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Database: PDB
Entry: 1I94
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Original site: 1I94 
HEADER    RIBOSOME                                18-MAR-01   1I94              
TITLE     CRYSTAL STRUCTURES OF THE SMALL RIBOSOMAL SUBUNIT WITH                
TITLE    2 TETRACYCLINE, EDEINE AND IF3                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 16S RRNA;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 30S RIBOSOMAL PROTEIN S2;                                  
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 30S RIBOSOMAL PROTEIN S3;                                  
COMPND   9 CHAIN: C;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 30S RIBOSOMAL PROTEIN S4;                                  
COMPND  12 CHAIN: D;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: 30S RIBOSOMAL PROTEIN S5;                                  
COMPND  15 CHAIN: E;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND  18 CHAIN: F;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 30S RIBOSOMAL PROTEIN S7;                                  
COMPND  21 CHAIN: G;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 30S RIBOSOMAL PROTEIN S8;                                  
COMPND  24 CHAIN: H;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 30S RIBOSOMAL PROTEIN S9;                                  
COMPND  27 CHAIN: I;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 30S RIBOSOMAL PROTEIN S10;                                 
COMPND  30 CHAIN: J;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 30S RIBOSOMAL PROTEIN S11;                                 
COMPND  33 CHAIN: K;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 30S RIBOSOMAL PROTEIN S12;                                 
COMPND  36 CHAIN: L;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 30S RIBOSOMAL PROTEIN S13;                                 
COMPND  39 CHAIN: M;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: 30S RIBOSOMAL PROTEIN S14;                                 
COMPND  42 CHAIN: N;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: 30S RIBOSOMAL PROTEIN S15;                                 
COMPND  45 CHAIN: O;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: 30S RIBOSOMAL PROTEIN S16;                                 
COMPND  48 CHAIN: P;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: 30S RIBOSOMAL PROTEIN S17;                                 
COMPND  51 CHAIN: Q;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: 30S RIBOSOMAL PROTEIN S18;                                 
COMPND  54 CHAIN: R;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: 30S RIBOSOMAL PROTEIN S19;                                 
COMPND  57 CHAIN: S;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: 30S RIBOSOMAL PROTEIN S20;                                 
COMPND  60 CHAIN: T;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: 30S RIBOSOMAL PROTEIN THX;                                 
COMPND  63 CHAIN: U                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 274;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   6 ORGANISM_TAXID: 274;                                                 
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   9 ORGANISM_TAXID: 274;                                                 
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  12 ORGANISM_TAXID: 274;                                                 
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  15 ORGANISM_TAXID: 274;                                                 
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  18 ORGANISM_TAXID: 274;                                                 
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  21 ORGANISM_TAXID: 274;                                                 
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  24 ORGANISM_TAXID: 274;                                                 
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  27 ORGANISM_TAXID: 274;                                                 
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  30 ORGANISM_TAXID: 274;                                                 
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  33 ORGANISM_TAXID: 274;                                                 
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  36 ORGANISM_TAXID: 274;                                                 
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  39 ORGANISM_TAXID: 274;                                                 
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  42 ORGANISM_TAXID: 274;                                                 
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  45 ORGANISM_TAXID: 274;                                                 
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  48 ORGANISM_TAXID: 274;                                                 
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  51 ORGANISM_TAXID: 274;                                                 
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  54 ORGANISM_TAXID: 274;                                                 
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  57 ORGANISM_TAXID: 274;                                                 
SOURCE  58 MOL_ID: 20;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  60 ORGANISM_TAXID: 274;                                                 
SOURCE  61 MOL_ID: 21;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  63 ORGANISM_TAXID: 274                                                  
KEYWDS    30S RIBOSOME                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PIOLETTI,F.SCHLUENZEN,J.HARMS,R.ZARIVACH,M.GLUEHMANN,               
AUTHOR   2 H.AVILA,H.BARTELS,C.JACOBI,T.HARTSCH,A.YONATH,F.FRANCESCHI           
REVDAT   3   24-FEB-09 1I94    1       VERSN                                    
REVDAT   2   01-APR-03 1I94    1       JRNL                                     
REVDAT   1   12-APR-01 1I94    0                                                
JRNL        AUTH   M.PIOLETTI,F.SCHLUNZEN,J.HARMS,R.ZARIVACH,                   
JRNL        AUTH 2 M.GLUHMANN,H.AVILA,A.BASHAN,H.BARTELS,T.AUERBACH,            
JRNL        AUTH 3 C.JACOBI,T.HARTSCH,A.YONATH,F.FRANCESCHI                     
JRNL        TITL   CRYSTAL STRUCTURES OF COMPLEXES OF THE SMALL                 
JRNL        TITL 2 RIBOSOMAL SUBUNIT WITH TETRACYCLINE, EDEINE AND              
JRNL        TITL 3 IF3.                                                         
JRNL        REF    EMBO J.                       V.  20  1829 2001              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   11296217                                                     
JRNL        DOI    10.1093/EMBOJ/20.8.1829                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.SCHLUENZEN,A.TOCILJ,R.ZARIVACH,J.HARMS,                    
REMARK   1  AUTH 2 M.GLUEHMANN,D.JANELL,A.BASHAN,H.BARTELS,I.AGMON,             
REMARK   1  AUTH 3 F.FRANCESCHI,A.YONATH                                        
REMARK   1  TITL   STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL                    
REMARK   1  TITL 2 RIBOSOMAL SUBUNIT AT 3.3 A RESOLUTION                        
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 102   615 2000              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/S0092-8674(00)00084-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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 : NONE                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 228166                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 22815                           
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
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            : 11859                                   
REMARK   3   NUCLEIC ACID ATOMS       : 32534                                   
REMARK   3   HETEROGEN ATOMS          : 1225                                    
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 1I94 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013059.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-00; 01-JUN-00; 01-JUL-      
REMARK 200                                   00; 01-APR-00                      
REMARK 200  TEMPERATURE           (KELVIN) : 85; 85; 85; 85                     
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 7                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : APS; ESRF; MPG/DESY, HAMBURG;      
REMARK 200                                   EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : 19-ID; ID14-2; BW6; BW7B           
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M; M                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2096; 0.9330; 1.2130; 0.8424     
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR,      
REMARK 200                                   SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATOR, SI(222);            
REMARK 200                                   DIAMOND; DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR, SI(111); DOUBLE     
REMARK 200                                   CRYSTAL FOCUSSING MONOCHROMATOR    
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; IMAGE PLATE; IMAGE       
REMARK 200                                   PLATE                              
REMARK 200  DETECTOR MANUFACTURER          : SBC; ADSC QUANTUM 4;               
REMARK 200                                   MARRESEARCH; MARRESEARCH           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 221133                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : 0.01400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH;          
REMARK 200                       SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, MAGNESIUM CHLORIDE,                 
REMARK 280  SPERMIDINE, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  291.K                                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       86.55000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      203.15000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      203.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.27500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      203.15000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      203.15000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      129.82500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      203.15000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      203.15000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.27500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      203.15000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      203.15000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      129.82500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       86.55000            
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: 21-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU B   251                                                      
REMARK 465     SER B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     VAL B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     ALA B   256                                                      
REMARK 465     ILE C   208                                                      
REMARK 465     GLY C   209                                                      
REMARK 465     GLY C   210                                                      
REMARK 465     GLN C   211                                                      
REMARK 465     LYS C   212                                                      
REMARK 465     PRO C   213                                                      
REMARK 465     LYS C   214                                                      
REMARK 465     ALA C   215                                                      
REMARK 465     ARG C   216                                                      
REMARK 465     PRO C   217                                                      
REMARK 465     GLU C   218                                                      
REMARK 465     LEU C   219                                                      
REMARK 465     PRO C   220                                                      
REMARK 465     LYS C   221                                                      
REMARK 465     ALA C   222                                                      
REMARK 465     GLU C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     ARG C   225                                                      
REMARK 465     PRO C   226                                                      
REMARK 465     ARG C   227                                                      
REMARK 465     ARG C   228                                                      
REMARK 465     ARG C   229                                                      
REMARK 465     ARG C   230                                                      
REMARK 465     PRO C   231                                                      
REMARK 465     ALA C   232                                                      
REMARK 465     VAL C   233                                                      
REMARK 465     ARG C   234                                                      
REMARK 465     VAL C   235                                                      
REMARK 465     LYS C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     GLU C   238                                                      
REMARK 465     GLU C   239                                                      
REMARK 465     ALA E   158                                                      
REMARK 465     GLN E   159                                                      
REMARK 465     ALA E   160                                                      
REMARK 465     GLN E   161                                                      
REMARK 465     GLY E   162                                                      
REMARK 465     MET I     1                                                      
REMARK 465     PRO J     2                                                      
REMARK 465     VAL J   101                                                      
REMARK 465     GLY J   102                                                      
REMARK 465     GLY J   103                                                      
REMARK 465     GLY J   104                                                      
REMARK 465     ARG J   105                                                      
REMARK 465     ALA K     2                                                      
REMARK 465     LYS K     3                                                      
REMARK 465     LYS K     4                                                      
REMARK 465     PRO K     5                                                      
REMARK 465     SER K     6                                                      
REMARK 465     GLY M    95                                                      
REMARK 465     LEU M    96                                                      
REMARK 465     PRO M    97                                                      
REMARK 465     VAL M    98                                                      
REMARK 465     ARG M    99                                                      
REMARK 465     GLY M   100                                                      
REMARK 465     GLN M   101                                                      
REMARK 465     ARG M   102                                                      
REMARK 465     THR M   103                                                      
REMARK 465     ARG M   104                                                      
REMARK 465     THR M   105                                                      
REMARK 465     ASN M   106                                                      
REMARK 465     ALA M   107                                                      
REMARK 465     ARG M   108                                                      
REMARK 465     THR M   109                                                      
REMARK 465     ARG M   110                                                      
REMARK 465     LYS M   111                                                      
REMARK 465     GLY M   112                                                      
REMARK 465     PRO M   113                                                      
REMARK 465     ARG M   114                                                      
REMARK 465     LYS M   115                                                      
REMARK 465     THR M   116                                                      
REMARK 465     VAL M   117                                                      
REMARK 465     ALA M   118                                                      
REMARK 465     GLY M   119                                                      
REMARK 465     LYS M   120                                                      
REMARK 465     LYS M   121                                                      
REMARK 465     LYS M   122                                                      
REMARK 465     ALA M   123                                                      
