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Database: PDB
Entry: 2ZJP
LinkDB: 2ZJP
Original site: 2ZJP 
HEADER    RIBOSOME/ANTIBIOTIC                     07-MAR-08   2ZJP              
TITLE     THIOPEPTIDE ANTIBIOTIC NOSIHEPTIDE BOUND TO THE LARGE RIBOSOMAL       
TITLE    2 SUBUNIT OF DEINOCOCCUS RADIODURANS                                   
CAVEAT     2ZJP    U X 2592 HAS WRONG CHIRALITY FOR A D-NUCLEIC ACID            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 50S RIBOSOMAL PROTEIN L33;                                 
COMPND   3 CHAIN: 1;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 50S RIBOSOMAL PROTEIN L34;                                 
COMPND   6 CHAIN: 2;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 50S RIBOSOMAL PROTEIN L35;                                 
COMPND   9 CHAIN: 3;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 50S RIBOSOMAL PROTEIN L36;                                 
COMPND  12 CHAIN: 4;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: NOSIHEPTIDE;                                               
COMPND  15 CHAIN: 5;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 50S RIBOSOMAL PROTEIN L2;                                  
COMPND  18 CHAIN: A;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 50S RIBOSOMAL PROTEIN L3;                                  
COMPND  21 CHAIN: B;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 50S RIBOSOMAL PROTEIN L4;                                  
COMPND  24 CHAIN: C;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 50S RIBOSOMAL PROTEIN L5;                                  
COMPND  27 CHAIN: D;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 50S RIBOSOMAL PROTEIN L6;                                  
COMPND  30 CHAIN: E;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 50S RIBOSOMAL PROTEIN L11;                                 
COMPND  33 CHAIN: F;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 50S RIBOSOMAL PROTEIN L13;                                 
COMPND  36 CHAIN: G;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 50S RIBOSOMAL PROTEIN L14;                                 
COMPND  39 CHAIN: H;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: 50S RIBOSOMAL PROTEIN L15;                                 
COMPND  42 CHAIN: I;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: 50S RIBOSOMAL PROTEIN L16;                                 
COMPND  45 CHAIN: J;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: 50S RIBOSOMAL PROTEIN L17;                                 
COMPND  48 CHAIN: K;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: 50S RIBOSOMAL PROTEIN L18;                                 
COMPND  51 CHAIN: L;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: 50S RIBOSOMAL PROTEIN L19;                                 
COMPND  54 CHAIN: M;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: 50S RIBOSOMAL PROTEIN L20;                                 
COMPND  57 CHAIN: N;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: 50S RIBOSOMAL PROTEIN L21;                                 
COMPND  60 CHAIN: O;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: 50S RIBOSOMAL PROTEIN L22;                                 
COMPND  63 CHAIN: P;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: 50S RIBOSOMAL PROTEIN L23;                                 
COMPND  66 CHAIN: Q;                                                            
COMPND  67 MOL_ID: 23;                                                          
COMPND  68 MOLECULE: 50S RIBOSOMAL PROTEIN L24;                                 
COMPND  69 CHAIN: R;                                                            
COMPND  70 MOL_ID: 24;                                                          
COMPND  71 MOLECULE: 50S RIBOSOMAL PROTEIN L25;                                 
COMPND  72 CHAIN: S;                                                            
COMPND  73 SYNONYM: GENERAL STRESS PROTEIN CTC;                                 
COMPND  74 MOL_ID: 25;                                                          
COMPND  75 MOLECULE: 50S RIBOSOMAL PROTEIN L27;                                 
COMPND  76 CHAIN: T;                                                            
COMPND  77 MOL_ID: 26;                                                          
COMPND  78 MOLECULE: 50S RIBOSOMAL PROTEIN L28;                                 
COMPND  79 CHAIN: U;                                                            
COMPND  80 MOL_ID: 27;                                                          
COMPND  81 MOLECULE: 50S RIBOSOMAL PROTEIN L29;                                 
COMPND  82 CHAIN: V;                                                            
COMPND  83 MOL_ID: 28;                                                          
COMPND  84 MOLECULE: 50S RIBOSOMAL PROTEIN L30;                                 
COMPND  85 CHAIN: W;                                                            
COMPND  86 MOL_ID: 29;                                                          
COMPND  87 MOLECULE: RIBOSOMAL 23S RNA;                                         
COMPND  88 CHAIN: X;                                                            
COMPND  89 MOL_ID: 30;                                                          
COMPND  90 MOLECULE: 50S RIBOSOMAL PROTEIN L32;                                 
COMPND  91 CHAIN: Y;                                                            
COMPND  92 MOL_ID: 31;                                                          
COMPND  93 MOLECULE: RIBOSOMAL 5S RNA;                                          
COMPND  94 CHAIN: Z                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 1299;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   6 ORGANISM_TAXID: 1299;                                                
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   9 ORGANISM_TAXID: 1299;                                                
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  12 ORGANISM_TAXID: 1299;                                                
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: STREPTOMYCES ACTUOSUS;                          
SOURCE  15 ORGANISM_TAXID: 1885;                                                
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  18 ORGANISM_TAXID: 1299;                                                
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  21 ORGANISM_TAXID: 1299;                                                
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  24 ORGANISM_TAXID: 1299;                                                
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  27 ORGANISM_TAXID: 1299;                                                
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  30 ORGANISM_TAXID: 1299;                                                
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  33 ORGANISM_TAXID: 1299;                                                
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  36 ORGANISM_TAXID: 1299;                                                
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  39 ORGANISM_TAXID: 1299;                                                
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  42 ORGANISM_TAXID: 1299;                                                
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  45 ORGANISM_TAXID: 1299;                                                
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  48 ORGANISM_TAXID: 1299;                                                
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  51 ORGANISM_TAXID: 1299;                                                
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  54 ORGANISM_TAXID: 1299;                                                
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  57 ORGANISM_TAXID: 1299;                                                
SOURCE  58 MOL_ID: 20;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  60 ORGANISM_TAXID: 1299;                                                
SOURCE  61 MOL_ID: 21;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  63 ORGANISM_TAXID: 1299;                                                
SOURCE  64 MOL_ID: 22;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  66 ORGANISM_TAXID: 1299;                                                
SOURCE  67 MOL_ID: 23;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  69 ORGANISM_TAXID: 1299;                                                
SOURCE  70 MOL_ID: 24;                                                          
SOURCE  71 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  72 ORGANISM_TAXID: 1299;                                                
SOURCE  73 MOL_ID: 25;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  75 ORGANISM_TAXID: 1299;                                                
SOURCE  76 MOL_ID: 26;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  78 ORGANISM_TAXID: 1299;                                                
SOURCE  79 MOL_ID: 27;                                                          
SOURCE  80 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  81 ORGANISM_TAXID: 1299;                                                
SOURCE  82 MOL_ID: 28;                                                          
SOURCE  83 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  84 ORGANISM_TAXID: 1299;                                                
SOURCE  85 MOL_ID: 29;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  87 ORGANISM_TAXID: 1299;                                                
SOURCE  88 MOL_ID: 30;                                                          
SOURCE  89 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  90 ORGANISM_TAXID: 1299;                                                
SOURCE  91 MOL_ID: 31;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE  93 ORGANISM_TAXID: 1299                                                 
KEYWDS    NOSIHEPTIDE, THIOPEPTIDE, THIAZOLE, ANTIBIOTIC, L11, S50,             
KEYWDS   2 ANTIBACTERIAL, RIBOSOME-ANTIBIOTIC COMPLEX, RIBOSOME, ZINC-FINGER,   
KEYWDS   3 TRANSLATION REGULATION, RNA-BINDING                                  
EXPDTA    X-RAY DIFFRACTION                                                     
MDLTYP    CA ATOMS ONLY, CHAIN 1, 2, 3                                          
AUTHOR    J.M.HARMS,D.N.WILSON,F.SCHLUENZEN,S.R.CONNELL,T.STACHELHAUS,          
AUTHOR   2 Z.ZABOROWSKA,C.M.T.SPAHN,P.FUCINI                                    
REVDAT   7   16-OCT-19 2ZJP    1       COMPND SEQRES LINK                       
REVDAT   6   28-DEC-11 2ZJP    1       HETATM LINK                              
REVDAT   5   30-NOV-11 2ZJP    1       DBREF                                    
REVDAT   4   27-JUL-11 2ZJP    1       DBREF  MODRES REMARK                     
REVDAT   3   13-JUL-11 2ZJP    1       VERSN                                    
REVDAT   2   24-FEB-09 2ZJP    1       VERSN                                    
REVDAT   1   17-JUN-08 2ZJP    0                                                
JRNL        AUTH   J.M.HARMS,D.N.WILSON,F.SCHLUENZEN,S.R.CONNELL,T.STACHELHAUS, 
JRNL        AUTH 2 Z.ZABOROWSKA,C.M.SPAHN,P.FUCINI                              
JRNL        TITL   TRANSLATIONAL REGULATION VIA L11: MOLECULAR SWITCHES ON THE  
JRNL        TITL 2 RIBOSOME TURNED ON AND OFF BY THIOSTREPTON AND MICROCOCCIN.  
JRNL        REF    MOL.CELL                      V.  30    26 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   18406324                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.01.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 216249                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.300                           
REMARK   3   FREE R VALUE                     : 0.340                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24145                                   
REMARK   3   NUCLEIC ACID ATOMS       : 60249                                   
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.380                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000028057.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-06; 03-DEC-07               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 7                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SLS; ESRF                          
REMARK 200  BEAMLINE                       : X06SA; ID29                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 0.97                          
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; ADSC QUANTUM 315      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 216249                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.63000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2ZJR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       84.95000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      204.45000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      347.25000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       84.95000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      204.45000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      347.25000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       84.95000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      204.45000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      347.25000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       84.95000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      204.45000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      347.25000            
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: 31-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, 5, A, B, C, D, E,         
REMARK 350                    AND CHAINS: F, G, H, I, J, K, L, M, N,            
REMARK 350                    AND CHAINS: O, P, Q, R, S, T, U, V, W, X,         
REMARK 350                    AND CHAINS: Y, Z                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 NOSIHEPTIDE IS A MEMBER OF A SULPHUR-RICH HETEROCYCLIC PEPTIDES      
REMARK 400 CLASS. ALL SHARE A MACROCYLIC CORE, CONSISTING OF A NITROGEN         
REMARK 400 CONTAINING, SIX-MEMBERED RING CENTRAL TO DEHYDROAMINO ACIDS AND A    
REMARK 400 SUBSET OF FIVE MEMBER RING STRUCTURES INCLUDING THIAZOLES,           
REMARK 400 THIAZOLINES AND OXAZOLES. THE MAIN CHARACTERISTIC OF THE             
REMARK 400 NOSIHEPTIDE STRUCTURE IS A GENERAL TENDENCY TO BE MORE OXIDIZED      
REMARK 400 THAN THE THIOSTREPTON ONE. NO THIAZOLINE, OR HYDROGENATED QUINALDIC  
REMARK 400 PRECURSOR NOR TETRAHYDROPYRIDINE RINGS ARE PRESENT IN NOSIHEPTIDE.   
REMARK 400 ALL THE CORRESPONDING RINGS ARE UNSATURATED. NOSIHEPTIDE POSSESS AN  
REMARK 400 INDOLIC ACID RING SYSTEM THAT IS APPENDED TO THE SIDE CHAINS OF THE  
REMARK 400 SER/CYS AND A CENTRAL 6-MEMBERED NITROGEN HETEROCYCLE PRODUCED BY    
REMARK 400 CYCLIZATION BETWEEN TWO CORRESPONDING DEHYDROALANINE ACIDS WITH      
REMARK 400 INCORPORATION OF AN ADJACENT CARBONYL GROUP. THIAZOLE FORMATION IS   
REMARK 400 BY NUCLEOPHILIC ADDITION OF EACH CYS SIDE CHAIN TO THE PROCEEDING    
REMARK 400 CARBONYL GROUP FOLLOWED BY DEHYDRATION AND DEHYDROGENATION. HERE,    
REMARK 400 NOSIHEPTIDE IS REPRESENTED BY GROUPING TOGETHER THE SEQUENCE         
REMARK 400 (SEQRES) AND THE ONE LIGAND (HET) NO1.                               
REMARK 400                                                                      
REMARK 400 THE NOSIHEPTIDE IS THIOPEPTIDE, A MEMBER OF ANTIBIOTIC CLASS.        
