R 207    CG   CD   OE1  OE2                                  
REMARK 470     GLU R 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS R 231    CG   CD   CE   NZ                                   
REMARK 470     LYS S  41    CG   CD   CE   NZ                                   
REMARK 470     GLN S  53    CG   CD   OE1  NE2                                  
REMARK 470     LYS S 189    CG   CD   CE   NZ                                   
REMARK 470     LYS S 217    CG   CD   CE   NZ                                   
REMARK 470     ASP S 218    CG   OD1  OD2                                       
REMARK 470     LEU S 236    CG   CD1  CD2                                       
REMARK 470     GLU S 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU S 238    CG   CD   OE1  OE2                                  
REMARK 470     ARG S 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR T   5    OG1  CG2                                            
REMARK 470     LYS T  42    CG   CD   CE   NZ                                   
REMARK 470     LYS T  56    CG   CD   CE   NZ                                   
REMARK 470     GLU T  60    CG   CD   OE1  OE2                                  
REMARK 470     ARG T 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU T 234    CG   CD   OE1  OE2                                  
REMARK 470     LYS T 244    CG   CD   CE   NZ                                   
REMARK 470     ARG U   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS U  55    CG   CD   CE   NZ                                   
REMARK 470     LYS U  59    CG   CD   CE   NZ                                   
REMARK 470     GLU U 145    CG   CD   OE1  OE2                                  
REMARK 470     GLU U 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN U 147    CG   CD   OE1  NE2                                  
REMARK 470     VAL U 170    CG1  CG2                                            
REMARK 470     LYS U 171    CG   CD   CE   NZ                                   
REMARK 470     LYS U 181    CG   CD   CE   NZ                                   
REMARK 470     LYS U 184    CG   CD   CE   NZ                                   
REMARK 470     LYS U 186    CG   CD   CE   NZ                                   
REMARK 470     GLN U 193    CG   CD   OE1  NE2                                  
REMARK 470     ASP U 209    CG   OD1  OD2                                       
REMARK 470     LYS U 226    CG   CD   CE   NZ                                   
REMARK 470     LYS V 180    CG   CD   CE   NZ                                   
REMARK 470     LYS V 182    CG   CD   CE   NZ                                   
REMARK 470     LYS V 194    CG   CD   CE   NZ                                   
REMARK 470     LYS V 195    CG   CD   CE   NZ                                   
REMARK 470     ARG V 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG V 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG V 203    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS V 204    SG                                                  
REMARK 470     GLU V 205    CG   CD   OE1  OE2                                  
REMARK 470     LYS V 206    CG   CD   CE   NZ                                   
REMARK 470     GLU V 220    CG   CD   OE1  OE2                                  
REMARK 470     HIS W 161    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS W 191    CG   CD   CE   NZ                                   
REMARK 470     GLU X 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU X 111    CG   CD   OE1  OE2                                  
REMARK 470     ARG X 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP X 192    OD1  OD2                                            
REMARK 470     ASN X 193    OD1  ND2                                            
REMARK 470     ARG Z   1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN Z 160    CG   OD1  ND2                                       
REMARK 470     VAL Z 161    CG1  CG2                                            
REMARK 470     GLU Z 162    CG   CD   OE1  OE2                                  
REMARK 470     LYS a 156    CG   CD   CE   NZ                                   
REMARK 470     GLU a 206    CG   CD   OE1  OE2                                  
REMARK 470     VAL b 199    CG1  CG2                                            
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   O    HOH S   467     O    HOH S   497              2.14            
REMARK 500   ND2  ASN F   105     O    HOH F   401              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU W  77   CD    GLU W  77   OE2     0.109                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B   4   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    GLU D 175   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    ASN I  17   C   -  N   -  CA  ANGL. DEV. =  22.2 DEGREES          
REMARK 500    ASN I  17   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ARG I  25   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG I  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LEU O 181   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    LEU R 121   C   -  N   -  CA  ANGL. DEV. =  25.7 DEGREES          
REMARK 500    GLY T   6   N   -  CA  -  C   ANGL. DEV. =  22.4 DEGREES          
REMARK 500    ARG U  11   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASN W  17   C   -  N   -  CA  ANGL. DEV. =  23.4 DEGREES          
REMARK 500    ARG W  25   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG W  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG Y 158   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG Y 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  50       49.53    -69.24                                   
REMARK 500    LYS A  52     -121.46    -68.54                                   
REMARK 500    SER A  53      132.00    -12.65                                   
REMARK 500    GLN A 122      -33.71   -140.83                                   
REMARK 500    ARG A 176      -20.24   -163.70                                   
REMARK 500    PHE A 198      -81.80    -82.61                                   
REMARK 500    GLU A 199      106.89     69.51                                   
REMARK 500    GLN A 201      125.75     75.84                                   
REMARK 500    ARG B   8       64.89     60.07                                   
REMARK 500    ASN B  51       80.38    -63.86                                   
REMARK 500    GLU B  58       90.50     67.36                                   
REMARK 500    ASN B  69     -165.24   -161.41                                   
REMARK 500    MET B 201       66.33   -104.61                                   
REMARK 500    VAL B 203       66.49   -154.94                                   
REMARK 500    SER B 204      -99.30   -140.87                                   
REMARK 500    LYS C  47      -97.58     13.15                                   
REMARK 500    VAL C  50     -128.15     65.66                                   
REMARK 500    ALA C  51      115.90     85.93                                   
REMARK 500    GLN C 200      -78.03    -37.12                                   
REMARK 500    SER C 201       77.15   -102.50                                   
REMARK 500    LYS C 204     -112.03     72.52                                   
REMARK 500    ASN C 205       59.02   -103.03                                   
REMARK 500    ASP C 214      -31.53     75.37                                   
REMARK 500    SER C 216      165.56     69.80                                   
REMARK 500    LYS C 236       43.72    -96.42                                   
REMARK 500    ARG D  53       73.82     70.87                                   
REMARK 500    GLU D 126        8.02   -161.98                                   
REMARK 500    ALA D 128     -158.49   -107.45                                   
REMARK 500    GLU D 175      -81.16    -54.28                                   
REMARK 500    PHE D 226      128.11    -35.96                                   
REMARK 500    SER E  40     -166.65   -114.35                                   
REMARK 500    HIS E  59      121.80    119.26                                   
REMARK 500    ALA E 151       -0.13     81.93                                   
REMARK 500    ASP E 226     -124.67     54.82                                   
REMARK 500    LYS F 207      -70.07    -72.58                                   
REMARK 500    ARG G   3       80.92     69.58                                   
REMARK 500    VAL G  56       73.95   -119.31                                   
REMARK 500    TRP G 189       49.08     33.50                                   
REMARK 500    GLU G 192      -43.84   -133.39                                   
REMARK 500    ASP G 209       88.97     64.79                                   
REMARK 500    GLU G 244       61.89   -100.82                                   
REMARK 500    SER H 171     -130.82     63.19                                   
REMARK 500    GLN I  30     -123.40     53.81                                   
REMARK 500    LYS I  97       33.37    -96.32                                   
REMARK 500    ASP I 134      -64.39   -127.82                                   
REMARK 500    CYS I 141       46.36   -108.99                                   
REMARK 500    ASN J  24     -117.15     68.21                                   
REMARK 500    ALA J 122       27.59     83.93                                   
REMARK 500    LEU J 175       78.59   -109.98                                   
REMARK 500    PRO K  39       -9.82    -59.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     124 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU C  237     GLU C  238                  145.15                    
REMARK 500 GLU D  175     GLY D  176                 -144.06                    
REMARK 500 GLU D  175     GLY D  176                  140.70                    
REMARK 500 GLY I   78     ARG I   79                 -139.45                    
REMARK 500 MET J    1     GLU J    2                 -149.01                    
REMARK 500 MET J    1     GLU J    2                 -149.05                    
REMARK 500 HIS P   53     LYS P   54                  148.82                    
REMARK 500 LYS P   54     LEU P   55                  149.86                    
REMARK 500 GLU P  244     ALA P  245                 -143.60                    
REMARK 500 ALA P  245     LYS P  246                   56.23                    
REMARK 500 LYS Q   47     LYS Q   48                 -145.10                    
REMARK 500 SER Q   49     VAL Q   50                 -147.53                    
REMARK 500 PRO R  130     GLY R  131                  138.83                    
REMARK 500 GLY W   78     ARG W   79                 -139.33                    
REMARK 500 MET X    1     GLU X    2                 -148.31                    
REMARK 500 TYR Y  199     SER Y  200                  -35.36                    
REMARK 500 ILE a  215     SER a  216                 -128.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 500        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH G 572        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH I 542        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH J 519        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH M 541        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH O 471        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH R 509        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH X 509        DISTANCE =  6.12 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G 303   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  14   OG1                                                    
REMARK 620 2 TYR G 125   O    92.1                                              
REMARK 620 3 ASN G 128   O    83.5  95.9                                        
REMARK 620 4 MET G 131   O   160.4 106.7  99.6                                  
REMARK 620 5 HOH G 450   O    71.6 154.8 100.9  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H  91   OE1                                                    
REMARK 620 2 HOH N 410   O    77.8                                              
REMARK 620 3 HOH H 515   O    94.0 166.3                                        
REMARK 620 4 HOH N 492   O    79.2  93.2  96.0                                  
REMARK 620 5 HOH N 411   O   165.5  94.7  95.5  89.0                            
REMARK 620 6 HOH N 470   O   103.7  86.9  84.3 177.1  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE H 163   O                                                      
REMARK 620 2 ASP H 166   O   104.2                                              
REMARK 620 3 SER H 169   O    91.4  85.8                                        
REMARK 620 4 ASP Z 213   O   110.0 145.5  98.3                                  
REMARK 620 5 HOH H 478   O    89.0  93.7 179.4  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL I 174   O                                                      
REMARK 620 2 ASP I 177   O    83.4                                              
REMARK 620 3 SER I 180   O    97.8  87.2                                        
REMARK 620 4 HOH I 414   O    81.9 164.2 100.3                                  
REMARK 620 5 HOH I 477   O   152.6  84.1 105.8 106.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 304  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 204   O                                                      
REMARK 620 2 THR Y 164   O   109.6                                              
REMARK 620 3 ASP Y 167   O   148.6  99.9                                        
REMARK 620 4 SER Y 170   O    93.7 100.9  90.8                                  
REMARK 620 5 HOH Y 442   O    86.8  76.9  89.9 177.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR K 164   O                                                      
REMARK 620 2 ASP K 167   O   106.2                                              
REMARK 620 3 SER K 170   O    98.0  92.4                                        
REMARK 620 4 ASP W 204   O   105.9 147.1  90.2                                  
REMARK 620 5 HOH K 466   O    84.7 101.7 164.4  74.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K L 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA L 183   O                                                      
REMARK 620 2 ASP L 186   O    89.5                                              
REMARK 620 3 THR L 189   O    93.4  76.9                                        
REMARK 620 4 HOH L 421   O    92.1 166.5  89.7                                  
REMARK 620 5 HOH L 433   O   142.8  94.8 123.6  92.1                            
REMARK 620 6 HOH L 444   O    55.5 120.9 140.7  70.4  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 213   O                                                      
REMARK 620 2 ILE V 163   O   106.6                                              
REMARK 620 3 ASP V 166   O   153.8  98.7                                        
REMARK 620 4 SER V 169   O   101.8  87.8  85.4                                  
REMARK 620 5 HOH V 466   O    80.6  87.9  94.0 175.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K N 306   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET N 164   O                                                      
REMARK 620 2 ASP N 167   O    81.9                                              
REMARK 620 3 SER N 170   O    97.0  67.9                                        
REMARK 620 4 HOH N 530   O    87.6 162.1  99.3                                  
REMARK 620 5 HOH N 454   O    88.6  81.1 147.2 113.2                            
REMARK 620 6 HOH N 490   O   146.7 125.6 110.1  69.7  79.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K U 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR U  14   OG1                                                    
REMARK 620 2 TYR U 125   O    89.5                                              
REMARK 620 3 ASN U 128   O    81.5  96.3                                        
REMARK 620 4 MET U 131   O   158.8 110.1 103.6                                  
REMARK 620 5 HOH U 423   O    69.8 150.1 101.4  89.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN V  91   OE1                                                    
REMARK 620 2 HOH V 446   O    76.5                                              
REMARK 620 3 HOH V 458   O    73.4  89.1                                        
REMARK 620 4 HOH b 405   O    70.7 106.2 136.0                                  
REMARK 620 5 HOH b 478   O   151.4  84.3 128.0  95.0                            
REMARK 620 6 HOH b 445   O    88.0 164.1  83.3  71.0 111.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG W 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL W 174   O                                                      
REMARK 620 2 ASP W 177   O    86.5                                              
REMARK 620 3 SER W 180   O   100.5  89.0                                        
REMARK 620 4 HOH W 440   O   158.1  91.1 101.3                                  
REMARK 620 5 HOH W 459   O    88.0 172.4  97.2  91.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K Z 302   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA Z 183   O                                                      
REMARK 620 2 ASP Z 186   O    92.5                                              
REMARK 620 3 THR Z 189   O    92.5  78.9                                        
REMARK 620 4 HOH Z 464   O   142.6  98.4 124.7                                  
REMARK 620 5 HOH Z 434   O    91.8 157.0  78.4  91.7                            
REMARK 620 6 HOH Z 456   O    60.0 127.8 139.0  85.6  73.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K b 306   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET b 164   O                                                      
REMARK 620 2 ASP b 167   O    76.8                                              
REMARK 620 3 SER b 170   O    89.9  62.7                                        
REMARK 620 4 HOH b 410   O   165.7 113.4 103.6                                  
REMARK 620 5 HOH b 459   O    91.6  78.4 139.5  81.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH J 406   O                                                      
REMARK 620 2 HOH J 453   O    91.5                                              
REMARK 620 3 HOH J 495   O    88.8  97.4                                        
REMARK 620 4 HOH J 516   O    84.9 168.1  93.8                                  
REMARK 620 5 HOH K 483   O   172.0  87.8  99.2  94.3                            