REMARK 465     PRO M   124                                                      
REMARK 465     ARG M   125                                                      
REMARK 465     LYS M   126                                                      
REMARK 465     SER R     2                                                      
REMARK 465     THR R     3                                                      
REMARK 465     LYS R     4                                                      
REMARK 465     ASN R     5                                                      
REMARK 465     ALA R     6                                                      
REMARK 465     GLY S    82                                                      
REMARK 465     HIS S    83                                                      
REMARK 465     GLY S    84                                                      
REMARK 465     LYS S    85                                                      
REMARK 465     GLU S    86                                                      
REMARK 465     ALA S    87                                                      
REMARK 465     LYS S    88                                                      
REMARK 465     ALA S    89                                                      
REMARK 465     THR S    90                                                      
REMARK 465     LYS S    91                                                      
REMARK 465     LYS S    92                                                      
REMARK 465     LYS S    93                                                      
REMARK 465     ALA T     2                                                      
REMARK 465     GLN T     3                                                      
REMARK 465     LYS T     4                                                      
REMARK 465     LYS T     5                                                      
REMARK 465     PRO T     6                                                      
REMARK 465     LYS T     7                                                      
REMARK 465     LYS U    26                                                      
REMARK 465     LYS U    27                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS K     7     O21  WO2 K  1014              1.33            
REMARK 500   O    ASN B    37     O26  WO2 B  1001              1.44            
REMARK 500   CB   ALA E   156     O20  WO2 E  1005              1.58            
REMARK 500   CB   SER R    45     O52  WO2 R  1008              1.72            
REMARK 500   O    LYS E   153     O49  WO2 E  1005              1.76            
REMARK 500   N    LYS K     8     O44  WO2 K  1014              1.97            
REMARK 500   CB   ASN G   148     O51  WO2 G  1006              1.97            
REMARK 500   CB   LYS B    75     O26  WO2 B  1004              2.01            
REMARK 500   O    ARG D    25     N    TYR D    27              2.04            
REMARK 500   O2'  C   A   700     OP2  G   A   701              2.05            
REMARK 500   O    GLU I    12     O    GLY I    67              2.06            
REMARK 500   O    ALA G   147     O51  WO2 G  1006              2.06            
REMARK 500   O2'  U   A  1283     OP1  C   A  1284              2.09            
REMARK 500   N    LYS B    75     O26  WO2 B  1004              2.09            
REMARK 500   O2'  A   A   952     OP2  G   A   953              2.10            
REMARK 500   O    GLN L     9     O    ARG L    12              2.10            
REMARK 500   O    SER E   125     N    ASN E   127              2.11            
REMARK 500   O2'  A   A    51     OP2  G   A    52              2.12            
REMARK 500   C    LYS E   153     O49  WO2 E  1005              2.12            
REMARK 500   O2'  G   A  1046     N2   G   A  1171              2.13            
REMARK 500   O    VAL E    90     N    LYS E   121              2.14            
REMARK 500   O2'  A   A   849     O5'  A   A   850              2.15            
REMARK 500   O2'  G   A   867     OP2  U   A   868              2.16            
REMARK 500   O    LEU J    90     O49  WO2 J  1009              2.16            
REMARK 500   CB   TYR G   151     O48  WO2 G  1006              2.16            
REMARK 500   O2'  G   A  1163     OP2  A   A  1164              2.16            
REMARK 500   O2'  A   A   954     OP2  C   A   956              2.16            
REMARK 500   CB   LYS K     8     O14  WO2 K  1014              2.16            
REMARK 500   O2'  C   A   684     OP2  A   A   685              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N    GLU T    50     O25  WO2 K  1014     3555     1.97            
REMARK 500   OP1  A   A   407     O54  WO2 E  1005     7557     2.07            
REMARK 500   CB   LYS T    48     O48  WO2 K  1014     3555     2.07            
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      G A 738   C5      G A 738   C6     -0.065                       
REMARK 500      A A 849   C5'     A A 849   C4'    -0.049                       
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      U A  13   N1  -  C1' -  C2' ANGL. DEV. =  11.6 DEGREES          
REMARK 500      G A  31   N9  -  C1' -  C2' ANGL. DEV. =  10.0 DEGREES          
REMARK 500      C A  47   N1  -  C1' -  C2' ANGL. DEV. =  12.7 DEGREES          
REMARK 500      A A 102   N9  -  C1' -  C2' ANGL. DEV. =   8.0 DEGREES          
REMARK 500      A A 241   N9  -  C1' -  C2' ANGL. DEV. =  12.2 DEGREES          
REMARK 500      C A 323   N1  -  C1' -  C2' ANGL. DEV. =   9.3 DEGREES          
REMARK 500      U A 362   N1  -  C1' -  C2' ANGL. DEV. =  11.5 DEGREES          
REMARK 500      C A 367   N1  -  C1' -  C2' ANGL. DEV. =   8.3 DEGREES          
REMARK 500      A A 542   N9  -  C1' -  C2' ANGL. DEV. =   8.3 DEGREES          
REMARK 500      C A 545   N1  -  C1' -  C2' ANGL. DEV. =   8.1 DEGREES          
REMARK 500      G A 558   C2' -  C3' -  O3' ANGL. DEV. =  10.2 DEGREES          
REMARK 500      G A 558   N9  -  C1' -  C2' ANGL. DEV. =  10.7 DEGREES          
REMARK 500      U A 624   N1  -  C1' -  C2' ANGL. DEV. =   8.5 DEGREES          
REMARK 500      A A 636   N9  -  C1' -  C2' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      U A 937   N1  -  C1' -  C2' ANGL. DEV. =   7.9 DEGREES          
REMARK 500      U A1031   N1  -  C1' -  C2' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      A A1280   N9  -  C1' -  C2' ANGL. DEV. =   8.1 DEGREES          
REMARK 500      C A1303   N1  -  C1' -  C2' ANGL. DEV. =   8.9 DEGREES          
REMARK 500      A A1479   N9  -  C1' -  C2' ANGL. DEV. =   8.9 DEGREES          
REMARK 500      G A1481   N9  -  C1' -  C2' ANGL. DEV. =  10.0 DEGREES          
REMARK 500      U A1483   N1  -  C1' -  C2' ANGL. DEV. =   9.2 DEGREES          
REMARK 500      U A1505   C2' -  C3' -  O3' ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL B   3       77.56   -108.47                                   
REMARK 500    GLU B   4       75.22    -39.76                                   
REMARK 500    ILE B   5        8.50     51.87                                   
REMARK 500    LYS B   8      120.36     63.74                                   
REMARK 500    LEU B  10       41.87   -104.96                                   
REMARK 500    GLU B  12       99.54    -68.31                                   
REMARK 500    ALA B  13      -85.11    -47.51                                   
REMARK 500    ARG B  21       39.54    -59.70                                   
REMARK 500    LYS B  22       33.78     38.27                                   
REMARK 500    ILE B  32      138.45     11.64                                   
REMARK 500    TYR B  33     -129.69   -134.49                                   
REMARK 500    ASP B  43      -13.18     56.03                                   
REMARK 500    LEU B  44      -72.29     37.28                                   
REMARK 500    GLN B  45       -7.92    -50.99                                   
REMARK 500    ARG B  53      -76.38    -49.28                                   
REMARK 500    THR B  54      -72.77    -39.12                                   
REMARK 500    PHE B  55       -8.92    -50.51                                   
REMARK 500    ALA B  62      -77.78    -59.00                                   
REMARK 500    ARG B  64        3.01    -64.27                                   
REMARK 500    GLN B  76       21.78    -68.47                                   
REMARK 500    ALA B  77      -90.86   -162.82                                   
REMARK 500    GLN B  78      -89.08     34.90                                   
REMARK 500    GLU B  84        0.11    -69.63                                   
REMARK 500    ALA B  85      -68.02    -90.69                                   
REMARK 500    ASN B  94      -74.90    -93.74                                   
REMARK 500    GLN B  95     -103.73    -34.81                                   
REMARK 500    MET B 101      -36.13    -27.29                                   
REMARK 500    ASN B 104        7.89   -164.22                                   
REMARK 500    PHE B 105      -58.51    -26.33                                   
REMARK 500    LYS B 106       13.32    -49.36                                   
REMARK 500    THR B 107      -41.51   -148.65                                   
REMARK 500    PHE B 122       30.53    -86.56                                   
REMARK 500    GLU B 126       -4.89    -58.54                                   
REMARK 500    GLU B 128       92.31     71.60                                   
REMARK 500    GLU B 129       -5.06   -144.89                                   
REMARK 500    LYS B 132      -37.24    -39.20                                   
REMARK 500    GLU B 141      -80.24    -50.41                                   
REMARK 500    LEU B 142      -41.60    -28.98                                   
REMARK 500    VAL B 164      132.99    -39.23                                   
REMARK 500    ASP B 166       81.38     84.65                                   
REMARK 500    PRO B 167       34.90    -72.09                                   
REMARK 500    ARG B 175      -74.34    -72.91                                   
REMARK 500    ALA B 188      146.95     62.13                                   
REMARK 500    ASP B 189     -145.16   -141.62                                   
REMARK 500    ASP B 191       54.62    -94.33                                   
REMARK 500    ASP B 193       78.59   -100.12                                   
REMARK 500    PRO B 194       15.46    -62.14                                   
REMARK 500    ILE B 201       79.87   -152.64                                   
REMARK 500    PRO B 202       50.90    -50.36                                   
REMARK 500    ASP B 206     -149.30    -87.22                                   
REMARK 500    ALA B 207       92.86     62.30                                   
REMARK 500    ILE B 222      -70.86    -59.43                                   
REMARK 500    ARG B 226      -90.59     74.25                                   
REMARK 500    VAL B 229     -106.87    -72.15                                   
REMARK 500    VAL B 230       89.24     47.88                                   
REMARK 500    SER B 233      161.38     52.65                                   
REMARK 500    ALA B 237      -32.22    103.71                                   
REMARK 500    GLU B 243      -64.21    128.10                                   
REMARK 500    ALA B 244     -121.57     52.79                                   
REMARK 500    THR B 247      116.84     27.42                                   
REMARK 500    LYS C   4       92.49     71.13                                   
REMARK 500    ILE C   8      -72.70    -67.58                                   
REMARK 500    ILE C  14     -142.98   -111.21                                   
REMARK 500    THR C  15       59.48    -24.01                                   
REMARK 500    ARG C  16      137.31    159.72                                   
REMARK 500    ALA C  24     -127.64    159.54                                   
REMARK 500    LYS C  26      -79.20     71.77                                   
REMARK 500    TYR C  29      -76.59    -24.79                                   
REMARK 500    GLU C  46      -74.36   -108.52                                   
REMARK 500    LEU C  47       42.15    -63.45                                   
REMARK 500    SER C  49       -7.75    -47.47                                   
REMARK 500    ALA C  60       37.60   -151.89                                   
REMARK 500    ALA C  61      104.53     79.81                                   
REMARK 500    ALA C  65      -66.99   -105.88                                   
REMARK 500    VAL C  66      106.36     59.57                                   
REMARK 500    LYS C  72       68.07   -112.29                                   
REMARK 500    ILE C  77      -79.89    -58.26                                   
REMARK 500    LYS C  93       -4.86    -49.30                                   
REMARK 500    ASN C  98       85.53     64.23                                   
REMARK 500    LEU C 101      115.84   -166.22                                   
REMARK 500    GLN C 107       91.42    -63.86                                   
REMARK 500    ASN C 108       84.95     60.57                                   
REMARK 500    ASN C 110       12.14    -66.98                                   
REMARK 500    ILE C 134      -80.35    -58.58                                   
REMARK 500    SER C 144       52.56   -117.82                                   
REMARK 500    ALA C 146      145.95     54.28                                   
REMARK 500    LYS C 150      118.51   -171.03                                   
REMARK 500    SER C 154     -142.88    -48.11                                   
REMARK 500    ILE C 157      102.32    -56.93                                   
REMARK 500    TRP C 167     -108.91   -106.38                                   
REMARK 500    ALA C 168      134.53     71.01                                   
REMARK 500    ALA C 169      132.81    175.07                                   
REMARK 500    LEU C 178       52.71    -63.19                                   
REMARK 500    ARG C 179      -35.29   -164.23                                   
REMARK 500    ASN C 181       70.68     73.78                                   
REMARK 500    GLU C 206      -90.92   -142.29                                   
REMARK 500    TYR D   4     -102.32     49.63                                   
REMARK 500    ILE D   5      111.48     63.59                                   
REMARK 500    VAL D   8      -64.85   -108.32                                   
REMARK 500    CYS D   9      -19.66    -40.77                                   
REMARK 500    LYS D  22       -5.25   -140.03                                   
REMARK 500    GLU D  24     -168.80    -67.00                                   
REMARK 500    ARG D  25      -70.24     55.46                                   
REMARK 500    CYS D  26       27.96    -51.18                                   
REMARK 500    TYR D  27      -40.33   -134.63                                   
REMARK 500    PRO D  29       77.22    -56.47                                   
REMARK 500    LYS D  30        2.66   -169.47                                   
REMARK 500    CYS D  31       21.40    -76.08                                   
REMARK 500    ALA D  32      -51.88     69.04                                   
REMARK 500    MET D  33        2.83    -55.30                                   
REMARK 500    ARG D  36       40.55    158.96                                   
REMARK 500    LYS D  46     -175.00    -55.90                                   
REMARK 500    ARG D  50      109.36    -40.88                                   
REMARK 500    GLN D  62      -19.42    -48.51                                   
REMARK 500    ARG D  76      -73.34    -50.52                                   
REMARK 500    ASN D  77      -34.36    -34.11                                   
REMARK 500    ALA D  82      -85.04    -47.34                                   
REMARK 500    SER D  83      -49.14    -12.65                                   
REMARK 500    THR D  89      -60.97    -27.36                                   
REMARK 500    PHE D 110      -25.55    -36.63                                   
REMARK 500    SER D 137       18.04    -67.64                                   
REMARK 500    ARG D 153       -8.31    -52.47                                   
REMARK 500    LYS D 166       91.01    -49.92                                   
REMARK 500    PRO D 172        5.86    -61.73                                   
REMARK 500    SER D 175      145.37   -173.71                                   
REMARK 500    MET D 181       43.36     38.84                                   
REMARK 500    ARG D 191      -45.56    -21.48                                   
REMARK 500    ALA D 195       64.99   -104.17                                   
REMARK 500    PHE E   6     -159.45   -133.43                                   
REMARK 500    ALA E  17      124.85     52.32                                   
REMARK 500    ARG E  37       17.47     85.98                                   