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: NOSIHEPTIDE                                                  
REMARK 400   CHAIN: 5                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_2: RESIDUE NO1                                           
REMARK 400   DESCRIPTION: NOSIHEPTIDE IS A HETROCYCLIC THIOPEPTIDE, CONSISTING  
REMARK 400                OF FIVE THIAZOLES AND ONE 3-HYDROXYPYRIDINE RINGS. A  
REMARK 400                MODIFIED INDOLE RING NO1(14) IS LINKED VIA THE SIDE   
REMARK 400                CHAINS OF 3-HYDROXY 3GL(6) AND CYS(8). THE OBSERVED   
REMARK 400                C-TERMINAL AMINO GROUP NH2(13) IS LIKELY TO BE A      
REMARK 400                POST-TRANSLATIONAL DECARBOXYLATED REMNANT OF A SER C- 
REMARK 400                TERMINAL RESIDUE                                      
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 1     1                                                      
REMARK 465     VAL 1    55                                                      
REMARK 465     GLU 2    47                                                      
REMARK 465     MET 3     1                                                      
REMARK 465     GLY 3    65                                                      
REMARK 465     LYS 3    66                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     TYR A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     MET A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ARG A   273                                                      
REMARK 465     ARG A   274                                                      
REMARK 465     LYS A   275                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     LYS B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     GLY B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C   199                                                      
REMARK 465     ALA C   200                                                      
REMARK 465     GLY C   201                                                      
REMARK 465     GLU C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     GLN C   204                                                      
REMARK 465     GLN C   205                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     GLN D   180                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     ILE E     4                                                      
REMARK 465     ALA E   176                                                      
REMARK 465     GLY E   177                                                      
REMARK 465     ALA E   178                                                      
REMARK 465     THR E   179                                                      
REMARK 465     GLY E   180                                                      
REMARK 465     GLY E   181                                                      
REMARK 465     LYS E   182                                                      
REMARK 465     GLY E   183                                                      
REMARK 465     LYS E   184                                                      
REMARK 465     LYS E   185                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     PHE G     3                                                      
REMARK 465     PRO G     4                                                      
REMARK 465     ASP G     5                                                      
REMARK 465     THR G     6                                                      
REMARK 465     ASP G     7                                                      
REMARK 465     VAL G     8                                                      
REMARK 465     SER G     9                                                      
REMARK 465     PRO G    10                                                      
REMARK 465     PRO G    11                                                      
REMARK 465     ARG G    12                                                      
REMARK 465     GLY G    13                                                      
REMARK 465     GLY G    14                                                      
REMARK 465     PRO G    15                                                      
REMARK 465     SER G    16                                                      
REMARK 465     SER G    17                                                      
REMARK 465     PRO G    18                                                      
REMARK 465     ALA G    19                                                      
REMARK 465     LYS G    20                                                      
REMARK 465     SER G    21                                                      
REMARK 465     PRO G    22                                                      
REMARK 465     LEU G    23                                                      
REMARK 465     LEU G    24                                                      
REMARK 465     ARG G    25                                                      
REMARK 465     SER G    26                                                      
REMARK 465     PHE G    27                                                      
REMARK 465     LYS G    28                                                      
REMARK 465     VAL G    29                                                      
REMARK 465     GLU G   172                                                      
REMARK 465     VAL G   173                                                      
REMARK 465     LYS G   174                                                      
REMARK 465     MET I     1                                                      
REMARK 465     LYS I     2                                                      
REMARK 465     LEU I     3                                                      
REMARK 465     VAL I   145                                                      
REMARK 465     GLN I   146                                                      
REMARK 465     THR I   147                                                      
REMARK 465     GLN I   148                                                      
REMARK 465     GLN I   149                                                      
REMARK 465     ASP I   150                                                      
REMARK 465     ASP I   151                                                      
REMARK 465     ALA I   152                                                      
REMARK 465     GLN I   153                                                      
REMARK 465     LYS I   154                                                      
REMARK 465     ALA I   155                                                      
REMARK 465     GLU I   156                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     LEU J     3                                                      
REMARK 465     LEU J     4                                                      
REMARK 465     PRO J     5                                                      
REMARK 465     GLN J   142                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ARG K     2                                                      
REMARK 465     VAL K   116                                                      
REMARK 465     MET L     1                                                      
REMARK 465     ALA L     2                                                      
REMARK 465     THR L     3                                                      
REMARK 465     ALA L     4                                                      
REMARK 465     THR L     5                                                      
REMARK 465     THR L     6                                                      
REMARK 465     ILE L     7                                                      
REMARK 465     LEU L   112                                                      
REMARK 465     ASP L   113                                                      
REMARK 465     PHE L   114                                                      
REMARK 465     MET M     1                                                      
REMARK 465     LEU M   110                                                      
REMARK 465     ARG M   111                                                      
REMARK 465     GLY M   112                                                      
REMARK 465     LYS M   113                                                      
REMARK 465     ALA M   114                                                      
REMARK 465     ALA M   115                                                      
REMARK 465     ARG M   116                                                      
REMARK 465     ILE M   117                                                      
REMARK 465     LYS M   118                                                      
REMARK 465     SER M   119                                                      
REMARK 465     ASP M   120                                                      
REMARK 465     ARG M   121                                                      
REMARK 465     SER M   122                                                      
REMARK 465     ARG M   123                                                      
REMARK 465     VAL M   124                                                      
REMARK 465     MET M   125                                                      
REMARK 465     LYS M   126                                                      
REMARK 465     ASP M   127                                                      
REMARK 465     ALA M   128                                                      
REMARK 465     ALA M   129                                                      
REMARK 465     ARG M   130                                                      
REMARK 465     ALA M   131                                                      
REMARK 465     GLN M   132                                                      
REMARK 465     GLN M   133                                                      
REMARK 465     ASP M   134                                                      
REMARK 465     LYS M   135                                                      
REMARK 465     ALA M   136                                                      
REMARK 465     ASN M   137                                                      
REMARK 465     ALA M   138                                                      
REMARK 465     SER M   139                                                      
REMARK 465     ALA M   140                                                      
REMARK 465     SER M   141                                                      
REMARK 465     GLN M   142                                                      
REMARK 465     ALA M   143                                                      
REMARK 465     ALA M   144                                                      
REMARK 465     ALA M   145                                                      
REMARK 465     ALA M   146                                                      
REMARK 465     GLN M   147                                                      
REMARK 465     ALA M   148                                                      
REMARK 465     ASP M   149                                                      
REMARK 465     VAL M   150                                                      
REMARK 465     THR M   151                                                      
REMARK 465     VAL M   152                                                      
REMARK 465     ILE M   153                                                      
REMARK 465     SER M   154                                                      
REMARK 465     ALA M   155                                                      
REMARK 465     ALA M   156                                                      
REMARK 465     PRO M   157                                                      
REMARK 465     GLU M   158                                                      
REMARK 465     VAL M   159                                                      
REMARK 465     ALA M   160                                                      
REMARK 465     PRO M   161                                                      
REMARK 465     GLU M   162                                                      
REMARK 465     THR M   163                                                      
REMARK 465     GLN M   164                                                      
REMARK 465     GLY M   165                                                      
REMARK 465     GLU M   166                                                      
REMARK 465     MET N     1                                                      
REMARK 465     MET O     1                                                      
REMARK 465     PHE O     2                                                      
REMARK 465     ALA O     3                                                      
REMARK 465     ILE O     4                                                      
REMARK 465     GLN O    99                                                      
REMARK 465     GLY O   100                                                      
REMARK 465     MET P     1                                                      
REMARK 465     THR P     2                                                      
REMARK 465     ALA P     3                                                      
REMARK 465     PRO P     4                                                      
REMARK 465     GLU P     5                                                      
REMARK 465     GLN P     6                                                      
REMARK 465     THR P     7                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     ALA Q    95                                                      
REMARK 465     MET R     1                                                      
REMARK 465     PRO R     2                                                      
REMARK 465     ARG R     3                                                      
REMARK 465     ILE R   114                                                      
REMARK 465     ASP R   115                                                      
REMARK 465     LEU S   176                                                      
REMARK 465     THR S   177                                                      
REMARK 465     ALA S   178                                                      
REMARK 465     GLU S   179                                                      
REMARK 465     GLU S   180                                                      
REMARK 465     LEU S   181                                                      
REMARK 465     GLU S   182                                                      
REMARK 465     ALA S   183                                                      
REMARK 465     GLU S   184                                                      
REMARK 465     VAL S   185                                                      
REMARK 465     GLN S   186                                                      
REMARK 465     ALA S   187                                                      
REMARK 465     ALA S   188                                                      
REMARK 465     GLN S   189                                                      
REMARK 465     VAL S   190                                                      
REMARK 465     ALA S   191                                                      
REMARK 465     GLY S   192                                                      
REMARK 465     LEU S   193                                                      
REMARK 465     VAL S   194                                                      
REMARK 465     ALA S   195                                                      
REMARK 465     ALA S   196                                                      
REMARK 465     GLY S   197                                                      
REMARK 465     GLU S   198                                                      
REMARK 465     LEU S   199                                                      
REMARK 465     SER S   200                                                      
REMARK 465     GLU S   201                                                      
REMARK 465     GLU S   202                                                      
REMARK 465     ALA S   203                                                      
REMARK 465     ALA S   204                                                      
REMARK 465     GLU S   205                                                      
REMARK 465     ALA S   206                                                      
REMARK 465     VAL S   207                                                      
REMARK 465     LEU S   208                                                      
REMARK 465     GLU S   209                                                      
REMARK 465     GLY S   210                                                      
REMARK 465     ASP S   211                                                      
REMARK 465     ALA S   212                                                      
REMARK 465     SER S   213                                                      
REMARK 465     LEU S   214                                                      
REMARK 465     GLU S   215                                                      
REMARK 465     GLU S   216                                                      
REMARK 465     VAL S   217                                                      
REMARK 465     LYS S   218                                                      
REMARK 465     ALA S   219                                                      
REMARK 465     GLU S   220                                                      
REMARK 465     ALA S   221                                                      
REMARK 465     SER S   222                                                      
REMARK 465     GLU S   223                                                      
REMARK 465     ASP S   224                                                      
REMARK 465     ASN S   225                                                      
REMARK 465     ALA S   226                                                      
REMARK 465     GLY S   227                                                      
REMARK 465     THR S   228                                                      
REMARK 465     ASP S   229                                                      
REMARK 465     SER S   230                                                      
REMARK 465     GLU S   231                                                      
REMARK 465     ASP S   232                                                      
REMARK 465     ASN S   233                                                      
REMARK 465     SER S   234                                                      
REMARK 465     ASP S   235                                                      
REMARK 465     ALA S   236                                                      
REMARK 465     GLN S   237                                                      
REMARK 465     MET T     1                                                      
REMARK 465     THR T    86                                                      
REMARK 465     GLU T    87                                                      
REMARK 465     VAL T    88                                                      
REMARK 465     ALA T    89                                                      
REMARK 465     ALA T    90                                                      
REMARK 465     ASP T    91                                                      
REMARK 465     MET U     1                                                      
REMARK 465     SER U     2                                                      
REMARK 465     ARG U     3                                                      
REMARK 465     GLU U     4                                                      
REMARK 465     CYS U     5                                                      
REMARK 465     TYR U     6                                                      
REMARK 465     LEU U     7                                                      
REMARK 465     LEU U    80                                                      
REMARK 465     ILE U    81                                                      
REMARK 465     GLN V    67                                                      
REMARK 465       A X   249                                                      
REMARK 465       C X   250                                                      
REMARK 465       C X   251                                                      
REMARK 465       G X   252                                                      
REMARK 465       A X   253                                                      
REMARK 465       A X   254                                                      
REMARK 465       A X   255                                                      
REMARK 465       C X   256                                                      
REMARK 465       G X   257                                                      
REMARK 465       C X   258                                                      
REMARK 465       U X   259                                                      
REMARK 465       U X   260                                                      
REMARK 465       G X   261                                                      
REMARK 465       C X   262                                                      
REMARK 465       G X   263                                                      
REMARK 465       U X   264                                                      
REMARK 465       U X   265                                                      
REMARK 465       U X   266                                                      
REMARK 465       C X   267                                                      
REMARK 465       G X   268                                                      
REMARK 465       G X   269                                                      
REMARK 465       G X   270                                                      
REMARK 465       G X   271                                                      
REMARK 465       U X   272                                                      
REMARK 465       U X   273                                                      
REMARK 465       G X   274                                                      
REMARK 465       U X   275                                                      
REMARK 465       A X   276                                                      
REMARK 465       G X   277                                                      
REMARK 465       G X   278                                                      
REMARK 465       A X   279                                                      
REMARK 465       C X   280                                                      
REMARK 465       C X   281                                                      
REMARK 465       A X   282                                                      
REMARK 465       G X   283                                                      
REMARK 465       U X   284                                                      
REMARK 465       U X   285                                                      
REMARK 465       U X   286                                                      
REMARK 465       U X   287                                                      
REMARK 465       U X   288                                                      
REMARK 465       A X   289                                                      
REMARK 465       A X   290                                                      
REMARK 465       G X   291                                                      
REMARK 465       A X   292                                                      
REMARK 465       U X   293                                                      
REMARK 465       U X   294                                                      
REMARK 465       C X   295                                                      
REMARK 465       A X   296                                                      
REMARK 465       A X   297                                                      
REMARK 465       C X   298                                                      
REMARK 465       C X   299                                                      
REMARK 465       C X   300                                                      
REMARK 465       C X   301                                                      
REMARK 465       C X   362                                                      
REMARK 465       G X   363                                                      
REMARK 465       G X   364                                                      
REMARK 465       U X   365                                                      
REMARK 465       U X   366                                                      
REMARK 465       G X   367                                                      
REMARK 465       A X   368                                                      
REMARK 465       C X   369                                                      
REMARK 465       U X   370                                                      
REMARK 465       G X   371                                                      
REMARK 465       U X   372                                                      
REMARK 465       A X   373                                                      
REMARK 465       C X   374                                                      
REMARK 465       U X   375                                                      
REMARK 465       G X   376                                                      
REMARK 465       G X   377                                                      
REMARK 465       C X   378                                                      
REMARK 465       A X   379                                                      
REMARK 465       C X   380                                                      
REMARK 465       C X   381                                                      
REMARK 465       U X   382                                                      
REMARK 465       G X   383                                                      
REMARK 465       A X   384                                                      
REMARK 465       G X   385                                                      
REMARK 465       U X   386                                                      
REMARK 465       G X   892                                                      
REMARK 465       G X   893                                                      
REMARK 465       G X   894                                                      
REMARK 465       G X   895                                                      
REMARK 465       G X   896                                                      
REMARK 465       C X   897                                                      
REMARK 465       C X   898                                                      
REMARK 465       U X   899                                                      
REMARK 465       A X   900                                                      
REMARK 465       C X   901                                                      
REMARK 465       C X   902                                                      
REMARK 465       A X   903                                                      
REMARK 465       G X   904                                                      
REMARK 465       C X   905                                                      
REMARK 465       U X   906                                                      
REMARK 465       U X   907                                                      
REMARK 465       A X   908                                                      
REMARK 465       C X   909                                                      
REMARK 465       C X   910                                                      
REMARK 465       G X  1889                                                      
REMARK 465       G X  1890                                                      
REMARK 465       C X  1891                                                      
REMARK 465       C X  1892                                                      
REMARK 465       G X  1893                                                      
REMARK 465       U X  1894                                                      
REMARK 465       A X  1895                                                      
REMARK 465       A X  1896                                                      
REMARK 465       C X  1897                                                      
REMARK 465       U X  1898                                                      
REMARK 465       A X  1899                                                      
REMARK 465       U X  1900                                                      
REMARK 465       A X  1901                                                      
REMARK 465       A X  1902                                                      
REMARK 465       C X  1903                                                      
REMARK 465       G X  1904                                                      
REMARK 465       G X  1905                                                      
REMARK 465       U X  1906                                                      
REMARK 465       C X  1907                                                      
REMARK 465       C X  1908                                                      
REMARK 465       C X  2091                                                      
REMARK 465       U X  2092                                                      
REMARK 465       G X  2093                                                      
REMARK 465       C X  2094                                                      
REMARK 465       G X  2095                                                      
REMARK 465       U X  2096                                                      
REMARK 465       A X  2097                                                      
REMARK 465       G X  2098                                                      
REMARK 465       G X  2099                                                      
REMARK 465       A X  2100                                                      
REMARK 465       U X  2101                                                      
REMARK 465       A X  2102                                                      
REMARK 465       G X  2103                                                      
REMARK 465       G X  2104                                                      
REMARK 465       U X  2105                                                      
REMARK 465       G X  2106                                                      
REMARK 465       G X  2107                                                      
REMARK 465       G X  2108                                                      
REMARK 465       A X  2109                                                      
REMARK 465       G X  2110                                                      
REMARK 465       C X  2111                                                      
REMARK 465       C X  2112                                                      
REMARK 465       U X  2113                                                      
REMARK 465       G X  2114                                                      
REMARK 465       C X  2115                                                      
REMARK 465       G X  2116                                                      
REMARK 465       A X  2117                                                      
REMARK 465       A X  2118                                                      
REMARK 465       A X  2119                                                      
REMARK 465       C X  2120                                                      
REMARK 465       U X  2121                                                      
REMARK 465       G X  2122                                                      
REMARK 465       G X  2123                                                      
REMARK 465       C X  2124                                                      
REMARK 465       C X  2125                                                      
REMARK 465       U X  2126                                                      
REMARK 465       U X  2127                                                      
REMARK 465       U X  2128                                                      
REMARK 465       U X  2129                                                      
REMARK 465       G X  2130                                                      
REMARK 465       G X  2131                                                      
REMARK 465       G X  2132                                                      
REMARK 465       G X  2133                                                      
REMARK 465       U X  2134                                                      
REMARK 465       C X  2135                                                      
REMARK 465       G X  2136                                                      
REMARK 465       G X  2137                                                      
REMARK 465       U X  2138                                                      
REMARK 465       G X  2139                                                      
REMARK 465       G X  2140                                                      
REMARK 465       A X  2141                                                      
REMARK 465       G X  2142                                                      
REMARK 465       G X  2143                                                      
REMARK 465       C X  2144                                                      
REMARK 465       A X  2145                                                      
REMARK 465       A X  2146                                                      
REMARK 465       C X  2147                                                      
REMARK 465       G X  2148                                                      
REMARK 465       G X  2149                                                      
REMARK 465       U X  2150                                                      
REMARK 465       G X  2151                                                      
REMARK 465       A X  2152                                                      
REMARK 465       A X  2153                                                      
REMARK 465       A X  2154                                                      
REMARK 465       U X  2155                                                      
REMARK 465       A X  2156                                                      
REMARK 465       C X  2157                                                      
REMARK 465       C X  2158                                                      
REMARK 465       A X  2159                                                      
REMARK 465       C X  2160                                                      
REMARK 465       C X  2161                                                      
REMARK 465       C X  2162                                                      
REMARK 465       U X  2163                                                      
REMARK 465       G X  2164                                                      
REMARK 465       C X  2878                                                      
REMARK 465       U X  2879                                                      
REMARK 465       C X  2880                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     VAL Y    60                                                      
REMARK 465       A Z     1                                                      
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   N6     A X   719     O2'    G X   738              2.02            
REMARK 500   O    ARG M   101     N    LYS M   103              2.07            
REMARK 500   OP2    A X  1355     O4     U X  1618              2.08            
REMARK 500   NZ   LYS I    38     OP2    U X   954              2.08            
REMARK 500   N2     G X  1850     N7     A X  1867              2.08            
REMARK 500   O    PRO M    82     N    ALA M    84              2.09            
REMARK 500   OG1  THR B   113     OP1    A X  2798              2.11            
REMARK 500   O    GLN G   107     N    GLY G   109              2.12            
REMARK 500   O2'    U X   571     O4'    A X   581              2.12            
REMARK 500   O    VAL C    74     N    THR C    76              2.12            
REMARK 500   NH2  ARG I    40     OP1    U X   577              2.13            
REMARK 500   O    ILE N    62     OD1  ASN N    66              2.14            
REMARK 500   OD1  ASP H    85     N    SER H    87              2.14            
REMARK 500   N2     G X  1857     OP2    A X  1860              2.14            
REMARK 500   O    ASN G    73     OE1  GLN G   140              2.15            
REMARK 500   O    PHE P    91     N    LYS P    93              2.15            
REMARK 500   O    ARG Y    19     N    SER Y    21              2.15            
REMARK 500   O    ASN G    36     N    GLU G    38              2.15            
REMARK 500   O    LYS S    13     O    GLU S    16              2.15            
REMARK 500   O    LYS Y    15     N    MET Y    18              2.16            
REMARK 500   ND2  ASN H    41     O2'    A X  2653              2.16            
REMARK 500   O4'    A X  1355     O2'    U X  1410              2.17            
REMARK 500   O2'    G X   588     OP1    A X  2002              2.17            
REMARK 500   O    LEU R    25     O    SER R    79              2.18            
REMARK 500   O    ILE M    55     O    LYS M   103              2.18            
REMARK 500   O    THR K    39     N    LYS K    42              2.18            
REMARK 500   O    VAL C    74     N    PHE C    77              2.18            
REMARK 500   N3     G X  1849     N6     A X  1868              2.19            
REMARK 500   O    LEU D    16     N    PHE D    20              2.19            
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    SER 5   1   CA    SER 5   1   CB     -0.151                       
REMARK 500      C X 722   N1      C X 722   C2     -0.062                       
REMARK 500      G X 728   C2'     G X 728   C1'     0.073                       
REMARK 500      A X 731   C2'     A X 731   C1'     0.066                       
REMARK 500      C X 976   N1      C X 976   C2      0.061                       
REMARK 500      U X1056   P       U X1056   O5'     0.062                       
REMARK 500      G X1350   C5'     G X1350   C4'    -0.043                       
REMARK 500      C X1677   N3      C X1677   C4     -0.046                       
REMARK 500      G X1684   C5'     G X1684   C4'    -0.050                       
REMARK 500      G X1749   C5'     G X1749   C4'    -0.043                       
REMARK 500      C X1858   N1      C X1858   C2     -0.062                       
REMARK 500      C X1862   N1      C X1862   C2     -0.062                       
REMARK 500      A X2189   N9      A X2189   C4      0.044                       
REMARK 500      C X2195   N1      C X2195   C2     -0.060                       
REMARK 500      C X2199   N1      C X2199   C2     -0.061                       
REMARK 500      G X2424   C5      G X2424   C6     -0.075                       
REMARK 500      C X2491   C5'     C X2491   C4'    -0.045                       
REMARK 500      G X2492   C5      G X2492   C6     -0.093                       
REMARK 500      G X2527   C5'     G X2527   C4'    -0.043                       
REMARK 500      U X2533   N1      U X2533   C2      0.088                       
REMARK 500      U X2533   C4      U X2533   C5      0.074                       
REMARK 500      U X2594   N1      U X2594   C2      0.056                       
REMARK 500      U X2663   C5'     U X2663   C4'    -0.051                       
REMARK 500      G X2687   C5'     G X2687   C4'    -0.057                       
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    SER 5   1   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    BB9 5   2   C   -  N   -  CA  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    PRO B  86   C   -  N   -  CD  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    PRO B 126   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO B 189   C   -  N   -  CA  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    PRO C 171   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    LEU H  25   CA  -  CB  -  CG  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    PRO J  40   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    PRO K  91   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO M  29   C   -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO P  61   C   -  N   -  CA  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    PRO P  61   C   -  N   -  CD  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    LEU P  72   CA  -  CB  -  CG  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    PRO S 164   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500      A X 176   N9  -  C1' -  C2' ANGL. DEV. =   8.8 DEGREES          
REMARK 500      A X 414   OP1 -  P   -  OP2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500      A X 415   OP1 -  P   -  OP2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500      A X 415   N9  -  C1' -  C2' ANGL. DEV. =  11.8 DEGREES          
REMARK 500      U X 416   OP1 -  P   -  OP2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500      C X 417   OP1 -  P   -  OP2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      C X 417   C3' -  C2' -  C1' ANGL. DEV. =   7.3 DEGREES          
REMARK 500      C X 417   N1  -  C1' -  C2' ANGL. DEV. =  23.2 DEGREES          
REMARK 500      C X 417   O4' -  C1' -  N1  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500      C X 417   C3' -  O3' -  P   ANGL. DEV. =   9.0 DEGREES          
REMARK 500      C X 418   OP1 -  P   -  OP2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      C X 418   N1  -  C1' -  C2' ANGL. DEV. =   9.9 DEGREES          
REMARK 500      G X 419   OP1 -  P   -  OP2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      C X 420   OP1 -  P   -  OP2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500      A X 459   N9  -  C1' -  C2' ANGL. DEV. =   8.2 DEGREES          
REMARK 500      U X 460   N1  -  C1' -  C2' ANGL. DEV. =  14.7 DEGREES          
REMARK 500      A X 489   N9  -  C1' -  C2' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      C X 550   OP1 -  P   -  OP2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500      A X 551   OP1 -  P   -  OP2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500      C X 552   OP1 -  P   -  OP2 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500      C X 553   OP1 -  P   -  OP2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500      U X 554   OP1 -  P   -  OP2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      U X 554   C6  -  N1  -  C2  ANGL. DEV. =   6.5 DEGREES          
REMARK 500      U X 554   N1  -  C2  -  N3  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500      U X 554   N1  -  C2  -  O2  ANGL. DEV. =   5.3 DEGREES          
REMARK 500      U X 555   OP1 -  P   -  OP2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500      U X 555   O4' -  C4' -  C3' ANGL. DEV. =  -7.7 DEGREES          
REMARK 500      U X 555   C3' -  C2' -  C1' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500      A X 556   OP1 -  P   -  OP2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      A X 556   C3' -  C2' -  C1' ANGL. DEV. =   4.8 DEGREES          
REMARK 500      A X 556   N9  -  C1' -  C2' ANGL. DEV. =  16.5 DEGREES          
REMARK 500      A X 556   C3' -  O3' -  P   ANGL. DEV. =  13.2 DEGREES          
REMARK 500      U X 557   OP1 -  P   -  OP2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500      U X 557   C3' -  C2' -  C1' ANGL. DEV. =   8.4 DEGREES          
REMARK 500      U X 557   N1  -  C1' -  C2' ANGL. DEV. =  25.5 DEGREES          
REMARK 500      U X 557   O4' -  C1' -  N1  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     273 ANGLE DEVIATIONS.                             