REMARK 620 6 HOH J 445   O    80.0  90.6 166.4  77.7  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH X 402   O                                                      
REMARK 620 2 HOH X 432   O    75.3                                              
REMARK 620 3 HOH X 505   O    81.7  87.0                                        
REMARK 620 4 HOH Y 508   O   174.6 106.4  93.2                                  
REMARK 620 5 HOH X 441   O    89.9  97.3 169.4  94.9                            
REMARK 620 6 HOH X 480   O    80.1 152.5  77.5  97.1  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K G 303                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE H 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL I 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE K 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE N 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K N 306                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL O 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL P 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Q 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL R 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL S 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K U 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL V 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL W 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE W 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL Y 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE Z 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K Z 302                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE a 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE b 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K b 306                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL c 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL f 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6V1 E 148         
REMARK 800  through PRO E 149 bound to THR E 147                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO c 5 bound to THR H 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO c 5 bound to THR H 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO d 5 bound to THR K 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO d 5 bound to THR K 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO e 5 bound to THR N 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO e 5 bound to THR N 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6V1 S 148         
REMARK 800  through PRO S 149 bound to THR S 147                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO f 5 bound to THR V 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO f 5 bound to THR V 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO g 5 bound to THR Y 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO g 5 bound to THR Y 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO h 5 bound to THR b 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO h 5 bound to THR b 1   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO c 5 bound to THR c 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO d 5 bound to THR d 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO e 5 bound to THR e 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO f 5 bound to THR f 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO g 5 bound to THR g 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VO h 5 bound to THR h 4   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP U 46 and 6V1 U     
REMARK 800  47                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6V1 U 47 and ALA U     
REMARK 800  48                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide TYR U 160 and 6V1 U    
REMARK 800  161                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6V1 U 161 and GLY U    
REMARK 800  162                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP X 90 and 6V1 X     
REMARK 800  91                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6V1 X 91 and LEU X     
REMARK 800  92                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE c 1 and IML c 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML c 2 and ILE c 3    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE d 1 and IML d 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML d 2 and ILE d 3    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE e 1 and IML e 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML e 2 and ILE e 3    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE f 1 and IML f 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML f 2 and ILE f 3    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE g 1 and IML g 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML g 2 and ILE g 3    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE h 1 and IML h 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IML h 2 and ILE h 3    
DBREF  5LF0 A    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LF0 B    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LF0 C    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LF0 D    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LF0 E    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LF0 F    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LF0 G    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LF0 H    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LF0 I    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LF0 J    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LF0 K    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LF0 L    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LF0 M    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LF0 N    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LF0 O    0   233  UNP    P25787   PSA2_HUMAN       1    234             
DBREF  5LF0 P    1   261  UNP    P25789   PSA4_HUMAN       1    261             
DBREF  5LF0 Q    1   248  UNP    O14818   PSA7_HUMAN       1    248             
DBREF  5LF0 R    1   241  UNP    P28066   PSA5_HUMAN       1    241             
DBREF  5LF0 S    1   263  UNP    P25786   PSA1_HUMAN       1    263             
DBREF  5LF0 T    0   254  UNP    P25788   PSA3_HUMAN       1    255             
DBREF  5LF0 U    1   246  UNP    P60900   PSA6_HUMAN       1    246             
DBREF  5LF0 V    1   234  UNP    Q99436   PSB7_HUMAN      44    277             
DBREF  5LF0 W    0   204  UNP    P49720   PSB3_HUMAN       1    205             
DBREF  5LF0 X    1   201  UNP    P49721   PSB2_HUMAN       1    201             
DBREF  5LF0 Y    1   204  UNP    P28074   PSB5_HUMAN      60    263             
DBREF  5LF0 Z    1   213  UNP    P20618   PSB1_HUMAN      29    241             
DBREF  5LF0 a    1   219  UNP    P28070   PSB4_HUMAN      46    264             
DBREF  5LF0 b    1   205  UNP    P28072   PSB6_HUMAN      35    239             
DBREF  5LF0 c    1     5  PDB    5LF0     5LF0             1      5             
DBREF  5LF0 d    1     5  PDB    5LF0     5LF0             1      5             
DBREF  5LF0 e    1     5  PDB    5LF0     5LF0             1      5             
DBREF  5LF0 f    1     5  PDB    5LF0     5LF0             1      5             
DBREF  5LF0 g    1     5  PDB    5LF0     5LF0             1      5             
DBREF  5LF0 h    1     5  PDB    5LF0     5LF0             1      5             
SEQADV 5LF0 6V1 E  148  UNP  P25786    CYS   148 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 G   47  UNP  P60900    CYS    47 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 G  161  UNP  P60900    CYS   161 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 J   91  UNP  P49721    CYS    91 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 S  148  UNP  P25786    CYS   148 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 U   47  UNP  P60900    CYS    47 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 U  161  UNP  P60900    CYS   161 MODIFIED RESIDUE               
SEQADV 5LF0 6V1 X   91  UNP  P49721    CYS    91 MODIFIED RESIDUE               
SEQRES   1 A  234  MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE          
SEQRES   2 A  234  SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU          
SEQRES   3 A  234  ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS          
SEQRES   4 A  234  ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN          
SEQRES   5 A  234  LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL          
SEQRES   6 A  234  GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY          
SEQRES   7 A  234  MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG          
SEQRES   8 A  234  LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO          
SEQRES   9 A  234  ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL          
SEQRES  10 A  234  MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 A  234  GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG          
SEQRES  12 A  234  PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE          
SEQRES  13 A  234  ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN          
SEQRES  14 A  234  GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU          
SEQRES  15 A  234  GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU          
SEQRES  16 A  234  LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE          
SEQRES  17 A  234  GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU          
SEQRES  18 A  234  THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA          
SEQRES   1 B  261  MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER          
SEQRES   2 B  261  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU          
SEQRES   3 B  261  ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA          
SEQRES   4 B  261  ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE          
SEQRES   5 B  261  HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE          
SEQRES   6 B  261  TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY          
SEQRES   7 B  261  ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG          
SEQRES   8 B  261  LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO          
SEQRES   9 B  261  ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE          
SEQRES  10 B  261  LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE          
SEQRES  11 B  261  GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR          
SEQRES  12 B  261  GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR          
SEQRES  13 B  261  GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA          
SEQRES  14 B  261  ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY          
SEQRES  15 B  261  GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS          
SEQRES  16 B  261  VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA          
SEQRES  17 B  261  GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY          
SEQRES  18 B  261  LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU          
SEQRES  19 B  261  GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA          
SEQRES  20 B  261  GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP          
SEQRES  21 B  261  LYS                                                          
SEQRES   1 C  248  MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP          
SEQRES   2 C  248  GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL          
SEQRES   3 C  248  LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP          
SEQRES   4 C  248  ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS          
SEQRES   5 C  248  LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU          
SEQRES   6 C  248  ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA          
SEQRES   7 C  248  ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS          
SEQRES   8 C  248  GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL          
SEQRES   9 C  248  GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG          
SEQRES  10 C  248  TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER          
SEQRES  11 C  248  ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG          
SEQRES  12 C  248  LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP          
SEQRES  13 C  248  LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG          
SEQRES  14 C  248  GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU          
SEQRES  15 C  248  THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU          
SEQRES  16 C  248  LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU          
SEQRES  17 C  248  ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN          
SEQRES  18 C  248  PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS          
SEQRES  19 C  248  GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA          
SEQRES  20 C  248  SER                                                          
SEQRES   1 D  241  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN          
SEQRES   2 D  241  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 D  241  ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 D  241  ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS          
SEQRES   5 D  241  ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU          
SEQRES   6 D  241  LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET          
SEQRES   7 D  241  SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS          
SEQRES   8 D  241  ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN          
SEQRES   9 D  241  GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER          
SEQRES  10 D  241  ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO          
SEQRES  11 D  241  GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE          
SEQRES  12 D  241  GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET          
SEQRES  13 D  241  ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA          
SEQRES  14 D  241  ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN          
SEQRES  15 D  241  GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE          
SEQRES  16 D  241  LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU          
SEQRES  17 D  241  LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN          
SEQRES  18 D  241  PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU          
SEQRES  19 D  241  GLU GLU VAL ILE LYS ASP ILE                                  
SEQRES   1 E  263  MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP          
SEQRES   2 E  263  SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET          
SEQRES   3 E  263  GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS          
SEQRES   4 E  263  SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA          
SEQRES   5 E  263  GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS          
SEQRES   6 E  263  VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR          
SEQRES   7 E  263  ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU          
SEQRES   8 E  263  CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO          
SEQRES   9 E  263  VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN          
SEQRES  10 E  263  ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL          
SEQRES  11 E  263  GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS          
SEQRES  12 E  263  ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS          
SEQRES  13 E  263  ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG          
SEQRES  14 E  263  THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS          
SEQRES  15 E  263  ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU          
SEQRES  16 E  263  ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS          
SEQRES  17 E  263  ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE          
SEQRES  18 E  263  THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU          
SEQRES  19 E  263  GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA          
SEQRES  20 E  263  GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO          
SEQRES  21 E  263  MET GLU HIS                                                  
SEQRES   1 F  255  MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER          
SEQRES   2 F  255  THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR          
SEQRES   3 F  255  ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY          
SEQRES   4 F  255  ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS          
SEQRES   5 F  255  LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS          
SEQRES   6 F  255  ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL          
SEQRES   7 F  255  ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE          
SEQRES   8 F  255  ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY          
SEQRES   9 F  255  TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA          
SEQRES  10 F  255  MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG          
SEQRES  11 F  255  PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL          
SEQRES  12 F  255  ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY          
SEQRES  13 F  255  VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA          
SEQRES  14 F  255  ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET          
SEQRES  15 F  255  LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA          
SEQRES  16 F  255  LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS          
SEQRES  17 F  255  ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR          
SEQRES  18 F  255  ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU          
SEQRES  19 F  255  GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU          
SEQRES  20 F  255  ASP GLU SER ASP ASP ASP ASN MET                              
SEQRES   1 G  246  MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE          
SEQRES   2 G  246  THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU          
SEQRES   3 G  246  TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER          
SEQRES   4 G  246  VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR          
SEQRES   5 G  246  GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR          
SEQRES   6 G  246  VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS          
SEQRES   7 G  246  VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL          