REMARK 500    VAL E  51      -51.56    -28.85                                   
REMARK 500    ALA E  62      -73.38    -56.20                                   
REMARK 500    ASN E  65       63.30   -111.04                                   
REMARK 500    GLU E  68      108.59    -50.47                                   
REMARK 500    ASN E  73      -90.15     72.96                                   
REMARK 500    ILE E  80      140.20   -173.41                                   
REMARK 500    PHE E  84     -115.74   -132.25                                   
REMARK 500    VAL E 100      -78.52    -71.17                                   
REMARK 500    ILE E 101       78.81     80.60                                   
REMARK 500    VAL E 105      -82.22    -68.74                                   
REMARK 500    PRO E 106      -32.04    -36.14                                   
REMARK 500    THR E 116      -23.62   -146.50                                   
REMARK 500    LEU E 123       30.29   -161.67                                   
REMARK 500    SER E 125       63.78     12.96                                   
REMARK 500    ARG E 126       53.18    -60.16                                   
REMARK 500    PRO E 128      -36.92    -30.63                                   
REMARK 500    ALA E 132      -75.50    -57.34                                   
REMARK 500    LYS E 145       22.22     80.43                                   
REMARK 500    LYS E 153     -178.15    -69.63                                   
REMARK 500    ALA E 156       91.61     96.69                                   
REMARK 500    GLN F  16      -33.08    -28.81                                   
REMARK 500    LEU F  45      121.38     60.62                                   
REMARK 500    LYS F  54       -5.08     63.57                                   
REMARK 500    GLU F  69      -59.07    -10.45                                   
REMARK 500    ASP F  70      -11.25    -44.88                                   
REMARK 500    VAL F  72      -67.91    -23.87                                   
REMARK 500    GLU F  95      165.84    -37.26                                   
REMARK 500    LEU F  98      130.73    -28.53                                   
REMARK 500    ALA F  99      129.46   -173.66                                   
REMARK 500    ASN F 100     -176.83    149.42                                   
REMARK 500    ARG G   3      -82.75    -60.95                                   
REMARK 500    ARG G   4     -159.95   -103.31                                   
REMARK 500    ARG G   5      -18.22     67.82                                   
REMARK 500    ARG G   6       80.28     39.29                                   
REMARK 500    ALA G   7      143.96    -21.31                                   
REMARK 500    VAL G   9      106.41    -50.05                                   
REMARK 500    PRO G  14      163.99    -46.01                                   
REMARK 500    TYR G  18      -21.09   -140.93                                   
REMARK 500    ASP G  20       86.16   -159.49                                   
REMARK 500    VAL G  21      -88.48      5.87                                   
REMARK 500    LEU G  22      -37.65    -24.86                                   
REMARK 500    LYS G  36      -97.61     21.30                                   
REMARK 500    ASN G  37      -67.40    -19.09                                   
REMARK 500    ILE G  49      -12.89    -44.46                                   
REMARK 500    GLU G  52      -89.16    -87.56                                   
REMARK 500    LYS G  53       -8.43    -40.52                                   
REMARK 500    GLU G  57      152.73    -49.12                                   
REMARK 500    VAL G  69      -68.95    -90.95                                   
REMARK 500    LYS G  70      120.50    -15.55                                   
REMARK 500    GLU G  74     -144.15   -131.76                                   
REMARK 500    VAL G  75       76.81   -164.54                                   
REMARK 500    SER G  77      150.46    -49.21                                   
REMARK 500    ARG G  79       74.19   -109.81                                   
REMARK 500    VAL G  80       11.09    -59.64                                   
REMARK 500    VAL G  87      104.68     49.33                                   
REMARK 500    SER G  98      -70.37    -36.97                                   
REMARK 500    ALA G 100      -78.38    -36.80                                   
REMARK 500    GLN G 106      -74.18    -71.60                                   
REMARK 500    ARG G 111      172.53    -56.22                                   
REMARK 500    GLU G 113      147.63    -31.76                                   
REMARK 500    ALA G 116      -63.62   -106.15                                   
REMARK 500    GLU G 129        8.76   -152.07                                   
REMARK 500    VAL G 141      -80.48    -81.84                                   
REMARK 500    GLU G 142       -2.15    -44.77                                   
REMARK 500    MET G 144        5.41    -67.01                                   
REMARK 500    ALA G 147      -40.79    164.49                                   
REMARK 500    ASN G 148     -148.69     71.15                                   
REMARK 500    ARG G 149       69.86   -173.72                                   
REMARK 500    ALA G 150       84.49     74.65                                   
REMARK 500    ARG G 155      -55.21     12.02                                   
REMARK 500    ALA H   7      -38.93    -35.16                                   
REMARK 500    SER H  23      148.97   -173.15                                   
REMARK 500    SER H  29      138.28    172.40                                   
REMARK 500    ARG H  30      -71.26    -34.23                                   
REMARK 500    PHE H  31      -73.45    -39.47                                   
REMARK 500    ASP H  54      -10.54     75.91                                   
REMARK 500    TYR H  65     -137.82   -126.59                                   
REMARK 500    ASP H  73       79.90     47.47                                   
REMARK 500    ILE H  80       78.95   -101.21                                   
REMARK 500    ILE H  86      -67.22   -105.08                                   
REMARK 500    ARG H  91        8.54    171.22                                   
REMARK 500    ARG H  92      113.66    -24.73                                   
REMARK 500    VAL H 103      123.90     45.92                                   
REMARK 500    ARG H 104       47.87     29.45                                   
REMARK 500    ARG H 105       63.48     37.13                                   
REMARK 500    ALA H 110       93.34   -164.29                                   
REMARK 500    PRO H 115        7.56    -52.74                                   
REMARK 500    ASP H 121      -49.69    -19.70                                   
REMARK 500    ARG H 122      -92.37    -57.78                                   
REMARK 500    GLU H 123      -66.06    -26.99                                   
REMARK 500    ARG I   9       98.54   -165.73                                   
REMARK 500    GLU I  12        1.85     81.80                                   
REMARK 500    PRO I  21       51.98    -62.38                                   
REMARK 500    LYS I  25      132.57    -14.44                                   
REMARK 500    ASN I  29       -4.46     47.28                                   
REMARK 500    PHE I  37       39.24    -81.54                                   
REMARK 500    GLN I  38      -89.99    -20.45                                   
REMARK 500    LEU I  40      129.22    -39.82                                   
REMARK 500    ASP I  54       80.06     81.54                                   
REMARK 500    ALA I  55     -158.06   -126.40                                   
REMARK 500    ARG I  58      -30.91   -141.97                                   
REMARK 500    ARG I  66      120.56    171.75                                   
REMARK 500    PRO I  90       -9.56    -51.73                                   
REMARK 500    ALA I  94      -22.98    -34.20                                   
REMARK 500    VAL I 109      102.05    -52.21                                   
REMARK 500    TYR I 114      148.85    -33.16                                   
REMARK 500    HIS I 117      -72.56    -52.99                                   
REMARK 500    LYS I 118       63.84   -118.56                                   
REMARK 500    ALA I 119      -61.02     81.11                                   
REMARK 500    SER I 126     -170.73    174.31                                   
REMARK 500    LYS I 127      118.65     56.08                                   
REMARK 500    LEU J  16      -65.52   -130.99                                   
REMARK 500    SER J  19      -58.22    -26.93                                   
REMARK 500    VAL J  24      -81.92    -70.46                                   
REMARK 500    ARG J  28       27.11    -70.43                                   
REMARK 500    SER J  30      -69.54   -165.23                                   
REMARK 500    VAL J  34      161.95     69.09                                   
REMARK 500    PRO J  39      -97.58    -63.89                                   
REMARK 500    LEU J  40      135.09     97.90                                   
REMARK 500    ARG J  51      -79.16    -64.07                                   
REMARK 500    PHE J  54      134.16     62.92                                   
REMARK 500    LYS J  55     -163.79     31.17                                   
REMARK 500    ASP J  58       15.38    -67.12                                   
REMARK 500    SER J  59      -85.69   -102.96                                   
REMARK 500    ARG J  60      146.34     57.57                                   
REMARK 500    LEU J  71      -31.06   -142.53                                   
REMARK 500    VAL J  72      -90.72     63.66                                   
REMARK 500    ASP J  73       92.09     79.44                                   
REMARK 500    ASN J  76       80.77     31.33                                   
REMARK 500    ARG J  79      -73.25     21.41                                   
REMARK 500    ILE J  82        5.23    -60.84                                   
REMARK 500    GLU J  83      -92.62    -69.93                                   
REMARK 500    LEU J  88       41.94   -168.32                                   
REMARK 500    THR J  92      -67.39   -107.85                                   
REMARK 500    LYS K   8      -97.33     95.59                                   
REMARK 500    VAL K  10      116.53     42.50                                   
REMARK 500    ALA K  15      -43.18     63.06                                   
REMARK 500    ALA K  19       69.73   -150.52                                   
REMARK 500    TYR K  25       31.57    -62.59                                   
REMARK 500    ASN K  26      -40.67   -147.45                                   
REMARK 500    PRO K  35       -5.09    -47.09                                   
REMARK 500    ASN K  38      130.41    -37.39                                   
REMARK 500    SER K  43     -155.22   -124.23                                   
REMARK 500    SER K  44     -143.95    178.43                                   
REMARK 500    TYR K  50      114.18      6.47                                   
REMARK 500    ALA K  60      -16.91    -44.55                                   
REMARK 500    ALA K  61      -78.75    -89.38                                   
REMARK 500    ALA K  65       23.61    -68.43                                   
REMARK 500    MET K  77      109.97     11.78                                   
REMARK 500    GLU K  92      -43.01     62.38                                   
REMARK 500    ILE K  95      -70.46    -65.66                                   
REMARK 500    LYS K 106      -77.28    -55.45                                   
REMARK 500    ASP K 111       14.58   -141.19                                   
REMARK 500    HIS K 116       46.78    -70.39                                   
REMARK 500    ASN K 117       90.05     67.56                                   
REMARK 500    CYS K 119      113.81     76.81                                   
REMARK 500    ARG K 126      -49.93   -170.33                                   
REMARK 500    ALA K 128      -48.95   -167.84                                   
REMARK 500    LYS L  13       65.18     67.42                                   
REMARK 500    LYS L  23       33.32    -87.52                                   
REMARK 500    VAL L  24       77.57   -155.92                                   
REMARK 500    PRO L  25       46.77    -60.38                                   
REMARK 500    LEU L  27      162.00    -13.62                                   
REMARK 500    LYS L  28       45.63     32.75                                   
REMARK 500    ALA L  30      126.77     44.90                                   
REMARK 500    CYS L  37      153.14    -48.83                                   
REMARK 500    THR L  38      -59.36   -127.00                                   
REMARK 500    VAL L  40       78.11   -101.46                                   
REMARK 500    ARG L  41     -162.44    -77.92                                   
REMARK 500    PRO L  45     -121.89    -82.50                                   
REMARK 500    LYS L  47      -70.03    -37.49                                   
REMARK 500    ALA L  51     -153.41    142.09                                   
REMARK 500    PRO L  71      172.12    -59.30                                   
REMARK 500    ASN L  76       54.46   -107.67                                   
REMARK 500    GLN L  78     -156.25   -128.91                                   
REMARK 500    HIS L  80        2.83   -151.36                                   
REMARK 500    ARG L  86      -99.62   -100.01                                   
REMARK 500    ARG L  97       10.96   -150.76                                   
REMARK 500    TYR L 105     -165.74     65.51                                   
REMARK 500    ASP L 106       -6.89    -40.79                                   
REMARK 500    ASP L 112      -15.47     66.82                                   
REMARK 500    ARG L 113      157.49    -48.71                                   
REMARK 500    LYS L 115      -55.07   -132.18                                   
REMARK 500    SER L 116      -83.23    -50.43                                   
REMARK 500    ARG L 117      -84.67     62.34                                   
REMARK 500    TYR L 120       31.34     87.50                                   
REMARK 500    LYS L 123      121.09    -35.43                                   
REMARK 500    LYS L 124      178.87    -56.45                                   
REMARK 500    GLU L 127       96.36     46.80                                   
REMARK 500    ALA L 128       -7.85     67.81                                   
REMARK 500    ALA L 129       72.81     50.35                                   
REMARK 500    THR L 131     -174.82    -61.74                                   
REMARK 500    ALA L 132       -4.03    -56.86                                   
REMARK 500    ALA L 133      100.06   -175.43                                   
REMARK 500    LYS L 134     -105.51   -154.21                                   
REMARK 500    ARG M   3      109.92    -52.92                                   
REMARK 500    ILE M   4     -108.57   -104.37                                   
REMARK 500    ILE M   9       76.08   -116.31                                   
REMARK 500    ASN M  12      -16.97     83.27                                   
REMARK 500    ASP M  16      -38.27    -38.62                                   
REMARK 500    LEU M  19      -19.83    -40.27                                   
REMARK 500    TYR M  21        4.62    -61.77                                   
REMARK 500    TYR M  23       98.72    -66.01                                   
REMARK 500    LYS M  27      -62.18     48.51                                   
REMARK 500    ALA M  28      -70.08    -53.39                                   
REMARK 500    GLU M  35      -74.61    -48.81                                   
REMARK 500    LYS M  36      -72.76    -53.72                                   
REMARK 500    THR M  37      -21.86    -38.70                                   
REMARK 500    ASN M  40      105.82    -46.20                                   
REMARK 500    ASN M  62       67.60   -104.44                                   
REMARK 500    THR M  63      -27.42   -173.16                                   
REMARK 500    GLU M  67     -147.39     37.27                                   
REMARK 500    ARG M  80      -76.48     -6.14                                   
REMARK 500    ARG M  93      -57.30   -120.04                                   
REMARK 500    GLU N   8       31.68   -143.86                                   
REMARK 500    LYS N  11       48.25    -97.59                                   
REMARK 500    ARG N  12      -83.71      6.81                                   