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    CYS 4  11     -162.10   -163.28                                   
REMARK 500    ASP 4  12       48.52    -92.38                                   
REMARK 500    ASN 4  13      -35.58   -147.67                                   
REMARK 500    CYS 4  14      109.14    -43.31                                   
REMARK 500    VAL 4  16       88.51    -57.78                                   
REMARK 500    ARG 4  19     -154.32    -74.63                                   
REMARK 500    HIS 4  20      105.22    -45.53                                   
REMARK 500    LYS 4  33       92.36    -62.47                                   
REMARK 500    CYS 5   8     -152.76   -121.76                                   
REMARK 500    THR A  34      141.45   -175.81                                   
REMARK 500    GLU A  35       74.55     61.92                                   
REMARK 500    ASN A  45     -159.69   -127.59                                   
REMARK 500    THR A  50      -77.05   -101.02                                   
REMARK 500    PHE A  53     -152.19     54.25                                   
REMARK 500    ILE A  54      104.28     33.71                                   
REMARK 500    HIS A  58      -54.56   -154.15                                   
REMARK 500    LYS A  59        4.17    158.11                                   
REMARK 500    ARG A  60      157.96    -41.67                                   
REMARK 500    ARG A  69       76.71     35.62                                   
REMARK 500    VAL A  79       98.93    -65.19                                   
REMARK 500    ALA A  80      -73.67    -67.35                                   
REMARK 500    PRO A  86     -160.92    -60.81                                   
REMARK 500    ASN A  87       10.63     48.68                                   
REMARK 500    ARG A  88      -35.46   -146.63                                   
REMARK 500    PRO A 108     -158.59    -59.79                                   
REMARK 500    ALA A 123      118.70   -163.63                                   
REMARK 500    PRO A 125       83.60    -44.85                                   
REMARK 500    VAL A 138      109.44    -54.50                                   
REMARK 500    VAL A 142     -161.65   -114.95                                   
REMARK 500    PRO A 149       96.91    -65.60                                   
REMARK 500    LYS A 151      -15.52     64.54                                   
REMARK 500    ALA A 156       89.71     40.81                                   
REMARK 500    ARG A 157      -41.07   -150.07                                   
REMARK 500    GLU A 169      -62.65   -107.04                                   
REMARK 500    SER A 170      -63.47   -154.14                                   
REMARK 500    SER A 187       26.10    -77.47                                   
REMARK 500    ALA A 191      149.35   -175.42                                   
REMARK 500    ASN A 198       73.75     54.26                                   
REMARK 500    ALA A 199     -148.73     59.32                                   
REMARK 500    LYS A 208     -161.72   -106.28                                   
REMARK 500    ALA A 209     -170.98    -62.78                                   
REMARK 500    LEU A 215      -76.21   -128.22                                   
REMARK 500    PRO A 219     -159.40    -59.59                                   
REMARK 500    HIS A 220      163.34    -45.63                                   
REMARK 500    ARG A 222       99.39    -64.39                                   
REMARK 500    SER A 224       13.83    -64.55                                   
REMARK 500    MET A 226     -145.36    -86.57                                   
REMARK 500    GLU A 237       94.24    -58.83                                   
REMARK 500    PRO A 246     -155.94    -87.01                                   
REMARK 500    VAL A 247       13.11    -67.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     758 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR N  32         0.09    SIDE CHAIN                              
REMARK 500      G X  24         0.07    SIDE CHAIN                              
REMARK 500      G X  26         0.06    SIDE CHAIN                              
REMARK 500      A X 228         0.05    SIDE CHAIN                              
REMARK 500      A X 321         0.07    SIDE CHAIN                              
REMARK 500      U X 331         0.06    SIDE CHAIN                              
REMARK 500      U X 339         0.06    SIDE CHAIN                              
REMARK 500      C X 347         0.06    SIDE CHAIN                              
REMARK 500      U X 396         0.10    SIDE CHAIN                              
REMARK 500      A X 415         0.07    SIDE CHAIN                              
REMARK 500      G X 462         0.07    SIDE CHAIN                              
REMARK 500      A X 468         0.08    SIDE CHAIN                              
REMARK 500      G X 474         0.06    SIDE CHAIN                              
REMARK 500      A X 489         0.06    SIDE CHAIN                              
REMARK 500      A X 515         0.05    SIDE CHAIN                              
REMARK 500      U X 529         0.08    SIDE CHAIN                              
REMARK 500      U X 557         0.07    SIDE CHAIN                              
REMARK 500      U X 563         0.08    SIDE CHAIN                              
REMARK 500      A X 565         0.05    SIDE CHAIN                              
REMARK 500      A X 576         0.06    SIDE CHAIN                              
REMARK 500      U X 578         0.07    SIDE CHAIN                              
REMARK 500      G X 582         0.10    SIDE CHAIN                              
REMARK 500      A X 587         0.06    SIDE CHAIN                              
REMARK 500      C X 596         0.07    SIDE CHAIN                              
REMARK 500      U X 598         0.07    SIDE CHAIN                              
REMARK 500      A X 618         0.05    SIDE CHAIN                              
REMARK 500      A X 683         0.06    SIDE CHAIN                              
REMARK 500      A X 688         0.06    SIDE CHAIN                              
REMARK 500      A X 689         0.07    SIDE CHAIN                              
REMARK 500      A X 690         0.07    SIDE CHAIN                              
REMARK 500      A X 698         0.06    SIDE CHAIN                              
REMARK 500      U X 716         0.07    SIDE CHAIN                              
REMARK 500      A X 731         0.07    SIDE CHAIN                              
REMARK 500      C X 765         0.09    SIDE CHAIN                              
REMARK 500      G X 767         0.06    SIDE CHAIN                              
REMARK 500      U X 800         0.07    SIDE CHAIN                              
REMARK 500      U X 810         0.07    SIDE CHAIN                              
REMARK 500      G X 814         0.06    SIDE CHAIN                              
REMARK 500      G X 818         0.07    SIDE CHAIN                              
REMARK 500      U X 820         0.06    SIDE CHAIN                              
REMARK 500      U X 823         0.14    SIDE CHAIN                              
REMARK 500      U X 824         0.14    SIDE CHAIN                              
REMARK 500      C X 829         0.09    SIDE CHAIN                              
REMARK 500      U X 837         0.07    SIDE CHAIN                              
REMARK 500      U X 839         0.07    SIDE CHAIN                              
REMARK 500      A X 842         0.08    SIDE CHAIN                              
REMARK 500      G X 843         0.07    SIDE CHAIN                              
REMARK 500      G X 844         0.05    SIDE CHAIN                              
REMARK 500      C X 853         0.07    SIDE CHAIN                              
REMARK 500      U X 873         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     205 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THE CHIRALITY OF THE 4-HYDROXY GLUTAMIC ACID (3GL) IS                
REMARK 600 NOT SATTELED. IN THE CURRENT ENTRY THE DIASTEREOMER IS               
REMARK 600 SHOWN TO BE (2S,4S), WHILES CCDC 15794 NOSHEP10 ENTRY                
REMARK 600 SHOWS IT TO BE (2S,4R) (DOI 10.1021/JA00461A039).                    
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                              ZN 4  38  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 4  11   SG                                                     
REMARK 620 2 CYS 4  14   SG  115.5                                              
REMARK 620 3 HIS 4  32   ND1  90.6 150.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X2890  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G X2036   OP2                                                    
REMARK 620 2   A X2556   OP1 108.4                                              
REMARK 620 3   G X2036   OP1  53.9 148.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Y  61  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Y  46   SG                                                     
REMARK 620 2 CYS Y  49   SG   81.9                                              
REMARK 620 3 CYS Y  36   SG   92.3  79.0                                        
REMARK 620 4 CYS Y  33   SG  130.0  93.3 135.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "HA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 4 38                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG M 167                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2881                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2882                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2883                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2884                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2885                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2886                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2887                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2888                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2889                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2890                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2894                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2895                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2896                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2897                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Y 61                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 124                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 127                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES 5 1 to 14         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D8T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-MGGDP COMPLEXED     
REMARK 900 WITH THE THIOPEPTIDE GE2270A.                                        
REMARK 900 RELATED ID: 1E9W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THIOPEPTIDE THIOSTREPTON                        
REMARK 900 RELATED ID: 1OLN   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THIOPEPTIDE THIOSTREPTON BINDING TO L11        
REMARK 900 SUBSTRATE FROM 50S RIBOSOMAL RNA                                     
REMARK 900 RELATED ID: 2C77   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-GNP COMPLEXED WITH  
REMARK 900 THIOPEPTIDE GE2270A.                                                 
REMARK 900 RELATED ID: 2JQ7   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE COMPLEX OF THIOPEPTIDE THIOSTREPTON AND    
REMARK 900 RIBOSOMAL L11-RNA                                                    
REMARK 900 RELATED ID: 3CF5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RIBOSOMAL L11-RNA COMPLEXED WITH THE            
REMARK 900 THIOPEPTIDE THIOSTREPTON                                             
REMARK 900 RELATED ID: 2ZJQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ICROCCOCIN COMPLEXED WITH THE LARGE RIBOSOMAL   
REMARK 900 SUBUNIT (50S) FROM DEINOCOCCUS RADIODURANS                           
REMARK 900 RELATED ID: 2ZJR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT (50S) FROM          
REMARK 900 DEINOCOCCUS RADIODURANS                                              
DBREF1 2ZJP X    1  2880  GB                   11612676                         
DBREF2 2ZJP X     AE000513                      2587937     2590816             
DBREF1 2ZJP Z    1   123  GB                   11612676                         
DBREF2 2ZJP Z     AE000513                       254392      254514             
DBREF  2ZJP A    2   275  UNP    Q9RXJ9   RL2_DEIRA        2    275             
DBREF  2ZJP B    1   211  UNP    Q9RXK2   RL3_DEIRA        1    211             
DBREF  2ZJP C    1   205  UNP    Q9RXK1   RL4_DEIRA        1    205             
DBREF  2ZJP D    1   180  UNP    Q9RXJ0   RL5_DEIRA        1    180             
DBREF  2ZJP E    1   185  UNP    Q9RSL3   RL6_DEIRA        1    185             
DBREF  2ZJP F    1   144  UNP    Q9RSS7   RL11_DEIRA       1    144             
DBREF  2ZJP G    1   174  UNP    Q9RXY1   RL13_DEIRA       1    174             
DBREF  2ZJP H    1   134  UNP    Q9RXJ2   RL14_DEIRA       1    134             
DBREF  2ZJP I    1   156  UNP    Q9RSK9   RL15_DEIRA       1    156             
DBREF  2ZJP J    2   142  UNP    Q9RXJ5   RL16_DEIRA       1    141             
DBREF  2ZJP K    1   116  UNP    Q9RSJ5   RL17_DEIRA       1    116             
DBREF  2ZJP L    1   114  UNP    Q9RSL2   RL18_DEIRA       1    114             
DBREF  2ZJP M    1   166  UNP    Q9RWB4   RL19_DEIRA       1    166             
DBREF  2ZJP N    1   118  UNP    Q9RSW7   RL20_DEIRA       1    118             
DBREF  2ZJP O    1   100  UNP    Q9RY64   RL21_DEIRA       1    100             
DBREF  2ZJP P    1   134  UNP    Q9RXJ7   RL22_DEIRA       1    134             
DBREF  2ZJP Q    1    95  UNP    Q9RXK0   RL23_DEIRA       1     95             
DBREF  2ZJP R    1   115  UNP    Q9RXJ1   RL24_DEIRA       1    115             
DBREF  2ZJP S    1   237  UNP    Q9RX88   RL25_DEIRA       1    237             