SEQRES   8 G  246  GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS          
SEQRES   9 G  246  TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG          
SEQRES  10 G  246  ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU          
SEQRES  11 G  246  MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE          
SEQRES  12 G  246  ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO          
SEQRES  13 G  246  ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY          
SEQRES  14 G  246  VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS          
SEQRES  15 G  246  VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL          
SEQRES  16 G  246  GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE          
SEQRES  17 G  246  ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR          
SEQRES  18 G  246  VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU          
SEQRES  19 G  246  ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP              
SEQRES   1 H  234  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 H  234  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 H  234  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 H  234  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 H  234  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 H  234  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 H  234  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 H  234  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 H  234  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 H  234  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 H  234  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 H  234  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 H  234  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 H  234  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 H  234  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 H  234  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 H  234  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE          
SEQRES  18 H  234  GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER          
SEQRES   1 I  205  MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA          
SEQRES   2 I  205  MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG          
SEQRES   3 I  205  ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE          
SEQRES   4 I  205  GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY          
SEQRES   5 I  205  LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN          
SEQRES   6 I  205  ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU          
SEQRES   7 I  205  GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL          
SEQRES   8 I  205  ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR          
SEQRES   9 I  205  THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE          
SEQRES  10 I  205  LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO          
SEQRES  11 I  205  MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA          
SEQRES  12 I  205  GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO          
SEQRES  13 I  205  ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN          
SEQRES  14 I  205  ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY          
SEQRES  15 I  205  MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE          
SEQRES  16 I  205  THR THR ARG THR LEU LYS ALA ARG MET ASP                      
SEQRES   1 J  201  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 J  201  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 J  201  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 J  201  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 J  201  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 J  201  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 J  201  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1          
SEQRES   8 J  201  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 J  201  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 J  201  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 J  201  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 J  201  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 J  201  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 J  201  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 J  201  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 J  201  PHE PRO LYS GLN GLY SER                                      
SEQRES   1 K  204  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 K  204  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 K  204  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 K  204  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 K  204  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 K  204  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 K  204  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 K  204  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 K  204  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 K  204  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 K  204  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 K  204  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 K  204  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 K  204  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 K  204  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 K  204  HIS GLU LYS TYR SER GLY SER THR PRO                          
SEQRES   1 L  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 L  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 L  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 L  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 L  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 L  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 L  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 L  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 L  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 L  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 L  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 L  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 L  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 L  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 L  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 L  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 L  213  SER LEU ARG LYS ASP                                          
SEQRES   1 M  219  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 M  219  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 M  219  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 M  219  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 M  219  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 M  219  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 M  219  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 M  219  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 M  219  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 M  219  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 M  219  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 M  219  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 M  219  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 M  219  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 M  219  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 M  219  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 M  219  TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU                  
SEQRES   1 N  205  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 N  205  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 N  205  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 N  205  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 N  205  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 N  205  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 N  205  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 N  205  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 N  205  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 N  205  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 N  205  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 N  205  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 N  205  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 N  205  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 N  205  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 N  205  LYS PHE ALA VAL ALA THR LEU PRO PRO ALA                      
SEQRES   1 O  234  MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE          
SEQRES   2 O  234  SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU          
SEQRES   3 O  234  ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS          
SEQRES   4 O  234  ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN          
SEQRES   5 O  234  LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL          
SEQRES   6 O  234  GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY          
SEQRES   7 O  234  MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG          
SEQRES   8 O  234  LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO          
SEQRES   9 O  234  ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL          
SEQRES  10 O  234  MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE          
SEQRES  11 O  234  GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG          
SEQRES  12 O  234  PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE          
SEQRES  13 O  234  ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN          
SEQRES  14 O  234  GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU          
SEQRES  15 O  234  GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU          
SEQRES  16 O  234  LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE          
SEQRES  17 O  234  GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU          
SEQRES  18 O  234  THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA          
SEQRES   1 P  261  MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER          
SEQRES   2 P  261  PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU          
SEQRES   3 P  261  ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA          
SEQRES   4 P  261  ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE          
SEQRES   5 P  261  HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE          
SEQRES   6 P  261  TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY          
SEQRES   7 P  261  ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG          
SEQRES   8 P  261  LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO          
SEQRES   9 P  261  ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE          
SEQRES  10 P  261  LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE          
SEQRES  11 P  261  GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR          
SEQRES  12 P  261  GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR          
SEQRES  13 P  261  GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA          
SEQRES  14 P  261  ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY          
SEQRES  15 P  261  GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS          
SEQRES  16 P  261  VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA          
SEQRES  17 P  261  GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY          
SEQRES  18 P  261  LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU          
SEQRES  19 P  261  GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA          
SEQRES  20 P  261  GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP          
SEQRES  21 P  261  LYS                                                          
SEQRES   1 Q  248  MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP          
SEQRES   2 Q  248  GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL          
SEQRES   3 Q  248  LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP          
SEQRES   4 Q  248  ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS          
SEQRES   5 Q  248  LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU          
SEQRES   6 Q  248  ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA          
SEQRES   7 Q  248  ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS          
SEQRES   8 Q  248  GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL          
SEQRES   9 Q  248  GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG          
SEQRES  10 Q  248  TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER          
SEQRES  11 Q  248  ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG          
SEQRES  12 Q  248  LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP          
SEQRES  13 Q  248  LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG          
SEQRES  14 Q  248  GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU          
SEQRES  15 Q  248  THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU          
SEQRES  16 Q  248  LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU          
SEQRES  17 Q  248  ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN          
SEQRES  18 Q  248  PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS          
SEQRES  19 Q  248  GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA          
SEQRES  20 Q  248  SER                                                          
SEQRES   1 R  241  MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN          
SEQRES   2 R  241  THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR          
SEQRES   3 R  241  ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY          
SEQRES   4 R  241  ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS          
SEQRES   5 R  241  ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU          
SEQRES   6 R  241  LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET          
SEQRES   7 R  241  SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS          
SEQRES   8 R  241  ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN          
SEQRES   9 R  241  GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER          
SEQRES  10 R  241  ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO          
SEQRES  11 R  241  GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE          
SEQRES  12 R  241  GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET          
SEQRES  13 R  241  ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA          
SEQRES  14 R  241  ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN          
SEQRES  15 R  241  GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE          
SEQRES  16 R  241  LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU          
SEQRES  17 R  241  LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN          
SEQRES  18 R  241  PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU          
SEQRES  19 R  241  GLU GLU VAL ILE LYS ASP ILE                                  
SEQRES   1 S  263  MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP          
SEQRES   2 S  263  SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET          
SEQRES   3 S  263  GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS          
SEQRES   4 S  263  SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA          
SEQRES   5 S  263  GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS          
SEQRES   6 S  263  VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR          
SEQRES   7 S  263  ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU          
SEQRES   8 S  263  CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO          
SEQRES   9 S  263  VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN          
SEQRES  10 S  263  ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL          
SEQRES  11 S  263  GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS          
SEQRES  12 S  263  ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS          
SEQRES  13 S  263  ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG          
SEQRES  14 S  263  THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS          
SEQRES  15 S  263  ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU          
SEQRES  16 S  263  ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS          
SEQRES  17 S  263  ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE          
SEQRES  18 S  263  THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU          
SEQRES  19 S  263  GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA          
SEQRES  20 S  263  GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO          
SEQRES  21 S  263  MET GLU HIS                                                  
SEQRES   1 T  255  MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER          
SEQRES   2 T  255  THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR          
SEQRES   3 T  255  ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY          
SEQRES   4 T  255  ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS          
SEQRES   5 T  255  LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS          
SEQRES   6 T  255  ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL          
SEQRES   7 T  255  ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE          
SEQRES   8 T  255  ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY          
SEQRES   9 T  255  TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA          
SEQRES  10 T  255  MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG          
SEQRES  11 T  255  PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL          
SEQRES  12 T  255  ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY          
SEQRES  13 T  255  VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA          
SEQRES  14 T  255  ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET          
SEQRES  15 T  255  LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA          
SEQRES  16 T  255  LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS          
SEQRES  17 T  255  ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR          
SEQRES  18 T  255  ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU          
SEQRES  19 T  255  GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU          
SEQRES  20 T  255  ASP GLU SER ASP ASP ASP ASN MET                              
SEQRES   1 U  246  MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE          