REMARK 500    THR N  13       97.57    -29.99                                   
REMARK 500    LYS N  15      -32.24     83.21                                   
REMARK 500    LYS N  17      -39.92    -33.72                                   
REMARK 500    VAL N  18       -3.38    -55.97                                   
REMARK 500    ARG N  23      143.27     56.28                                   
REMARK 500    VAL N  25       60.90   -107.39                                   
REMARK 500    ARG N  26      -44.04    176.97                                   
REMARK 500    ARG N  29       89.42    -39.05                                   
REMARK 500    ARG N  31      -84.43    -55.55                                   
REMARK 500    ARG N  41      -22.24    -29.15                                   
REMARK 500    CYS N  43       23.80    -62.91                                   
REMARK 500    SER N  60      121.63    179.58                                   
REMARK 500    ILE O   3     -174.83    -27.98                                   
REMARK 500    THR O   4       93.18     93.18                                   
REMARK 500    LYS O   5      -41.66   -173.66                                   
REMARK 500    ALA O  16      105.79    -50.44                                   
REMARK 500    ARG O  17        2.53    -52.43                                   
REMARK 500    PHE O  18      151.81    174.44                                   
REMARK 500    PRO O  19      103.07    -42.77                                   
REMARK 500    ALA O  30      -82.94    -42.90                                   
REMARK 500    LEU O  31      -48.64    -29.13                                   
REMARK 500    VAL O  45      -73.51    -72.60                                   
REMARK 500    ASP O  74       67.62    158.27                                   
REMARK 500    ILE O  87     -157.45   -111.28                                   
REMARK 500    ARG O  88     -146.48     11.55                                   
REMARK 500    LYS P  12     -122.95     11.39                                   
REMARK 500    HIS P  13       -5.53    -57.48                                   
REMARK 500    ILE P  19       42.95    -79.49                                   
REMARK 500    THR P  22     -170.80   -170.84                                   
REMARK 500    ARG P  26     -177.79    -69.98                                   
REMARK 500    ARG P  28       51.84    -59.55                                   
REMARK 500    ASP P  29        8.80   -167.02                                   
REMARK 500    LYS P  31      163.08    -47.89                                   
REMARK 500    ARG P  42      -39.85    -34.12                                   
REMARK 500    LYS P  43       54.76     71.42                                   
REMARK 500    PRO P  46      -19.40    -36.55                                   
REMARK 500    TRP P  48      -90.90   -107.30                                   
REMARK 500    VAL P  53      -66.39    -24.26                                   
REMARK 500    GLU P  54      -78.41    -31.49                                   
REMARK 500    VAL P  79        5.09    -60.22                                   
REMARK 500    GLU P  83      115.60    -21.12                                   
REMARK 500    ARG P  85     -178.28    171.48                                   
REMARK 500    GLU P  86       72.39     51.71                                   
REMARK 500    VAL Q  11        1.22   -154.19                                   
REMARK 500    SER Q  12      121.32   -172.33                                   
REMARK 500    GLU Q  49       14.38     59.04                                   
REMARK 500    VAL Q  53      159.75    -40.85                                   
REMARK 500    ALA Q  62     -169.65   -171.00                                   
REMARK 500    SER Q  66      177.07    150.42                                   
REMARK 500    ARG Q  68      -39.28    107.39                                   
REMARK 500    ARG Q  70       13.43   -144.82                                   
REMARK 500    LEU Q  74      -84.71    -55.20                                   
REMARK 500    VAL Q  77        5.79   -152.60                                   
REMARK 500    GLU Q  78      109.90    151.46                                   
REMARK 500    GLU Q  79       30.92    -77.06                                   
REMARK 500    ARG Q  81       84.29   -170.13                                   
REMARK 500    GLN Q  93      -34.61    -27.51                                   
REMARK 500    ALA Q  96      -19.61    -33.92                                   
REMARK 500    SER Q  99      153.87     52.84                                   
REMARK 500    LYS Q 100      -83.20     79.40                                   
REMARK 500    ARG Q 101      -37.78    -31.11                                   
REMARK 500    GLU R  11      -30.56     74.25                                   
REMARK 500    ALA R  12       17.20     50.69                                   
REMARK 500    PRO R  16       72.03    -56.85                                   
REMARK 500    SER R  17       30.55     34.81                                   
REMARK 500    ARG R  18      -79.29     50.04                                   
REMARK 500    LYS R  19      119.30     64.12                                   
REMARK 500    LYS R  21      103.58    -24.23                                   
REMARK 500    VAL R  22      -81.80     13.74                                   
REMARK 500    THR R  25       90.97     61.72                                   
REMARK 500    LEU R  26     -170.29     73.90                                   
REMARK 500    GLU R  28       85.72     56.26                                   
REMARK 500    ASP R  30      171.47    -42.69                                   
REMARK 500    TYR R  34       36.80    -82.31                                   
REMARK 500    ARG R  35      -35.82   -155.54                                   
REMARK 500    ASN R  36       28.24    -59.37                                   
REMARK 500    VAL R  37      -71.35    -21.67                                   
REMARK 500    GLU R  38      -41.00    -17.26                                   
REMARK 500    LYS R  41      -16.18    -46.42                                   
REMARK 500    PHE R  43       55.66    -92.39                                   
REMARK 500    SER R  45     -177.31    -63.01                                   
REMARK 500    ARG R  55     -132.11    -91.44                                   
REMARK 500    THR R  56      -90.63     32.67                                   
REMARK 500    LYS R  68      -17.81    -44.65                                   
REMARK 500    ARG R  87      165.86     76.09                                   
REMARK 500    LYS S   6     -100.37     91.96                                   
REMARK 500    ASP S  13       25.82    -72.93                                   
REMARK 500    GLU S  17       -3.77    -58.04                                   
REMARK 500    LEU S  30      127.63     71.00                                   
REMARK 500    SER S  35       46.42    -64.80                                   
REMARK 500    GLU S  43      -14.60    -41.45                                   
REMARK 500    VAL S  45      140.93    -39.60                                   
REMARK 500    HIS S  47     -176.93    -42.56                                   
REMARK 500    LYS S  55      -59.01   -142.91                                   
REMARK 500    ASN S  65       32.48    -73.88                                   
REMARK 500    MET S  66       55.14   -169.88                                   
REMARK 500    HIS S  69     -175.10    -58.48                                   
REMARK 500    LEU S  71      -77.29     18.25                                   
REMARK 500    THR S  77      -44.59   -131.35                                   
REMARK 500    SER T  19      -72.56    -26.79                                   
REMARK 500    ARG T  25      -70.34    -57.54                                   
REMARK 500    LYS T  30      -72.21    -52.96                                   
REMARK 500    SER T  37      -70.68    -58.71                                   
REMARK 500    ILE T  41      -82.15    -70.22                                   
REMARK 500    GLN T  42      -57.49    -12.71                                   
REMARK 500    LYS T  48       98.11    -53.87                                   
REMARK 500    ALA T  49      -93.85    -45.52                                   
REMARK 500    GLU T  51      -27.15    -35.92                                   
REMARK 500    ALA T  59      -70.08    -41.79                                   
REMARK 500    SER T  61      -72.13    -54.19                                   
REMARK 500    LEU T  62      -49.23    -26.12                                   
REMARK 500    ILE T  63      -84.59    -48.00                                   
REMARK 500    SER T  70       31.00   -155.21                                   
REMARK 500    HIS T  73     -172.52     42.78                                   
REMARK 500    LYS T  74     -140.82     49.89                                   
REMARK 500    ARG T  80      -77.66    -29.07                                   
REMARK 500    LYS T  81      -74.51    -40.08                                   
REMARK 500    MET T  85       11.84    -59.27                                   
REMARK 500    VAL T  88      -75.40    -62.26                                   
REMARK 500    ALA T  95       95.75     59.78                                   
REMARK 500    ALA T  97       93.16     60.57                                   
REMARK 500    PRO T  98       96.94    -58.26                                   
REMARK 500    LEU T 104       82.06   -152.61                                   
REMARK 500    SER T 105      100.62    -53.56                                   
REMARK 500    LYS U   3      -50.92     -2.21                                   
REMARK 500    ASP U   5       96.03    -60.08                                   
REMARK 500    ARG U   7       63.50   -113.38                                   
REMARK 500    THR U   8     -169.17   -161.66                                   
REMARK 500    ARG U   9      -74.27    -66.06                                   
REMARK 500    ARG U  22       73.96   -157.31                                   
REMARK 500    PRO U  23      172.50    -58.20                                   
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      U A   2         0.12    SIDE_CHAIN                              
REMARK 500      G A   3         0.09    SIDE_CHAIN                              
REMARK 500      A A   8         0.05    SIDE_CHAIN                              
REMARK 500      U A  45         0.06    SIDE_CHAIN                              
REMARK 500      C A  47         0.12    SIDE_CHAIN                              
REMARK 500      C A  48         0.06    SIDE_CHAIN                              
REMARK 500      U A  49         0.07    SIDE_CHAIN                              
REMARK 500      A A  50         0.06    SIDE_CHAIN                              
REMARK 500      A A  51         0.06    SIDE_CHAIN                              
REMARK 500      U A  79         0.08    SIDE_CHAIN                              
REMARK 500      G A 101         0.06    SIDE_CHAIN                              
REMARK 500      A A 124         0.05    SIDE_CHAIN                              
REMARK 500      U A 174         0.07    SIDE_CHAIN                              
REMARK 500      U A 196         0.07    SIDE_CHAIN                              
REMARK 500      U A 208         0.07    SIDE_CHAIN                              
REMARK 500      U A 224         0.09    SIDE_CHAIN                              
REMARK 500      U A 239         0.07    SIDE_CHAIN                              
REMARK 500      A A 241         0.09    SIDE_CHAIN                              
REMARK 500      G A 261         0.07    SIDE_CHAIN                              
REMARK 500      C A 275         0.07    SIDE_CHAIN                              
REMARK 500      C A 367         0.07    SIDE_CHAIN                              
REMARK 500      C A 374         0.07    SIDE_CHAIN                              
REMARK 500      U A 400         0.08    SIDE_CHAIN                              
REMARK 500      G A 423         0.05    SIDE_CHAIN                              
REMARK 500      U A 424         0.07    SIDE_CHAIN                              
REMARK 500      U A 478         0.07    SIDE_CHAIN                              
REMARK 500      G A 512         0.08    SIDE_CHAIN                              
REMARK 500      A A 516         0.07    SIDE_CHAIN                              
REMARK 500      A A 546         0.07    SIDE_CHAIN                              
REMARK 500      G A 551         0.05    SIDE_CHAIN                              
REMARK 500      G A 553         0.05    SIDE_CHAIN                              
REMARK 500      U A 554         0.07    SIDE_CHAIN                              
REMARK 500      G A 558         0.12    SIDE_CHAIN                              
REMARK 500      A A 594         0.06    SIDE_CHAIN                              
REMARK 500      G A 704         0.05    SIDE_CHAIN                              
REMARK 500      U A 784         0.07    SIDE_CHAIN                              
REMARK 500      C A 809         0.06    SIDE_CHAIN                              
REMARK 500      A A 842         0.06    SIDE_CHAIN                              
REMARK 500      U A 847         0.07    SIDE_CHAIN                              
REMARK 500      G A 867         0.06    SIDE_CHAIN                              
REMARK 500      A A 877         0.06    SIDE_CHAIN                              
REMARK 500      A A 896         0.05    SIDE_CHAIN                              
REMARK 500      U A 897         0.07    SIDE_CHAIN                              
REMARK 500      G A 970         0.05    SIDE_CHAIN                              
REMARK 500      U A1031         0.11    SIDE_CHAIN                              
REMARK 500      A A1049         0.06    SIDE_CHAIN                              
REMARK 500      U A1068         0.07    SIDE_CHAIN                              
REMARK 500      G A1106         0.05    SIDE_CHAIN                              
REMARK 500      G A1121         0.05    SIDE_CHAIN                              
REMARK 500      U A1130         0.07    SIDE_CHAIN                              
REMARK 500      G A1162         0.05    SIDE_CHAIN                              
REMARK 500      G A1163         0.05    SIDE_CHAIN                              
REMARK 500      U A1175         0.07    SIDE_CHAIN                              
REMARK 500      G A1205         0.07    SIDE_CHAIN                              
REMARK 500      A A1261         0.07    SIDE_CHAIN                              
REMARK 500      C A1278         0.06    SIDE_CHAIN                              
REMARK 500      C A1303         0.10    SIDE_CHAIN                              
REMARK 500      U A1326         0.08    SIDE_CHAIN                              
REMARK 500      G A1328         0.06    SIDE_CHAIN                              
REMARK 500      U A1332         0.08    SIDE_CHAIN                              
REMARK 500      G A1352         0.07    SIDE_CHAIN                              
REMARK 500      U A1362         0.07    SIDE_CHAIN                              
REMARK 500      G A1383         0.06    SIDE_CHAIN                              
REMARK 500      C A1432         0.06    SIDE_CHAIN                              
REMARK 500      A A1479         0.06    SIDE_CHAIN                              
REMARK 500      U A1483         0.10    SIDE_CHAIN                              
REMARK 500      G A1503         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1526  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A  67   O2'                                                    
REMARK 620 2   A A 166   O4' 158.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1527  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 183   O5'                                                    
REMARK 620 2   C A 184   OP2 129.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1528  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 190   O5'                                                    
REMARK 620 2   G A 190   O4'  84.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1530  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 294   O6                                                     
REMARK 620 2   G A 541   OP1 138.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1538  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 526   O3'                                                    
REMARK 620 2   G A 527   OP1  71.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1540  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 555   OP2                                                    
REMARK 620 2   A A 557   OP2 147.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1543  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 579   OP2                                                    