DBREF  2ZJP T    1    91  UNP    Q9RY65   RL27_DEIRA       1     91             
DBREF  2ZJP U    1    81  UNP    Q9RRG8   RL28_DEIRA       1     81             
DBREF  2ZJP V    1    67  UNP    Q9RXJ4   RL29_DEIRA       1     67             
DBREF  2ZJP W    1    55  UNP    Q9RSL0   RL30_DEIRA       1     55             
DBREF  2ZJP Y    1    60  UNP    P49228   RL32_DEIRA       1     60             
DBREF  2ZJP 1    1    55  UNP    Q9RSS4   RL33_DEIRA       1     55             
DBREF  2ZJP 2    1    47  UNP    Q9RSH2   RL34_DEIRA       1     47             
DBREF  2ZJP 3    1    66  UNP    Q9RSW6   RL35_DEIRA       1     66             
DBREF  2ZJP 4    1    37  UNP    Q9RSK0   RL36_DEIRA       1     37             
DBREF  2ZJP 5    1    13  UNP    C6FX52   NOSM_STRAS      38     50             
SEQADV 2ZJP MET J    1  UNP  Q9RXJ5              INITIATING METHIONINE          
SEQRES   1 1   55  MET ALA LYS ASP GLY PRO ARG ILE ILE VAL LYS MET GLU          
SEQRES   2 1   55  SER SER ALA GLY THR GLY PHE TYR TYR THR THR THR LYS          
SEQRES   3 1   55  ASN ARG ARG ASN THR GLN ALA LYS LEU GLU LEU LYS LYS          
SEQRES   4 1   55  TYR ASP PRO VAL ALA LYS LYS HIS VAL VAL PHE ARG GLU          
SEQRES   5 1   55  LYS LYS VAL                                                  
SEQRES   1 2   47  MET LYS ARG THR TYR GLN PRO ASN ASN ARG LYS ARG ALA          
SEQRES   2 2   47  LYS THR HIS GLY PHE ARG ALA ARG MET LYS THR LYS SER          
SEQRES   3 2   47  GLY ARG ASN ILE LEU ALA ARG ARG ARG ALA LYS GLY ARG          
SEQRES   4 2   47  HIS GLN LEU THR VAL SER ASP GLU                              
SEQRES   1 3   66  MET PRO LYS MET LYS THR HIS LYS MET ALA LYS ARG ARG          
SEQRES   2 3   66  ILE LYS ILE THR GLY THR GLY LYS VAL MET ALA PHE LYS          
SEQRES   3 3   66  SER GLY LYS ARG HIS GLN ASN THR GLY LYS SER GLY ASP          
SEQRES   4 3   66  GLU ILE ARG GLY LYS GLY LYS GLY PHE VAL LEU ALA LYS          
SEQRES   5 3   66  ALA GLU TRP ALA ARG MET LYS LEU MET LEU PRO ARG GLY          
SEQRES   6 3   66  LYS                                                          
SEQRES   1 4   37  MET LYS VAL ARG SER SER VAL LYS LYS MET CYS ASP ASN          
SEQRES   2 4   37  CYS LYS VAL VAL ARG ARG HIS GLY ARG VAL LEU VAL ILE          
SEQRES   3 4   37  CYS SER ASN VAL LYS HIS LYS GLN ARG GLN GLY                  
SEQRES   1 5   13  SER BB9 THR DBU BB9 3GL BB9 CYS BB9 MH6 BB9 DHA NH2          
SEQRES   1 A  274  ALA VAL LYS LYS TYR ARG PRO TYR THR PRO SER ARG ARG          
SEQRES   2 A  274  GLN MET THR THR ALA ASP PHE SER GLY LEU THR LYS LYS          
SEQRES   3 A  274  ARG PRO GLU LYS ALA LEU THR GLU ALA LEU PRO LYS THR          
SEQRES   4 A  274  GLY GLY ARG ASN ASN ARG GLY ARG ILE THR SER ARG PHE          
SEQRES   5 A  274  ILE GLY GLY GLY HIS LYS ARG LEU TYR ARG ILE ILE ASP          
SEQRES   6 A  274  PHE LYS ARG ARG ASP LYS SER GLY VAL ASN ALA LYS VAL          
SEQRES   7 A  274  ALA ALA ILE GLU TYR ASP PRO ASN ARG SER ALA ARG ILE          
SEQRES   8 A  274  ALA LEU LEU HIS TYR ALA ASP GLY GLU LYS ARG TYR ILE          
SEQRES   9 A  274  LEU ALA PRO GLU GLY LEU THR VAL GLY ALA THR VAL ASN          
SEQRES  10 A  274  ALA GLY PRO GLU ALA GLU PRO LYS LEU GLY ASN ALA LEU          
SEQRES  11 A  274  PRO LEU ARG PHE VAL PRO VAL GLY ALA VAL VAL HIS ALA          
SEQRES  12 A  274  LEU GLU LEU VAL PRO GLY LYS GLY ALA GLN LEU ALA ARG          
SEQRES  13 A  274  SER ALA GLY THR SER VAL GLN VAL GLN GLY LYS GLU SER          
SEQRES  14 A  274  ASP TYR VAL ILE VAL ARG LEU PRO SER GLY GLU LEU ARG          
SEQRES  15 A  274  ARG VAL HIS SER GLU CYS TYR ALA THR ILE GLY ALA VAL          
SEQRES  16 A  274  GLY ASN ALA GLU HIS LYS ASN ILE VAL LEU GLY LYS ALA          
SEQRES  17 A  274  GLY ARG SER ARG TRP LEU GLY ARG LYS PRO HIS GLN ARG          
SEQRES  18 A  274  GLY SER ALA MET ASN PRO VAL ASP HIS PRO HIS GLY GLY          
SEQRES  19 A  274  GLY GLU GLY ARG THR GLY ALA GLY ARG VAL PRO VAL THR          
SEQRES  20 A  274  PRO TRP GLY LYS PRO THR LYS GLY LEU LYS THR ARG ARG          
SEQRES  21 A  274  LYS ARG LYS THR SER ASP ARG PHE ILE VAL THR ARG ARG          
SEQRES  22 A  274  LYS                                                          
SEQRES   1 B  211  MET LYS GLY ILE LEU GLY THR LYS ILE GLY MET THR GLN          
SEQRES   2 B  211  ILE TRP LYS ASN ASP ARG ALA ILE PRO VAL THR VAL VAL          
SEQRES   3 B  211  LEU ALA GLY PRO CYS PRO ILE VAL GLN ARG LYS THR ALA          
SEQRES   4 B  211  GLN THR ASP GLY TYR GLU ALA VAL GLN ILE GLY TYR ALA          
SEQRES   5 B  211  PRO LYS ALA GLU ARG LYS VAL ASN LYS PRO MET GLN GLY          
SEQRES   6 B  211  HIS PHE ALA LYS ALA GLY VAL ALA PRO THR ARG ILE LEU          
SEQRES   7 B  211  ARG GLU PHE ARG GLY PHE ALA PRO ASP GLY ASP SER VAL          
SEQRES   8 B  211  ASN VAL ASP ILE PHE ALA GLU GLY GLU LYS ILE ASP ALA          
SEQRES   9 B  211  THR GLY THR SER LYS GLY LYS GLY THR GLN GLY VAL MET          
SEQRES  10 B  211  LYS ARG TRP ASN PHE ALA GLY GLY PRO ALA SER HIS GLY          
SEQRES  11 B  211  SER LYS LYS TRP HIS ARG ARG PRO GLY SER ILE GLY GLN          
SEQRES  12 B  211  ARG LYS THR PRO GLY ARG VAL TYR LYS GLY LYS ARG MET          
SEQRES  13 B  211  ALA GLY HIS MET GLY MET GLU ARG VAL THR VAL GLN ASN          
SEQRES  14 B  211  LEU GLU VAL VAL GLU ILE ARG ALA GLY GLU ASN LEU ILE          
SEQRES  15 B  211  LEU VAL LYS GLY ALA ILE PRO GLY ALA ASN GLY GLY LEU          
SEQRES  16 B  211  VAL VAL LEU ARG SER ALA ALA LYS ALA SER ALA ALA LYS          
SEQRES  17 B  211  GLY GLY LYS                                                  
SEQRES   1 C  205  MET ALA GLN ILE ASN VAL ILE GLY GLN ASN GLY GLY ARG          
SEQRES   2 C  205  THR ILE GLU LEU PRO LEU PRO GLU VAL ASN SER GLY VAL          
SEQRES   3 C  205  LEU HIS GLU VAL VAL THR TRP GLN LEU ALA SER ARG ARG          
SEQRES   4 C  205  ARG GLY THR ALA SER THR ARG THR ARG ALA GLN VAL SER          
SEQRES   5 C  205  LYS THR GLY ARG LYS MET TYR GLY GLN LYS GLY THR GLY          
SEQRES   6 C  205  ASN ALA ARG HIS GLY ASP ARG SER VAL PRO THR PHE VAL          
SEQRES   7 C  205  GLY GLY GLY VAL ALA PHE GLY PRO LYS PRO ARG SER TYR          
SEQRES   8 C  205  ASP TYR THR LEU PRO ARG GLN VAL ARG GLN LEU GLY LEU          
SEQRES   9 C  205  ALA MET ALA ILE ALA SER ARG GLN GLU GLY GLY LYS LEU          
SEQRES  10 C  205  VAL ALA VAL ASP GLY PHE ASP ILE ALA ASP ALA LYS THR          
SEQRES  11 C  205  LYS ASN PHE ILE SER TRP ALA LYS GLN ASN GLY LEU ASP          
SEQRES  12 C  205  GLY THR GLU LYS VAL LEU LEU VAL THR ASP ASP GLU ASN          
SEQRES  13 C  205  THR ARG ARG ALA ALA ARG ASN VAL SER TRP VAL SER VAL          
SEQRES  14 C  205  LEU PRO VAL ALA GLY VAL ASN VAL TYR ASP ILE LEU ARG          
SEQRES  15 C  205  HIS ASP ARG LEU VAL ILE ASP ALA ALA ALA LEU GLU ILE          
SEQRES  16 C  205  VAL GLU GLU GLU ALA GLY GLU GLU GLN GLN                      
SEQRES   1 D  180  MET GLN GLN LEU LYS THR LYS TYR ASN ASP GLN VAL ARG          
SEQRES   2 D  180  PRO ALA LEU MET GLN GLN PHE GLY TYR SER SER VAL MET          
SEQRES   3 D  180  ALA VAL PRO ARG ILE GLU LYS ILE VAL VAL ASN GLU GLY          
SEQRES   4 D  180  LEU GLY SER SER LYS GLU ASP SER LYS ALA ILE ASP LYS          
SEQRES   5 D  180  ALA ALA LYS GLU LEU ALA LEU ILE THR LEU GLN LYS PRO          
SEQRES   6 D  180  ILE ILE THR LYS ALA LYS LYS SER ILE SER ASN PHE LYS          
SEQRES   7 D  180  LEU ARG GLN GLY MET PRO VAL GLY ILE LYS VAL THR LEU          
SEQRES   8 D  180  ARG GLY GLU ARG MET TYR VAL PHE LEU GLU LYS LEU ILE          
SEQRES   9 D  180  ASN ILE GLY LEU PRO ARG ILE ARG ASP PHE ARG GLY ILE          
SEQRES  10 D  180  ASN PRO ASN ALA PHE ASP GLY ARG GLY ASN TYR ASN LEU          
SEQRES  11 D  180  GLY ILE LYS GLU GLN LEU ILE PHE PRO GLU ILE THR TYR          
SEQRES  12 D  180  ASP MET VAL ASP LYS THR ARG GLY MET ASP ILE THR ILE          
SEQRES  13 D  180  VAL THR THR ALA LYS THR ASP GLU GLU ALA ARG ALA LEU          
SEQRES  14 D  180  LEU GLN SER MET GLY LEU PRO PHE ARG LYS GLN                  
SEQRES   1 E  185  MET SER ARG ILE GLY LYS GLN PRO ILE ALA VAL PRO SER          
SEQRES   2 E  185  GLY VAL THR VAL ASN ALA GLN ASP GLY VAL PHE LYS VAL          
SEQRES   3 E  185  LYS GLY PRO LYS GLY GLU LEU THR VAL PRO TYR ASN THR          
SEQRES   4 E  185  GLU LEU THR VAL ARG GLN ASP GLY ASP GLN LEU LEU VAL          
SEQRES   5 E  185  GLU ARG PRO SER ASP ALA GLN LYS HIS ARG ALA LEU HIS          
SEQRES   6 E  185  GLY LEU THR ARG THR LEU VAL ALA ASN ALA VAL LYS GLY          
SEQRES   7 E  185  VAL SER ASP GLY TYR THR ILE ASN LEU GLU LEU ARG GLY          
SEQRES   8 E  185  VAL GLY PHE ARG ALA LYS LEU THR GLY LYS ALA LEU GLU          
SEQRES   9 E  185  MET ASN ILE GLY TYR SER HIS PRO VAL ILE ILE GLU PRO          
SEQRES  10 E  185  PRO ALA GLY VAL THR PHE ALA VAL PRO GLU PRO THR ARG          
SEQRES  11 E  185  ILE ASP VAL SER GLY ILE ASP LYS GLN LEU VAL GLY GLN          
SEQRES  12 E  185  VAL ALA ALA ASN VAL ARG LYS VAL ARG LYS PRO ASP ALA          
SEQRES  13 E  185  TYR HIS GLY LYS GLY VAL ARG PHE VAL GLY GLU GLN ILE          
SEQRES  14 E  185  ALA LEU LYS ALA GLY LYS ALA GLY ALA THR GLY GLY LYS          
SEQRES  15 E  185  GLY LYS LYS                                                  
SEQRES   1 F  144  MET LYS LYS VAL ALA GLY ILE VAL LYS LEU GLN LEU PRO          
SEQRES   2 F  144  ALA GLY LYS ALA THR PRO ALA PRO PRO VAL GLY PRO ALA          
SEQRES   3 F  144  LEU GLY GLN TYR GLY ALA ASN ILE MET GLU PHE THR LYS          
SEQRES   4 F  144  ALA PHE ASN ALA GLN THR ALA ASP LYS GLY ASP ALA ILE          
SEQRES   5 F  144  ILE PRO VAL GLU ILE THR ILE TYR ALA ASP ARG SER PHE          
SEQRES   6 F  144  THR PHE ILE THR LYS THR PRO PRO MET SER TYR LEU ILE          
SEQRES   7 F  144  ARG LYS ALA ALA GLY ILE GLY LYS GLY SER SER THR PRO          
SEQRES   8 F  144  ASN LYS ALA LYS VAL GLY LYS LEU ASN TRP ASP GLN VAL          
SEQRES   9 F  144  LEU GLU ILE ALA LYS THR LYS MET PRO ASP LEU ASN ALA          
SEQRES  10 F  144  GLY SER VAL GLU ALA ALA ALA ASN THR VAL ALA GLY THR          
SEQRES  11 F  144  ALA ARG SER MET GLY VAL THR VAL GLU GLY GLY PRO ASN          
SEQRES  12 F  144  ALA                                                          
SEQRES   1 G  174  MET ALA PHE PRO ASP THR ASP VAL SER PRO PRO ARG GLY          
SEQRES   2 G  174  GLY PRO SER SER PRO ALA LYS SER PRO LEU LEU ARG SER          
SEQRES   3 G  174  PHE LYS VAL LYS THR TYR ILE PRO LYS ASN ASP GLU GLN          
SEQRES   4 G  174  ASN TRP VAL VAL VAL ASP ALA SER GLY VAL PRO LEU GLY          
SEQRES   5 G  174  ARG LEU ALA THR LEU ILE ALA SER ARG ILE ARG GLY LYS          
SEQRES   6 G  174  HIS ARG PRO ASP PHE THR PRO ASN MET ILE GLN GLY ASP          
SEQRES   7 G  174  PHE VAL VAL VAL ILE ASN ALA ALA GLN VAL ALA LEU THR          
SEQRES   8 G  174  GLY LYS LYS LEU ASP ASP LYS VAL TYR THR ARG TYR THR          
SEQRES   9 G  174  GLY TYR GLN GLY GLY LEU LYS THR GLU THR ALA ARG GLU          
SEQRES  10 G  174  ALA LEU SER LYS HIS PRO GLU ARG VAL ILE GLU HIS ALA          
SEQRES  11 G  174  VAL PHE GLY MET LEU PRO LYS GLY ARG GLN GLY ARG ALA          
SEQRES  12 G  174  MET HIS THR ARG LEU LYS VAL TYR ALA GLY GLU THR HIS          
SEQRES  13 G  174  PRO HIS SER ALA GLN LYS PRO GLN VAL LEU LYS THR GLN          
SEQRES  14 G  174  PRO LEU GLU VAL LYS                                          
SEQRES   1 H  134  MET ILE MET PRO GLN SER ARG LEU ASP VAL ALA ASP ASN          
SEQRES   2 H  134  SER GLY ALA ARG GLU ILE MET CYS ILE ARG VAL LEU ASN          
SEQRES   3 H  134  SER GLY ILE GLY GLY LYS GLY LEU THR THR GLY GLY GLY          
SEQRES   4 H  134  GLY ASN LYS ARG TYR ALA HIS VAL GLY ASP ILE ILE VAL          
SEQRES   5 H  134  ALA SER VAL LYS ASP ALA ALA PRO ARG GLY ALA VAL LYS          
SEQRES   6 H  134  ALA GLY ASP VAL VAL LYS ALA VAL VAL VAL ARG THR SER          
SEQRES   7 H  134  HIS ALA ILE LYS ARG ALA ASP GLY SER THR ILE ARG PHE          
SEQRES   8 H  134  ASP ARG ASN ALA ALA VAL ILE ILE ASN ASN GLN GLY GLU          
SEQRES   9 H  134  PRO ARG GLY THR ARG VAL PHE GLY PRO VAL ALA ARG GLU          
SEQRES  10 H  134  LEU ARG ASP ARG ARG PHE MET LYS ILE VAL SER LEU ALA          
SEQRES  11 H  134  PRO GLU VAL LEU                                              
SEQRES   1 I  156  MET LYS LEU HIS ASP LEU LYS PRO THR PRO GLY SER ARG          
SEQRES   2 I  156  LYS ASP ARG LYS ARG VAL GLY ARG GLY PRO GLY GLY THR          
SEQRES   3 I  156  ASP LYS THR ALA GLY ARG GLY HIS LYS GLY GLN LYS SER          
SEQRES   4 I  156  ARG SER GLY ALA GLY LYS GLY ALA PHE PHE GLU GLY GLY          
SEQRES   5 I  156  ARG SER ARG LEU ILE ALA ARG LEU PRO LYS ARG GLY PHE          
SEQRES   6 I  156  ASN ASN VAL GLY THR THR TYR GLU VAL VAL LYS LEU SER          
SEQRES   7 I  156  GLN LEU GLN ASP LEU GLU ASP THR THR PHE ASP ARG ASP          
SEQRES   8 I  156  THR LEU GLU ALA TYR ARG LEU VAL ARG ARG LYS ASN ARG          
SEQRES   9 I  156  PRO VAL LYS LEU LEU ALA SER GLY GLU ILE SER ARG ALA          
SEQRES  10 I  156  VAL THR VAL HIS VAL ASP ALA ALA SER ALA ALA ALA ILE          
SEQRES  11 I  156  LYS ALA VAL GLU ALA ALA GLY GLY ARG VAL VAL LEU PRO          
SEQRES  12 I  156  GLU VAL GLN THR GLN GLN ASP ASP ALA GLN LYS ALA GLU          
SEQRES   1 J  142  MET MET LEU LEU PRO LYS ARG THR LYS PHE ARG LYS GLN          
SEQRES   2 J  142  PHE ARG GLY ARG MET THR GLY ASP ALA LYS GLY GLY ASP          
SEQRES   3 J  142  TYR VAL ALA PHE GLY ASP TYR GLY LEU ILE ALA MET GLU          
SEQRES   4 J  142  PRO ALA TRP ILE LYS SER ASN GLN ILE GLU ALA CYS ARG          
SEQRES   5 J  142  ILE VAL MET SER ARG HIS PHE ARG ARG GLY GLY LYS ILE          
SEQRES   6 J  142  TYR ILE ARG ILE PHE PRO ASP LYS PRO VAL THR LYS LYS          
SEQRES   7 J  142  PRO ALA GLU THR ARG MET GLY LYS GLY LYS GLY ALA VAL          
SEQRES   8 J  142  GLU TYR TRP VAL SER VAL VAL LYS PRO GLY ARG VAL MET          
SEQRES   9 J  142  PHE GLU VAL ALA GLY VAL THR GLU GLU GLN ALA LYS GLU          
SEQRES  10 J  142  ALA PHE ARG LEU ALA GLY HIS LYS LEU PRO ILE GLN THR          
SEQRES  11 J  142  LYS MET VAL LYS ARG GLU VAL TYR ASP GLU ALA GLN              
SEQRES   1 K  116  MET ARG HIS GLY LYS ALA GLY ARG LYS LEU ASN ARG ASN          
SEQRES   2 K  116  SER SER ALA ARG VAL ALA LEU ALA ARG ALA GLN ALA THR          
SEQRES   3 K  116  ALA LEU LEU ARG GLU GLY ARG ILE GLN THR THR LEU THR          
SEQRES   4 K  116  LYS ALA LYS GLU LEU ARG PRO PHE VAL GLU GLN LEU ILE          
SEQRES   5 K  116  THR THR ALA LYS GLY GLY ASP LEU HIS SER ARG ARG LEU          
SEQRES   6 K  116  VAL ALA GLN ASP ILE HIS ASP LYS ASP VAL VAL ARG LYS          