SEQRES   2 U  246  THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU          
SEQRES   3 U  246  TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER          
SEQRES   4 U  246  VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR          
SEQRES   5 U  246  GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR          
SEQRES   6 U  246  VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS          
SEQRES   7 U  246  VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL          
SEQRES   8 U  246  GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS          
SEQRES   9 U  246  TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG          
SEQRES  10 U  246  ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU          
SEQRES  11 U  246  MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE          
SEQRES  12 U  246  ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO          
SEQRES  13 U  246  ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY          
SEQRES  14 U  246  VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS          
SEQRES  15 U  246  VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL          
SEQRES  16 U  246  GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE          
SEQRES  17 U  246  ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR          
SEQRES  18 U  246  VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU          
SEQRES  19 U  246  ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP              
SEQRES   1 V  234  THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL          
SEQRES   2 V  234  LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL          
SEQRES   3 V  234  ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO          
SEQRES   4 V  234  ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR          
SEQRES   5 V  234  ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU          
SEQRES   6 V  234  HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR          
SEQRES   7 V  234  ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN          
SEQRES   8 V  234  GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP          
SEQRES   9 V  234  VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY          
SEQRES  10 V  234  SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY          
SEQRES  11 V  234  SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG          
SEQRES  12 V  234  PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER          
SEQRES  13 V  234  GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER          
SEQRES  14 V  234  GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS          
SEQRES  15 V  234  LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS          
SEQRES  16 V  234  GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR          
SEQRES  17 V  234  THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE          
SEQRES  18 V  234  GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER          
SEQRES   1 W  205  MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA          
SEQRES   2 W  205  MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG          
SEQRES   3 W  205  ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE          
SEQRES   4 W  205  GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY          
SEQRES   5 W  205  LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN          
SEQRES   6 W  205  ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU          
SEQRES   7 W  205  GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL          
SEQRES   8 W  205  ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR          
SEQRES   9 W  205  THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE          
SEQRES  10 W  205  LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO          
SEQRES  11 W  205  MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA          
SEQRES  12 W  205  GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO          
SEQRES  13 W  205  ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN          
SEQRES  14 W  205  ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY          
SEQRES  15 W  205  MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE          
SEQRES  16 W  205  THR THR ARG THR LEU LYS ALA ARG MET ASP                      
SEQRES   1 X  201  MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL          
SEQRES   2 X  201  LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL          
SEQRES   3 X  201  GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER          
SEQRES   4 X  201  GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP          
SEQRES   5 X  201  THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN          
SEQRES   6 X  201  LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR          
SEQRES   7 X  201  ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1          
SEQRES   8 X  201  LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU          
SEQRES   9 X  201  ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR          
SEQRES  10 X  201  MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA          
SEQRES  11 X  201  ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU          
SEQRES  12 X  201  ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA          
SEQRES  13 X  201  VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS          
SEQRES  14 X  201  ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE          
SEQRES  15 X  201  ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER          
SEQRES  16 X  201  PHE PRO LYS GLN GLY SER                                      
SEQRES   1 Y  204  THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE          
SEQRES   2 Y  204  VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE          
SEQRES   3 Y  204  ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO          
SEQRES   4 Y  204  TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS          
SEQRES   5 Y  204  SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE          
SEQRES   6 Y  204  TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA          
SEQRES   7 Y  204  ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS          
SEQRES   8 Y  204  GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP          
SEQRES   9 Y  204  ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU          
SEQRES  10 Y  204  GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER          
SEQRES  11 Y  204  GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR          
SEQRES  12 Y  204  SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA          
SEQRES  13 Y  204  ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR          
SEQRES  14 Y  204  SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP          
SEQRES  15 Y  204  GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU          
SEQRES  16 Y  204  HIS GLU LYS TYR SER GLY SER THR PRO                          
SEQRES   1 Z  213  ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU          
SEQRES   2 Z  213  ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP          
SEQRES   3 Z  213  THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP          
SEQRES   4 Z  213  SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE          
SEQRES   5 Z  213  GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR          
SEQRES   6 Z  213  LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER          
SEQRES   7 Z  213  ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET          
SEQRES   8 Z  213  LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR          
SEQRES   9 Z  213  TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY          
SEQRES  10 Z  213  LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR          
SEQRES  11 Z  213  GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA          
SEQRES  12 Z  213  MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS          
SEQRES  13 Z  213  ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP          
SEQRES  14 Z  213  ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA          
SEQRES  15 Z  213  ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE          
SEQRES  16 Z  213  CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL          
SEQRES  17 Z  213  SER LEU ARG LYS ASP                                          
SEQRES   1 a  219  THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY          
SEQRES   2 a  219  VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET          
SEQRES   3 a  219  LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE          
SEQRES   4 a  219  SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY          
SEQRES   5 a  219  ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN          
SEQRES   6 a  219  VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY          
SEQRES   7 a  219  ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP          
SEQRES   8 a  219  LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN          
SEQRES   9 a  219  PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP          
SEQRES  10 a  219  GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL          
SEQRES  11 a  219  ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA          
SEQRES  12 a  219  TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS          
SEQRES  13 a  219  GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL          
SEQRES  14 a  219  GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG          
SEQRES  15 a  219  SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS          
SEQRES  16 a  219  GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN          
SEQRES  17 a  219  TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU                  
SEQRES   1 b  205  THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL          
SEQRES   2 b  205  LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE          
SEQRES   3 b  205  ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP          
SEQRES   4 b  205  ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR          
SEQRES   5 b  205  GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE          
SEQRES   6 b  205  HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR          
SEQRES   7 b  205  ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG          
SEQRES   8 b  205  GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP          
SEQRES   9 b  205  PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY          
SEQRES  10 b  205  GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER          
SEQRES  11 b  205  GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR          
SEQRES  12 b  205  ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR          
SEQRES  13 b  205  ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER          
SEQRES  14 b  205  SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER          
SEQRES  15 b  205  GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO          
SEQRES  16 b  205  LYS PHE ALA VAL ALA THR LEU PRO PRO ALA                      
SEQRES   1 c    5  ACE IML ILE THR 6VO                                          
SEQRES   1 d    5  ACE IML ILE THR 6VO                                          
SEQRES   1 e    5  ACE IML ILE THR 6VO                                          
SEQRES   1 f    5  ACE IML ILE THR 6VO                                          
SEQRES   1 g    5  ACE IML ILE THR 6VO                                          
SEQRES   1 h    5  ACE IML ILE THR 6VO                                          
MODRES 5LF0 YCM C   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LF0 YCM G  137  CYS  MODIFIED RESIDUE                                   
MODRES 5LF0 YCM Q   63  CYS  MODIFIED RESIDUE                                   
MODRES 5LF0 YCM U  137  CYS  MODIFIED RESIDUE                                   
HET    YCM  C  63      10                                                       
HET    6V1  E 148      15                                                       
HET    6V1  G  47      15                                                       
HET    YCM  G 137      10                                                       
HET    6V1  G 161      15                                                       
HET    6V1  J  91      15                                                       
HET    YCM  Q  63      10                                                       
HET    6V1  S 148      15                                                       
HET    6V1  U  47      15                                                       
HET    YCM  U 137      10                                                       
HET    6V1  U 161      15                                                       
HET    6V1  X  91      15                                                       
HET    ACE  c   1       3                                                       
HET    IML  c   2       9                                                       
HET    6VO  c   5      12                                                       
HET    ACE  d   1       3                                                       
HET    IML  d   2       9                                                       
HET    6VO  d   5      12                                                       
HET    ACE  e   1       3                                                       
HET    IML  e   2       9                                                       
HET    6VO  e   5      12                                                       
HET    ACE  f   1       3                                                       
HET    IML  f   2       9                                                       
HET    6VO  f   5      12                                                       
HET    ACE  g   1       3                                                       
HET    IML  g   2       9                                                       
HET    6VO  g   5      12                                                       
HET    ACE  h   1       3                                                       
HET    IML  h   2       9                                                       
HET    6VO  h   5      12                                                       
HET     CL  A 301       1                                                       
HET     CL  A 302       1                                                       
HET     CL  A 303       1                                                       
HET     CL  A 304       1                                                       
HET     CL  B 301       1                                                       
HET     CL  B 302       1                                                       
HET     CL  C 301       1                                                       
HET     CL  C 302       1                                                       
HET     CL  D 301       1                                                       
HET     CL  E 301       1                                                       
HET     CL  E 302       1                                                       
HET     CL  E 303       1                                                       
HET     CL  E 304       1                                                       
HET     CL  F 301       1                                                       
HET     CL  G 301       1                                                       
HET     CL  G 302       1                                                       
HET      K  G 303       1                                                       
HET     MG  H 301       1                                                       
HET     MG  H 302       1                                                       
HET     CL  H 303       1                                                       
HET    1PE  H 304      16                                                       
HET     MG  I 301       1                                                       
HET     CL  I 302       1                                                       
HET    1PE  I 303      16                                                       
HET     MG  I 304       1                                                       
HET     MG  J 301       1                                                       
HET     MG  K 301       1                                                       
HET     CL  K 302       1                                                       
HET     CL  K 303       1                                                       
HET     CL  K 304       1                                                       
HET     CL  K 305       1                                                       
HET    1PE  K 306      16                                                       
HET    1PE  L 301      16                                                       
HET      K  L 302       1                                                       
HET     MG  L 303       1                                                       
HET     CL  M 301       1                                                       
HET     CL  M 302       1                                                       
HET     CL  M 303       1                                                       
HET     CL  N 301       1                                                       
HET     CL  N 302       1                                                       
HET     CL  N 303       1                                                       
HET     CL  N 304       1                                                       
HET    1PE  N 305      16                                                       
HET      K  N 306       1                                                       
HET     CL  O 301       1                                                       
HET     CL  O 302       1                                                       
HET     CL  O 303       1                                                       
HET     CL  O 304       1                                                       
HET     CL  P 301       1                                                       
HET     CL  Q 301       1                                                       
HET     CL  Q 302       1                                                       
HET     CL  R 301       1                                                       
HET     CL  R 302       1                                                       