REMARK 620 2   G A 580   OP2 129.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1564  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 921   OP1                                                    
REMARK 620 2   G A 922   OP2  90.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1567  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1178   OP1                                                    
REMARK 620 2   G A1179   OP2  76.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1571  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A1284   OP1                                                    
REMARK 620 2   G A1285   OP2 132.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1574  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1477   OP2                                                    
REMARK 620 2   G A1482   OP1 112.9                                              
REMARK 620 3   G A1482   OP2 121.0  66.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 210  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG D   3   N                                                      
REMARK 620 2 ARG D   3   O    77.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 211  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG D 114   N                                                      
REMARK 620 2 ARG D 115   N    87.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E   1  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 120   O                                                      
REMARK 620 2 LYS E 121   N    58.3                                              
REMARK 620 3 GLU E 122   N   145.4 101.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG P  89  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG P  28   N                                                      
REMARK 620 2 ASP P  29   N    75.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Q 106  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG Q  25   O                                                      
REMARK 620 2 ARG Q  38   N   130.3                                              
REMARK 620 3 ARG Q  38   O   135.5  70.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG T 108  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS T  16   O                                                      
REMARK 620 2 GLN T  18   N   114.5                                              
REMARK 620 3 SER T  19   N   142.4  77.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1517                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 136                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1520                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1521                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1522                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1523                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1524                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1526                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 107                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1527                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1528                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 106                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 107                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1530                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 89                   
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 108                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 109                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1532                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 137                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1535                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 210                  
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 211                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 138                  
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1538                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1539                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1540                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1541                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1542                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1543                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1544                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1545                 
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1546                 
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 130                  
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 157                  
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1548                 
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1549                 
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1550                 
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1551                 
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1552                 
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1553                 
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1555                 
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1556                 
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1558                 
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1560                 
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1561                 
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1562                 
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1563                 
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1564                 
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1565                 
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1567                 
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1568                 
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1569                 
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1570                 
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1571                 
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1572                 
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 106                  
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1574                 
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 76                   
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 212                  
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1001                
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1002                
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 C 1003                
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1004                
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 E 1005                
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 G 1006                
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 G 1007                
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 R 1008                
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 J 1009                
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 H 1010                
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 A 1576                
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 D 1012                
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 T 1013                
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 K 1014                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FKA   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL RIBOSOMAL SUBUNIT          
REMARK 900 AT 3.3 A RESOLUTION                                                  
REMARK 900 RELATED ID: 1I95   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS          
REMARK 900 THERMOPHILUS IN COMPLEX WITH EDEINE                                  
REMARK 900 RELATED ID: 1I96   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS          
REMARK 900 THERMOPHILUS IN COMPLEX WITH THE TRANSLATION INITIATION              
REMARK 900 FACTOR IF3 (C-TERMINAL DOMAIN)                                       
REMARK 900 RELATED ID: 1I97   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS          
REMARK 900 THERMOPHILUS IN COMPLEX WITH TETRACYCLINE                            
DBREF  1I94 A    2  1515  GB     155076   M26923         648   2161             
DBREF  1I94 B    2   256  GB     13446664 CAC35061         2    256             
DBREF  1I94 C    2   239  GB     13446666 CAC35062         2    239             
DBREF  1I94 D    2   209  UNP    P80373   RS4_THETH        1    208             
DBREF  1I94 E    2   162  UNP    P27152   RS5_THETH        1    161             
DBREF  1I94 F    1   101  UNP    P23370   RS6_THETH        1    101             
DBREF  1I94 G    2   156  UNP    P17291   P17291           1    155             
DBREF  1I94 H    1   138  UNP    P24319   RS8_THETH        1    138             
DBREF  1I94 I    1   128  GB     13446668 CAC35063         1    128             
DBREF  1I94 J    2   105  UNP    P80375   RS10_THETH       1    104             
DBREF  1I94 K    2   129  GB     4519421  BAA75547         2    129             
DBREF  1I94 L    5   135  UNP    P17293   RS12_THETH       5    135             
DBREF  1I94 M    2   126  GB     4519420  BAA75546         2    126             
DBREF  1I94 N    2    61  UNP    P24320   RS14_THETH       1     60             
DBREF  1I94 O    2    89  UNP    P80378   RS15_THETH       1     88             
DBREF  1I94 P    1    88  GB     12056104 CAC21226         1     88             
DBREF  1I94 Q    2   105  UNP    P24321   RS17_THETH       1    104             
DBREF  1I94 R    2    88  GB     6739549  AAF27297         2     88             
DBREF  1I94 S    2    93  UNP    P80381   RS19_THETH       1     92             
DBREF  1I94 T    2   106  GB     11125386 CAC15067         2    106             
DBREF  1I94 U    2    27  GB     11125387 CAC15068         2     27             
SEQRES   1 A 1514    U   G   U   U   G   G   A   G   A   G   U   U   U          
SEQRES   2 A 1514    G   A   U   C   C   U   G   G   C   U   C   A   G          
SEQRES   3 A 1514    G   G   U   G   A   A   C   G   C   U   G   G   C          
SEQRES   4 A 1514    G   G   C   G   U   G   C   C   U   A   A   G   A          
SEQRES   5 A 1514    C   A   U   G   C   A   A   G   U   C   G   U   G          
SEQRES   6 A 1514    C   G   G   G   C   C   G   C   G   G   G   G   U          
SEQRES   7 A 1514    U   U   U   A   C   U   C   C   G   U   G   G   U          
SEQRES   8 A 1514    C   A   G   C   G   G   C   G   G   A   C   G   G          
SEQRES   9 A 1514    G   U   G   A   G   U   A   A   C   G   C   G   U          
SEQRES  10 A 1514    G   G   G   U   G   A   C   C   U   A   C   C   C          
SEQRES  11 A 1514    G   G   A   A   G   A   G   G   G   G   G   A   C          
SEQRES  12 A 1514    A   A   C   C   C   G   G   G   G   A   A   A   C          
SEQRES  13 A 1514    U   C   G   G   G   C   U   A   A   U   C   C   C          
SEQRES  14 A 1514    C   C   A   U   G   U   G   G   A   C   C   C   G          
SEQRES  15 A 1514    C   C   C   C   U   U   G   G   G   G   U   G   U          
SEQRES  16 A 1514    G   U   C   C   A   A   A   G   G   G   C   U   U          
SEQRES  17 A 1514    U   G   C   C   C   G   C   U   U   C   C   G   G          
SEQRES  18 A 1514    A   U   G   G   G   C   C   C   G   C   G   U   C          
SEQRES  19 A 1514    C   C   A   U   C   A   G   C   U   A   G   U   U          
SEQRES  20 A 1514    G   G   U   G   G   G   G   U   A   A   U   G   G          
SEQRES  21 A 1514    C   C   C   A   C   C   A   A   G   G   C   G   A          
SEQRES  22 A 1514    C   G   A   C   G   G   G   U   A   G   C   C   G          
SEQRES  23 A 1514    G   U   C   U   G   A   G   A   G   G   A   U   G          
SEQRES  24 A 1514    G   C   C   G   G   C   C   A   C   A   G   G   G          
SEQRES  25 A 1514    G   C   A   C   U   G   A   G   A   C   A   C   G          
SEQRES  26 A 1514    G   G   C   C   C   C   A   C   U   C   C   U   A          
SEQRES  27 A 1514    C   G   G   G   A   G   G   C   A   G   C   A   G          
SEQRES  28 A 1514    U   U   A   G   G   A   A   U   C   U   U   C   C          
SEQRES  29 A 1514    G   C   A   A   U   G   G   G   C   G   C   A   A          
SEQRES  30 A 1514    G   C   C   U   G   A   C   G   G   A   G   C   G          
SEQRES  31 A 1514    A   C   G   C   C   G   C   U   U   G   G   A   G          
SEQRES  32 A 1514    G   A   A   G   A   A   G   C   C   C   U   U   C          
SEQRES  33 A 1514    G   G   G   G   U   G   U   A   A   A   C   U   C          
SEQRES  34 A 1514    C   U   G   A   A   C   C   C   G   G   G   A   C          
SEQRES  35 A 1514    G   A   A   A   C   C   C   C   C   G   A   C   G          
SEQRES  36 A 1514    A   G   G   G   G   A   C   U   G   A   C   G   G          
SEQRES  37 A 1514    U   A   C   C   G   G   G   G   U   A   A   U   A          
SEQRES  38 A 1514    G   C   G   C   C   G   G   C   C   A   A   C   U          
SEQRES  39 A 1514    C   C   G   U   G   C   C   A   G   C   A   G   C          
SEQRES  40 A 1514    C   G   C   G   G   U   A   A   U   A   C   G   G          
SEQRES  41 A 1514    A   G   G   G   C   G   C   G   A   G   C   G   U          
SEQRES  42 A 1514    U   A   C   C   C   G   G   A   U   U   C   A   C          
SEQRES  43 A 1514    U   G   G   G   C   G   U   A   A   A   G   G   G          
SEQRES  44 A 1514    C   G   U   G   U   A   G   G   C   G   G   C   C          
SEQRES  45 A 1514    U   G   G   G   G   C   G   U   C   C   C   A   U          
SEQRES  46 A 1514    G   U   G   A   A   A   G   A   C   C   A   C   G          
SEQRES  47 A 1514    G   C   U   C   A   A   C   C   G   U   G   G   G          
SEQRES  48 A 1514    G   G   A   G   C   G   U   G   G   G   A   U   A          
SEQRES  49 A 1514    C   G   C   U   C   A   G   G   C   U   A   G   A          
SEQRES  50 A 1514    C   G   G   U   G   G   G   A   G   A   G   G   G          
SEQRES  51 A 1514    U   G   G   U   G   G   A   A   U   U   C   C   C          
SEQRES  52 A 1514    G   G   A   G   U   A   G   C   G   G   U   G   A          
SEQRES  53 A 1514    A   A   U   G   C   G   C   A   G   A   U   A   C          
SEQRES  54 A 1514    C   G   G   G   A   G   G   A   A   C   G   C   C          
SEQRES  55 A 1514    G   A   U   G   G   C   G   A   A   G   G   C   A          
SEQRES  56 A 1514    G   C   C   A   C   C   U   G   G   U   C   C   A          
SEQRES  57 A 1514    C   C   C   G   U   G   A   C   G   C   U   G   A          
SEQRES  58 A 1514    G   G   C   G   C   G   A   A   A   G   C   G   U          
SEQRES  59 A 1514    G   G   G   G   A   G   C   A   A   A   C   C   G          
SEQRES  60 A 1514    G   A   U   U   A   G   A   U   A   C   C   C   G          
SEQRES  61 A 1514    G   G   U   A   G   U   C   C   A   C   G   C   C          
SEQRES  62 A 1514    C   U   A   A   A   C   G   A   U   G   C   G   C          
SEQRES  63 A 1514    G   C   U   A   G   G   U   C   U   C   U   G   G          
SEQRES  64 A 1514    G   U   C   U   C   C   U   G   G   G   G   G   C          
SEQRES  65 A 1514    C   G   A   A   G   C   U   A   A   C   G   C   G          
SEQRES  66 A 1514    U   U   A   A   G   C   G   C   G   C   C   G   C          
SEQRES  67 A 1514    C   U   G   G   G   G   A   G   U   A   C   G   G          
SEQRES  68 A 1514    C   C   G   C   A   A   G   G   C   U   G   A   A          
SEQRES  69 A 1514    A   C   U   C   A   A   A   G   G   A   A   U   U          
SEQRES  70 A 1514    G   A   C   G   G   G   G   G   C   C   C   G   C          
SEQRES  71 A 1514    A   C   A   A   G   C   G   G   U   G   G   A   G          
SEQRES  72 A 1514    C   A   U   G   U   G   G   U   U   U   A   A   U          
SEQRES  73 A 1514    U   C   G   A   A   G   C   A   A   C   G   C   G          
SEQRES  74 A 1514    A   A   G   A   A   C   C   U   U   A   C   C   A          
SEQRES  75 A 1514    G   G   C   C   U   U   G   A   C   A   U   G   C          
SEQRES  76 A 1514    U   A   G   G   G   A   A   C   C   C   G   G   G          
SEQRES  77 A 1514    U   G   A   A   A   G   C   C   U   G   G   G   G          
SEQRES  78 A 1514    U   G   C   C   C   C   G   C   G   A   G   G   G          
SEQRES  79 A 1514    G   A   G   C   C   C   U   A   G   C   A   C   A          
SEQRES  80 A 1514    G   G   U   G   C   U   G   C   A   U   G   G   C          
SEQRES  81 A 1514    C   G   U   C   G   U   C   A   G   C   U   C   G          
SEQRES  82 A 1514    U   G   C   C   G   U   G   A   G   G   U   G   U          
SEQRES  83 A 1514    U   G   G   G   U   U   A   A   G   U   C   C   C          
SEQRES  84 A 1514    G   C   A   A   C   G   A   G   C   G   C   A   A          
SEQRES  85 A 1514    C   C   C   C   C   G   C   C   G   U   U   A   G          
SEQRES  86 A 1514    U   U   G   C   C   A   G   C   G   G   U   U   C          
SEQRES  87 A 1514    G   G   C   C   G   G   G   C   A   C   U   C   U          
SEQRES  88 A 1514    A   A   C   G   G   G   A   C   U   G   C   C   C          
SEQRES  89 A 1514    G   C   G   A   A   A   G   C   G   G   G   A   G          