SEQRES   7 K  116  VAL MET ASP GLU VAL ALA PRO LYS TYR ALA GLU ARG PRO          
SEQRES   8 K  116  GLY GLY TYR THR ARG ILE LEU ARG VAL GLY THR ARG ARG          
SEQRES   9 K  116  GLY ASP GLY VAL THR MET ALA LEU ILE GLU LEU VAL              
SEQRES   1 L  114  MET ALA THR ALA THR THR ILE ARG ARG LYS LEU ARG THR          
SEQRES   2 L  114  ARG ARG LYS VAL ARG THR THR THR ALA ALA SER GLY ARG          
SEQRES   3 L  114  LEU ARG LEU SER VAL TYR ARG SER SER LYS HIS ILE TYR          
SEQRES   4 L  114  ALA GLN ILE ILE ASP ASP SER ARG GLY GLN THR LEU ALA          
SEQRES   5 L  114  ALA ALA SER SER ALA ALA LEU LYS SER GLY ASN LYS THR          
SEQRES   6 L  114  ASP THR ALA ALA ALA VAL GLY LYS ALA LEU ALA ALA ALA          
SEQRES   7 L  114  ALA ALA GLU LYS GLY ILE LYS GLN VAL VAL PHE ASP ARG          
SEQRES   8 L  114  GLY SER TYR LYS TYR HIS GLY ARG VAL LYS ALA LEU ALA          
SEQRES   9 L  114  ASP ALA ALA ARG GLU GLY GLY LEU ASP PHE                      
SEQRES   1 M  166  MET GLN THR HIS ILE LYS ILE ASN ARG GLY GLU LEU LEU          
SEQRES   2 M  166  ARG GLY ILE GLU GLN ASP HIS THR ARG GLN LEU PRO ASP          
SEQRES   3 M  166  PHE ARG PRO GLY ASP THR VAL ARG VAL ASP THR LYS VAL          
SEQRES   4 M  166  ARG GLU GLY ASN ARG THR ARG SER GLN ALA PHE GLU GLY          
SEQRES   5 M  166  VAL VAL ILE ALA ILE ASN GLY SER GLY SER ARG LYS SER          
SEQRES   6 M  166  PHE THR VAL ARG LYS ILE SER PHE GLY GLU GLY VAL GLU          
SEQRES   7 M  166  ARG VAL PHE PRO PHE ALA SER PRO LEU VAL ASN GLN VAL          
SEQRES   8 M  166  THR ILE VAL GLU ARG GLY LYS VAL ARG ARG ALA LYS LEU          
SEQRES   9 M  166  TYR TYR LEU ARG GLU LEU ARG GLY LYS ALA ALA ARG ILE          
SEQRES  10 M  166  LYS SER ASP ARG SER ARG VAL MET LYS ASP ALA ALA ARG          
SEQRES  11 M  166  ALA GLN GLN ASP LYS ALA ASN ALA SER ALA SER GLN ALA          
SEQRES  12 M  166  ALA ALA ALA GLN ALA ASP VAL THR VAL ILE SER ALA ALA          
SEQRES  13 M  166  PRO GLU VAL ALA PRO GLU THR GLN GLY GLU                      
SEQRES   1 N  118  MET PRO ARG ALA LYS THR GLY ILE VAL ARG ARG ARG ARG          
SEQRES   2 N  118  HIS LYS LYS VAL LEU LYS ARG ALA LYS GLY PHE TRP GLY          
SEQRES   3 N  118  SER ARG SER LYS GLN TYR ARG ASN ALA PHE GLN THR LEU          
SEQRES   4 N  118  LEU ASN ALA ALA THR TYR GLU TYR ARG ASP ARG ARG ASN          
SEQRES   5 N  118  LYS LYS ARG ASP PHE ARG ARG LEU TRP ILE GLN ARG ILE          
SEQRES   6 N  118  ASN ALA GLY ALA ARG LEU HIS GLY MET ASN TYR SER THR          
SEQRES   7 N  118  PHE ILE ASN GLY LEU LYS ARG ALA ASN ILE ASP LEU ASN          
SEQRES   8 N  118  ARG LYS VAL LEU ALA ASP ILE ALA ALA ARG GLU PRO GLU          
SEQRES   9 N  118  ALA PHE LYS ALA LEU VAL ASP ALA SER ARG ASN ALA ARG          
SEQRES  10 N  118  GLN                                                          
SEQRES   1 O  100  MET PHE ALA ILE ILE GLN THR GLY GLY LYS GLN TYR ARG          
SEQRES   2 O  100  VAL SER GLU GLY ASP VAL ILE ARG VAL GLU SER LEU GLN          
SEQRES   3 O  100  GLY GLU ALA GLY ASP LYS VAL GLU LEU LYS ALA LEU PHE          
SEQRES   4 O  100  VAL GLY GLY GLU GLN THR VAL PHE GLY GLU ASP ALA GLY          
SEQRES   5 O  100  LYS TYR THR VAL GLN ALA GLU VAL VAL GLU HIS GLY ARG          
SEQRES   6 O  100  GLY LYS LYS ILE TYR ILE ARG LYS TYR LYS SER GLY VAL          
SEQRES   7 O  100  GLN TYR ARG ARG ARG THR GLY HIS ARG GLN ASN PHE THR          
SEQRES   8 O  100  ALA ILE LYS ILE LEU GLY ILE GLN GLY                          
SEQRES   1 P  134  MET THR ALA PRO GLU GLN THR PHE ARG ASN LYS LYS GLN          
SEQRES   2 P  134  ARG LYS GLN GLN VAL LYS LEU ARG LYS PRO GLY PHE ALA          
SEQRES   3 P  134  VAL ALA LYS TYR VAL ARG MET SER PRO ARG LYS VAL ARG          
SEQRES   4 P  134  LEU VAL VAL ASP VAL ILE ARG GLY LYS SER VAL GLN ASP          
SEQRES   5 P  134  ALA GLU ASP LEU LEU ARG PHE ILE PRO ARG SER ALA SER          
SEQRES   6 P  134  GLU PRO VAL ALA LYS VAL LEU ASN SER ALA LYS ALA ASN          
SEQRES   7 P  134  ALA LEU HIS ASN ASP GLU MET LEU GLU ASP ARG LEU PHE          
SEQRES   8 P  134  VAL LYS GLU ALA TYR VAL ASP ALA GLY PRO THR LEU LYS          
SEQRES   9 P  134  ARG LEU ILE PRO ARG ALA ARG GLY SER ALA ASN ILE ILE          
SEQRES  10 P  134  LYS LYS ARG THR SER HIS ILE THR ILE ILE VAL ALA GLU          
SEQRES  11 P  134  LYS GLY ASN LYS                                              
SEQRES   1 Q   95  MET SER HIS TYR ASP ILE LEU GLN ALA PRO VAL ILE SER          
SEQRES   2 Q   95  GLU LYS ALA TYR SER ALA MET GLU ARG GLY VAL TYR SER          
SEQRES   3 Q   95  PHE TRP VAL SER PRO LYS ALA THR LYS THR GLU ILE LYS          
SEQRES   4 Q   95  ASP ALA ILE GLN GLN ALA PHE GLY VAL ARG VAL ILE GLY          
SEQRES   5 Q   95  ILE SER THR MET ASN VAL PRO GLY LYS ARG LYS ARG VAL          
SEQRES   6 Q   95  GLY ARG PHE ILE GLY GLN ARG ASN ASP ARG LYS LYS ALA          
SEQRES   7 Q   95  ILE VAL ARG LEU ALA GLU GLY GLN SER ILE GLU ALA LEU          
SEQRES   8 Q   95  ALA GLY GLN ALA                                              
SEQRES   1 R  115  MET PRO ARG PRO SER ALA GLY SER HIS HIS ASN ASP LYS          
SEQRES   2 R  115  LEU HIS PHE LYS LYS GLY ASP THR VAL ILE VAL LEU SER          
SEQRES   3 R  115  GLY LYS HIS LYS GLY GLN THR GLY LYS VAL LEU LEU ALA          
SEQRES   4 R  115  LEU PRO ARG ASP GLN LYS VAL VAL VAL GLU GLY VAL ASN          
SEQRES   5 R  115  VAL ILE THR LYS ASN VAL LYS PRO SER MET THR ASN PRO          
SEQRES   6 R  115  GLN GLY GLY GLN GLU GLN ARG GLU LEU ALA LEU HIS ALA          
SEQRES   7 R  115  SER LYS VAL ALA LEU VAL ASP PRO GLU THR GLY LYS ALA          
SEQRES   8 R  115  THR ARG VAL ARG LYS GLN ILE VAL ASP GLY LYS LYS VAL          
SEQRES   9 R  115  ARG VAL ALA VAL ALA SER GLY LYS THR ILE ASP                  
SEQRES   1 S  237  MET GLU LEU THR ALA LYS PRO ARG THR PRO LYS GLN LYS          
SEQRES   2 S  237  LEU ASP GLU SER MET ILE ALA ALA VAL ALA TYR ASN LYS          
SEQRES   3 S  237  GLU ASN ASN VAL SER PHE ALA LEU ASP ARG LYS ALA PHE          
SEQRES   4 S  237  ASP ARG ALA PHE ARG GLN GLN SER THR THR GLY LEU PHE          
SEQRES   5 S  237  ASP ILE THR VAL GLU GLY GLY GLU THR PHE PRO ALA LEU          
SEQRES   6 S  237  VAL LYS ALA VAL GLN MET ASP LYS ARG LYS ARG ALA PRO          
SEQRES   7 S  237  ILE HIS VAL ASP PHE TYR MET VAL THR TYR GLY GLU PRO          
SEQRES   8 S  237  VAL GLU VAL SER VAL PRO VAL HIS THR THR GLY ARG SER          
SEQRES   9 S  237  GLN GLY GLU VAL GLN GLY GLY LEU VAL ASP ILE VAL VAL          
SEQRES  10 S  237  HIS ASN LEU GLN ILE VAL ALA PRO GLY PRO ARG ARG ILE          
SEQRES  11 S  237  PRO GLN GLU LEU VAL VAL ASP VAL THR LYS MET ASN ILE          
SEQRES  12 S  237  GLY ASP HIS ILE THR ALA GLY ASP ILE LYS LEU PRO GLU          
SEQRES  13 S  237  GLY CYS THR LEU ALA ALA ASP PRO GLU LEU THR VAL VAL          
SEQRES  14 S  237  SER VAL LEU PRO PRO ARG LEU THR ALA GLU GLU LEU GLU          
SEQRES  15 S  237  ALA GLU VAL GLN ALA ALA GLN VAL ALA GLY LEU VAL ALA          
SEQRES  16 S  237  ALA GLY GLU LEU SER GLU GLU ALA ALA GLU ALA VAL LEU          
SEQRES  17 S  237  GLU GLY ASP ALA SER LEU GLU GLU VAL LYS ALA GLU ALA          
SEQRES  18 S  237  SER GLU ASP ASN ALA GLY THR ASP SER GLU ASP ASN SER          
SEQRES  19 S  237  ASP ALA GLN                                                  
SEQRES   1 T   91  MET ALA HIS LYS LYS GLY VAL GLY SER SER LYS ASN GLY          
SEQRES   2 T   91  ARG ASP SER ASN PRO LYS TYR LEU GLY VAL LYS LYS PHE          
SEQRES   3 T   91  GLY GLY GLU VAL VAL LYS ALA GLY ASN ILE LEU VAL ARG          
SEQRES   4 T   91  GLN ARG GLY THR LYS PHE LYS ALA GLY GLN GLY VAL GLY          
SEQRES   5 T   91  MET GLY ARG ASP HIS THR LEU PHE ALA LEU SER ASP GLY          
SEQRES   6 T   91  LYS VAL VAL PHE ILE ASN LYS GLY LYS GLY ALA ARG PHE          
SEQRES   7 T   91  ILE SER ILE GLU ALA ALA GLN THR GLU VAL ALA ALA ASP          
SEQRES   1 U   81  MET SER ARG GLU CYS TYR LEU THR GLY LYS LYS ASN LEU          
SEQRES   2 U   81  VAL VAL ASN SER VAL ILE ARG ARG GLY LYS ALA ARG ALA          
SEQRES   3 U   81  ASP GLY GLY VAL GLY ARG LYS THR THR GLY ILE THR LYS          
SEQRES   4 U   81  ARG VAL GLN ARG ALA ASN LEU HIS LYS LYS ALA ILE ARG          
SEQRES   5 U   81  GLU ASN GLY GLN VAL LYS THR VAL TRP LEU SER ALA ASN          
SEQRES   6 U   81  ALA LEU ARG THR LEU SER LYS GLY PRO TYR LYS GLY ILE          
SEQRES   7 U   81  GLU LEU ILE                                                  
SEQRES   1 V   67  MET LYS PRO SER GLU MET ARG ASN LEU GLN ALA THR ASP          
SEQRES   2 V   67  PHE ALA LYS GLU ILE ASP ALA ARG LYS LYS GLU LEU MET          
SEQRES   3 V   67  GLU LEU ARG PHE GLN ALA ALA ALA GLY GLN LEU ALA GLN          
SEQRES   4 V   67  PRO HIS ARG VAL ARG GLN LEU ARG ARG GLU VAL ALA GLN          
SEQRES   5 V   67  LEU ASN THR VAL LYS ALA GLU LEU ALA ARG LYS GLY GLU          
SEQRES   6 V   67  GLN GLN                                                      
SEQRES   1 W   55  MET LYS ILE LYS LEU VAL ARG SER VAL ILE GLY ARG PRO          
SEQRES   2 W   55  GLY ASN GLN VAL LYS THR VAL GLN ALA LEU GLY LEU ARG          
SEQRES   3 W   55  LYS ILE GLY ASP SER ARG GLU VAL SER ASP THR PRO ALA          
SEQRES   4 W   55  VAL ARG GLY MET VAL LYS THR VAL LYS HIS LEU LEU GLU          
SEQRES   5 W   55  VAL GLN GLU                                                  
SEQRES   1 X 2880    G   G   U   C   A   A   G   A   U   A   G   U   A          
SEQRES   2 X 2880    A   G   G   G   U   C   C   A   C   G   G   U   G          
SEQRES   3 X 2880    G   A   U   G   C   C   C   U   G   G   C   G   C          
SEQRES   4 X 2880    U   G   G   A   G   C   C   G   A   U   G   A   A          
SEQRES   5 X 2880    G   G   A   C   G   C   G   A   U   U   A   C   C          
SEQRES   6 X 2880    U   G   C   G   A   A   A   A   G   C   C   C   C          
SEQRES   7 X 2880    G   A   C   G   A   G   C   U   G   G   A   G   A          
SEQRES   8 X 2880    U   A   C   G   C   U   U   U   G   A   C   U   C          
SEQRES   9 X 2880    G   G   G   G   A   U   G   U   C   C   G   A   A          
SEQRES  10 X 2880    U   G   G   G   G   A   A   A   C   C   C   A   C          
SEQRES  11 X 2880    C   U   C   G   U   A   A   G   A   G   G   U   A          
SEQRES  12 X 2880    U   C   C   G   C   A   A   G   G   A   U   G   G          
SEQRES  13 X 2880    G   A   A   C   U   C   A   G   G   G   A   A   C          
SEQRES  14 X 2880    U   G   A   A   A   C   A   U   C   U   C   A   G          
SEQRES  15 X 2880    U   A   C   C   U   G   A   A   G   G   A   G   A          
SEQRES  16 X 2880    A   G   A   A   A   G   A   G   A   A   U   U   C          
SEQRES  17 X 2880    G   A   U   U   C   C   G   U   U   A   G   U   A          
SEQRES  18 X 2880    G   C   G   G   C   G   A   G   C   G   A   A   C          
SEQRES  19 X 2880    C   C   G   G   A   U   C   A   G   C   C   C   A          
SEQRES  20 X 2880    A   A   C   C   G   A   A   A   C   G   C   U   U          
SEQRES  21 X 2880    G   C   G   U   U   U   C   G   G   G   G   U   U          
SEQRES  22 X 2880    G   U   A   G   G   A   C   C   A   G   U   U   U          
SEQRES  23 X 2880    U   U   A   A   G   A   U   U   C   A   A   C   C          
SEQRES  24 X 2880    C   C   U   C   A   A   G   C   C   G   A   A   G          
SEQRES  25 X 2880    U   G   G   C   U   G   G   A   A   A   G   C   U          
SEQRES  26 X 2880    A   C   A   C   C   U   C   A   G   A   A   G   G          
SEQRES  27 X 2880    U   G   A   G   A   G   U   C   C   U   G   U   A          
SEQRES  28 X 2880    G   G   C   G   A   A   C   G   A   G   C   G   G          
SEQRES  29 X 2880    U   U   G   A   C   U   G   U   A   C   U   G   G          
SEQRES  30 X 2880    C   A   C   C   U   G   A   G   U   A   G   G   U          
SEQRES  31 X 2880    C   G   U   U   G   U   U   C   G   U   G   A   A          
SEQRES  32 X 2880    A   C   G   A   U   G   A   C   U   G   A   A   U          
SEQRES  33 X 2880    C   C   G   C   G   C   G   G   A   C   C   A   C          
SEQRES  34 X 2880    C   G   C   G   C   A   A   G   G   C   U   A   A          
SEQRES  35 X 2880    A   U   A   C   U   C   C   C   A   G   U   G   A          
SEQRES  36 X 2880    C   C   G   A   U   A   G   C   G   C   A   U   A          
SEQRES  37 X 2880    G   U   A   C   C   G   U   G   A   G   G   G   A          
SEQRES  38 X 2880    A   A   G   G   U   G   A   A   A   A   G   A   A          
SEQRES  39 X 2880    C   C   C   C   G   G   G   A   G   G   G   G   A          
SEQRES  40 X 2880    G   U   G   A   A   A   G   A   G   A   A   C   C          
SEQRES  41 X 2880    U   G   A   A   A   C   C   G   U   G   G   A   C          
SEQRES  42 X 2880    U   U   A   C   A   A   G   C   A   G   U   C   A          
SEQRES  43 X 2880    U   G   G   C   A   C   C   U   U   A   U   G   C          
SEQRES  44 X 2880    G   U   G   U   U   A   U   G   G   C   G   U   G          
SEQRES  45 X 2880    C   C   U   A   U   U   G   A   A   G   C   A   U          
SEQRES  46 X 2880    G   A   G   C   C   G   G   C   G   A   C   U   U          
SEQRES  47 X 2880    A   G   A   C   C   U   G   A   C   G   U   G   C          
SEQRES  48 X 2880    G   A   G   C   U   U   A   A   G   U   U   G   A          
SEQRES  49 X 2880    A   A   A   A   C   G   G   A   G   G   C   G   G          
SEQRES  50 X 2880    A   G   C   G   A   A   A   G   C   G   A   G   U          
SEQRES  51 X 2880    C   C   G   A   A   U   A   G   G   G   C   G   G          
SEQRES  52 X 2880    C   A   U   U   A   G   U   A   C   G   U   C   G          
SEQRES  53 X 2880    G   G   C   U   A   G   A   C   U   C   G   A   A          
SEQRES  54 X 2880    A   C   C   A   G   G   U   G   A   G   C   U   A          
SEQRES  55 X 2880    A   G   C   A   U   G   A   C   C   A   G   G   U          
SEQRES  56 X 2880    U   G   A   A   A   C   C   C   C   C   G   U   G          
SEQRES  57 X 2880    A   C   A   G   G   G   G   G   C   G   G   A   G          
SEQRES  58 X 2880    G   A   C   C   G   A   A   C   C   G   G   U   G          
SEQRES  59 X 2880    C   C   U   G   C   U   G   A   A   A   C   A   G          
SEQRES  60 X 2880    U   C   U   C   G   G   A   U   G   A   G   U   U          
SEQRES  61 X 2880    G   U   G   U   U   U   A   G   G   A   G   U   G          
SEQRES  62 X 2880    A   A   A   A   G   C   U   A   A   C   C   G   A          
SEQRES  63 X 2880    A   C   C   U   G   G   A   G   A   U   A   G   C          
SEQRES  64 X 2880    U   A   G   U   U   C   U   C   C   C   C   G   A          
SEQRES  65 X 2880    A   A   U   G   U   A   U   U   G   A   G   G   U          