HET     CL  S 301       1                                                       
HET     CL  S 302       1                                                       
HET     CL  S 303       1                                                       
HET     CL  U 301       1                                                       
HET      K  U 302       1                                                       
HET     MG  V 301       1                                                       
HET     CL  V 302       1                                                       
HET     MG  W 301       1                                                       
HET     CL  W 302       1                                                       
HET    1PE  W 303      16                                                       
HET     MG  X 301       1                                                       
HET     CL  Y 301       1                                                       
HET     CL  Y 302       1                                                       
HET     CL  Y 303       1                                                       
HET     CL  Y 304       1                                                       
HET     CL  Y 305       1                                                       
HET    1PE  Z 301      16                                                       
HET      K  Z 302       1                                                       
HET     CL  a 301       1                                                       
HET     CL  a 302       1                                                       
HET     CL  a 303       1                                                       
HET    1PE  a 304      16                                                       
HET     CL  b 301       1                                                       
HET     CL  b 302       1                                                       
HET     CL  b 303       1                                                       
HET     CL  b 304       1                                                       
HET    1PE  b 305      16                                                       
HET      K  b 306       1                                                       
HET     CL  c 101       1                                                       
HET     CL  f 101       1                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     6V1 (2~{R})-2-AZANYL-3-[(3~{R})-1-ETHYL-2,5-                         
HETNAM   2 6V1  BIS(OXIDANYLIDENE)PYRROLIDIN-3-YL]SULFANYL-PROPANOIC            
HETNAM   3 6V1  ACID                                                            
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     IML N-METHYL-ISOLEUCINE                                              
HETNAM     6VO (3~{R},4~{S})-4-AZANYL-2,6-DIMETHYL-HEPTANE-2,3-DIOL             
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     1PE PEG400                                                           
FORMUL   3  YCM    4(C5 H10 N2 O3 S)                                            
FORMUL   5  6V1    8(C9 H14 N2 O4 S)                                            
FORMUL  29  ACE    6(C2 H4 O)                                                   
FORMUL  29  IML    6(C7 H15 N O2)                                               
FORMUL  29  6VO    6(C9 H21 N O2)                                               
FORMUL  35   CL    58(CL 1-)                                                    
FORMUL  51    K    6(K 1+)                                                      
FORMUL  52   MG    10(MG 2+)                                                    
FORMUL  55  1PE    9(C10 H22 O6)                                                
FORMUL  18  HOH   *3173(H2 O)                                                   
HELIX    1 AA1 LEU A   18  GLY A   30  1                                  13    
HELIX    2 AA2 MET A   78  GLN A  101  1                                  24    
HELIX    3 AA3 PRO A  105  TYR A  120  1                                  16    
HELIX    4 AA4 ASN A  165  LYS A  175  1                                  11    
HELIX    5 AA5 GLU A  182  SER A  197  1                                  16    
HELIX    6 AA6 THR A  221  ALA A  230  1                                  10    
HELIX    7 AA7 LEU B   18  ALA B   31  1                                  14    
HELIX    8 AA8 ILE B   79  GLN B  102  1                                  24    
HELIX    9 AA9 PRO B  106  PHE B  124  1                                  19    
HELIX   10 AB1 ASN B  167  TYR B  179  1                                  13    
HELIX   11 AB2 THR B  185  MET B  201  1                                  17    
HELIX   12 AB3 LYS B  229  ALA B  247  1                                  19    
HELIX   13 AB4 SER C   11  HIS C   15  5                                   5    
HELIX   14 AB5 LEU C   16  GLY C   29  1                                  14    
HELIX   15 AB6 ASP C   55  ARG C   60  5                                   6    
HELIX   16 AB7 LEU C   76  GLU C   99  1                                  24    
HELIX   17 AB8 THR C  103  TYR C  118  1                                  16    
HELIX   18 AB9 GLY C  164  TYR C  176  1                                  13    
HELIX   19 AC1 THR C  177  GLU C  182  5                                   6    
HELIX   20 AC2 THR C  183  VAL C  199  1                                  17    
HELIX   21 AC3 ASN C  221  LYS C  234  1                                  14    
HELIX   22 AC4 LEU D   21  LYS D   32  1                                  12    
HELIX   23 AC5 GLU D   60  ILE D   64  5                                   5    
HELIX   24 AC6 LEU D   81  ASN D  104  1                                  24    
HELIX   25 AC7 THR D  108  ASN D  118  1                                  11    
HELIX   26 AC8 ALA D  173  TYR D  185  1                                  13    
HELIX   27 AC9 THR D  190  MET D  206  1                                  17    
HELIX   28 AD1 THR D  230  LYS D  239  1                                  10    
HELIX   29 AD2 ILE E   19  GLN E   31  1                                  13    
HELIX   30 AD3 LEU E   77  ASP E  100  1                                  24    
HELIX   31 AD4 PRO E  104  ILE E  118  1                                  15    
HELIX   32 AD5 PRO E  119  ARG E  122  5                                   4    
HELIX   33 AD6 ARG E  164  MET E  180  1                                  17    
HELIX   34 AD7 ASN E  183  THR E  198  1                                  16    
HELIX   35 AD8 VAL E  229  GLU E  234  1                                   6    
HELIX   36 AD9 VAL F   20  ASN F   32  1                                  13    
HELIX   37 AE1 LEU F   80  GLY F  103  1                                  24    
HELIX   38 AE2 PRO F  107  TYR F  122  1                                  16    
HELIX   39 AE3 ALA F  168  GLU F  177  1                                  10    
HELIX   40 AE4 LYS F  178  LEU F  179  5                                   2    
HELIX   41 AE5 GLN F  180  MET F  184  5                                   5    
HELIX   42 AE6 THR F  185  HIS F  201  1                                  17    
HELIX   43 AE7 LEU F  219  ASN F  221  5                                   3    
HELIX   44 AE8 PRO F  228  LYS F  244  1                                  17    
HELIX   45 AE9 LEU G   22  GLN G   34  1                                  13    
HELIX   46 AF1 ASP G   62  VAL G   66  5                                   5    
HELIX   47 AF2 MET G   83  GLY G  106  1                                  24    
HELIX   48 AF3 PRO G  110  ASN G  128  1                                  19    
HELIX   49 AF4 LYS G  171  LYS G  186  1                                  16    
HELIX   50 AF5 PHE G  187  THR G  190  5                                   4    
HELIX   51 AF6 GLN G  193  SER G  207  1                                  15    
HELIX   52 AF7 LYS G  211  SER G  213  5                                   3    
HELIX   53 AF8 THR G  231  GLU G  244  1                                  14    
HELIX   54 AF9 THR H   48  GLY H   71  1                                  24    
HELIX   55 AG1 ARG H   75  TYR H   90  1                                  16    
HELIX   56 AG2 GLY H  130  PHE H  142  1                                  13    
HELIX   57 AG3 GLU H  147  ASP H  166  1                                  20    
HELIX   58 AG4 SER I    1  TYR I    5  5                                   5    
HELIX   59 AG5 LEU I   55  GLU I   77  1                                  23    
HELIX   60 AG6 LYS I   82  LYS I   97  1                                  16    
HELIX   61 AG7 CYS I  141  TRP I  153  1                                  13    
HELIX   62 AG8 ASP I  158  ASP I  175  1                                  18    
HELIX   63 AG9 GLY J   51  GLY J   72  1                                  22    
HELIX   64 AH1 SER J   76  LEU J   92  1                                  17    
HELIX   65 AH2 TYR J  134  TYR J  147  1                                  14    
HELIX   66 AH3 SER J  152  PHE J  171  1                                  20    
HELIX   67 AH4 GLY K   48  LYS K   71  1                                  24    
HELIX   68 AH5 SER K   75  GLN K   89  1                                  15    
HELIX   69 AH6 GLY K  131  TYR K  143  1                                  13    
HELIX   70 AH7 GLU K  148  ASP K  167  1                                  20    
HELIX   71 AH8 VAL K  192  SER K  200  1                                   9    
HELIX   72 AH9 PHE L   57  ASN L   80  1                                  24    
HELIX   73 AI1 THR L   84  ARG L   99  1                                  16    
HELIX   74 AI2 ALA L  141  VAL L  153  1                                  13    
HELIX   75 AI3 SER L  167  ASP L  186  1                                  20    
HELIX   76 AI4 TYR M   57  GLY M   78  1                                  22    
HELIX   77 AI5 SER M   84  LYS M  102  1                                  19    
HELIX   78 AI6 TYR M  141  ALA M  146  1                                   6    
HELIX   79 AI7 ALA M  146  GLN M  157  1                                  12    
HELIX   80 AI8 SER M  161  ASP M  180  1                                  20    
HELIX   81 AI9 TRP M  209  MET M  214  5                                   6    
HELIX   82 AJ1 SER N   48  ASN N   71  1                                  24    
HELIX   83 AJ2 LEU N   75  TYR N   90  1                                  16    
HELIX   84 AJ3 ARG N   91  LEU N   94  5                                   4    
HELIX   85 AJ4 GLY N  129  TYR N  134  5                                   6    
HELIX   86 AJ5 ILE N  135  TYR N  143  1                                   9    
HELIX   87 AJ6 THR N  148  ASP N  167  1                                  20    
HELIX   88 AJ7 LEU N  190  ILE N  194  5                                   5    
HELIX   89 AJ8 LEU O   18  GLY O   30  1                                  13    
HELIX   90 AJ9 MET O   78  GLN O  101  1                                  24    
HELIX   91 AK1 PRO O  105  TYR O  120  1                                  16    
HELIX   92 AK2 ASN O  165  LYS O  175  1                                  11    
HELIX   93 AK3 GLU O  182  SER O  197  1                                  16    
HELIX   94 AK4 THR O  221  LEU O  229  1                                   9    
HELIX   95 AK5 LEU P   18  ALA P   31  1                                  14    
HELIX   96 AK6 ILE P   79  GLN P  102  1                                  24    
HELIX   97 AK7 PRO P  106  PHE P  124  1                                  19    
HELIX   98 AK8 ASN P  167  TYR P  179  1                                  13    
HELIX   99 AK9 THR P  185  MET P  201  1                                  17    
HELIX  100 AL1 LYS P  229  GLU P  244  1                                  16    
HELIX  101 AL2 LEU Q   16  GLY Q   29  1                                  14    
HELIX  102 AL3 ASP Q   55  ARG Q   60  5                                   6    
HELIX  103 AL4 LEU Q   76  GLU Q   99  1                                  24    
HELIX  104 AL5 THR Q  103  TYR Q  118  1                                  16    
HELIX  105 AL6 GLY Q  164  TYR Q  176  1                                  13    
HELIX  106 AL7 THR Q  177  GLU Q  182  5                                   6    
HELIX  107 AL8 THR Q  183  GLU Q  197  1                                  15    
HELIX  108 AL9 ASN Q  221  LYS Q  234  1                                  14    
HELIX  109 AM1 LYS Q  234  ASN Q  239  1                                   6    
HELIX  110 AM2 LEU R   21  LYS R   32  1                                  12    
HELIX  111 AM3 GLU R   60  ILE R   64  5                                   5    
HELIX  112 AM4 LEU R   81  ASN R  104  1                                  24    
HELIX  113 AM5 THR R  108  ASN R  118  1                                  11    
HELIX  114 AM6 ALA R  173  TYR R  185  1                                  13    
HELIX  115 AM7 THR R  190  MET R  206  1                                  17    
HELIX  116 AM8 THR R  230  LYS R  239  1                                  10    
HELIX  117 AM9 ARG S    3  ASP S    7  5                                   5    
HELIX  118 AN1 ILE S   19  GLY S   32  1                                  14    
HELIX  119 AN2 LEU S   77  ASP S  100  1                                  24    
HELIX  120 AN3 PRO S  104  ILE S  118  1                                  15    
HELIX  121 AN4 PRO S  119  ARG S  122  5                                   4    
HELIX  122 AN5 ARG S  164  MET S  180  1                                  17    
HELIX  123 AN6 ASN S  183  THR S  198  1                                  16    
HELIX  124 AN7 VAL S  229  GLU S  234  1                                   6    
HELIX  125 AN8 VAL T   20  ASN T   32  1                                  13    
HELIX  126 AN9 LEU T   80  GLY T  103  1                                  24    
HELIX  127 AO1 PRO T  107  TYR T  122  1                                  16    
HELIX  128 AO2 ALA T  168  GLU T  177  1                                  10    
HELIX  129 AO3 LYS T  178  LEU T  179  5                                   2    
HELIX  130 AO4 GLN T  180  MET T  184  5                                   5    
HELIX  131 AO5 THR T  185  HIS T  201  1                                  17    
HELIX  132 AO6 LEU T  219  ASN T  221  5                                   3    
HELIX  133 AO7 PRO T  228  LYS T  244  1                                  17    
HELIX  134 AO8 LEU U   22  GLN U   34  1                                  13    
HELIX  135 AO9 ASP U   62  VAL U   66  5                                   5    
HELIX  136 AP1 MET U   83  GLY U  106  1                                  24    
HELIX  137 AP2 PRO U  110  ASN U  128  1                                  19    
HELIX  138 AP3 LYS U  171  LYS U  184  1                                  14    
HELIX  139 AP4 THR U  194  SER U  207  1                                  14    
HELIX  140 AP5 LYS U  211  SER U  213  5                                   3    
HELIX  141 AP6 THR U  231  GLU U  244  1                                  14    
HELIX  142 AP7 THR V   48  GLY V   71  1                                  24    
HELIX  143 AP8 ARG V   75  TYR V   90  1                                  16    
HELIX  144 AP9 GLY V  130  PHE V  142  1                                  13    
HELIX  145 AQ1 GLU V  147  ASP V  166  1                                  20    
HELIX  146 AQ2 SER W    1  TYR W    5  5                                   5    
HELIX  147 AQ3 LEU W   55  GLU W   77  1                                  23    
HELIX  148 AQ4 LYS W   82  GLU W   96  1                                  15    
HELIX  149 AQ5 CYS W  141  TRP W  153  1                                  13    
HELIX  150 AQ6 ASP W  158  ASP W  175  1                                  18    
HELIX  151 AQ7 GLY X   51  GLY X   72  1                                  22    
HELIX  152 AQ8 SER X   76  ARG X   93  1                                  18    
HELIX  153 AQ9 TYR X  134  TYR X  147  1                                  14    
HELIX  154 AR1 SER X  152  PHE X  171  1                                  20    
HELIX  155 AR2 GLY Y   48  LYS Y   71  1                                  24    
HELIX  156 AR3 SER Y   75  GLN Y   89  1                                  15    
HELIX  157 AR4 GLY Y  131  TYR Y  143  1                                  13    
HELIX  158 AR5 GLU Y  148  ASP Y  167  1                                  20    
HELIX  159 AR6 VAL Y  192  TYR Y  199  1                                   8    
HELIX  160 AR7 PHE Z   57  ASN Z   80  1                                  24    
HELIX  161 AR8 THR Z   84  ARG Z   99  1                                  16    
HELIX  162 AR9 ALA Z  141  VAL Z  153  1                                  13    
HELIX  163 AS1 SER Z  167  ASP Z  186  1                                  20    
HELIX  164 AS2 TYR a   57  GLY a   78  1                                  22    
HELIX  165 AS3 SER a   84  LYS a  102  1                                  19    
HELIX  166 AS4 TYR a  141  ALA a  146  1                                   6    
HELIX  167 AS5 ALA a  146  GLN a  157  1                                  12    
HELIX  168 AS6 SER a  161  ASP a  180  1                                  20    
HELIX  169 AS7 TRP a  209  MET a  214  5                                   6    
HELIX  170 AS8 SER b   48  ASN b   71  1                                  24    
HELIX  171 AS9 LEU b   75  TYR b   90  1                                  16    
HELIX  172 AT1 ARG b   91  LEU b   94  5                                   4    
HELIX  173 AT2 GLY b  129  TYR b  134  5                                   6    
HELIX  174 AT3 ILE b  135  TYR b  143  1                                   9    
HELIX  175 AT4 THR b  148  ASP b  167  1                                  20    
HELIX  176 AT5 LEU b  190  ILE b  194  5                                   5    
SHEET    1 AA1 5 ALA A 159  MET A 162  0                                        
SHEET    2 AA1 5 SER A  34  LYS A  38 -1  N  SER A  34   O  MET A 162           
SHEET    3 AA1 5 VAL A  43  GLU A  48 -1  O  ALA A  46   N  VAL A  35           
SHEET    4 AA1 5 ILE A 207  ASN A 213 -1  O  GLY A 210   N  LEU A  45           
SHEET    5 AA1 5 GLY A 216  ARG A 219 -1  O  ARG A 218   N  ILE A 211           
SHEET    1 AA2 5 GLU A  65  PRO A  66  0                                        
SHEET    2 AA2 5 ILE A  71  GLY A  77 -1  O  LEU A  73   N  GLU A  65           
SHEET    3 AA2 5 VAL A 131  TRP A 138 -1  O  CYS A 136   N  GLY A  72           
SHEET    4 AA2 5 PRO A 143  SER A 148 -1  O  PHE A 146   N  ILE A 135           