SEQRES  90 A 1514    G   A   A   G   G   A   G   G   G   G   A   C   G          
SEQRES  91 A 1514    A   C   G   U   C   U   G   G   U   C   A   G   C          
SEQRES  92 A 1514    A   U   G   G   C   C   C   U   U   A   C   G   G          
SEQRES  93 A 1514    C   C   U   G   G   G   C   G   A   C   A   C   A          
SEQRES  94 A 1514    C   G   U   G   C   U   A   C   A   A   U   G   C          
SEQRES  95 A 1514    C   C   A   C   U   A   C   A   A   A   G   C   G          
SEQRES  96 A 1514    A   U   G   C   C   A   C   C   C   G   G   C   A          
SEQRES  97 A 1514    A   C   G   G   G   G   A   G   C   U   A   A   U          
SEQRES  98 A 1514    C   G   C   A   A   A   A   A   G   G   U   G   G          
SEQRES  99 A 1514    G   C   C   C   A   G   U   U   C   G   G   A   U          
SEQRES 100 A 1514    U   G   G   G   G   U   C   U   G   C   A   A   C          
SEQRES 101 A 1514    C   C   G   A   C   C   C   C   A   U   G   A   A          
SEQRES 102 A 1514    G   C   C   G   G   A   A   U   C   G   C   U   A          
SEQRES 103 A 1514    G   U   A   A   U   C   G   C   G   G   A   U   C          
SEQRES 104 A 1514    A   G   C   C   A   U   G   C   C   G   C   G   G          
SEQRES 105 A 1514    U   G   A   A   U   A   C   G   U   U   C   C   C          
SEQRES 106 A 1514    G   G   G   C   C   U   U   G   U   A   C   A   C          
SEQRES 107 A 1514    A   C   C   G   C   C   C   G   U   C   A   C   G          
SEQRES 108 A 1514    C   C   A   U   G   G   G   A   G   C   G   G   G          
SEQRES 109 A 1514    C   U   C   U   A   C   C   C   G   A   A   G   U          
SEQRES 110 A 1514    C   G   C   C   G   G   G   A   G   C   C   U   A          
SEQRES 111 A 1514    C   G   G   G   C   A   G   G   C   G   C   C   G          
SEQRES 112 A 1514    A   G   G   G   U   A   G   G   G   C   C   C   G          
SEQRES 113 A 1514    U   G   A   C   U   G   G   G   G   C   G   A   A          
SEQRES 114 A 1514    G   U   C   G   U   A   A   C   A   A   G   G   U          
SEQRES 115 A 1514    A   G   C   U   G   U   A   C   C   G   G   A   A          
SEQRES 116 A 1514    G   G   U   G   C   G   G   C   U   G   G   A   U          
SEQRES 117 A 1514    C   A   C   C   U   C                                      
SEQRES   1 B  255  PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA GLY          
SEQRES   2 B  255  VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO LYS          
SEQRES   3 B  255  PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE HIS          
SEQRES   4 B  255  ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU ARG          
SEQRES   5 B  255  THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY GLY          
SEQRES   6 B  255  THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN ASP          
SEQRES   7 B  255  ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO TYR          
SEQRES   8 B  255  VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN PHE          
SEQRES   9 B  255  LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU LEU          
SEQRES  10 B  255  GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG PRO          
SEQRES  11 B  255  LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU ARG          
SEQRES  12 B  255  LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS ARG          
SEQRES  13 B  255  LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS GLU          
SEQRES  14 B  255  ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE PRO          
SEQRES  15 B  255  VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP LEU          
SEQRES  16 B  255  VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE ARG          
SEQRES  17 B  255  SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU ILE          
SEQRES  18 B  255  ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO SER          
SEQRES  19 B  255  TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR PRO          
SEQRES  20 B  255  GLU GLY GLU SER GLU VAL GLU ALA                              
SEQRES   1 C  238  GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY ILE          
SEQRES   2 C  238  THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS LYS          
SEQRES   3 C  238  GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE ARG          
SEQRES   4 C  238  GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU ALA          
SEQRES   5 C  238  ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA VAL          
SEQRES   6 C  238  THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY ARG          
SEQRES   7 C  238  GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU ALA          
SEQRES   8 C  238  LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN GLU          
SEQRES   9 C  238  VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA GLN          
SEQRES  10 C  238  ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL ARG          
SEQRES  11 C  238  ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU SER          
SEQRES  12 C  238  GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG ILE          
SEQRES  13 C  238  GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA GLN          
SEQRES  14 C  238  GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE ASP          
SEQRES  15 C  238  TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL LEU          
SEQRES  16 C  238  GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE GLY          
SEQRES  17 C  238  GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS ALA          
SEQRES  18 C  238  GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG VAL          
SEQRES  19 C  238  LYS LYS GLU GLU                                              
SEQRES   1 D  208  GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG ARG          
SEQRES   2 D  208  GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS TYR          
SEQRES   3 D  208  SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO PRO          
SEQRES   4 D  208  GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER ASP          
SEQRES   5 D  208  TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG ARG          
SEQRES   6 D  208  ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU PHE          
SEQRES   7 D  208  GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER VAL          
SEQRES   8 D  208  PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL VAL          
SEQRES   9 D  208  TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA ARG          
SEQRES  10 D  208  GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY ARG          
SEQRES  11 D  208  ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY ASP          
SEQRES  12 D  208  GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU LEU          
SEQRES  13 D  208  ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS VAL          
SEQRES  14 D  208  GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS GLY          
SEQRES  15 D  208  LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA LEU          
SEQRES  16 D  208  PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER ARG          
SEQRES   1 E  161  PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE ARG          
SEQRES   2 E  161  ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE ARG          
SEQRES   3 E  161  PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY ARG          
SEQRES   4 E  161  VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO LEU          
SEQRES   5 E  161  ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN MET          
SEQRES   6 E  161  VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS GLU          
SEQRES   7 E  161  ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU LYS          
SEQRES   8 E  161  PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA VAL          
SEQRES   9 E  161  PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP ILE          
SEQRES  10 E  161  LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN ILE          
SEQRES  11 E  161  ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG THR          
SEQRES  12 E  161  LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA HIS          
SEQRES  13 E  161  ALA GLN ALA GLN GLY                                          
SEQRES   1 F  101  MET ARG ARG TYR GLU VAL ASN ILE VAL LEU ASN PRO ASN          
SEQRES   2 F  101  LEU ASP GLN SER GLN LEU ALA LEU GLU LYS GLU ILE ILE          
SEQRES   3 F  101  GLN ARG ALA LEU GLU ASN TYR GLY ALA ARG VAL GLU LYS          
SEQRES   4 F  101  VAL GLU GLU LEU GLY LEU ARG ARG LEU ALA TYR PRO ILE          
SEQRES   5 F  101  ALA LYS ASP PRO GLN GLY TYR PHE LEU TRP TYR GLN VAL          
SEQRES   6 F  101  GLU MET PRO GLU ASP ARG VAL ASN ASP LEU ALA ARG GLU          
SEQRES   7 F  101  LEU ARG ILE ARG ASP ASN VAL ARG ARG VAL MET VAL VAL          
SEQRES   8 F  101  LYS SER GLN GLU PRO PHE LEU ALA ASN ALA                      
SEQRES   1 G  155  ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN PRO          
SEQRES   2 G  155  ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE ILE          
SEQRES   3 G  155  ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA ALA          
SEQRES   4 G  155  ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU LYS          
SEQRES   5 G  155  THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA VAL          
SEQRES   6 G  155  GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG ARG          
SEQRES   7 G  155  VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL SER          
SEQRES   8 G  155  PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU VAL          
SEQRES   9 G  155  GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA VAL          
SEQRES  10 G  155  ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY LYS          
SEQRES  11 G  155  GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG MET          
SEQRES  12 G  155  ALA GLU ALA ASN ARG ALA TYR ALA HIS TYR ARG TRP              
SEQRES   1 H  138  MET LEU THR ASP PRO ILE ALA ASP MET LEU THR ARG ILE          
SEQRES   2 H  138  ARG ASN ALA THR ARG VAL TYR LYS GLU SER THR GLU VAL          
SEQRES   3 H  138  PRO ALA SER ARG PHE LYS GLU GLU ILE LEU LYS ILE LEU          
SEQRES   4 H  138  ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL GLU          
SEQRES   5 H  138  VAL ASP GLY LYS PRO TYR LEU ARG ILE HIS LEU LYS TYR          
SEQRES   6 H  138  GLY PRO ARG ARG GLN GLY PRO ASP PRO ARG PRO GLU GLN          
SEQRES   7 H  138  VAL ILE LYS HIS ILE ARG ARG ILE SER ARG PRO GLY ARG          
SEQRES   8 H  138  ARG VAL TYR VAL GLY VAL LYS GLU ILE PRO ARG VAL ARG          
SEQRES   9 H  138  ARG GLY LEU GLY ILE ALA ILE LEU SER THR PRO LYS GLY          
SEQRES  10 H  138  VAL LEU THR ASP ARG GLU ALA ARG LYS LEU GLY VAL GLY          
SEQRES  11 H  138  GLY GLU LEU ILE CYS GLU VAL TRP                              
SEQRES   1 I  128  MET GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA          
SEQRES   2 I  128  VAL ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL          
SEQRES   3 I  128  THR VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY          
SEQRES   4 I  128  LEU VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA          
SEQRES   5 I  128  VAL ASP ALA LEU GLY ARG PHE ASP ALA TYR ILE THR VAL          
SEQRES   6 I  128  ARG GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS          
SEQRES   7 I  128  LEU GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP          
SEQRES   8 I  128  TYR ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG          
SEQRES   9 I  128  ASP ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS          
SEQRES  10 I  128  LYS ALA ARG ARG ALA PRO GLN TYR SER LYS ARG                  
SEQRES   1 J  104  PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS LYS          
SEQRES   2 J  104  THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA ALA          
SEQRES   3 J  104  ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO LEU          
SEQRES   4 J  104  PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY PRO          
SEQRES   5 J  104  PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU ARG          
SEQRES   6 J  104  THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN ARG          
SEQRES   7 J  104  LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO THR          
SEQRES   8 J  104  GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY ARG          
SEQRES   1 K  128  ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN VAL          
SEQRES   2 K  128  ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN ASN          
SEQRES   3 K  128  THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO ILE          
SEQRES   4 K  128  THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY SER          
SEQRES   5 K  128  ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA LEU          
SEQRES   6 K  128  ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN SER          
SEQRES   7 K  128  VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG GLU          
SEQRES   8 K  128  GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN VAL          
SEQRES   9 K  128  LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN GLY          
SEQRES  10 K  128  CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER                  
SEQRES   1 L  131  PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU LYS          
SEQRES   2 L  131  VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY ALA          
SEQRES   3 L  131  PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR VAL          
SEQRES   4 L  131  THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL ALA          
SEQRES   5 L  131  LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA TYR          
SEQRES   6 L  131  ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL          
SEQRES   7 L  131  VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY          
SEQRES   8 L  131  VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA ALA          
SEQRES   9 L  131  GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR GLY          
SEQRES  10 L  131  THR LYS LYS PRO LYS GLU ALA ALA LYS THR ALA ALA LYS          
SEQRES  11 L  131  LYS                                                          
SEQRES   1 M  125  ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS ARG          
SEQRES   2 M  125  VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY LYS          
SEQRES   3 M  125  ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE ASN          
SEQRES   4 M  125  PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU VAL          
SEQRES   5 M  125  VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS LEU          
SEQRES   6 M  125  GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE LYS          
SEQRES   7 M  125  ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG HIS          
SEQRES   8 M  125  ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG THR          
SEQRES   9 M  125  ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL ALA          
SEQRES  10 M  125  GLY LYS LYS LYS ALA PRO ARG LYS                              
SEQRES   1 N   60  ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR PRO          
SEQRES   2 N   60  LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG CYS          
SEQRES   3 N   60  GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU CYS          
SEQRES   4 N   60  ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN LEU          
SEQRES   5 N   60  PRO GLY VAL ARG LYS ALA SER TRP                              
SEQRES   1 O   88  PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN GLU          
SEQRES   2 O   88  PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU VAL          
SEQRES   3 O   88  GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU SER          
SEQRES   4 O   88  GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER HIS          
SEQRES   5 O   88  ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG LEU          
SEQRES   6 O   88  LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR ARG          
SEQRES   7 O   88  ALA LEU ILE GLU LYS LEU GLY ILE ARG GLY                      
SEQRES   1 P   88  MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS          
SEQRES   2 P   88  ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG          
SEQRES   3 P   88  LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR          
SEQRES   4 P   88  ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP          
SEQRES   5 P   88  VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN          
SEQRES   6 P   88  PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY          
SEQRES   7 P   88  VAL PHE ARG GLN GLU ALA ARG GLU GLY ALA                      
SEQRES   1 Q  104  PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP LYS          
SEQRES   2 Q  104  MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN PHE          
SEQRES   3 Q  104  PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER LYS          
SEQRES   4 Q  104  LYS TYR LEU ALA HIS ASP PRO GLU GLU ARG TYR LYS VAL          
SEQRES   5 Q  104  GLY ASP VAL VAL GLU ILE ILE GLU ALA ARG PRO ILE SER          
SEQRES   6 Q  104  LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU GLU          
SEQRES   7 Q  104  GLY ARG LEU ASP LEU VAL GLU LYS TYR LEU VAL ARG ARG          
SEQRES   8 Q  104  GLN ASN TYR ALA SER LEU SER LYS ARG GLY GLY LYS ALA          