SEQRES  66 X 2880    A   C   A   G   C   C   U   C   G   G   A   U   G          
SEQRES  67 X 2880    U   U   G   A   C   C   A   U   G   U   C   C   U          
SEQRES  68 X 2880    G   U   A   G   A   G   C   A   C   U   C   A   C          
SEQRES  69 X 2880    A   A   G   G   C   U   A   G   G   G   G   G   C          
SEQRES  70 X 2880    C   U   A   C   C   A   G   C   U   U   A   C   C          
SEQRES  71 X 2880    A   A   A   C   C   U   U   A   U   G   A   A   A          
SEQRES  72 X 2880    C   U   C   C   G   A   A   G   G   G   G   C   A          
SEQRES  73 X 2880    C   G   C   G   U   U   U   A   G   U   C   C   G          
SEQRES  74 X 2880    G   G   A   G   U   G   A   G   G   C   U   G   C          
SEQRES  75 X 2880    G   A   G   A   G   C   U   A   A   C   U   U   C          
SEQRES  76 X 2880    C   G   U   A   G   C   C   G   A   G   A   G   G          
SEQRES  77 X 2880    G   A   A   A   C   A   A   C   C   C   A   G   A          
SEQRES  78 X 2880    C   C   A   U   C   A   G   C   U   A   A   G   G          
SEQRES  79 X 2880    U   C   C   C   U   A   A   A   U   G   A   U   C          
SEQRES  80 X 2880    G   C   U   C   A   G   U   G   G   U   U   A   A          
SEQRES  81 X 2880    G   G   A   U   G   U   G   U   C   G   U   C   G          
SEQRES  82 X 2880    C   A   U   A   G   A   C   A   G   C   C   A   G          
SEQRES  83 X 2880    G   A   G   G   U   U   G   G   C   U   U   A   G          
SEQRES  84 X 2880    A   A   G   C   A   G   C   C   A   C   C   C   U          
SEQRES  85 X 2880    U   C   A   A   A   G   A   G   U   G   C   G   U          
SEQRES  86 X 2880    A   A   U   A   G   C   U   C   A   C   U   G   G          
SEQRES  87 X 2880    U   C   G   A   G   U   G   A   C   G   A   U   G          
SEQRES  88 X 2880    C   G   C   C   G   A   A   A   A   U   G   A   U          
SEQRES  89 X 2880    C   G   G   G   G   C   U   C   A   A   G   U   G          
SEQRES  90 X 2880    A   U   C   U   A   C   C   G   A   A   G   C   U          
SEQRES  91 X 2880    A   U   G   G   A   U   U   C   A   A   C   U   C          
SEQRES  92 X 2880    G   C   G   A   A   G   C   G   A   G   U   U   G          
SEQRES  93 X 2880    U   C   U   G   G   U   A   G   G   G   G   A   G          
SEQRES  94 X 2880    C   G   U   U   C   A   G   U   C   C   G   C   G          
SEQRES  95 X 2880    G   A   G   A   A   G   C   C   A   U   A   C   C          
SEQRES  96 X 2880    G   G   A   A   G   G   A   G   U   G   G   U   G          
SEQRES  97 X 2880    G   A   G   C   C   G   A   C   U   G   A   A   G          
SEQRES  98 X 2880    U   G   C   G   G   A   U   G   C   C   G   G   C          
SEQRES  99 X 2880    A   U   G   A   G   U   A   A   C   G   A   U   A          
SEQRES 100 X 2880    A   A   A   G   A   A   G   U   G   A   G   A   A          
SEQRES 101 X 2880    U   C   U   U   C   U   U   C   G   C   C   G   U          
SEQRES 102 X 2880    A   A   G   G   A   C   A   A   G   G   G   U   U          
SEQRES 103 X 2880    C   C   U   G   G   G   G   A   A   G   G   G   U          
SEQRES 104 X 2880    C   G   U   C   C   G   C   C   C   A   G   G   G          
SEQRES 105 X 2880    A   A   A   G   U   C   G   G   G   A   C   C   U          
SEQRES 106 X 2880    A   A   G   G   U   G   A   G   G   C   C   G   A          
SEQRES 107 X 2880    A   C   G   G   C   G   C   A   G   C   C   G   A          
SEQRES 108 X 2880    U   G   G   A   C   A   G   C   A   G   G   U   C          
SEQRES 109 X 2880    A   A   G   A   U   U   C   C   U   G   C   A   C          
SEQRES 110 X 2880    C   G   A   U   C   A   U   G   U   G   G   A   G          
SEQRES 111 X 2880    U   G   A   U   G   G   A   G   G   G   A   C   G          
SEQRES 112 X 2880    C   A   U   U   A   C   G   C   U   A   U   C   C          
SEQRES 113 X 2880    A   A   U   G   C   C   A   A   G   C   U   A   U          
SEQRES 114 X 2880    G   G   C   U   A   U   G   C   U   G   G   U   U          
SEQRES 115 X 2880    G   G   U   A   C   G   C   U   C   A   A   G   G          
SEQRES 116 X 2880    G   C   G   A   U   C   G   G   G   U   C   A   G          
SEQRES 117 X 2880    A   A   A   A   U   C   U   A   C   C   G   G   U          
SEQRES 118 X 2880    C   A   C   A   U   G   C   C   U   C   A   G   A          
SEQRES 119 X 2880    C   G   U   A   U   C   G   G   G   A   G   C   U          
SEQRES 120 X 2880    U   C   C   U   C   G   G   A   A   G   C   G   A          
SEQRES 121 X 2880    A   G   U   U   G   G   A   A   A   C   G   C   G          
SEQRES 122 X 2880    A   C   G   G   U   G   C   C   A   A   G   A   A          
SEQRES 123 X 2880    A   A   G   C   U   U   C   U   A   A   A   C   G          
SEQRES 124 X 2880    U   U   G   A   A   A   C   A   U   G   A   U   U          
SEQRES 125 X 2880    G   C   C   C   G   U   A   C   C   G   C   A   A          
SEQRES 126 X 2880    A   C   C   G   A   C   A   C   A   G   G   U   G          
SEQRES 127 X 2880    U   C   C   G   A   G   U   G   U   C   A   A   U          
SEQRES 128 X 2880    G   C   A   C   U   A   A   G   G   C   G   C   G          
SEQRES 129 X 2880    C   G   A   G   A   G   A   A   C   C   C   U   C          
SEQRES 130 X 2880    G   U   U   A   A   G   G   A   A   C   U   U   U          
SEQRES 131 X 2880    G   C   A   A   U   C   U   C   A   C   C   C   C          
SEQRES 132 X 2880    G   U   A   A   C   U   U   C   G   G   A   A   G          
SEQRES 133 X 2880    A   A   G   G   G   G   U   C   C   C   C   A   C          
SEQRES 134 X 2880    G   C   U   U   C   G   C   G   U   G   G   G   G          
SEQRES 135 X 2880    C   G   C   A   G   U   G   A   A   U   A   G   G          
SEQRES 136 X 2880    C   C   C   A   G   G   C   G   A   C   U   G   U          
SEQRES 137 X 2880    U   U   A   C   C   A   A   A   A   U   C   A   C          
SEQRES 138 X 2880    A   G   C   A   C   U   C   U   G   C   C   A   A          
SEQRES 139 X 2880    C   A   C   G   A   A   C   A   G   U   G   G   A          
SEQRES 140 X 2880    C   G   U   A   U   A   G   G   G   U   G   U   G          
SEQRES 141 X 2880    A   C   G   C   C   U   G   C   C   C   G   G   U          
SEQRES 142 X 2880    G   C   C   G   G   A   A   G   G   U   C   A   A          
SEQRES 143 X 2880    G   U   G   G   A   G   C   G   G   U   G   C   A          
SEQRES 144 X 2880    A   G   C   U   G   C   G   A   A   A   U   G   A          
SEQRES 145 X 2880    A   G   C   C   C   C   G   G   U   G   A   A   C          
SEQRES 146 X 2880    G   G   C   G   G   C   C   G   U   A   A   C   U          
SEQRES 147 X 2880    A   U   A   A   C   G   G   U   C   C   U   A   A          
SEQRES 148 X 2880    G   G   U   A   G   C   G   A   A   A   U   U   C          
SEQRES 149 X 2880    C   U   U   G   U   C   G   G   G   U   A   A   G          
SEQRES 150 X 2880    U   U   C   C   G   A   C   C   U   G   C   A   C          
SEQRES 151 X 2880    G   A   A   A   G   G   C   G   U   A   A   C   G          
SEQRES 152 X 2880    A   U   C   U   G   G   G   C   G   C   U   G   U          
SEQRES 153 X 2880    C   U   C   A   A   C   G   A   G   G   G   A   C          
SEQRES 154 X 2880    U   C   G   G   U   G   A   A   A   U   U   G   A          
SEQRES 155 X 2880    A   U   U   G   G   C   U   G   U   A   A   A   G          
SEQRES 156 X 2880    A   U   G   C   G   G   C   C   U   A   C   C   C          
SEQRES 157 X 2880    G   U   A   G   C   A   G   G   A   C   G   A   A          
SEQRES 158 X 2880    A   A   G   A   C   C   C   C   G   U   G   G   A          
SEQRES 159 X 2880    G   C   U   U   U   A   C   U   A   U   A   G   U          
SEQRES 160 X 2880    C   U   G   G   C   A   U   U   G   G   G   A   U          
SEQRES 161 X 2880    U   C   G   G   G   U   U   U   C   U   C   U   G          
SEQRES 162 X 2880    C   G   U   A   G   G   A   U   A   G   G   U   G          
SEQRES 163 X 2880    G   G   A   G   C   C   U   G   C   G   A   A   A          
SEQRES 164 X 2880    C   U   G   G   C   C   U   U   U   U   G   G   G          
SEQRES 165 X 2880    G   U   C   G   G   U   G   G   A   G   G   C   A          
SEQRES 166 X 2880    A   C   G   G   U   G   A   A   A   U   A   C   C          
SEQRES 167 X 2880    A   C   C   C   U   G   A   G   A   A   A   C   U          
SEQRES 168 X 2880    U   G   G   A   U   U   U   C   U   A   A   C   C          
SEQRES 169 X 2880    U   G   A   A   A   A   A   U   C   A   C   U   U          
SEQRES 170 X 2880    U   C   G   G   G   G   A   C   C   G   U   G   C          
SEQRES 171 X 2880    U   U   G   G   C   G   G   G   U   A   G   U   U          
SEQRES 172 X 2880    U   G   A   C   U   G   G   G   G   C   G   G   U          
SEQRES 173 X 2880    C   G   C   C   U   C   C   C   A   A   A   A   U          
SEQRES 174 X 2880    G   U   A   A   C   G   G   A   G   G   C   G   C          
SEQRES 175 X 2880    C   C   A   A   A   G   G   U   C   A   C   C   U          
SEQRES 176 X 2880    C   A   A   G   A   C   G   G   U   U   G   G   A          
SEQRES 177 X 2880    A   A   U   C   G   U   C   U   G   U   A   G   A          
SEQRES 178 X 2880    G   C   G   C   A   A   A   G   G   U   A   G   A          
SEQRES 179 X 2880    A   G   G   U   G   G   C   U   U   G   A   C   U          
SEQRES 180 X 2880    G   C   G   A   G   A   C   U   G   A   C   A   C          
SEQRES 181 X 2880    G   U   C   G   A   G   C   A   G   G   G   A   G          
SEQRES 182 X 2880    G   A   A   A   C   U   C   G   G   G   C   U   U          
SEQRES 183 X 2880    A   G   U   G   A   A   C   C   G   G   U   G   G          
SEQRES 184 X 2880    U   A   C   C   G   U   G   U   G   G   A   A   G          
SEQRES 185 X 2880    G   G   C   C   A   U   C   G   A   U   C   A   A          
SEQRES 186 X 2880    C   G   G   A   U   A   A   A   A   G   U   U   A          
SEQRES 187 X 2880    C   C   C   C   G   G   G   G   A   U   A   A   C          
SEQRES 188 X 2880    A   G   G   C   U   G   A   U   C   U   C   C   C          
SEQRES 189 X 2880    C   C   G   A   G   A   G   U   C   C   A   U   A          
SEQRES 190 X 2880    U   C   G   G   C   G   G   G   G   A   G   G   U          
SEQRES 191 X 2880    U   U   G   G   C   A   C   C   U   C   G   A   U          
SEQRES 192 X 2880    G   U   C   G   G   C   U   C   G   U   C   G   C          
SEQRES 193 X 2880    A   U   C   C   U   G   G   G   G   C   U   G   A          
SEQRES 194 X 2880    A   G   A   A   G   G   U   C   C   C   A   A   G          
SEQRES 195 X 2880    G   G   U   U   G   G   G   C   U   G   U   U   C          
SEQRES 196 X 2880    G   C   C   C   A   U   U   A   A   A   G   C   G          
SEQRES 197 X 2880    G   C   A   C   G   C   G   A   G   C   U   G   G          
SEQRES 198 X 2880    G   U   U   C   A   G   A   A   C   G   U   C   G          
SEQRES 199 X 2880    U   G   A   G   A   C   A   G   U   U   C   G   G          
SEQRES 200 X 2880    U   C   U   C   U   A   U   C   C   G   C   U   A          
SEQRES 201 X 2880    C   G   G   G   C   G   C   A   G   G   A   G   A          
SEQRES 202 X 2880    A   U   U   G   A   G   G   G   G   A   G   U   U          
SEQRES 203 X 2880    G   C   U   C   C   U   A   G   U   A   C   G   A          
SEQRES 204 X 2880    G   A   G   G   A   C   C   G   G   A   G   U   G          
SEQRES 205 X 2880    A   A   C   G   G   A   C   C   G   C   U   G   G          
SEQRES 206 X 2880    U   C   U   C   C   C   U   G   C   U   G   U   C          
SEQRES 207 X 2880    G   U   A   C   C   A   A   C   G   G   C   A   C          
SEQRES 208 X 2880    A   U   G   C   A   G   G   G   U   A   G   C   U          
SEQRES 209 X 2880    A   U   G   U   C   C   G   G   A   A   C   G   G          
SEQRES 210 X 2880    A   U   A   A   C   C   G   C   U   G   A   A   A          
SEQRES 211 X 2880    G   C   A   U   C   U   A   A   G   C   G   G   G          
SEQRES 212 X 2880    A   A   G   C   C   A   G   C   C   C   C   A   A          
SEQRES 213 X 2880    G   A   U   G   A   G   U   U   C   U   C   C   C          
SEQRES 214 X 2880    A   C   U   G   U   U   U   A   U   C   A   G   G          
SEQRES 215 X 2880    U   A   A   G   A   C   U   C   C   C   G   G   A          
SEQRES 216 X 2880    A   G   A   C   C   A   C   C   G   G   G   U   U          
SEQRES 217 X 2880    A   A   G   A   G   G   C   C   A   G   G   C   G          
SEQRES 218 X 2880    U   G   C   A   C   G   C   A   U   A   G   C   A          
SEQRES 219 X 2880    A   U   G   U   G   U   U   C   A   G   C   G   G          
SEQRES 220 X 2880    A   C   U   G   G   U   G   C   U   C   A   U   C          
SEQRES 221 X 2880    A   G   U   C   G   A   G   G   U   C   U   U   G          
SEQRES 222 X 2880    A   C   C   A   C   U   C                                  
SEQRES   1 Y   60  MET ALA LYS HIS PRO VAL PRO LYS LYS LYS THR SER LYS          
SEQRES   2 Y   60  SER LYS ARG ASP MET ARG ARG SER HIS HIS ALA LEU THR          
SEQRES   3 Y   60  ALA PRO ASN LEU THR GLU CYS PRO GLN CYS HIS GLY LYS          
SEQRES   4 Y   60  LYS LEU SER HIS HIS ILE CYS PRO ASN CYS GLY TYR TYR          
SEQRES   5 Y   60  ASP GLY ARG GLN VAL LEU ALA VAL                              
SEQRES   1 Z  123    A   C   A   C   C   C   C   C   G   U   G   C   C          
SEQRES   2 Z  123    C   A   U   A   G   C   A   C   U   G   U   G   G          
SEQRES   3 Z  123    A   A   C   C   A   C   C   C   C   A   C   C   C          
SEQRES   4 Z  123    C   A   U   G   C   C   G   A   A   C   U   G   G          
SEQRES   5 Z  123    G   U   C   G   U   G   A   A   A   C   A   C   A          
SEQRES   6 Z  123    G   C   A   G   C   G   C   C   A   A   U   G   A          
SEQRES   7 Z  123    U   A   C   U   C   G   G   A   C   C   G   C   A          
SEQRES   8 Z  123    G   G   G   U   C   C   C   G   G   A   A   A   A          
SEQRES   9 Z  123    G   U   C   G   G   U   C   A   G   C   G   C   G          
SEQRES  10 Z  123    G   G   G   G   U   U                                      
MODRES 2ZJP BB9 5    2  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP DBU 5    4  THR  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP BB9 5    5  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP 3GL 5    6  GLU  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP BB9 5    7  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP BB9 5    9  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP MH6 5   10  SER  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP BB9 5   11  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP DHA 5   12  SER  POST-TRANSLATIONAL MODIFICATION                    