SHEET    5 AA2 5 TYR A 154  ALA A 156 -1  O  PHE A 155   N  GLN A 147           
SHEET    1 AA3 5 ALA B 161  ILE B 164  0                                        
SHEET    2 AA3 5 CYS B  34  ALA B  39 -1  N  CYS B  34   O  ILE B 164           
SHEET    3 AA3 5 GLY B  42  GLU B  48 -1  O  ALA B  46   N  LEU B  35           
SHEET    4 AA3 5 VAL B 211  ARG B 218 -1  O  LEU B 216   N  VAL B  43           
SHEET    5 AA3 5 THR B 223  VAL B 227 -1  O  VAL B 224   N  THR B 217           
SHEET    1 AA4 5 ILE B  65  ASN B  69  0                                        
SHEET    2 AA4 5 MET B  72  GLY B  78 -1  O  CYS B  74   N  TYR B  66           
SHEET    3 AA4 5 VAL B 132  ASP B 140 -1  O  ILE B 137   N  ALA B  73           
SHEET    4 AA4 5 GLY B 144  SER B 150 -1  O  TYR B 148   N  TYR B 136           
SHEET    5 AA4 5 TYR B 156  GLY B 158 -1  O  GLY B 157   N  GLN B 149           
SHEET    1 AA5 5 ALA C 158  ILE C 161  0                                        
SHEET    2 AA5 5 ALA C  32  ARG C  36 -1  N  ALA C  32   O  ILE C 161           
SHEET    3 AA5 5 ILE C  40  GLU C  46 -1  O  GLY C  44   N  VAL C  33           
SHEET    4 AA5 5 ILE C 206  ARG C 212 -1  O  ALA C 209   N  LEU C  43           
SHEET    5 AA5 5 LYS C 218  LEU C 220 -1  O  LEU C 220   N  LEU C 208           
SHEET    1 AA6 5 ILE C  62  ALA C  64  0                                        
SHEET    2 AA6 5 VAL C  69  GLY C  75 -1  O  MET C  71   N  YCM C  63           
SHEET    3 AA6 5 ILE C 129  PHE C 136 -1  O  LEU C 132   N  ALA C  72           
SHEET    4 AA6 5 PRO C 142  THR C 147 -1  O  TYR C 145   N  ILE C 133           
SHEET    5 AA6 5 TYR C 153  ALA C 155 -1  O  HIS C 154   N  GLN C 146           
SHEET    1 AA7 5 ALA D 167  ILE D 170  0                                        
SHEET    2 AA7 5 ALA D  37  THR D  42 -1  N  GLY D  39   O  ARG D 168           
SHEET    3 AA7 5 GLY D  45  GLU D  51 -1  O  ALA D  49   N  ILE D  38           
SHEET    4 AA7 5 ILE D 215  VAL D 220 -1  O  ALA D 218   N  LEU D  48           
SHEET    5 AA7 5 HIS D 227  MET D 228 -1  O  HIS D 227   N  THR D 219           
SHEET    1 AA8 5 ILE D  67  ASP D  71  0                                        
SHEET    2 AA8 5 ILE D  74  GLY D  80 -1  O  ILE D  74   N  ILE D  70           
SHEET    3 AA8 5 VAL D 139  ASP D 147 -1  O  GLY D 144   N  GLY D  75           
SHEET    4 AA8 5 GLY D 150  MET D 156 -1  O  GLN D 152   N  GLY D 145           
SHEET    5 AA8 5 PHE D 162  GLN D 164 -1  O  VAL D 163   N  HIS D 155           
SHEET    1 AA9 5 ALA E 158  ILE E 161  0                                        
SHEET    2 AA9 5 THR E  35  LYS E  39 -1  N  GLY E  37   O  MET E 159           
SHEET    3 AA9 5 HIS E  43  LEU E  49 -1  O  VAL E  45   N  LEU E  38           
SHEET    4 AA9 5 VAL E 210  GLY E 216 -1  O  VAL E 215   N  ALA E  44           
SHEET    5 AA9 5 LEU E 219  ASP E 225 -1  O  TYR E 224   N  ILE E 212           
SHEET    1 AB1 5 ILE E  63  ASP E  67  0                                        
SHEET    2 AB1 5 ILE E  70  GLY E  76 -1  O  ILE E  72   N  LEU E  64           
SHEET    3 AB1 5 VAL E 130  ASP E 138 -1  O  LEU E 133   N  SER E  73           
SHEET    4 AB1 5 GLY E 141  THR E 147 -1  O  PHE E 145   N  ILE E 134           
SHEET    5 AB1 5 TYR E 153  CYS E 156 -1  O  CYS E 156   N  ILE E 144           
SHEET    1 AB2 5 GLY F 162  ILE F 165  0                                        
SHEET    2 AB2 5 ALA F  36  CYS F  41 -1  N  GLY F  38   O  CYS F 163           
SHEET    3 AB2 5 GLY F  44  LEU F  52 -1  O  GLY F  48   N  ILE F  37           
SHEET    4 AB2 5 PHE F 209  GLY F 217 -1  O  GLU F 210   N  LYS F  51           
SHEET    5 AB2 5 GLU F 225  ILE F 226 -1  O  GLU F 225   N  TRP F 215           
SHEET    1 AB3 5 LEU F  66  ASP F  70  0                                        
SHEET    2 AB3 5 VAL F  73  GLY F  79 -1  O  MET F  75   N  PHE F  67           
SHEET    3 AB3 5 CYS F 133  SER F 141 -1  O  MET F 136   N  ALA F  76           
SHEET    4 AB3 5 GLY F 145  ILE F 151 -1  O  ILE F 151   N  PHE F 135           
SHEET    5 AB3 5 SER F 157  GLY F 159 -1  O  TYR F 158   N  MET F 150           
SHEET    1 AB4 5 ALA G 165  GLY G 169  0                                        
SHEET    2 AB4 5 THR G  38  ARG G  43 -1  N  ALA G  41   O  THR G 166           
SHEET    3 AB4 5 6V1 G  47  GLN G  53 -1  O  VAL G  51   N  VAL G  40           
SHEET    4 AB4 5 ILE G 215  THR G 221 -1  O  VAL G 220   N  ALA G  48           
SHEET    5 AB4 5 ARG G 228  ILE G 229 -1  O  ARG G 228   N  VAL G 219           
SHEET    1 AB5 5 LEU G  69  THR G  73  0                                        
SHEET    2 AB5 5 ILE G  76  GLY G  82 -1  O  ILE G  76   N  ILE G  72           
SHEET    3 AB5 5 CYS G 136  ASP G 144 -1  O  ILE G 141   N  GLY G  77           
SHEET    4 AB5 5 GLY G 148  CYS G 154 -1  O  TYR G 152   N  LEU G 140           
SHEET    5 AB5 5 TYR G 160  PHE G 163 -1  O  PHE G 163   N  VAL G 151           
SHEET    1 AB6 5 TYR H 124  MET H 127  0                                        
SHEET    2 AB6 5 ILE H   3  TYR H   8 -1  N  ILE H   3   O  MET H 127           
SHEET    3 AB6 5 GLY H  11  ASP H  17 -1  O  GLY H  15   N  ALA H   4           
SHEET    4 AB6 5 ILE H 173  SER H 179 -1  O  ASP H 174   N  ALA H  16           
SHEET    5 AB6 5 LEU H 183  THR H 190 -1  O  ASP H 184   N  VAL H 177           
SHEET    1 AB7 2 ALA H  20  GLU H  22  0                                        
SHEET    2 AB7 2 VAL H  25  ASP H  28 -1  O  VAL H  25   N  GLU H  22           
SHEET    1 AB8 5 ILE H  34  SER H  38  0                                        
SHEET    2 AB8 5 ILE H  41  GLY H  47 -1  O  CYS H  43   N  HIS H  35           
SHEET    3 AB8 5 ALA H  96  ASP H 104 -1  O  ALA H  97   N  ALA H  46           
SHEET    4 AB8 5 GLY H 107  ILE H 113 -1  O  TYR H 111   N  LEU H 100           
SHEET    5 AB8 5 THR H 119  LYS H 121 -1  O  ASP H 120   N  SER H 112           
SHEET    1 AB9 6 VAL H 211  PRO H 218  0                                        
SHEET    2 AB9 6 LYS I 193  LEU I 199 -1  O  THR I 198   N  LEU H 212           
SHEET    3 AB9 6 VAL I 184  GLU I 190 -1  N  VAL I 186   O  ARG I 197           
SHEET    4 AB9 6 CYS I  18  ASP I  24 -1  N  VAL I  19   O  ILE I 189           
SHEET    5 AB9 6 ALA I   9  LYS I  14 -1  N  MET I  11   O  ALA I  22           
SHEET    6 AB9 6 PHE I 135  GLY I 139 -1  O  SER I 138   N  VAL I  10           
SHEET    1 AC1 2 PHE I  27  ILE I  29  0                                        
SHEET    2 AC1 2 GLN I  32  THR I  35 -1  O  THR I  35   N  PHE I  27           
SHEET    1 AC2 5 ILE I  41  PRO I  43  0                                        
SHEET    2 AC2 5 LEU I  48  GLY I  54 -1  O  ILE I  50   N  PHE I  42           
SHEET    3 AC2 5 THR I 104  LEU I 111 -1  O  VAL I 107   N  GLY I  51           
SHEET    4 AC2 5 PRO I 118  LEU I 123 -1  O  PHE I 119   N  GLY I 110           
SHEET    5 AC2 5 PRO I 129  VAL I 131 -1  O  MET I 130   N  SER I 122           
SHEET    1 AC3 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC3 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC3 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC3 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC3 5 GLY J 187  ASP J 190 -1  O  HIS J 189   N  ILE J 182           
SHEET    1 AC4 5 PHE J 129  HIS J 132  0                                        
SHEET    2 AC4 5 LEU J   4  GLN J   8 -1  N  GLY J   6   O  ALA J 130           
SHEET    3 AC4 5 VAL J  13  ASP J  18 -1  O  LEU J  14   N  ILE J   7           
SHEET    4 AC4 5 THR J 177  ASP J 184 -1  O  ARG J 181   N  VAL J  15           
SHEET    5 AC4 5 ILE J 194  SER J 195 -1  O  ILE J 194   N  PHE J 178           
SHEET    1 AC5 2 ALA J  21  SER J  23  0                                        
SHEET    2 AC5 2 VAL J  26  LYS J  29 -1  O  MET J  28   N  ALA J  21           
SHEET    1 AC6 5 MET J  35  SER J  39  0                                        
SHEET    2 AC6 5 ILE J  42  GLY J  48 -1  O  LEU J  44   N  PHE J  36           
SHEET    3 AC6 5 VAL J 100  ASP J 108 -1  O  ASN J 101   N  VAL J  47           
SHEET    4 AC6 5 GLY J 112  MET J 118 -1  O  MET J 118   N  LEU J 102           
SHEET    5 AC6 5 LEU J 124  LYS J 126 -1  O  ALA J 125   N  TYR J 117           
SHEET    1 AC7 5 THR K 125  VAL K 128  0                                        
SHEET    2 AC7 5 THR K   3  PHE K   8 -1  N  THR K   3   O  VAL K 128           
SHEET    3 AC7 5 GLY K  11  ALA K  16 -1  O  ALA K  15   N  LEU K   4           
SHEET    4 AC7 5 ALA K 173  ARG K 180 -1  O  VAL K 179   N  VAL K  12           
SHEET    5 AC7 5 GLY K 183  ASN K 191 -1  O  ASP K 190   N  VAL K 174           
SHEET    1 AC8 2 ALA K  20  ALA K  22  0                                        
SHEET    2 AC8 2 TYR K  25  SER K  28 -1  O  SER K  28   N  ALA K  20           
SHEET    1 AC9 4 VAL K  34  ASN K  38  0                                        
SHEET    2 AC9 4 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AC9 4 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AC9 4 ALA K  46  GLY K  47 -1  N  ALA K  46   O  GLY K  98           
SHEET    1 AD1 5 VAL K  34  ASN K  38  0                                        
SHEET    2 AD1 5 LEU K  41  THR K  44 -1  O  GLY K  43   N  ILE K  35           
SHEET    3 AD1 5 MET K  97  ASP K 105 -1  O  CYS K 102   N  LEU K  42           
SHEET    4 AD1 5 GLY K 108  ASP K 115 -1  O  VAL K 114   N  THR K  99           
SHEET    5 AD1 5 ARG K 120  SER K 122 -1  O  ILE K 121   N  TYR K 113           
SHEET    1 AD2 5 PHE L 135  GLY L 139  0                                        
SHEET    2 AD2 5 THR L  11  ALA L  16 -1  N  ILE L  12   O  GLY L 138           
SHEET    3 AD2 5 ALA L  21  ASP L  26 -1  O  ALA L  24   N  LEU L  13           
SHEET    4 AD2 5 ALA L 192  THR L 199 -1  O  ARG L 194   N  SER L  25           
SHEET    5 AD2 5 GLY L 202  SER L 209 -1  O  VAL L 208   N  LEU L 193           
SHEET    1 AD3 2 LEU L  29  GLU L  31  0                                        
SHEET    2 AD3 2 SER L  34  THR L  37 -1  O  HIS L  36   N  LEU L  29           
SHEET    1 AD4 5 CYS L  43  THR L  47  0                                        
SHEET    2 AD4 5 THR L  50  GLY L  56 -1  O  THR L  50   N  LEU L  46           
SHEET    3 AD4 5 VAL L 106  LEU L 113 -1  O  GLY L 111   N  VAL L  51           
SHEET    4 AD4 5 GLY L 119  PHE L 124 -1  O  TYR L 122   N  ILE L 110           
SHEET    5 AD4 5 TYR L 130  ASP L 133 -1  O  ASP L 133   N  VAL L 121           
SHEET    1 AD5 5 LEU M  33  PHE M  36  0                                        
SHEET    2 AD5 5 GLY M  28  TYR M  30 -1  N  GLY M  28   O  PHE M  36           
SHEET    3 AD5 5 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD5 5 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD5 5 ILE M  42  ASN M  46 -1  N  MET M  43   O  LEU M  51           
SHEET    1 AD6 7 LEU M  33  PHE M  36  0                                        
SHEET    2 AD6 7 GLY M  28  TYR M  30 -1  N  GLY M  28   O  PHE M  36           
SHEET    3 AD6 7 VAL M   6  GLY M   8 -1  N  THR M   7   O  SER M  29           
SHEET    4 AD6 7 THR M  49  ASP M  56 -1  O  GLY M  55   N  GLY M   8           
SHEET    5 AD6 7 ASN M 108  ALA M 116 -1  O  GLY M 113   N  MET M  50           
SHEET    6 AD6 7 GLU M 119  VAL M 125 -1  O  VAL M 125   N  MET M 110           
SHEET    7 AD6 7 ALA M 131  GLU M 133 -1  O  TYR M 132   N  TYR M 124           
SHEET    1 AD7 5 SER M 136  ALA M 138  0                                        
SHEET    2 AD7 5 VAL M  11  PHE M  16 -1  N  GLY M  13   O  LEU M 137           
SHEET    3 AD7 5 GLY M  19  ASP M  25 -1  O  GLY M  19   N  PHE M  16           
SHEET    4 AD7 5 PHE M 187  THR M 193 -1  O  ALA M 190   N  ILE M  22           
SHEET    5 AD7 5 GLY M 196  LEU M 203 -1  O  GLU M 200   N  ILE M 189           
SHEET    1 AD8 5 PHE N 125  GLY N 128  0                                        
SHEET    2 AD8 5 ILE N   3  PHE N   8 -1  N  ALA N   5   O  ALA N 126           
SHEET    3 AD8 5 GLY N  11  ALA N  16 -1  O  GLY N  15   N  MET N   4           
SHEET    4 AD8 5 ILE N 174  ALA N 180 -1  O  ILE N 179   N  VAL N  12           
SHEET    5 AD8 5 GLY N 183  LEU N 189 -1  O  LEU N 189   N  ILE N 174           
SHEET    1 AD9 3 TYR N  25  ASN N  28  0                                        
SHEET    2 AD9 3 THR N  20  THR N  22 -1  N  THR N  20   O  ASN N  28           
SHEET    3 AD9 3 ILE e   3  THR e   4 -1  O  THR e   4   N  THR N  21           
SHEET    1 AE1 5 LEU N  34  HIS N  38  0                                        
SHEET    2 AE1 5 ILE N  41  GLY N  47 -1  O  ILE N  41   N  ILE N  37           
SHEET    3 AE1 5 ALA N  96  ASP N 104 -1  O  ILE N  99   N  CYS N  44           
SHEET    4 AE1 5 GLY N 108  VAL N 114 -1  O  TYR N 112   N  ILE N 100           
SHEET    5 AE1 5 VAL N 121  ARG N 122 -1  O  VAL N 121   N  SER N 113           
SHEET    1 AE2 5 ALA O 159  MET O 162  0                                        
SHEET    2 AE2 5 SER O  34  LYS O  38 -1  N  SER O  34   O  MET O 162           
SHEET    3 AE2 5 VAL O  43  GLU O  48 -1  O  ALA O  46   N  VAL O  35           
SHEET    4 AE2 5 ILE O 207  ASN O 213 -1  O  GLY O 210   N  LEU O  45           
SHEET    5 AE2 5 GLY O 216  ARG O 219 -1  O  ARG O 218   N  ILE O 211           
SHEET    1 AE3 5 GLU O  65  PRO O  66  0                                        
SHEET    2 AE3 5 ILE O  71  GLY O  77 -1  O  LEU O  73   N  GLU O  65           
SHEET    3 AE3 5 VAL O 131  ASN O 139 -1  O  CYS O 136   N  GLY O  72           
SHEET    4 AE3 5 ARG O 142  SER O 148 -1  O  PHE O 146   N  ILE O 135           
SHEET    5 AE3 5 TYR O 154  ALA O 156 -1  O  PHE O 155   N  GLN O 147           
SHEET    1 AE4 5 ALA P 161  ILE P 164  0                                        
SHEET    2 AE4 5 CYS P  34  ALA P  39 -1  N  CYS P  34   O  ILE P 164           
SHEET    3 AE4 5 GLY P  42  GLU P  48 -1  O  ALA P  46   N  LEU P  35           
SHEET    4 AE4 5 VAL P 211  ARG P 218 -1  O  LEU P 216   N  VAL P  43           
SHEET    5 AE4 5 THR P 223  VAL P 227 -1  O  VAL P 224   N  THR P 217           
SHEET    1 AE5 5 ILE P  65  ASN P  69  0                                        
SHEET    2 AE5 5 MET P  72  GLY P  78 -1  O  CYS P  74   N  TYR P  66           
SHEET    3 AE5 5 VAL P 132  ASP P 140 -1  O  ILE P 137   N  ALA P  73           
SHEET    4 AE5 5 GLY P 144  SER P 150 -1  O  TYR P 148   N  TYR P 136           
SHEET    5 AE5 5 TYR P 156  GLY P 158 -1  O  GLY P 157   N  GLN P 149           
SHEET    1 AE6 5 ALA Q 158  ILE Q 161  0                                        
SHEET    2 AE6 5 ALA Q  32  ARG Q  36 -1  N  ALA Q  32   O  ILE Q 161           
SHEET    3 AE6 5 ILE Q  40  VAL Q  45 -1  O  GLY Q  44   N  VAL Q  33           
SHEET    4 AE6 5 GLU Q 207  ARG Q 212 -1  O  ALA Q 209   N  LEU Q  43           
SHEET    5 AE6 5 LYS Q 218  LEU Q 220 -1  O  LEU Q 220   N  LEU Q 208           
SHEET    1 AE7 5 ILE Q  62  ALA Q  64  0                                        
SHEET    2 AE7 5 VAL Q  69  GLY Q  75 -1  O  MET Q  71   N  YCM Q  63           
SHEET    3 AE7 5 ILE Q 129  PHE Q 136 -1  O  VAL Q 134   N  CYS Q  70           
SHEET    4 AE7 5 PRO Q 142  THR Q 147 -1  O  TYR Q 145   N  ILE Q 133           
SHEET    5 AE7 5 TYR Q 153  ALA Q 155 -1  O  HIS Q 154   N  GLN Q 146           
SHEET    1 AE8 5 ALA R 167  ILE R 170  0                                        
SHEET    2 AE8 5 ALA R  37  THR R  42 -1  N  GLY R  39   O  ARG R 168           
SHEET    3 AE8 5 GLY R  45  GLU R  51 -1  O  ALA R  49   N  ILE R  38           
SHEET    4 AE8 5 ILE R 215  VAL R 220 -1  O  ALA R 218   N  LEU R  48           
SHEET    5 AE8 5 HIS R 227  MET R 228 -1  O  HIS R 227   N  THR R 219           
SHEET    1 AE9 5 ILE R  67  ASP R  71  0                                        
SHEET    2 AE9 5 ILE R  74  GLY R  80 -1  O  ILE R  74   N  ILE R  70           
SHEET    3 AE9 5 VAL R 139  ASP R 147 -1  O  GLY R 144   N  GLY R  75           
SHEET    4 AE9 5 GLY R 150  MET R 156 -1  O  GLN R 152   N  GLY R 145           
SHEET    5 AE9 5 PHE R 162  GLN R 164 -1  O  VAL R 163   N  HIS R 155           
SHEET    1 AF1 5 ALA S 158  ILE S 161  0                                        
SHEET    2 AF1 5 THR S  35  LYS S  39 -1  N  GLY S  37   O  MET S 159           
SHEET    3 AF1 5 HIS S  43  LEU S  49 -1  O  VAL S  45   N  LEU S  38           
SHEET    4 AF1 5 VAL S 210  GLY S 216 -1  O  VAL S 215   N  ALA S  44           
SHEET    5 AF1 5 LEU S 219  ASP S 225 -1  O  TYR S 224   N  ILE S 212           
SHEET    1 AF2 5 ILE S  63  ASP S  67  0                                        
SHEET    2 AF2 5 ILE S  70  GLY S  76 -1  O  ILE S  72   N  LEU S  64           
SHEET    3 AF2 5 VAL S 130  ASP S 138 -1  O  ALA S 135   N  GLY S  71           
SHEET    4 AF2 5 GLY S 141  THR S 147 -1  O  PHE S 145   N  ILE S 134           
SHEET    5 AF2 5 TYR S 153  CYS S 156 -1  O  CYS S 156   N  ILE S 144           
SHEET    1 AF3 5 GLY T 162  ILE T 165  0                                        
SHEET    2 AF3 5 ALA T  36  CYS T  41 -1  N  ALA T  36   O  ILE T 165           
SHEET    3 AF3 5 GLY T  44  LEU T  52 -1  O  GLY T  48   N  ILE T  37           
SHEET    4 AF3 5 PHE T 209  GLY T 217 -1  O  GLU T 210   N  LYS T  51           
SHEET    5 AF3 5 GLU T 225  ILE T 226 -1  O  GLU T 225   N  TRP T 215           
SHEET    1 AF4 5 LEU T  66  ASP T  70  0                                        
SHEET    2 AF4 5 VAL T  73  GLY T  79 -1  O  MET T  75   N  PHE T  67           
SHEET    3 AF4 5 CYS T 133  SER T 141 -1  O  MET T 136   N  ALA T  76           
SHEET    4 AF4 5 GLY T 145  ILE T 151 -1  O  ILE T 151   N  PHE T 135           
SHEET    5 AF4 5 SER T 157  GLY T 159 -1  O  TYR T 158   N  MET T 150           
SHEET    1 AF5 5 ALA U 165  GLY U 169  0                                        
SHEET    2 AF5 5 THR U  38  ARG U  43 -1  N  ALA U  41   O  THR U 166           
SHEET    3 AF5 5 6V1 U  47  GLN U  53 -1  O  VAL U  51   N  VAL U  40           
SHEET    4 AF5 5 ILE U 215  THR U 221 -1  O  VAL U 220   N  ALA U  48           
SHEET    5 AF5 5 ARG U 228  ILE U 229 -1  O  ARG U 228   N  VAL U 219           
SHEET    1 AF6 5 LEU U  69  THR U  73  0                                        
SHEET    2 AF6 5 ILE U  76  GLY U  82 -1  O  ILE U  76   N  ILE U  72           
SHEET    3 AF6 5 CYS U 136  ASP U 144 -1  O  ILE U 141   N  GLY U  77           
SHEET    4 AF6 5 GLY U 148  CYS U 154 -1  O  TYR U 152   N  LEU U 140           
SHEET    5 AF6 5 TYR U 160  PHE U 163 -1  O  PHE U 163   N  VAL U 151           
SHEET    1 AF7 5 TYR V 124  MET V 127  0                                        
SHEET    2 AF7 5 ILE V   3  TYR V   8 -1  N  ILE V   3   O  MET V 127           
SHEET    3 AF7 5 GLY V  11  ASP V  17 -1  O  GLY V  15   N  ALA V   4           
SHEET    4 AF7 5 ILE V 173  SER V 179 -1  O  ASP V 174   N  ALA V  16           