SEQRES   1 R   87  SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN ARG          
SEQRES   2 R   87  ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU GLY          
SEQRES   3 R   87  GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL LEU          
SEQRES   4 R   87  LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO ARG          
SEQRES   5 R   87  ARG ARG THR GLY LEU SER GLY LYS GLU GLN ARG ILE LEU          
SEQRES   6 R   87  ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU LEU          
SEQRES   7 R   87  PRO PHE THR GLU LYS LEU VAL ARG LYS                          
SEQRES   1 S   92  PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP HIS          
SEQRES   2 S   92  LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY GLU          
SEQRES   3 S   92  LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR ILE          
SEQRES   4 S   92  VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR ASN          
SEQRES   5 S   92  GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN MET          
SEQRES   6 S   92  VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR          
SEQRES   7 S   92  TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS LYS          
SEQRES   8 S   92  LYS                                                          
SEQRES   1 T  105  ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU LYS          
SEQRES   2 T  105  ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN LYS          
SEQRES   3 T  105  ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS ALA          
SEQRES   4 T  105  ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA LEU          
SEQRES   5 T  105  LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS ALA          
SEQRES   6 T  105  ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA ARG          
SEQRES   7 T  105  ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU LEU          
SEQRES   8 T  105  GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU SER          
SEQRES   9 T  105  ALA                                                          
SEQRES   1 U   26  GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP          
SEQRES   2 U   26  ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS LYS          
HET     MG  E   1       1                                                       
HET     MG  A1516       1                                                       
HET     MG  A1517       1                                                       
HET     MG  A1518       1                                                       
HET     MG  L 136       1                                                       
HET     MG  A1519       1                                                       
HET     MG  A1520       1                                                       
HET     MG  A1521       1                                                       
HET     MG  A1522       1                                                       
HET     MG  A1523       1                                                       
HET     MG  A1524       1                                                       
HET     MG  A1525       1                                                       
HET     MG  A1526       1                                                       
HET     MG  T 107       1                                                       
HET     MG  A1527       1                                                       
HET     MG  A1528       1                                                       
HET     MG  A1529       1                                                       
HET     MG  Q 106       1                                                       
HET     MG  Q 107       1                                                       
HET     MG  A1530       1                                                       
HET     MG  P  89       1                                                       
HET     MG  T 108       1                                                       
HET     MG  T 109       1                                                       
HET     MG  A1531       1                                                       
HET     MG  A1532       1                                                       
HET     MG  A1533       1                                                       
HET     MG  L 137       1                                                       
HET     MG  A1534       1                                                       
HET     MG  A1535       1                                                       
HET     MG  D 210       1                                                       
HET     MG  D 211       1                                                       
HET     MG  A1536       1                                                       
HET     MG  A1537       1                                                       
HET     MG  L 138       1                                                       
HET     MG  A1538       1                                                       
HET     MG  A1539       1                                                       
HET     MG  A1540       1                                                       
HET     MG  A1541       1                                                       
HET     MG  A1542       1                                                       
HET     MG  A1543       1                                                       
HET     MG  A1544       1                                                       
HET     MG  A1545       1                                                       
HET     MG  A1546       1                                                       
HET     MG  A1547       1                                                       
HET     MG  K 130       1                                                       
HET     MG  G 157       1                                                       
HET     MG  A1548       1                                                       
HET     MG  A1549       1                                                       
HET     MG  A1550       1                                                       
HET     MG  A1551       1                                                       
HET     MG  A1552       1                                                       
HET     MG  A1553       1                                                       
HET     MG  A1554       1                                                       
HET     MG  A1555       1                                                       
HET     MG  A1556       1                                                       
HET     MG  A1557       1                                                       
HET     MG  A1558       1                                                       
HET     MG  A1559       1                                                       
HET     MG  A1560       1                                                       
HET     MG  A1561       1                                                       
HET     MG  A1562       1                                                       
HET     MG  A1563       1                                                       
HET     MG  A1564       1                                                       
HET     MG  A1565       1                                                       
HET     MG  A1566       1                                                       
HET     MG  A1567       1                                                       
HET     MG  A1568       1                                                       
HET     MG  A1569       1                                                       
HET     MG  A1570       1                                                       
HET     MG  A1571       1                                                       
HET     MG  A1572       1                                                       
HET     MG  J 106       1                                                       
HET     MG  A1573       1                                                       
HET     MG  A1574       1                                                       
HET     MG  A1575       1                                                       
HET     ZN  N  76       1                                                       
HET     ZN  D 212       1                                                       
HET    WO2  B1001      82                                                       
HET    WO2  B1002      82                                                       
HET    WO2  C1003      82                                                       
HET    WO2  B1004      82                                                       
HET    WO2  E1005      82                                                       
HET    WO2  G1006      82                                                       
HET    WO2  G1007      82                                                       
HET    WO2  R1008      82                                                       
HET    WO2  J1009      82                                                       
HET    WO2  H1010      82                                                       
HET    WO2  A1576      82                                                       
HET    WO2  D1012      82                                                       
HET    WO2  T1013      82                                                       
HET    WO2  K1014      82                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     WO2 OCTADECATUNGSTENYL DIPHOSPHATE                                   
FORMUL  22   MG    75(MG 2+)                                                    
FORMUL  97   ZN    2(ZN 2+)                                                     
FORMUL  99  WO2    14(O62 P2 W18)                                               
HELIX    1   1 LYS B   46  ARG B   64  1                                  19    
HELIX    2   2 GLN B   78  ARG B   87  1                                  10    
HELIX    3   3 ASN B  104  PHE B  122  1                                  19    
HELIX    4   4 PRO B  131  SER B  150  1                                  20    
HELIX    5   5 GLY B  151  LEU B  155  5                                   5    
HELIX    6   6 GLU B  170  LEU B  180  1                                  11    
HELIX    7   7 ALA B  207  GLN B  224  1                                  18    
HELIX    8   8 GLN C   28  LEU C   47  1                                  20    
HELIX    9   9 LYS C   72  GLY C   78  1                                   7    
HELIX   10  10 GLU C   82  LEU C   91  1                                  10    
HELIX   11  11 ASN C  108  LEU C  111  5                                   4    
HELIX   12  12 SER C  112  ARG C  126  1                                  15    
HELIX   13  13 ALA C  129  SER C  144  1                                  16    
HELIX   14  14 VAL D    8  GLU D   15  1                                   8    
HELIX   15  15 SER D   52  GLY D   69  1                                  18    
HELIX   16  16 SER D   71  LYS D   85  1                                  15    
HELIX   17  17 VAL D   88  GLU D   98  1                                  11    
HELIX   18  18 ARG D  100  LEU D  108  1                                   9    
HELIX   19  19 SER D  113  HIS D  123  1                                  11    
HELIX   20  20 GLU D  150  ARG D  153  5                                   4    
HELIX   21  21 LEU D  155  ALA D  164  1                                  10    
HELIX   22  22 ASN D  199  TYR D  207  1                                   9    
HELIX   23  23 GLU E   50  ASN E   65  1                                  16    
HELIX   24  24 GLY E  103  GLU E  111  1                                   9    
HELIX   25  25 ASN E  127  LEU E  142  1                                  16    
HELIX   26  26 LYS E  145  ARG E  150  1                                   6    
HELIX   27  27 ASP F   15  TYR F   33  1                                  19    
HELIX   28  28 PRO F   68  ASP F   70  5                                   3    
HELIX   29  29 ARG F   71  ARG F   80  1                                  10    
HELIX   30  30 VAL G   21  MET G   31  1                                  11    
HELIX   31  31 LYS G   36  LYS G   53  1                                  18    
HELIX   32  32 GLU G   57  GLU G   67  1                                  11    
HELIX   33  33 SER G   92  ARG G  111  1                                  20    
HELIX   34  34 ALA G  116  ALA G  128  1                                  13    
HELIX   35  35 GLY G  132  MET G  144  1                                  13    
HELIX   36  36 TYR G  151  ARG G  155  5                                   5    
HELIX   37  37 ASP H    4  VAL H   19  1                                  16    
HELIX   38  38 SER H   29  GLU H   42  1                                  14    
HELIX   39  39 VAL H  103  LEU H  107  5                                   5    
HELIX   40  40 THR H  120  GLY H  128  1                                   9    
HELIX   41  41 ASP I   32  PHE I   37  1                                   6    
HELIX   42  42 VAL I   44  ALA I   46  5                                   3    
HELIX   43  43 LEU I   47  ASP I   54  1                                   8    
HELIX   44  44 GLY I   69  GLN I   87  1                                  19    
HELIX   45  45 TYR I   92  LYS I   97  1                                   6    
HELIX   46  46 PRO I   98  GLY I  100  5                                   3    
HELIX   47  47 LEU J   16  ALA J   26  1                                  11    
HELIX   48  48 LYS J   80  THR J   87  1                                   8    
HELIX   49  49 GLY K   52  GLY K   56  5                                   5    
HELIX   50  50 THR K   57  THR K   57  5                                   1    
HELIX   51  51 PRO K   58  LEU K   63  1                                   6    
HELIX   52  52 LEU K   63  ALA K   74  1                                  12    
HELIX   53  53 GLU K   92  GLY K  102  1                                  11    
HELIX   54  54 THR L    6  ARG L   12  1                                   7    
HELIX   55  55 ARG M   14  LEU M   19  1                                   6    
HELIX   56  56 THR M   20  ILE M   22  5                                   3    
HELIX   57  57 LYS M   27  GLY M   38  1                                  12    
HELIX   58  58 THR M   49  ASN M   62  1                                  14    
HELIX   59  59 LEU M   66  ILE M   84  1                                  19    
HELIX   60  60 CYS M   86  LEU M   90  5                                   5    
HELIX   61  61 ARG N    3  ILE N    7  5                                   5    
HELIX   62  62 PHE N   16  ALA N   20  5                                   5    
HELIX   63  63 ARG N   41  GLU N   46  1                                   6    
HELIX   64  64 GLU N   46  GLY N   51  1                                   6    
HELIX   65  65 GLU O    6  ALA O   16  1                                  11    
HELIX   66  66 SER O   24  HIS O   46  1                                  23    
HELIX   67  67 ASP O   49  GLU O   73  1                                  25    
HELIX   68  68 ASP O   74  LYS O   84  1                                  11    
HELIX   69  69 ASP P   52  GLY P   63  1                                  12    
HELIX   70  70 THR P   67  GLY P   78  1                                  12    
HELIX   71  71 ARG Q   81  ALA Q   96  1                                  16    
HELIX   72  72 ASN R   36  LYS R   41  1                                   6    
HELIX   73  73 SER R   59  ILE R   75  1                                  17    
HELIX   74  74 LEU S   15  LEU S   20  1                                   6    
HELIX   75  75 GLU S   21  ASN S   23  5                                   3    
HELIX   76  76 VAL S   41  VAL S   45  5                                   5    
HELIX   77  77 THR S   63  VAL S   67  5                                   5    
HELIX   78  78 LYS S   70  ALA S   75  5                                   6    
HELIX   79  79 ALA T   12  GLY T   47  1                                  36    
HELIX   80  80 LYS T   48  GLY T   69  1                                  22    
HELIX   81  81 ASN T   75  LEU T   92  1                                  18    
HELIX   82  82 THR U    8  TRP U   14  1                                   7    
SHEET    1   A 2 PHE B  70  VAL B  71  0                                        
SHEET    2   A 2 TYR B  92  VAL B  93  1  N  VAL B  93   O  PHE B  70           
SHEET    1   B 2 ILE B 185  ALA B 186  0                                        
SHEET    2   B 2 TYR B 199  ILE B 200  1  O  TYR B 199   N  ALA B 186           
SHEET    1   C 3 VAL C  55  ASP C  56  0                                        
SHEET    2   C 3 THR C  67  VAL C  70 -1  N  THR C  67   O  ASP C  56           
SHEET    3   C 3 ASN C 102  GLU C 105  1  O  ASN C 102   N  VAL C  68           
SHEET    1   D 4 ALA C 169  GLY C 171  0                                        
SHEET    2   D 4 GLY C 148  VAL C 153 -1  N  ALA C 149   O  GLN C 170           
SHEET    3   D 4 LEU C 196  PHE C 203 -1  O  LYS C 199   N  ILE C 152           
SHEET    4   D 4 ILE C 182  ALA C 189 -1  N  ASP C 183   O  ILE C 202           
SHEET    1   E 3 ARG D 131  ARG D 132  0                                        