MODRES 2ZJP NH2 5   13  SER  POST-TRANSLATIONAL MODIFICATION                    
HET    BB9  5   2       6                                                       
HET    DBU  5   4       5                                                       
HET    BB9  5   5       6                                                       
HET    3GL  5   6       9                                                       
HET    BB9  5   7       6                                                       
HET    BB9  5   9       5                                                       
HET    MH6  5  10       5                                                       
HET    BB9  5  11       6                                                       
HET    DHA  5  12       5                                                       
HET    NH2  5  13       1                                                       
HET     ZN  4  38       1                                                       
HET    NO1  5  14      13                                                       
HET     MG  M 167       1                                                       
HET     MG  X2881       1                                                       
HET     MG  X2882       1                                                       
HET     MG  X2883       1                                                       
HET     MG  X2884       1                                                       
HET     MG  X2885       1                                                       
HET     MG  X2886       1                                                       
HET     MG  X2887       1                                                       
HET     MG  X2888       1                                                       
HET     MG  X2889       1                                                       
HET     MG  X2890       1                                                       
HET     MG  X2891       1                                                       
HET     MG  X2892       1                                                       
HET     MG  X2893       1                                                       
HET     MG  X2894       1                                                       
HET     MG  X2895       1                                                       
HET     MG  X2896       1                                                       
HET     MG  X2897       1                                                       
HET     MG  X2898       1                                                       
HET     MG  X2899       1                                                       
HET     MG  X2900       1                                                       
HET     MG  X2901       1                                                       
HET     MG  X2902       1                                                       
HET     MG  X2903       1                                                       
HET     MG  X2904       1                                                       
HET     MG  X2905       1                                                       
HET     MG  X2906       1                                                       
HET     MG  X2907       1                                                       
HET     MG  X2908       1                                                       
HET     ZN  Y  61       1                                                       
HET     MG  Z 124       1                                                       
HET     MG  Z 125       1                                                       
HET     MG  Z 126       1                                                       
HET     MG  Z 127       1                                                       
HET     MG  Z 128       1                                                       
HET     MG  Z 129       1                                                       
HETNAM     BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID                         
HETNAM     DBU (2Z)-2-AMINOBUT-2-ENOIC ACID                                     
HETNAM     3GL (2S,4S)-2-AMINO-4-HYDROXY-PENTANEDIOIC ACID                      
HETNAM     MH6 3-HYDROXY-2-IMINOPROPANOIC ACID                                  
HETNAM     DHA 2-AMINO-ACRYLIC ACID                                             
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     NO1 4-(HYDROXYMETHYL)-3-METHYL-1H-INDOLE-2-CARBOXYLIC ACID           
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     DBU Z-DEHYDROBUTYRINE                                                
HETSYN     3GL 4-HYDROXY-GLUTAMIC-ACID                                          
HETSYN     DHA 2,3-DIDEHYDROALANINE                                             
FORMUL   5  BB9    5(C3 H5 N O2 S)                                              
FORMUL   5  DBU    C4 H7 N O2                                                   
FORMUL   5  3GL    C5 H9 N O5                                                   
FORMUL   5  MH6    C3 H5 N O3                                                   
FORMUL   5  DHA    C3 H5 N O2                                                   
FORMUL   5  NH2    H2 N                                                         
FORMUL  32   ZN    2(ZN 2+)                                                     
FORMUL  33  NO1    C11 H11 N O3                                                 
FORMUL  34   MG    35(MG 2+)                                                    
HELIX    1   1 GLY A  210  LEU A  215  5                                   6    
HELIX    2   2 ARG A  222  MET A  226  5                                   5    
HELIX    3   3 ARG A  261  SER A  266  1                                   6    
HELIX    4   4 ALA B   55  VAL B   59  5                                   5    
HELIX    5   5 ASN B   60  LYS B   69  1                                  10    
HELIX    6   6 ASN C   23  ARG C   39  1                                  17    
HELIX    7   7 PRO C   96  GLU C  113  1                                  18    
HELIX    8   8 THR C  130  GLN C  139  1                                  10    
HELIX    9   9 ASP C  154  ARG C  159  1                                   6    
HELIX   10  10 ASN C  176  HIS C  183  1                                   8    
HELIX   11  11 LYS D    5  ASP D   10  1                                   6    
HELIX   12  12 VAL D   12  GLN D   18  1                                   7    
HELIX   13  13 LYS D   48  LEU D   62  1                                  15    
HELIX   14  14 GLY D   93  ILE D  106  1                                  14    
HELIX   15  15 THR D  142  VAL D  146  5                                   5    
HELIX   16  16 THR D  162  GLY D  174  1                                  13    
HELIX   17  17 GLN E   59  GLY E   82  1                                  24    
HELIX   18  18 ASP E  137  ARG E  152  1                                  16    
HELIX   19  19 ILE F   34  THR F   45  1                                  12    
HELIX   20  20 MET F   74  ALA F   82  1                                   9    
HELIX   21  21 ASN F  100  LEU F  105  5                                   6    
HELIX   22  22 VAL F  120  GLY F  135  1                                  16    
HELIX   23  23 PRO G   50  GLY G   64  1                                  15    
HELIX   24  24 GLU G  117  LEU G  119  5                                   3    
HELIX   25  25 HIS G  122  PHE G  132  1                                  11    
HELIX   26  26 GLY G  138  THR G  146  1                                   9    
HELIX   27  27 HIS G  156  GLN G  161  5                                   6    
HELIX   28  28 ALA H  115  ASP H  120  5                                   6    
HELIX   29  29 PHE H  123  LEU H  129  1                                   7    
HELIX   30  30 LEU I   77  GLN I   81  1                                   5    
HELIX   31  31 LEU I   93  VAL I   99  1                                   7    
HELIX   32  32 SER I  126  LYS I  131  1                                   6    
HELIX   33  33 SER J   45  PHE J   59  1                                  15    
HELIX   34  34 GLU J  117  LYS J  125  1                                   9    
HELIX   35  35 SER K   15  VAL K   18  5                                   4    
HELIX   36  36 ALA K   19  GLU K   31  1                                  13    
HELIX   37  37 LEU K   38  LYS K   56  1                                  19    
HELIX   38  38 ASP K   59  ILE K   70  1                                  12    
HELIX   39  39 ASP K   72  GLU K   82  1                                  11    
HELIX   40  40 GLU K   82  TYR K   87  1                                   6    
HELIX   41  41 ALA K   88  ARG K   90  5                                   3    
HELIX   42  42 ARG L    8  THR L   19  1                                  12    
HELIX   43  43 THR L   67  GLU L   81  1                                  15    
HELIX   44  44 GLY L   98  GLY L  111  1                                  14    
HELIX   45  45 ASN M    8  ASP M   19  1                                  12    
HELIX   46  46 SER M   60  LYS M   64  5                                   5    
HELIX   47  47 LEU M  104  ARG M  108  5                                   5    
HELIX   48  48 ILE N    8  LYS N   19  1                                  12    
HELIX   49  49 TRP N   25  LYS N   30  5                                   6    
HELIX   50  50 GLN N   31  GLY N   73  1                                  43    
HELIX   51  51 ASN N   75  ALA N   86  1                                  12    
HELIX   52  52 VAL N   94  GLU N  102  1                                   9    
HELIX   53  53 GLU N  102  ASN N  115  1                                  14    
HELIX   54  54 ASN P   10  LYS P   12  5                                   3    
HELIX   55  55 GLN P   13  VAL P   18  1                                   6    
HELIX   56  56 SER P   34  ARG P   46  1                                  13    
HELIX   57  57 SER P   49  ILE P   60  1                                  12    
HELIX   58  58 ALA P   64  LEU P   80  1                                  17    
HELIX   59  59 LEU P   86  ARG P   89  5                                   4    
HELIX   60  60 GLU Q   14  GLU Q   21  1                                   8    
HELIX   61  61 THR Q   34  PHE Q   46  1                                  13    
HELIX   62  62 PRO S   10  ASP S   15  1                                   6    
HELIX   63  63 ASP S   35  ARG S   44  1                                  10    
HELIX   64  64 GLN S   46  GLY S   50  5                                   5    
HELIX   65  65 SER U   63  LYS U   72  1                                  10    
HELIX   66  66 GLN V   10  GLU V   17  1                                   8    
HELIX   67  67 ALA V   20  GLY V   35  1                                  16    
HELIX   68  68 GLN V   39  VAL V   56  1                                  18    
HELIX   69  69 VAL V   56  ALA V   61  1                                   6    
HELIX   70  70 PRO W   13  GLY W   24  1                                  12    
HELIX   71  71 THR W   37  VAL W   47  1                                  11    
HELIX   72  72 LYS W   48  LEU W   50  5                                   3    
HELIX   73  73 SER Y   12  ARG Y   20  1                                   9    
SHEET    1  4A 3 LYS 4   2  VAL 4   3  0                                        
SHEET    2  4A 3 GLN 4  34  ARG 4  35  1  N  ARG 4  35   O  LYS 4   2           
SHEET    3  4A 3 LEU 4  24  VAL 4  25 -1  O  VAL 4  25   N  GLN 4  34           
SHEET    1  AA 4 ILE A 105  ALA A 107  0                                        
SHEET    2  AA 4 ALA A  90  TYR A  97 -1  O  ARG A  91   N  ALA A 107           
SHEET    3  AA 4 ASN A  76  ASP A  85 -1  N  LYS A  78   O  HIS A  96           
SHEET    4  AA 4 THR A 116  ASN A 118 -1  O  VAL A 117   N  ALA A  77           
SHEET    1  AB 2 VAL A 142  HIS A 143  0                                        
SHEET    2  AB 2 THR A 192  ILE A 193 -1  O  THR A 192   N  HIS A 143           
SHEET    1  AC 4 VAL A 165  LYS A 168  0                                        
SHEET    2  AC 4 TYR A 172  ARG A 176 -1  O  ILE A 174   N  GLN A 166           
SHEET    3  AC 4 LEU A 182  HIS A 186 -1  N  ARG A 183   O  VAL A 175           
SHEET    4  AC 4 ASP A 267  ARG A 268 -1  O  ARG A 268   N  LEU A 182           
SHEET    1  BA 2 ARG B 164  THR B 166  0                                        
SHEET    2  BA 2 LYS B 101  THR B 107 -1  O  GLY B 106   N  VAL B 165           
SHEET    1  BB 2 LEU B 170  GLU B 171  0                                        
SHEET    2  BB 2 LYS B 101  THR B 107  1  O  ILE B 102   N  LEU B 170           
SHEET    1  BC 7 GLU B 174  ARG B 176  0                                        
SHEET    2  BC 7 LEU B 181  LYS B 185 -1  O  LEU B 181   N  ARG B 176           
SHEET    3  BC 7 ILE B  21  LEU B  27 -1  O  THR B  24   N  VAL B 184           
SHEET    4  BC 7 GLY B   3  ILE B  14 -1  O  THR B   7   N  LEU B  27           
SHEET    5  BC 7 LEU B 195  SER B 200 -1  O  VAL B 196   N  GLY B   6           
SHEET    6  BC 7 LYS B 101  THR B 107 -1  O  ASP B 103   N  ARG B 199           
SHEET    7  BC 7 ARG B 164  THR B 166 -1  O  VAL B 165   N  GLY B 106           
SHEET    1  BD 7 GLU B 174  ARG B 176  0                                        
SHEET    2  BD 7 LEU B 181  LYS B 185 -1  O  LEU B 181   N  ARG B 176           
SHEET    3  BD 7 ILE B  21  LEU B  27 -1  O  THR B  24   N  VAL B 184           
SHEET    4  BD 7 GLY B   3  ILE B  14 -1  O  THR B   7   N  LEU B  27           
SHEET    5  BD 7 LEU B 195  SER B 200 -1  O  VAL B 196   N  GLY B   6           
SHEET    6  BD 7 LYS B 101  THR B 107 -1  O  ASP B 103   N  ARG B 199           
SHEET    7  BD 7 LEU B 170  GLU B 171  1  O  LEU B 170   N  ILE B 102           
SHEET    1  BE 4 LEU B  78  ARG B  79  0                                        
SHEET    2  BE 4 ALA B  46  GLY B  50 -1  O  ILE B  49   N  ARG B  79           
SHEET    3  BE 4 CYS B  31  LYS B  37 -1  O  PRO B  32   N  GLY B  50           
SHEET    4  BE 4 ASP B  89  SER B  90 -1  O  SER B  90   N  CYS B  31           
SHEET    1  BF 2 GLY B 110  THR B 113  0                                        
SHEET    2  BF 2 HIS B 159  GLY B 161 -1  O  MET B 160   N  LYS B 111           
SHEET    1  CA 3 VAL C 169  LEU C 170  0                                        