SHEET    5 AF7 5 LEU V 183  THR V 190 -1  O  ASP V 184   N  VAL V 177           
SHEET    1 AF8 2 ALA V  20  GLU V  22  0                                        
SHEET    2 AF8 2 VAL V  25  ASP V  28 -1  O  VAL V  25   N  GLU V  22           
SHEET    1 AF9 5 ILE V  34  SER V  38  0                                        
SHEET    2 AF9 5 ILE V  41  GLY V  47 -1  O  CYS V  43   N  HIS V  35           
SHEET    3 AF9 5 ALA V  96  ASP V 104 -1  O  ALA V  97   N  ALA V  46           
SHEET    4 AF9 5 GLY V 107  ILE V 113 -1  O  TYR V 111   N  LEU V 100           
SHEET    5 AF9 5 THR V 119  LYS V 121 -1  O  ASP V 120   N  SER V 112           
SHEET    1 AG1 6 VAL V 211  PRO V 218  0                                        
SHEET    2 AG1 6 LYS W 193  LEU W 199 -1  O  THR W 198   N  LEU V 212           
SHEET    3 AG1 6 VAL W 184  GLU W 190 -1  N  VAL W 186   O  ARG W 197           
SHEET    4 AG1 6 CYS W  18  ASP W  24 -1  N  VAL W  19   O  ILE W 189           
SHEET    5 AG1 6 ALA W   9  LYS W  14 -1  N  MET W  11   O  ALA W  22           
SHEET    6 AG1 6 PHE W 135  GLY W 139 -1  O  SER W 138   N  VAL W  10           
SHEET    1 AG2 2 PHE W  27  ILE W  29  0                                        
SHEET    2 AG2 2 GLN W  32  THR W  35 -1  O  VAL W  34   N  PHE W  27           
SHEET    1 AG3 5 ILE W  41  PRO W  43  0                                        
SHEET    2 AG3 5 LEU W  48  GLY W  54 -1  O  ILE W  50   N  PHE W  42           
SHEET    3 AG3 5 THR W 104  LEU W 111 -1  O  VAL W 107   N  GLY W  51           
SHEET    4 AG3 5 PRO W 118  LEU W 123 -1  O  PHE W 119   N  GLY W 110           
SHEET    5 AG3 5 PRO W 129  VAL W 131 -1  O  MET W 130   N  SER W 122           
SHEET    1 AG4 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG4 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG4 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG4 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG4 5 GLY X 187  ASP X 190 -1  O  HIS X 189   N  ILE X 182           
SHEET    1 AG5 5 PHE X 129  HIS X 132  0                                        
SHEET    2 AG5 5 LEU X   4  GLN X   8 -1  N  GLY X   6   O  ALA X 130           
SHEET    3 AG5 5 VAL X  13  ASP X  18 -1  O  LEU X  14   N  ILE X   7           
SHEET    4 AG5 5 THR X 177  ASP X 184 -1  O  ARG X 181   N  VAL X  15           
SHEET    5 AG5 5 ILE X 194  SER X 195 -1  O  ILE X 194   N  PHE X 178           
SHEET    1 AG6 2 ALA X  21  SER X  23  0                                        
SHEET    2 AG6 2 VAL X  26  LYS X  29 -1  O  MET X  28   N  ALA X  21           
SHEET    1 AG7 5 MET X  35  SER X  39  0                                        
SHEET    2 AG7 5 ILE X  42  GLY X  48 -1  O  LEU X  44   N  PHE X  36           
SHEET    3 AG7 5 VAL X 100  ASP X 108 -1  O  ASN X 101   N  VAL X  47           
SHEET    4 AG7 5 GLY X 112  MET X 118 -1  O  MET X 118   N  LEU X 102           
SHEET    5 AG7 5 LEU X 124  LYS X 126 -1  O  ALA X 125   N  TYR X 117           
SHEET    1 AG8 5 THR Y 125  VAL Y 128  0                                        
SHEET    2 AG8 5 THR Y   3  PHE Y   8 -1  N  ALA Y   5   O  PHE Y 126           
SHEET    3 AG8 5 GLY Y  11  ALA Y  16 -1  O  ALA Y  15   N  LEU Y   4           
SHEET    4 AG8 5 ALA Y 173  ARG Y 180 -1  O  TYR Y 177   N  VAL Y  14           
SHEET    5 AG8 5 GLY Y 183  ASN Y 191 -1  O  ASP Y 190   N  VAL Y 174           
SHEET    1 AG9 2 ALA Y  20  ALA Y  22  0                                        
SHEET    2 AG9 2 TYR Y  25  SER Y  28 -1  O  SER Y  28   N  ALA Y  20           
SHEET    1 AH1 4 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AH1 4 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AH1 4 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AH1 4 ALA Y  46  GLY Y  47 -1  N  ALA Y  46   O  GLY Y  98           
SHEET    1 AH2 5 VAL Y  34  ASN Y  38  0                                        
SHEET    2 AH2 5 LEU Y  41  THR Y  44 -1  O  GLY Y  43   N  ILE Y  35           
SHEET    3 AH2 5 MET Y  97  ASP Y 105 -1  O  CYS Y 102   N  LEU Y  42           
SHEET    4 AH2 5 GLY Y 108  ASP Y 115 -1  O  VAL Y 114   N  THR Y  99           
SHEET    5 AH2 5 ARG Y 120  SER Y 122 -1  O  ILE Y 121   N  TYR Y 113           
SHEET    1 AH3 5 PHE Z 135  GLY Z 139  0                                        
SHEET    2 AH3 5 THR Z  11  ALA Z  16 -1  N  ILE Z  12   O  GLY Z 138           
SHEET    3 AH3 5 ALA Z  21  ASP Z  26 -1  O  ALA Z  24   N  LEU Z  13           
SHEET    4 AH3 5 ALA Z 192  THR Z 199 -1  O  ARG Z 194   N  SER Z  25           
SHEET    5 AH3 5 GLY Z 202  SER Z 209 -1  O  VAL Z 208   N  LEU Z 193           
SHEET    1 AH4 2 LEU Z  29  GLU Z  31  0                                        
SHEET    2 AH4 2 SER Z  34  THR Z  37 -1  O  HIS Z  36   N  LEU Z  29           
SHEET    1 AH5 5 CYS Z  43  THR Z  47  0                                        
SHEET    2 AH5 5 THR Z  50  GLY Z  56 -1  O  THR Z  50   N  LEU Z  46           
SHEET    3 AH5 5 VAL Z 106  LEU Z 113 -1  O  GLY Z 111   N  VAL Z  51           
SHEET    4 AH5 5 GLY Z 119  PHE Z 124 -1  O  TYR Z 122   N  ILE Z 110           
SHEET    5 AH5 5 TYR Z 130  ASP Z 133 -1  O  ASP Z 133   N  VAL Z 121           
SHEET    1 AH6 5 LEU a  33  PHE a  36  0                                        
SHEET    2 AH6 5 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH6 5 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH6 5 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH6 5 ILE a  42  ASN a  46 -1  N  MET a  43   O  LEU a  51           
SHEET    1 AH7 7 LEU a  33  PHE a  36  0                                        
SHEET    2 AH7 7 GLY a  28  TYR a  30 -1  N  TYR a  30   O  LEU a  33           
SHEET    3 AH7 7 VAL a   6  GLY a   8 -1  N  THR a   7   O  SER a  29           
SHEET    4 AH7 7 THR a  49  ASP a  56 -1  O  GLY a  55   N  GLY a   8           
SHEET    5 AH7 7 ASN a 108  ALA a 116 -1  O  GLY a 113   N  MET a  50           
SHEET    6 AH7 7 GLU a 119  VAL a 125 -1  O  VAL a 125   N  MET a 110           
SHEET    7 AH7 7 ALA a 131  GLU a 133 -1  O  TYR a 132   N  TYR a 124           
SHEET    1 AH8 5 SER a 136  ALA a 138  0                                        
SHEET    2 AH8 5 VAL a  11  PHE a  16 -1  N  GLY a  13   O  LEU a 137           
SHEET    3 AH8 5 GLY a  19  ASP a  25 -1  O  GLY a  19   N  PHE a  16           
SHEET    4 AH8 5 PHE a 187  THR a 193 -1  O  ALA a 190   N  ILE a  22           
SHEET    5 AH8 5 GLY a 196  LEU a 203 -1  O  GLU a 200   N  ILE a 189           
SHEET    1 AH9 5 PHE b 125  GLY b 128  0                                        
SHEET    2 AH9 5 ILE b   3  PHE b   8 -1  N  ALA b   5   O  ALA b 126           
SHEET    3 AH9 5 GLY b  11  ALA b  16 -1  O  GLY b  15   N  MET b   4           
SHEET    4 AH9 5 ILE b 174  ALA b 180 -1  O  ALA b 177   N  LEU b  14           
SHEET    5 AH9 5 GLY b 183  LEU b 189 -1  O  LEU b 189   N  ILE b 174           
SHEET    1 AI1 3 TYR b  25  ASN b  28  0                                        
SHEET    2 AI1 3 THR b  20  THR b  22 -1  N  THR b  20   O  ASN b  28           
SHEET    3 AI1 3 ILE h   3  THR h   4 -1  O  THR h   4   N  THR b  21           
SHEET    1 AI2 5 LEU b  34  HIS b  38  0                                        
SHEET    2 AI2 5 ILE b  41  GLY b  47 -1  O  ILE b  41   N  ILE b  37           
SHEET    3 AI2 5 ALA b  96  ASP b 104 -1  O  ILE b  99   N  CYS b  44           
SHEET    4 AI2 5 GLY b 108  VAL b 114 -1  O  TYR b 112   N  ILE b 100           
SHEET    5 AI2 5 VAL b 121  ARG b 122 -1  O  VAL b 121   N  SER b 113           
LINK         C   ILE C  62                 N   YCM C  63     1555   1555  1.33  
LINK         C   YCM C  63                 N   ALA C  64     1555   1555  1.33  
LINK         C   THR E 147                 N   6V1 E 148     1555   1555  1.34  
LINK         C   6V1 E 148                 N   PRO E 149     1555   1555  1.33  
LINK         OG1 THR G  14                 K     K G 303     1555   1555  2.70  
LINK         C   ASP G  46                 N   6V1 G  47     1555   1555  1.33  
LINK         C   6V1 G  47                 N   ALA G  48     1555   1555  1.33  
LINK         O   TYR G 125                 K     K G 303     1555   1555  2.55  
LINK         O   ASN G 128                 K     K G 303     1555   1555  2.56  
LINK         O   MET G 131                 K     K G 303     1555   1555  2.45  
LINK         C   CYS G 136                 N   YCM G 137     1555   1555  1.32  
LINK         C   YCM G 137                 N   MET G 138     1555   1555  1.33  
LINK         C   TYR G 160                 N   6V1 G 161     1555   1555  1.32  
LINK         C   6V1 G 161                 N   GLY G 162     1555   1555  1.32  
LINK         N   THR H   1                 C23 6VO c   5     1555   1555  1.49  
LINK         OG1 THR H   1                 C21 6VO c   5     1555   1555  1.43  
LINK         OE1 GLN H  91                MG    MG H 301     1555   1555  2.51  
LINK         O   ILE H 163                MG    MG H 302     1555   1555  2.26  
LINK         O   ASP H 166                MG    MG H 302     1555   1555  2.29  
LINK         O   SER H 169                MG    MG H 302     1555   1555  2.32  
LINK         O   VAL I 174                MG    MG I 301     1555   1555  2.33  
LINK         O   ASP I 177                MG    MG I 301     1555   1555  2.27  
LINK         O   SER I 180                MG    MG I 301     1555   1555  2.26  
LINK         O   ASP I 204                MG    MG I 304     1555   1555  2.17  
LINK         C   ASP J  90                 N   6V1 J  91     1555   1555  1.33  
LINK         C   6V1 J  91                 N   LEU J  92     1555   1555  1.34  
LINK         N   THR K   1                 C23 6VO d   5     1555   1555  1.49  
LINK         OG1 THR K   1                 C21 6VO d   5     1555   1555  1.42  
LINK         O   THR K 164                MG    MG K 301     1555   1555  2.26  
LINK         O   ASP K 167                MG    MG K 301     1555   1555  2.12  
LINK         O   SER K 170                MG    MG K 301     1555   1555  2.44  
LINK         O   ALA L 183                 K     K L 302     1555   1555  2.74  
LINK         O   ASP L 186                 K     K L 302     1555   1555  3.00  
LINK         O   THR L 189                 K     K L 302     1555   1555  2.84  
LINK         O   ASP L 213                MG    MG L 303     1555   1555  2.23  
LINK         N   THR N   1                 C23 6VO e   5     1555   1555  1.48  
LINK         OG1 THR N   1                 C21 6VO e   5     1555   1555  1.43  
LINK         O   MET N 164                 K     K N 306     1555   1555  2.51  
LINK         O   ASP N 167                 K     K N 306     1555   1555  2.74  
LINK         O   SER N 170                 K     K N 306     1555   1555  2.72  
LINK         C   ILE Q  62                 N   YCM Q  63     1555   1555  1.33  
LINK         C   YCM Q  63                 N   ALA Q  64     1555   1555  1.33  
LINK         C   THR S 147                 N   6V1 S 148     1555   1555  1.34  
LINK         C   6V1 S 148                 N   PRO S 149     1555   1555  1.34  
LINK         OG1 THR U  14                 K     K U 302     1555   1555  2.80  
LINK         C   ASP U  46                 N   6V1 U  47     1555   1555  1.33  
LINK         C   6V1 U  47                 N   ALA U  48     1555   1555  1.33  
LINK         O   TYR U 125                 K     K U 302     1555   1555  2.56  
LINK         O   ASN U 128                 K     K U 302     1555   1555  2.54  
LINK         O   MET U 131                 K     K U 302     1555   1555  2.33  
LINK         C   CYS U 136                 N   YCM U 137     1555   1555  1.32  
LINK         C   YCM U 137                 N   MET U 138     1555   1555  1.33  
LINK         C   TYR U 160                 N   6V1 U 161     1555   1555  1.32  
LINK         C   6V1 U 161                 N   GLY U 162     1555   1555  1.33  
LINK         N   THR V   1                 C23 6VO f   5     1555   1555  1.49  
LINK         OG1 THR V   1                 C21 6VO f   5     1555   1555  1.43  
LINK         OE1 GLN V  91                MG    MG V 301     1555   1555  2.58  
LINK         O   ILE V 163                MG    MG L 303     1555   1555  2.42  
LINK         O   ASP V 166                MG    MG L 303     1555   1555  2.32  
LINK         O   SER V 169                MG    MG L 303     1555   1555  2.28  
LINK         O   VAL W 174                MG    MG W 301     1555   1555  2.26  
LINK         O   ASP W 177                MG    MG W 301     1555   1555  2.22  
LINK         O   SER W 180                MG    MG W 301     1555   1555  2.24  
LINK         O   ASP W 204                MG    MG K 301     1555   1555  2.20  
LINK         C   ASP X  90                 N   6V1 X  91     1555   1555  1.34  
LINK         C   6V1 X  91                 N   LEU X  92     1555   1555  1.34  
LINK         N   THR Y   1                 C23 6VO g   5     1555   1555  1.51  
LINK         OG1 THR Y   1                 C21 6VO g   5     1555   1555  1.42  
LINK         O   THR Y 164                MG    MG I 304     1555   1555  2.29  
LINK         O   ASP Y 167                MG    MG I 304     1555   1555  2.30  
LINK         O   SER Y 170                MG    MG I 304     1555   1555  2.34  
LINK         O   ALA Z 183                 K     K Z 302     1555   1555  2.76  
LINK         O   ASP Z 186                 K     K Z 302     1555   1555  2.85  
LINK         O   THR Z 189                 K     K Z 302     1555   1555  2.86  
LINK         O   ASP Z 213                MG    MG H 302     1555   1555  2.29  
LINK         N   THR b   1                 C23 6VO h   5     1555   1555  1.49  
LINK         OG1 THR b   1                 C21 6VO h   5     1555   1555  1.44  
LINK         O   MET b 164                 K     K b 306     1555   1555  2.61  
LINK         O   ASP b 167                 K     K b 306     1555   1555  2.93  
LINK         O   SER b 170                 K     K b 306     1555   1555  2.91  
LINK         C   ACE c   1                 N   IML c   2     1555   1555  1.37  
LINK         C   IML c   2                 N   ILE c   3     1555   1555  1.35  
LINK         C   THR c   4                 N3  6VO c   5     1555   1555  1.35  
LINK         C   ACE d   1                 N   IML d   2     1555   1555  1.32  
LINK         C   IML d   2                 N   ILE d   3     1555   1555  1.33  
LINK         C   THR d   4                 N3  6VO d   5     1555   1555  1.33  
LINK         C   ACE e   1                 N   IML e   2     1555   1555  1.34  
LINK         C   IML e   2                 N   ILE e   3     1555   1555  1.34  
LINK         C   THR e   4                 N3  6VO e   5     1555   1555  1.34  
LINK         C   ACE f   1                 N   IML f   2     1555   1555  1.35  
LINK         C   IML f   2                 N   ILE f   3     1555   1555  1.34  
LINK         C   THR f   4                 N3  6VO f   5     1555   1555  1.34  
LINK         C   ACE g   1                 N   IML g   2     1555   1555  1.31  
LINK         C   IML g   2                 N   ILE g   3     1555   1555  1.34  
LINK         C   THR g   4                 N3  6VO g   5     1555   1555  1.33  
LINK         C   ACE h   1                 N   IML h   2     1555   1555  1.34  
LINK         C   IML h   2                 N   ILE h   3     1555   1555  1.34  
LINK         C   THR h   4                 N3  6VO h   5     1555   1555  1.34  
LINK         K     K G 303                 O   HOH G 450     1555   1555  2.79  
LINK        MG    MG H 301                 O   HOH N 410     1555   1555  2.42  
LINK        MG    MG H 301                 O   HOH H 515     1555   1555  1.90  
LINK        MG    MG H 301                 O   HOH N 492     1555   1555  2.32  
LINK        MG    MG H 301                 O   HOH N 411     1555   1555  2.47  
LINK        MG    MG H 301                 O   HOH N 470     1555   1555  2.55  
LINK        MG    MG H 302                 O   HOH H 478     1555   1555  2.56  
LINK        MG    MG I 301                 O   HOH I 414     1555   1555  2.49  
LINK        MG    MG I 301                 O   HOH I 477     1555   1555  2.27  
LINK        MG    MG I 304                 O   HOH Y 442     1555   1555  2.77  
LINK        MG    MG J 301                 O   HOH J 406     1555   1555  2.18  
LINK        MG    MG J 301                 O   HOH J 453     1555   1555  2.23  
LINK        MG    MG J 301                 O   HOH J 495     1555   1555  1.87  
LINK        MG    MG J 301                 O   HOH J 516     1555   1555  2.28  
LINK        MG    MG J 301                 O   HOH K 483     1555   1555  1.99  
LINK        MG    MG J 301                 O   HOH J 445     1555   1555  2.44  
LINK        MG    MG K 301                 O   HOH K 466     1555   1555  2.82  
LINK         K     K L 302                 O   HOH L 421     1555   1555  2.46  
LINK         K     K L 302                 O   HOH L 433     1555   1555  3.26  
LINK         K     K L 302                 O   HOH L 444     1555   1555  3.23  
LINK        MG    MG L 303                 O   HOH V 466     1555   1555  2.74  
LINK         K     K N 306                 O   HOH N 530     1555   1555  2.54  
LINK         K     K N 306                 O   HOH N 454     1555   1555  2.72  
LINK         K     K N 306                 O   HOH N 490     1555   1555  2.89  
LINK         K     K U 302                 O   HOH U 423     1555   1555  2.87  
LINK        MG    MG V 301                 O   HOH V 446     1555   1555  1.97  
LINK        MG    MG V 301                 O   HOH V 458     1555   1555  2.33  
LINK        MG    MG V 301                 O   HOH b 405     1555   1555  2.42  
LINK        MG    MG V 301                 O   HOH b 478     1555   1555  2.45  
LINK        MG    MG V 301                 O   HOH b 445     1555   1555  2.51  
LINK        MG    MG W 301                 O   HOH W 440     1555   1555  2.04  
LINK        MG    MG W 301                 O   HOH W 459     1555   1555  2.36  
LINK        MG    MG X 301                 O   HOH X 402     1555   1555  2.30  
LINK        MG    MG X 301                 O   HOH X 432     1555   1555  2.04  
LINK        MG    MG X 301                 O   HOH X 505     1555   1555  2.30  
LINK        MG    MG X 301                 O   HOH Y 508     1555   1555  2.18  
LINK        MG    MG X 301                 O   HOH X 441     1555   1555  1.96  
LINK        MG    MG X 301                 O   HOH X 480     1555   1555  2.28  
LINK         K     K Z 302                 O   HOH Z 464     1555   1555  2.97  
LINK         K     K Z 302                 O   HOH Z 434     1555   1555  2.59  
LINK         K     K Z 302                 O   HOH Z 456     1555   1555  3.08  