SHEET    2   E 3 ILE D 126  VAL D 128 -1  N  VAL D 128   O  ARG D 131           
SHEET    3   E 3 ILE D 146  VAL D 148 -1  O  ALA D 147   N  THR D 127           
SHEET    1   F 2 SER D 175  ASP D 177  0                                        
SHEET    2   F 2 LYS D 182  LYS D 184 -1  O  LYS D 182   N  ASP D 177           
SHEET    1   G 3 GLU E   7  MET E  10  0                                        
SHEET    2   G 3 VAL E  32  GLY E  35 -1  N  VAL E  33   O  LYS E   9           
SHEET    3   G 3 VAL E  41  GLY E  44 -1  N  GLY E  42   O  VAL E  34           
SHEET    1   H 3 ARG E  14  ARG E  15  0                                        
SHEET    2   H 3 PHE E  28  GLY E  29 -1  N  GLY E  29   O  ARG E  14           
SHEET    3   H 3 LYS E  47  ALA E  48 -1  O  ALA E  48   N  PHE E  28           
SHEET    1   I 2 ARG E  18  GLN E  20  0                                        
SHEET    2   I 2 GLY E  23  ARG E  25 -1  O  GLY E  23   N  GLN E  20           
SHEET    1   J 3 ILE E  80  GLU E  81  0                                        
SHEET    2   J 3 VAL E  90  PRO E  93 -1  N  LEU E  91   O  ILE E  80           
SHEET    3   J 3 ILE E 118  LYS E 121 -1  O  LEU E 119   N  LYS E  92           
SHEET    1   K 4 VAL F  37  VAL F  40  0                                        
SHEET    2   K 4 TYR F  59  MET F  67 -1  O  GLN F  64   N  GLU F  38           
SHEET    3   K 4 ARG F   2  LEU F  10 -1  N  ARG F   2   O  MET F  67           
SHEET    4   K 4 ARG F  87  LYS F  92 -1  O  ARG F  87   N  VAL F   9           
SHEET    1   L 3 SER H  23  PRO H  27  0                                        
SHEET    2   L 3 LYS H  56  HIS H  62 -1  N  LEU H  59   O  VAL H  26           
SHEET    3   L 3 GLY H  47  VAL H  53 -1  O  GLY H  47   N  HIS H  62           
SHEET    1   M 2 ILE H  83  ARG H  85  0                                        
SHEET    2   M 2 CYS H 135  VAL H 137 -1  O  GLU H 136   N  ARG H  84           
SHEET    1   N 3 TYR H  94  VAL H  95  0                                        
SHEET    2   N 3 GLY H 131  LEU H 133 -1  O  GLY H 131   N  VAL H  95           
SHEET    3   N 3 LEU H 112  SER H 113 -1  N  SER H 113   O  GLU H 132           
SHEET    1   O 4 LEU I  19  ARG I  20  0                                        
SHEET    2   O 4 ASP I  60  VAL I  65 -1  N  ASP I  60   O  ARG I  20           
SHEET    3   O 4 ALA I  15  ARG I  16 -1  N  ARG I  16   O  THR I  64           
SHEET    4   O 4 THR I   7  GLY I   8 -1  O  GLY I   8   N  ALA I  15           
SHEET    1   P 3 LEU I  19  ARG I  20  0                                        
SHEET    2   P 3 ASP I  60  VAL I  65 -1  N  ASP I  60   O  ARG I  20           
SHEET    3   P 3 THR I  27  VAL I  28  1  O  THR I  27   N  ILE I  63           
SHEET    1   Q 4 ARG J  43  VAL J  49  0                                        
SHEET    2   Q 4 GLU J  61  ARG J  70 -1  N  GLU J  61   O  VAL J  49           
SHEET    3   Q 4 ARG J   5  GLY J  10 -1  O  LEU J   8   N  ARG J  70           
SHEET    4   Q 4 VAL J  94  LYS J  99 -1  N  GLU J  95   O  ARG J   9           
SHEET    1   R 3 ARG J  43  VAL J  49  0                                        
SHEET    2   R 3 GLU J  61  ARG J  70 -1  N  GLU J  61   O  VAL J  49           
SHEET    3   R 3 VAL N  56  ARG N  57 -1  O  ARG N  57   N  GLU J  64           
SHEET    1   S 6 PRO K  39  TRP K  42  0                                        
SHEET    2   S 6 ILE K  29  THR K  33 -1  O  ILE K  32   N  ILE K  40           
SHEET    3   S 6 SER K  16  HIS K  22 -1  O  ARG K  18   N  THR K  33           
SHEET    4   S 6 SER K  79  ARG K  85  1  O  SER K  79   N  GLY K  17           
SHEET    5   S 6 GLN K 104  ASP K 110  1  O  GLN K 104   N  VAL K  80           
SHEET    6   S 6 LEU R  85  VAL R  86 -1  O  LEU R  85   N  ASP K 110           
SHEET    1   T 5 GLU L  65  VAL L  66  0                                        
SHEET    2   T 5 VAL L  58  LEU L  60 -1  O  VAL L  58   N  VAL L  66           
SHEET    3   T 5 ARG L  33  CYS L  37 -1  O  VAL L  36   N  ARG L  59           
SHEET    4   T 5 VAL L  82  ILE L  85 -1  N  VAL L  83   O  GLY L  35           
SHEET    5   T 5 ILE L 100  VAL L 101 -1  N  VAL L 101   O  LEU L  84           
SHEET    1   U 2 THR L  42  VAL L  43  0                                        
SHEET    2   U 2 ARG L  53  LYS L  54 -1  N  ARG L  53   O  VAL L  43           
SHEET    1   V 2 VAL N  33  TYR N  34  0                                        
SHEET    2   V 2 LEU N  39  CYS N  40 -1  N  LEU N  39   O  TYR N  34           
SHEET    1   W 2 VAL P   2  ILE P   4  0                                        
SHEET    2   W 2 VAL P  21  ASP P  23 -1  O  THR P  22   N  LYS P   3           
SHEET    1   X 2 TYR P  17  ARG P  18  0                                        
SHEET    2   X 2 TYR P  38  TYR P  39 -1  O  TYR P  39   N  TYR P  17           
SHEET    1   Y 6 VAL Q   5  VAL Q  10  0                                        
SHEET    2   Y 6 THR Q  18  GLU Q  24 -1  N  LEU Q  22   O  VAL Q   9           
SHEET    3   Y 6 SER Q  39  HIS Q  45 -1  O  LYS Q  40   N  VAL Q  23           
SHEET    4   Y 6 PHE Q  71  VAL Q  73  1  O  PHE Q  71   N  HIS Q  45           
SHEET    5   Y 6 VAL Q  56  GLU Q  61 -1  O  ILE Q  60   N  ARG Q  72           
SHEET    6   Y 6 VAL Q   5  VAL Q  10 -1  O  LEU Q   6   N  ILE Q  59           
SHEET    1   Z 2 PHE Q  27  PRO Q  28  0                                        
SHEET    2   Z 2 VAL Q  35  ILE Q  36 -1  O  ILE Q  36   N  PHE Q  27           
SHEET    1  AA 3 ILE S  31  LYS S  32  0                                        
SHEET    2  AA 3 THR S  48  TYR S  52  1  O  THR S  48   N  ILE S  31           
SHEET    3  AA 3 HIS S  57  TYR S  61 -1  N  VAL S  58   O  VAL S  51           
LINK         OP1   G A  21                MG    MG A1517     1555   1555  2.44  
LINK         O2'   C A  67                MG    MG A1526     1555   1555  2.34  
LINK         O3'   G A  78                MG    MG A1523     1555   1555  2.47  
LINK         OP2   C A  93                MG    MG A1524     1555   1555  2.21  
LINK         OP2   G A 104                MG    MG A1521     1555   1555  1.94  
LINK         O4'   A A 166                MG    MG A1526     1555   1555  2.18  
LINK         O5'   G A 183                MG    MG A1527     1555   1555  2.44  
LINK         OP2   C A 184                MG    MG A1527     1555   1555  2.37  
LINK         O5'   G A 190                MG    MG A1528     1555   1555  2.17  
LINK         O4'   G A 190                MG    MG A1528     1555   1555  2.37  
LINK         O6    G A 294                MG    MG A1530     1555   1555  2.21  
LINK         OP2   A A 377                MG    MG A1535     1555   1555  2.36  
LINK         O3'   C A 526                MG    MG A1538     1555   1555  2.29  
LINK         OP1   G A 527                MG    MG A1538     1555   1555  2.07  
LINK         OP1   G A 541                MG    MG A1530     1555   1555  2.31  
LINK         OP2   A A 555                MG    MG A1540     1555   1555  2.34  
LINK         OP2   A A 557                MG    MG A1540     1555   1555  2.42  
LINK         OP2   C A 579                MG    MG A1543     1555   1555  2.30  
LINK         OP2   G A 580                MG    MG A1543     1555   1555  2.20  
LINK         OP2   A A 591                MG    MG A1544     1555   1555  2.15  
LINK         OP1   C A 911                MG    MG A1562     1555   1555  2.38  
LINK         OP2   A A 914                MG    MG A1563     1555   1555  2.37  
LINK         OP1   G A 921                MG    MG A1564     1555   1555  2.45  
LINK         OP2   G A 922                MG    MG A1564     1555   1555  2.31  
LINK         OP2   A A1092                MG    MG A1569     1555   1555  2.36  
LINK         OP2   A A1164                MG    MG A1570     1555   1555  2.33  
LINK         OP1   G A1178                MG    MG A1567     1555   1555  2.29  
LINK         OP2   G A1179                MG    MG A1567     1555   1555  2.33  
LINK         OP1   G A1205                MG    MG A1565     1555   1555  2.38  
LINK         OP1   C A1284                MG    MG A1571     1555   1555  2.43  
LINK         OP2   G A1285                MG    MG A1571     1555   1555  2.41  
LINK         OP2   A A1477                MG    MG A1574     1555   1555  1.97  
LINK         OP1   G A1482                MG    MG A1574     1555   1555  2.38  
LINK         OP2   G A1482                MG    MG A1574     1555   1555  2.37  
LINK         OP2   C A1513                MG    MG A1549     1555   1555  2.35  
LINK         N   ARG D   3                MG    MG D 210     1555   1555  2.29  
LINK         O   ARG D   3                MG    MG D 210     1555   1555  2.44  
LINK         N   ARG D 114                MG    MG D 211     1555   1555  2.43  
LINK         N   ARG D 115                MG    MG D 211     1555   1555  2.13  
LINK         O   THR E 120                MG    MG E   1     1555   1555  2.29  
LINK         N   LYS E 121                MG    MG E   1     1555   1555  2.37  
LINK         N   GLU E 122                MG    MG E   1     1555   1555  2.16  
LINK         O   TRP K  42                MG    MG K 130     1555   1555  2.38  
LINK         O   PHE L  32                MG    MG L 137     1555   1555  1.99  
LINK         N   ARG P  28                MG    MG P  89     1555   1555  2.29  
LINK         N   ASP P  29                MG    MG P  89     1555   1555  2.40  
LINK         O   ARG Q  25                MG    MG Q 106     1555   1555  2.40  
LINK         N   ARG Q  38                MG    MG Q 106     1555   1555  2.24  
LINK         O   ARG Q  38                MG    MG Q 106     1555   1555  2.14  
LINK         N   LYS Q  69                MG    MG Q 107     1555   1555  2.14  
LINK         N   LEU T  10                MG    MG T 109     1555   1555  2.27  
LINK         O   HIS T  16                MG    MG T 108     1555   1555  2.37  
LINK         N   GLN T  18                MG    MG T 108     1555   1555  2.37  
LINK         N   SER T  19                MG    MG T 108     1555   1555  2.27  
LINK         N   ALA T  78                MG    MG T 107     1555   1555  2.31  
CISPEP   1 LYS R    7    PRO R    8          0        -0.22                     
SITE     1 AC1  3 THR E 120  LYS E 121  GLU E 122                               
SITE     1 AC2  2   G A  21    A A 546                                          
SITE     1 AC3  3   U A  37  LYS L 124  PRO L 125                               
SITE     1 AC4  1   G A  64                                                     
SITE     1 AC5  2   C A 103    G A 104                                          
SITE     1 AC6  1   C A  71                                                     
SITE     1 AC7  2   G A  78    U A  79                                          
SITE     1 AC8  1   C A  93                                                     
SITE     1 AC9  3   C A  67    A A 165    A A 166                               
SITE     1 BC1  6 ALA T  76  ALA T  77  ALA T  78  ARG T  79                    
SITE     2 BC1  6 ARG T  80  LYS T  81                                          
SITE     1 BC2  2   G A 183    C A 184                                          
SITE     1 BC3  2   U A 189    G A 190                                          
SITE     1 BC4  3 ARG Q  25  LYS Q  37  ARG Q  38                               
SITE     1 BC5  5   G A 249  SER Q  66  LYS Q  67  ARG Q  68                    
SITE     2 BC5  5 LYS Q  69                                                     
SITE     1 BC6  2   G A 294    G A 541                                          
SITE     1 BC7  3 LYS P  27  ARG P  28  ASP P  29                               
SITE     1 BC8  6 ARG T  15  HIS T  16  ARG T  17  GLN T  18                    
SITE     2 BC8  6 SER T  19  LEU T  20                                          
SITE     1 BC9  4 ASN T   9  LEU T  10  SER T  11  ALA T  12                    
SITE     1 CC1  3   C A 325    G A 326    C A 347                               
SITE     1 CC2  3   A A 358  PHE L  32  ARG L  33                               
SITE     1 CC3  2   G A 375    A A 377                                          
SITE     1 CC4  2 GLY D   2  ARG D   3                                          
SITE     1 CC5  4 SER D 113  ARG D 114  ARG D 115  GLN D 116                    
SITE     1 CC6  3 THR L 131  ALA L 132  ALA L 133                               
SITE     1 CC7  2   C A 526    G A 527                                          
SITE     1 CC8  2   A A 542    U A 543                                          
SITE     1 CC9  4   U A 554    A A 555    A A 556    A A 557                    
SITE     1 DC1  2   G A 564    G A 741                                          
SITE     1 DC2  1   G A 571                                                     
SITE     1 DC3  4   G A 578    C A 579    G A 580    U A 581                    
SITE     1 DC4  2   A A 590    A A 591                                          
SITE     1 DC5  2   G A   3    U A   4                                          
SITE     1 DC6  1   G A 633                                                     
SITE     1 DC7  2   U A 669  TRP K  42                                          
SITE     1 DC8  1 GLY G  82                                                     
SITE     1 DC9  1   G A 683                                                     
SITE     1 EC1  2   C A1512    C A1513                                          
SITE     1 EC2  1   A A 751                                                     
SITE     1 EC3  1   U A 755                                                     
SITE     1 EC4  1   U A 784                                                     
SITE     1 EC5  2   G A 820    G A 821                                          
SITE     1 EC6  2   G A 835    G A 846                                          
SITE     1 EC7  1   A A 837                                                     
SITE     1 EC8  1   G A 880                                                     
SITE     1 EC9  1   A A 555                                                     
SITE     1 FC1  1   A A 895                                                     
SITE     1 FC2  2   C A 911    U A1326                                          
SITE     1 FC3  2   A A 914    G A 916                                          
SITE     1 FC4  2   G A 921    G A 922                                          
SITE     1 FC5  2   C A1204    G A1205                                          
SITE     1 FC6  3   C A1036    G A1178    G A1179                               
SITE     1 FC7  2   C A1048    A A1074                                          
SITE     1 FC8  2   A A1092    C A1170                                          
SITE     1 FC9  2   C A1153    A A1164                                          
SITE     1 GC1  2   C A1284    G A1285                                          
SITE     1 GC2  1   U A1289                                                     
SITE     1 GC3  1 HIS J  62                                                     
SITE     1 GC4  4   A A1476    A A1477    G A1481    G A1482                    
SITE     1 GC5  4 CYS N  24  CYS N  27  CYS N  40  CYS N  43                    
SITE     1 GC6  3 CYS D   9  CYS D  12  CYS D  31                               
SITE     1 GC7  8 ARG B  36  ASN B  37  GLY B  38  GLN B  76                    
SITE     2 GC7  8 ALA B 207  ILE B 208  ARG B 209  WO2 B1004                    
SITE     1 GC8  3 ALA C  71  LYS C  72  PRO C 109                               
SITE     1 GC9  4   G A1088  LYS C 147  GLY C 205  GLU C 206                    
SITE     1 HC1  4 LYS B  74  LYS B  75  GLN B  76  WO2 B1001                    
SITE     1 HC2  9   A A 407  SER D  28  PRO D  29  ARG E 152                    
SITE     2 HC2  9 LYS E 153  GLY E 154  GLU E 155  ALA E 156                    
SITE     3 HC2  9 PRO H  67                                                     
SITE     1 HC3 11 ALA G 147  ASN G 148  ARG G 149  ALA G 150                    
SITE     2 HC3 11 TYR G 151  ALA G 152  ARG G 155  TRP G 156                    
SITE     3 HC3 11 PRO K  58  TYR K  59  GLN K  93                               
SITE     1 HC4  3 GLU G 113  ARG G 114  VAL G 118                               
SITE     1 HC5  5 SER R  45  GLU R  46  LYS R  49  ILE R  50                    
SITE     2 HC5  5 LEU R  51                                                     
SITE     1 HC6  4 LYS J  14  ALA J  18  LEU J  90  PRO J  91                    
SITE     1 HC7  5 LYS D 166  GLY D 167  ARG H 105  GLY H 106                    
SITE     2 HC7  5 ARG H 122                                                     
SITE     1 HC8  1 GLN C 162                                                     
SITE     1 HC9  5 ALA C 129  ARG C 131  ARG D  49  ARG D  50                    
SITE     2 HC9  5 VAL E  51                                                     
SITE     1 IC1  2 LYS K   9  LYS T  54                                          
SITE     1 IC2  6 LYS K   7  LYS K   8  LYS T  48  ALA T  49                    
SITE     2 IC2  6 GLU T  50  GLU T  51                                          
CRYST1  406.300  406.300  173.100  90.00  90.00  90.00 P 41 21 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      0.002460  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005780        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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