SHEET    2  CA 3 LEU C 149  VAL C 151  1  O  LEU C 150   N  LEU C 170           
SHEET    3  CA 3 LEU C 186  VAL C 187  1  O  VAL C 187   N  VAL C 151           
SHEET    1  DA 4 THR D  90  LEU D  91  0                                        
SHEET    2  DA 4 LYS D  33  ASN D  37 -1  O  ILE D  34   N  LEU D  91           
SHEET    3  DA 4 ASP D 153  VAL D 157 -1  O  ASP D 153   N  ASN D  37           
SHEET    4  DA 4 ASN D 129  LEU D 130 -1  O  LEU D 130   N  ILE D 154           
SHEET    1  EA 3 VAL E  17  ASN E  18  0                                        
SHEET    2  EA 3 VAL E  23  VAL E  26 -1  O  LYS E  25   N  ASN E  18           
SHEET    3  EA 3 LEU E  33  PRO E  36 -1  O  LEU E  33   N  VAL E  26           
SHEET    1  EB 4 VAL E 121  ALA E 124  0                                        
SHEET    2  EB 4 ARG E 130  GLY E 135 -1  O  ASP E 132   N  ALA E 124           
SHEET    3  EB 4 TYR E  83  ARG E  90 -1  O  TYR E  83   N  GLY E 135           
SHEET    4  EB 4 GLY E 161  ARG E 163 -1  O  GLY E 161   N  ARG E  90           
SHEET    1  EC 3 ARG E  95  ALA E  96  0                                        
SHEET    2  EC 3 GLU E 104  ASN E 106 -1  O  ASN E 106   N  ARG E  95           
SHEET    3  EC 3 VAL E 113  ILE E 114 -1  O  VAL E 113   N  MET E 105           
SHEET    1  FA 3 VAL F   8  LEU F  10  0                                        
SHEET    2  FA 3 VAL F  55  ILE F  57 -1  O  VAL F  55   N  LEU F  10           
SHEET    3  FA 3 ILE F  68  THR F  69 -1  O  ILE F  68   N  GLU F  56           
SHEET    1  FB 2 GLY F  97  LYS F  98  0                                        
SHEET    2  FB 2 VAL F 136  THR F 137  1  N  THR F 137   O  GLY F  97           
SHEET    1  GA 3 TRP G  41  ASP G  45  0                                        
SHEET    2  GA 3 PHE G  79  ILE G  83  1  O  PHE G  79   N  VAL G  42           
SHEET    3  GA 3 LEU G 148  VAL G 150  1  O  LYS G 149   N  VAL G  82           
SHEET    1  GB 2 VAL G  99  ARG G 102  0                                        
SHEET    2  GB 2 THR G 112  ALA G 115 -1  O  THR G 112   N  ARG G 102           
SHEET    1  HA 7 ARG H   7  VAL H  10  0                                        
SHEET    2  HA 7 ALA H  16  VAL H  24 -1  O  ARG H  17   N  VAL H  10           
SHEET    3  HA 7 ILE H  50  ALA H  58 -1  O  VAL H  52   N  ILE H  22           
SHEET    4  HA 7 VAL H  69  ARG H  76 -1  O  VAL H  70   N  ALA H  53           
SHEET    5  HA 7 ALA H  95  ASN H 100  1  O  ALA H  95   N  ARG H  76           
SHEET    6  HA 7 ARG H   7  VAL H  10  0                                        
SHEET    1  HB 4 ILE H  81  LYS H  82  0                                        
SHEET    2  HB 4 THR H  88  PHE H  91 -1  O  ILE H  89   N  ILE H  81           
SHEET    3  HB 4 GLU M  75  PHE M  81 -1  O  GLU M  78   N  ARG H  90           
SHEET    4  HB 4 LYS M  70  SER M  72 -1  O  LYS M  70   N  VAL M  77           
SHEET    1  HC 5 ILE H  81  LYS H  82  0                                        
SHEET    2  HC 5 THR H  88  PHE H  91 -1  O  ILE H  89   N  ILE H  81           
SHEET    3  HC 5 GLU M  75  PHE M  81 -1  O  GLU M  78   N  ARG H  90           
SHEET    4  HC 5 PHE M  66  VAL M  68 -1  O  PHE M  66   N  PHE M  81           
SHEET    5  HC 5 VAL M  54  ALA M  56 -1  N  ILE M  55   O  THR M  67           
SHEET    1  MA 2 LYS M  70  SER M  72  0                                        
SHEET    2  MA 2 GLU M  75  PHE M  81 -1  O  GLU M  75   N  SER M  72           
SHEET    1  IA 2 VAL I  74  LYS I  76  0                                        
SHEET    2  IA 2 LYS I 107  LEU I 109  1  O  LYS I 107   N  VAL I  75           
SHEET    1  IB 2 VAL I 118  VAL I 120  0                                        
SHEET    2  IB 2 GLY I 138  VAL I 140  1  N  ARG I 139   O  VAL I 118           
SHEET    1  JA 3 ARG J 102  PHE J 105  0                                        
SHEET    2  JA 3 GLY J  34  ALA J  37 -1  O  LEU J  35   N  PHE J 105           
SHEET    3  JA 3 THR J 130  VAL J 133 -1  O  LYS J 131   N  ILE J  36           
SHEET    1  JB 2 LYS J  73  VAL J  75  0                                        
SHEET    2  JB 2 TYR J  93  VAL J  95 -1  O  TYR J  93   N  VAL J  75           
SHEET    1  KA 3 ARG K  33  THR K  37  0                                        
SHEET    2  KA 3 MET K 110  GLU K 114 -1  O  ALA K 111   N  THR K  36           
SHEET    3  KA 3 ARG K  96  LEU K  98 -1  O  ARG K  96   N  GLU K 114           
SHEET    1  LA 3 ARG L  28  LEU L  29  0                                        
SHEET    2  LA 3 ILE L  42  ASP L  44 -1  O  ILE L  43   N  ARG L  28           
SHEET    3  LA 3 GLN L  49  THR L  50 -1  O  GLN L  49   N  ASP L  44           
SHEET    1  MB 2 ALA M  49  GLU M  51  0                                        
SHEET    2  MB 2 ASP M  31  ASP M  36 -1  N  ARG M  34   O  PHE M  50           
SHEET    1  MC 2 VAL M  88  GLN M  90  0                                        
SHEET    2  MC 2 ASP M  31  ASP M  36 -1  O  VAL M  35   N  GLN M  90           
SHEET    1  MD 2 ILE M  93  GLU M  95  0                                        
SHEET    2  MD 2 ASP M  31  ASP M  36 -1  O  ASP M  31   N  VAL M  94           
SHEET    1  OA 4 GLY O  17  ILE O  20  0                                        
SHEET    2  OA 4 ASN O  89  ILE O  95 -1  O  THR O  91   N  ILE O  20           
SHEET    3  OA 4 VAL O  56  ARG O  65 -1  O  GLU O  59   N  LYS O  94           
SHEET    4  OA 4 LYS O  32  GLU O  34 -1  O  LYS O  32   N  ALA O  58           
SHEET    1  OB 2 ILE O  69  TYR O  74  0                                        
SHEET    2  OB 2 ARG O  81  HIS O  86 -1  O  ARG O  82   N  LYS O  73           
SHEET    1  PA 3 PHE P  25  VAL P  31  0                                        
SHEET    2  PA 3 ILE P 116  ILE P 127 -1  O  SER P 122   N  VAL P  31           
SHEET    3  PA 3 GLU P  94  LEU P 106 -1  O  GLU P  94   N  ILE P 127           
SHEET    1  QA 4 ALA Q   9  PRO Q  10  0                                        
SHEET    2  QA 4 SER Q  26  VAL Q  29 -1  N  TRP Q  28   O  ALA Q   9           
SHEET    3  QA 4 LYS Q  76  ILE Q  79 -1  O  LYS Q  76   N  VAL Q  29           
SHEET    4  QA 4 SER Q  54  THR Q  55 -1  O  SER Q  54   N  ILE Q  79           
SHEET    1  RA 4 LYS R  45  VAL R  48  0                                        
SHEET    2  RA 4 THR R  33  LEU R  40 -1  N  LEU R  37   O  VAL R  47           
SHEET    3  RA 4 THR R  21  ILE R  23 -1  O  VAL R  22   N  GLY R  34           
SHEET    4  RA 4 VAL R  81  ALA R  82 -1  O  VAL R  81   N  ILE R  23           
SHEET    1  RB 2 ASN R  52  VAL R  53  0                                        
SHEET    2  RB 2 ARG R  72  GLU R  73 -1  O  ARG R  72   N  VAL R  53           
SHEET    1  SA 2 ALA S  20  TYR S  24  0                                        
SHEET    2  SA 2 PRO S  78  MET S  85  1  O  ILE S  79   N  ALA S  20           
SHEET    1  SB 2 ALA S  64  VAL S  66  0                                        
SHEET    2  SB 2 PRO S  78  MET S  85 -1  O  TYR S  84   N  LEU S  65           
SHEET    1  SC 2 GLN S  70  MET S  71  0                                        
SHEET    2  SC 2 PRO S  78  MET S  85  1  N  ILE S  79   O  GLN S  70           
SHEET    1  SD 2 GLU S  93  PRO S  97  0                                        
SHEET    2  SD 2 ASN S 119  VAL S 123 -1  O  LEU S 120   N  VAL S  96           
SHEET    1  SE 3 LEU S 112  ASP S 114  0                                        
SHEET    2  SE 3 THR S 167  LEU S 172 -1  O  SER S 170   N  ASP S 114           
SHEET    3  SE 3 HIS S 146  THR S 148 -1  O  ILE S 147   N  VAL S 168           
SHEET    1  TA 4 GLY T  22  VAL T  23  0                                        
SHEET    2  TA 4 ILE T  36  ARG T  39 -1  O  ARG T  39   N  GLY T  22           
SHEET    3  TA 4 THR T  58  ALA T  61 -1  O  LEU T  59   N  LEU T  37           
SHEET    4  TA 4 VAL T  51  MET T  53 -1  O  GLY T  52   N  PHE T  60           
SHEET    1  TB 3 LYS T  46  ALA T  47  0                                        
SHEET    2  TB 3 ALA T  76  ILE T  81  1  O  ARG T  77   N  LYS T  46           
SHEET    3  TB 3 VAL T  67  LYS T  72 -1  O  VAL T  68   N  SER T  80           
SHEET    1  WA 2 LYS W   2  LYS W   4  0                                        
SHEET    2  WA 2 SER W  31  GLU W  33 -1  O  ARG W  32   N  ILE W   3           
SHEET    1  YA 2 THR Y  31  GLU Y  32  0                                        
SHEET    2  YA 2 LYS Y  39  LYS Y  40 -1  O  LYS Y  40   N  THR Y  31           
LINK        ZN    ZN 4  38                 SG  CYS 4  11     1555   1555  2.62  
LINK        ZN    ZN 4  38                 SG  CYS 4  14     1555   1555  2.22  
LINK        ZN    ZN 4  38                 ND1 HIS 4  32     1555   1555  1.73  
LINK         CB  SER 5   1                 CB  MH6 5  10     1555   1555  1.36  
LINK         C   SER 5   1                 N   BB9 5   2     1555   1555  1.29  
LINK         C   SER 5   1                 SG  BB9 5   2     1555   1555  1.72  
LINK         CA  SER 5   1                 C   BB9 5   9     1555   1555  1.44  
LINK         C   BB9 5   2                 N   THR 5   3     1555   1555  1.30  
LINK         C   THR 5   3                 N   DBU 5   4     1555   1555  1.33  
LINK         C   DBU 5   4                 N   BB9 5   5     1555   1555  1.34  
LINK         C   DBU 5   4                 SG  BB9 5   5     1555   1555  1.69  
LINK         C   BB9 5   5                 N   3GL 5   6     1555   1555  1.44  
LINK         OE1 3GL 5   6                 CF  NO1 5  14     1555   1555  1.56  
LINK         C   3GL 5   6                 SG  BB9 5   7     1555   1555  1.80  
LINK         C   3GL 5   6                 N   BB9 5   7     1555   1555  1.32  
LINK         C   BB9 5   7                 N   CYS 5   8     1555   1555  1.36  
LINK         SG  CYS 5   8                 C   NO1 5  14     1555   1555  1.86  
LINK         C   CYS 5   8                 SG  BB9 5   9     1555   1555  1.74  
LINK         C   CYS 5   8                 N   BB9 5   9     1555   1555  1.32  
LINK         C   BB9 5   9                 N   MH6 5  10     1555   1555  1.31  
LINK         C   MH6 5  10                 SG  BB9 5  11     1555   1555  1.68  
LINK         C   MH6 5  10                 N   BB9 5  11     1555   1555  1.37  
LINK         C   BB9 5  11                 N   DHA 5  12     1555   1555  1.39  
LINK         C   DHA 5  12                 N   NH2 5  13     1555   1555  1.42  
LINK        MG    MG X2882                 OP1   G X2415     1555   1555  2.64  
LINK        MG    MG X2884                 OP2   A X 747     1555   1555  2.11  
LINK        MG    MG X2886                 OP2   G X1767     1555   1555  2.02  
LINK        MG    MG X2887                 OP1   C X1765     1555   1555  2.28  
LINK        MG    MG X2890                 OP2   G X2036     1555   1555  2.54  
LINK        MG    MG X2890                 OP1   A X2556     1555   1555  2.71  
LINK        MG    MG X2890                 OP1   G X2036     1555   1555  2.97  
LINK        MG    MG X2894                 OP2   A X1980     1555   1555  2.49  
LINK        MG    MG X2897                 OP1   A X 815     1555   1555  2.03  
LINK        MG    MG X2900                 O2'   G X1760     1555   1555  1.99  
LINK        MG    MG X2904                 OP2   G X 464     1555   1555  2.78  
LINK        MG    MG X2905                 O4    U X 467     1555   1555  2.70  
LINK        MG    MG X2907                 O4    U X2564     1555   1555  2.18  
LINK        ZN    ZN Y  61                 SG  CYS Y  46     1555   1555  2.16  
LINK        ZN    ZN Y  61                 SG  CYS Y  49     1555   1555  2.46  
LINK        ZN    ZN Y  61                 SG  CYS Y  36     1555   1555  2.30  
LINK        ZN    ZN Y  61                 SG  CYS Y  33     1555   1555  2.18  
CISPEP   1 LEU C   19    PRO C   20          0         0.04                     
SITE     1 AC1  5 MET 4  10  CYS 4  11  CYS 4  14  CYS 4  27                    
SITE     2 AC1  5 HIS 4  32                                                     
SITE     1 AC2  1 ASN M  58                                                     
SITE     1 AC3  2   U X2057    U X2058                                          
SITE     1 AC4  1   G X2415                                                     
SITE     1 AC5  2   G X1369    U X1370                                          
SITE     1 AC6  3   G X 746    A X 747    A X 774                               
SITE     1 AC7  2   C X 745    G X 772                                          
SITE     1 AC8  1   G X1767                                                     
SITE     1 AC9  1   C X1765                                                     
SITE     1 BC1  1   G X2557                                                     
SITE     1 BC2  1   G X2743                                                     
SITE     1 BC3  3   G X2036    G X2555    A X2556                               
SITE     1 BC4  1   A X1980                                                     
SITE     1 BC5  3   G X2665    U X2666    U X2700                               
SITE     1 BC6  1   G X2699                                                     
SITE     1 BC7  1   A X 815                                                     
SITE     1 BC8  3   G X1760    G X1761    C X1941                               
SITE     1 BC9  1   G X1266                                                     
SITE     1 CC1  4 GLY C  79    A X 461    G X 462    G X 464                    
SITE     1 CC2  3   C X 463    C X 465    U X 467                               
SITE     1 CC3  2   C X2431    U X2564                                          
SITE     1 CC4  1   C X2480                                                     
SITE     1 CC5  4 CYS Y  33  CYS Y  36  CYS Y  46  CYS Y  49                    
SITE     1 CC6  2   G Z  99    G Z 100                                          
SITE     1 CC7  1   G Z 105                                                     
SITE     1 CC8  9 ALA F  20  PRO F  21  PRO F  25  ALA F  26                    
SITE     2 CC8  9 GLN F  29    A X1078    G X1079    A X1106                    
SITE     3 CC8  9   A X1107                                                     
CRYST1  169.900  408.900  694.500  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005886  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002446  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001440        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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