LINK         K     K b 306                 O   HOH b 410     1555   1555  2.76  
LINK         K     K b 306                 O   HOH b 459     1555   1555  2.78  
CISPEP   1 VAL B  203    SER B  204          0         8.37                     
CISPEP   2 LYS C   47    LYS C   48          0         2.69                     
CISPEP   3 GLY C  202    GLY C  203          0         5.50                     
CISPEP   4 GLY C  203    LYS C  204          0        26.81                     
CISPEP   5 ARG H  187    PRO H  188          0        -3.66                     
CISPEP   6 ARG H  187    PRO H  188          0        -3.74                     
CISPEP   7 GLY M  201    PRO M  202          0        -7.47                     
CISPEP   8 ILE P   52    HIS P   53          0       -21.38                     
CISPEP   9 LYS Q  204    ASN Q  205          0       -12.49                     
CISPEP  10 LEU Q  220    ASN Q  221          0        23.12                     
CISPEP  11 GLU S  234    GLY S  235          0       -22.33                     
CISPEP  12 GLU S  238    ARG S  239          0        -7.45                     
CISPEP  13 GLY T    6    TYR T    7          0        -6.69                     
CISPEP  14 ARG V  187    PRO V  188          0        -4.87                     
CISPEP  15 GLY a  201    PRO a  202          0        -6.34                     
CISPEP  16 GLY a  201    PRO a  202          0        -5.85                     
SITE     1 AC1  3 SER A   6  ARG C   5  HOH C 405                               
SITE     1 AC2  1 ARG A 219                                                     
SITE     1 AC3  3 HIS A  87  ARG A  90  LYS G 116                               
SITE     1 AC4  2 THR A  68  HOH A 441                                          
SITE     1 AC5  4 GLU B  70  GLN B  95   CL B 302  HOH B 491                    
SITE     1 AC6  3 ASN B  69   CL B 301  HOH B 414                               
SITE     1 AC7  3 VAL C  26  ILE C 161  GLY C 162                               
SITE     1 AC8  3 ARG C  86  ARG C 117  HOH C 404                               
SITE     1 AC9  3 ILE D  31  GLY D 171  SER D 174                               
SITE     1 AD1  5 6V1 E 148  ILE E 161  GLY E 162  SER E 165                    
SITE     2 AD1  5 HOH E 493                                                     
SITE     1 AD2  2 6V1 E 148  SER E 150                                          
SITE     1 AD3  2 THR D 161  LEU E  77                                          
SITE     1 AD4  4 GLY E  32  SER E  33  LYS E  62  GLY E  76                    
SITE     1 AD5  5 VAL F  30  ILE F 165  GLY F 166  ARG F 169                    
SITE     2 AD5  5 HOH F 403                                                     
SITE     1 AD6  3 HOH G 411  HOH G 474  HOH N 480                               
SITE     1 AD7  4 LYS G 186  GLU G 192  GLN G 193  THR G 197                    
SITE     1 AD8  5 THR G  14  TYR G 125  ASN G 128  MET G 131                    
SITE     2 AD8  5 HOH G 450                                                     
SITE     1 AD9  6 GLN H  91  HOH H 515  HOH N 410  HOH N 411                    
SITE     2 AD9  6 HOH N 470  HOH N 492                                          
SITE     1 AE1  5 ILE H 163  ASP H 166  SER H 169  HOH H 478                    
SITE     2 AE1  5 ASP Z 213                                                     
SITE     1 AE2  4 ASN H  80  ARG H  81  HOH H 522  HOH N 423                    
SITE     1 AE3  3 LEU H  58  TYR H  90  TYR I  95                               
SITE     1 AE4  5 VAL I 174  ASP I 177  SER I 180  HOH I 414                    
SITE     2 AE4  5 HOH I 477                                                     
SITE     1 AE5  2 ARG I  65  ARG I  69                                          
SITE     1 AE6  4 GLU I  96  LYS I  97  HOH I 502  ASP J  90                    
SITE     1 AE7  5 ASP I 204  THR Y 164  ASP Y 167  SER Y 170                    
SITE     2 AE7  5 HOH Y 442                                                     
SITE     1 AE8  6 HOH J 406  HOH J 445  HOH J 453  HOH J 495                    
SITE     2 AE8  6 HOH J 516  HOH K 483                                          
SITE     1 AE9  6 THR K 164  ASP K 167  ALA K 168  SER K 170                    
SITE     2 AE9  6 HOH K 466  ASP W 204                                          
SITE     1 AF1  3 GLY K 129  SER K 130  6VO d   5                               
SITE     1 AF2  2 LYS K  32  ASN K 175                                          
SITE     1 AF3  1 ARG K  69                                                     
SITE     1 AF4  2 ILE K 121  SER K 122                                          
SITE     1 AF5  3 HOH K 441  SER L  98  PHE L 101                               
SITE     1 AF6  2 PHE L  33   CL f 101                                          
SITE     1 AF7  4 ALA L 183  ASP L 186  THR L 189  HOH L 421                    
SITE     1 AF8  5 ASP L 213  ILE V 163  ASP V 166  SER V 169                    
SITE     2 AF8  5 HOH V 466                                                     
SITE     1 AF9  4 PHE M  36  ARG M  37  ASN M  38  HOH N 401                    
SITE     1 AG1  4 ARG M  35  PRO N 115  MET N 116   CL N 303                    
SITE     1 AG2  1 ARG M  44                                                     
SITE     1 AG3  4 THR N  31  ARG N  45  GLN N  53  6VO e   5                    
SITE     1 AG4  4 GLY N  47  GLY N 129  SER N 130  6VO e   5                    
SITE     1 AG5  6 ARG M  35   CL M 302  SER N  46  GLY N  97                    
SITE     2 AG5  6 GLY N 128  GLY N 129                                          
SITE     1 AG6  5 ARG N  19  ARG N  29  GLY N 171  GLY N 172                    
SITE     2 AG6  5 HOH a 420                                                     
SITE     1 AG7  5 TYR G 103  PHE H  88  TYR N  90  HOH N 446                    
SITE     2 AG7  5 HOH N 503                                                     
SITE     1 AG8  6 MET N 164  ASP N 167  SER N 170  HOH N 454                    
SITE     2 AG8  6 HOH N 490  HOH N 530                                          
SITE     1 AG9  3 SER O   6  ARG Q   5  HOH Q 445                               
SITE     1 AH1  1 TYR O 100                                                     
SITE     1 AH2  2 ARG O 218  ARG O 219                                          
SITE     1 AH3  3 HIS O  87  ARG O  90  SER V  69                               
SITE     1 AH4  3 GLU P  70  GLN P  95  HOH P 496                               
SITE     1 AH5  1 ARG Q  95                                                     
SITE     1 AH6  3 VAL Q  26  ILE Q 161  GLY Q 162                               
SITE     1 AH7  4 ILE R 170  GLY R 171  SER R 174  HOH R 491                    
SITE     1 AH8  2 THR R 161  THR S  78                                          
SITE     1 AH9  4 6V1 S 148  ILE S 161  GLY S 162  SER S 165                    
SITE     1 AI1  2 SER S 150  ASN S 152                                          
SITE     1 AI2  4 GLY S  32  SER S  33  LYS S  62  GLY S  76                    
SITE     1 AI3  1 HOH b 434                                                     
SITE     1 AI4  5 THR U  14  TYR U 125  ASN U 128  MET U 131                    
SITE     2 AI4  5 HOH U 423                                                     
SITE     1 AI5  7 GLN V  91  HOH V 446  HOH V 458  ASP b  93                    
SITE     2 AI5  7 HOH b 405  HOH b 445  HOH b 478                               
SITE     1 AI6  4 VAL V  77  ASN V  80  ARG V  81  HOH b 401                    
SITE     1 AI7  5 VAL W 174  ASP W 177  SER W 180  HOH W 440                    
SITE     2 AI7  5 HOH W 459                                                     
SITE     1 AI8  2 ARG W  65  ARG W  69                                          
SITE     1 AI9  3 GLU W  96  LYS W  97  HOH W 434                               
SITE     1 AJ1  6 HOH X 402  HOH X 432  HOH X 441  HOH X 480                    
SITE     2 AJ1  6 HOH X 505  HOH Y 508                                          
SITE     1 AJ2  3 GLY Y 129  SER Y 130  6VO g   5                               
SITE     1 AJ3  2 TYR Y  66  ARG Y  69                                          
SITE     1 AJ4  2 LYS Y  32  ASN Y 175                                          
SITE     1 AJ5  2 ILE Y 121  SER Y 122                                          
SITE     1 AJ6  1 HOH Y 454                                                     
SITE     1 AJ7  5 TYR Y  90  TYR Z  97  SER Z  98  PHE Z 101                    
SITE     2 AJ7  5 HOH Z 461                                                     
SITE     1 AJ8  6 ALA Z 183  ASP Z 186  THR Z 189  HOH Z 434                    
SITE     2 AJ8  6 HOH Z 456  HOH Z 464                                          
SITE     1 AJ9  4 PHE a  36  ARG a  37  ASN a  38  HOH b 429                    
SITE     1 AK1  4 ARG a  35  PRO b 115  MET b 116   CL b 302                    
SITE     1 AK2  2 MET a  43  ARG a  44                                          
SITE     1 AK3  4 SER H 129  PHE Z  33  TYR a 141  HOH a 498                    
SITE     1 AK4  4 GLY b  47  GLY b 129  SER b 130  6VO h   5                    
SITE     1 AK5  6 ARG a  35   CL a 302  SER b  46  GLY b  97                    
SITE     2 AK5  6 GLY b 128  GLY b 129                                          
SITE     1 AK6  5 HOH M 434  ARG b  19  ARG b  29  GLY b 171                    
SITE     2 AK6  5 GLY b 172                                                     
SITE     1 AK7  5 THR b  31  ARG b  45  GLN b  53  HOH b 442                    
SITE     2 AK7  5 6VO h   5                                                     
SITE     1 AK8  5 TYR U 103  PHE V  88  ARG V  89  TYR b  61                    
SITE     2 AK8  5 HOH b 497                                                     
SITE     1 AK9  5 MET b 164  ASP b 167  SER b 170  HOH b 410                    
SITE     2 AK9  5 HOH b 459                                                     
SITE     1 AL1  4 GLY H 128  SER H 129  HOH H 536  6VO c   5                    
SITE     1 AL2  4 1PE L 301  GLY V 128  SER V 129  6VO f   5                    
SITE     1 AL3 14 ALA E  25  PRO E 127  TYR E 128  VAL E 130                    
SITE     2 AL3 14 GLN E 146  THR E 147  SER E 150  ALA E 151                    
SITE     3 AL3 14 ASN E 152   CL E 301   CL E 302  HOH E 427                    
SITE     4 AL3 14 HOH E 438  HOH E 450                                          
SITE     1 AL4 11 THR H   1  ALA H  20  THR H  21  CYS H  31                    
SITE     2 AL4 11 GLY H  47  THR H  52  SER H 129  GLY H 168                    
SITE     3 AL4 11 HOH H 417  THR c   4   CL c 101                               
SITE     1 AL5 11 THR H   1  ALA H  20  THR H  21  CYS H  31                    
SITE     2 AL5 11 GLY H  47  THR H  52  SER H 129  GLY H 168                    
SITE     3 AL5 11 HOH H 417  THR c   4   CL c 101                               
SITE     1 AL6  8 THR K   1  ARG K  19  ALA K  20  GLY K  47                    
SITE     2 AL6  8 SER K 130  TYR K 169   CL K 302  THR d   4                    
SITE     1 AL7  8 THR K   1  ARG K  19  ALA K  20  GLY K  47                    
SITE     2 AL7  8 SER K 130  TYR K 169   CL K 302  THR d   4                    
SITE     1 AL8 10 THR N   1  ARG N  19  THR N  20  ARG N  45                    
SITE     2 AL8 10 GLY N  47  SER N 130  SER N 169   CL N 301                    
SITE     3 AL8 10  CL N 302  THR e   4                                          
SITE     1 AL9 10 THR N   1  ARG N  19  THR N  20  ARG N  45                    
SITE     2 AL9 10 GLY N  47  SER N 130  SER N 169   CL N 301                    
SITE     3 AL9 10  CL N 302  THR e   4                                          
SITE     1 AM1 12 ALA S  25  PRO S 127  TYR S 128  VAL S 130                    
SITE     2 AM1 12 GLN S 146  THR S 147  SER S 150  ALA S 151                    
SITE     3 AM1 12 ASN S 152   CL S 301  HOH S 421  HOH S 442                    
SITE     1 AM2 10 THR V   1  ALA V  20  THR V  21  CYS V  31                    
SITE     2 AM2 10 GLY V  47  SER V 129  GLY V 168  HOH V 430                    
SITE     3 AM2 10 THR f   4   CL f 101                                          
SITE     1 AM3 10 THR V   1  ALA V  20  THR V  21  CYS V  31                    
SITE     2 AM3 10 GLY V  47  SER V 129  GLY V 168  HOH V 430                    
SITE     3 AM3 10 THR f   4   CL f 101                                          
SITE     1 AM4  9 THR Y   1  ARG Y  19  ALA Y  20  GLY Y  47                    
SITE     2 AM4  9 SER Y 130  TYR Y 169   CL Y 301  HOH Y 428                    
SITE     3 AM4  9 THR g   4                                                     
SITE     1 AM5  9 THR Y   1  ARG Y  19  ALA Y  20  GLY Y  47                    
SITE     2 AM5  9 SER Y 130  TYR Y 169   CL Y 301  HOH Y 428                    
SITE     3 AM5  9 THR g   4                                                     
SITE     1 AM6 12 THR b   1  ARG b  19  THR b  20  THR b  21                    
SITE     2 AM6 12 ARG b  45  GLY b  47  THR b  52  SER b 130                    
SITE     3 AM6 12 SER b 169   CL b 301   CL b 304  THR h   4                    
SITE     1 AM7 12 THR b   1  ARG b  19  THR b  20  THR b  21                    
SITE     2 AM7 12 ARG b  45  GLY b  47  THR b  52  SER b 130                    
SITE     3 AM7 12 SER b 169   CL b 301   CL b 304  THR h   4                    
SITE     1 AM8 11 THR H   1  ALA H  20  THR H  21  CYS H  31                    
SITE     2 AM8 11 GLY H  47  THR H  52  SER H 129  GLY H 168                    
SITE     3 AM8 11 HOH H 417  THR c   4   CL c 101                               
SITE     1 AM9  8 THR K   1  ARG K  19  ALA K  20  GLY K  47                    
SITE     2 AM9  8 SER K 130  TYR K 169   CL K 302  THR d   4                    
SITE     1 AN1 10 THR N   1  ARG N  19  THR N  20  ARG N  45                    
SITE     2 AN1 10 GLY N  47  SER N 130  SER N 169   CL N 301                    
SITE     3 AN1 10  CL N 302  THR e   4                                          
SITE     1 AN2 10 THR V   1  ALA V  20  THR V  21  CYS V  31                    
SITE     2 AN2 10 GLY V  47  SER V 129  GLY V 168  HOH V 430                    
SITE     3 AN2 10 THR f   4   CL f 101                                          
SITE     1 AN3  9 THR Y   1  ARG Y  19  ALA Y  20  GLY Y  47                    
SITE     2 AN3  9 SER Y 130  TYR Y 169   CL Y 301  HOH Y 428                    
SITE     3 AN3  9 THR g   4                                                     
SITE     1 AN4 12 THR b   1  ARG b  19  THR b  20  THR b  21                    
SITE     2 AN4 12 ARG b  45  GLY b  47  THR b  52  SER b 130                    
SITE     3 AN4 12 SER b 169   CL b 301   CL b 304  THR h   4                    
SITE     1 AN5 12 ARG U  43  GLY U  44  LYS U  45  ALA U  48                    
SITE     2 AN5 12 PRO U 149  THR U 194  VAL U 195  VAL U 219                    
SITE     3 AN5 12 VAL U 220  THR U 221  VAL U 222  ARG U 228                    
SITE     1 AN6 11 VAL U  42  ARG U  43  GLY U  44  ASP U  46                    
SITE     2 AN6 11 VAL U  49  PRO U 149  THR U 194  VAL U 195                    
SITE     3 AN6 11 VAL U 219  VAL U 220  ARG U 228                               
SITE     1 AN7 12 LYS O  49  LYS O  50  TYR O  56  ASP O  57                    
SITE     2 AN7 12 SER O  60  VAL O  61  LYS U 116  TYR U 152                    
SITE     3 AN7 12 LYS U 153  TYR U 159  GLY U 162  PHE U 163                    
SITE     1 AN8 10 LYS O  49  LYS O  50  TYR O  56  ASP O  57                    
SITE     2 AN8 10 SER O  60  VAL U 151  TYR U 152  LYS U 153                    
SITE     3 AN8 10 TYR U 160  PHE U 163                                          
SITE     1 AN9 16 ARG W  65  PHE X  56  TYR X  59  ARG X  86                    
SITE     2 AN9 16 ASN X  87  LEU X  88  ALA X  89  LEU X  92                    
SITE     3 AN9 16 ARG X  93  SER X  94  THR X  96  PRO X  97                    
SITE     4 AN9 16 TYR X  98  HOH X 425  HOH X 429  HOH X 453                    
SITE     1 AO1 15 PHE X  56  TYR X  59  ASN X  87  LEU X  88                    
SITE     2 AO1 15 ALA X  89  ASP X  90  ARG X  93  SER X  94                    
SITE     3 AO1 15 THR X  96  PRO X  97  TYR X  98  LEU X 121                    
SITE     4 AO1 15 HOH X 408  HOH X 453  HOH X 458                               
SITE     1 AO2  7 GLU H  22  THR H  48  GLU I 105  ASP I 124                    
SITE     2 AO2  7 LEU I 125  ILE c   3  THR c   4                               
SITE     1 AO3 11 ALA H  20  THR H  21  GLU H  22  THR H  48                    
SITE     2 AO3 11 ALA H  49  ASP I 124  LEU I 125  CYS I 128                    
SITE     3 AO3 11 HOH I 406  ACE c   1  THR c   4                               
SITE     1 AO4  3 TYR L 107  PRO L 126  ILE d   3                               
SITE     1 AO5  9 ALA K  20  THR K  21  ALA K  49  TYR L 107                    
SITE     2 AO5  9 ASP L 125  PRO L 126  HOH L 408  ACE d   1                    
SITE     3 AO5  9 THR d   4                                                     
SITE     1 AO6  3 THR N  22  HOH N 466  ILE e   3                               
SITE     1 AO7  9 TYR H 114  THR N  20  THR N  21  THR N  22                    
SITE     2 AO7  9 ALA N  49  HOH N 464  HOH N 466  ACE e   1                    
SITE     3 AO7  9 THR e   4                                                     
SITE     1 AO8  5 GLU W 105  ASP W 124  LEU W 125  ILE f   3                    
SITE     2 AO8  5 THR f   4                                                     
SITE     1 AO9 10 ALA V  20  THR V  21  GLU V  22  ALA V  49                    
SITE     2 AO9 10 HOH V 414  ASP W 124  LEU W 125  CYS W 128                    
SITE     3 AO9 10 ACE f   1  THR f   4                                          
SITE     1 AP1  3 TYR Z 107  PRO Z 126  ILE g   3                               
SITE     1 AP2  9 ALA Y  20  THR Y  21  ALA Y  49  TYR Z 107                    
SITE     2 AP2  9 ASP Z 125  PRO Z 126  HOH Z 411  ACE g   1                    
SITE     3 AP2  9 THR g   4                                                     
SITE     1 AP3  2 THR b  22  ILE h   3                                          
SITE     1 AP4  7 SER V 118  THR b  21  THR b  22  ALA b  49                    
SITE     2 AP4  7 ACE h   1  THR h   4  HOH h 101                               
CRYST1  113.070  202.370  314.790  90.00  90.00  90.00 P 21 21 21   24          
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      0.008844  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004941  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003177        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system