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Database: PDB
Entry: 1IBL
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Original site: 1IBL 
HEADER    RIBOSOME                                28-MAR-01   1IBL              
TITLE     STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT           
TITLE    2 IN COMPLEX WITH A MESSENGER RNA FRAGMENT AND COGNATE                 
TITLE    3 TRANSFER RNA ANTICODON STEM-LOOP BOUND AT THE A SITE AND             
TITLE    4 WITH THE ANTIBIOTIC PAROMOMYCIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 16S RIBOSOMAL RNA;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: P-SITE MESSENGER RNA FRAGMENT;                             
COMPND   6 CHAIN: X;                                                            
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 3;                                                           
COMPND   9 MOLECULE: ANTICODON STEM-LOOP OF PHENYLALANINE TRANSFER              
COMPND  10 RNA;                                                                 
COMPND  11 CHAIN: Y;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: A-SITE MESSENGER RNA FRAGMENT;                             
COMPND  15 CHAIN: Z;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: 30S RIBOSOMAL PROTEIN S2;                                  
COMPND  19 CHAIN: B;                                                            
COMPND  20 MOL_ID: 6;                                                           
COMPND  21 MOLECULE: 30S RIBOSOMAL PROTEIN S3;                                  
COMPND  22 CHAIN: C;                                                            
COMPND  23 MOL_ID: 7;                                                           
COMPND  24 MOLECULE: 30S RIBOSOMAL PROTEIN S4;                                  
COMPND  25 CHAIN: D;                                                            
COMPND  26 MOL_ID: 8;                                                           
COMPND  27 MOLECULE: 30S RIBOSOMAL PROTEIN S5;                                  
COMPND  28 CHAIN: E;                                                            
COMPND  29 MOL_ID: 9;                                                           
COMPND  30 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND  31 CHAIN: F;                                                            
COMPND  32 MOL_ID: 10;                                                          
COMPND  33 MOLECULE: 30S RIBOSOMAL PROTEIN S7;                                  
COMPND  34 CHAIN: G;                                                            
COMPND  35 MOL_ID: 11;                                                          
COMPND  36 MOLECULE: 30S RIBOSOMAL PROTEIN S8;                                  
COMPND  37 CHAIN: H;                                                            
COMPND  38 MOL_ID: 12;                                                          
COMPND  39 MOLECULE: 30S RIBOSOMAL PROTEIN S9;                                  
COMPND  40 CHAIN: I;                                                            
COMPND  41 MOL_ID: 13;                                                          
COMPND  42 MOLECULE: 30S RIBOSOMAL PROTEIN S10;                                 
COMPND  43 CHAIN: J;                                                            
COMPND  44 MOL_ID: 14;                                                          
COMPND  45 MOLECULE: 30S RIBOSOMAL PROTEIN S11;                                 
COMPND  46 CHAIN: K;                                                            
COMPND  47 MOL_ID: 15;                                                          
COMPND  48 MOLECULE: 30S RIBOSOMAL PROTEIN S12;                                 
COMPND  49 CHAIN: L;                                                            
COMPND  50 MOL_ID: 16;                                                          
COMPND  51 MOLECULE: 30S RIBOSOMAL PROTEIN S13;                                 
COMPND  52 CHAIN: M;                                                            
COMPND  53 MOL_ID: 17;                                                          
COMPND  54 MOLECULE: 30S RIBOSOMAL PROTEIN S14;                                 
COMPND  55 CHAIN: N;                                                            
COMPND  56 MOL_ID: 18;                                                          
COMPND  57 MOLECULE: 30S RIBOSOMAL PROTEIN S15;                                 
COMPND  58 CHAIN: O;                                                            
COMPND  59 MOL_ID: 19;                                                          
COMPND  60 MOLECULE: 30S RIBOSOMAL PROTEIN S16;                                 
COMPND  61 CHAIN: P;                                                            
COMPND  62 MOL_ID: 20;                                                          
COMPND  63 MOLECULE: 30S RIBOSOMAL PROTEIN S17;                                 
COMPND  64 CHAIN: Q;                                                            
COMPND  65 MOL_ID: 21;                                                          
COMPND  66 MOLECULE: 30S RIBOSOMAL PROTEIN S18;                                 
COMPND  67 CHAIN: R;                                                            
COMPND  68 MOL_ID: 22;                                                          
COMPND  69 MOLECULE: 30S RIBOSOMAL PROTEIN S19;                                 
COMPND  70 CHAIN: S;                                                            
COMPND  71 MOL_ID: 23;                                                          
COMPND  72 MOLECULE: 30S RIBOSOMAL PROTEIN S20;                                 
COMPND  73 CHAIN: T;                                                            
COMPND  74 MOL_ID: 24;                                                          
COMPND  75 MOLECULE: 30S RIBOSOMAL PROTEIN THX;                                 
COMPND  76 CHAIN: V                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 274;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 SYNTHETIC: YES;                                                      
SOURCE   6 MOL_ID: 3;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 MOL_ID: 4;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 MOL_ID: 5;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  12 ORGANISM_TAXID: 274;                                                 
SOURCE  13 MOL_ID: 6;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  15 ORGANISM_TAXID: 274;                                                 
SOURCE  16 MOL_ID: 7;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  18 ORGANISM_TAXID: 274;                                                 
SOURCE  19 MOL_ID: 8;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  21 ORGANISM_TAXID: 274;                                                 
SOURCE  22 MOL_ID: 9;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  24 ORGANISM_TAXID: 274;                                                 
SOURCE  25 MOL_ID: 10;                                                          
SOURCE  26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  27 ORGANISM_TAXID: 274;                                                 
SOURCE  28 MOL_ID: 11;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  30 ORGANISM_TAXID: 274;                                                 
SOURCE  31 MOL_ID: 12;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  33 ORGANISM_TAXID: 274;                                                 
SOURCE  34 MOL_ID: 13;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  36 ORGANISM_TAXID: 274;                                                 
SOURCE  37 MOL_ID: 14;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  39 ORGANISM_TAXID: 274;                                                 
SOURCE  40 MOL_ID: 15;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  42 ORGANISM_TAXID: 274;                                                 
SOURCE  43 MOL_ID: 16;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  45 ORGANISM_TAXID: 274;                                                 
SOURCE  46 MOL_ID: 17;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  48 ORGANISM_TAXID: 274;                                                 
SOURCE  49 MOL_ID: 18;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  51 ORGANISM_TAXID: 274;                                                 
SOURCE  52 MOL_ID: 19;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  54 ORGANISM_TAXID: 274;                                                 
SOURCE  55 MOL_ID: 20;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  57 ORGANISM_TAXID: 274;                                                 
SOURCE  58 MOL_ID: 21;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  60 ORGANISM_TAXID: 274;                                                 
SOURCE  61 MOL_ID: 22;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  63 ORGANISM_TAXID: 274;                                                 
SOURCE  64 MOL_ID: 23;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  66 ORGANISM_TAXID: 274;                                                 
SOURCE  67 MOL_ID: 24;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  69 ORGANISM_TAXID: 274                                                  
KEYWDS    30S RIBOSOMAL SUBUNIT, RIBOSOME, A SITE, DECODING, TRANSFER           
KEYWDS   2 RNA, TRNA, ANTICODON, STEM-LOOP, MESSENGER RNA, MRNA, CODON,         
KEYWDS   3 ANTIBIOTIC, PAROMOMYCIN                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.OGLE,D.E.BRODERSEN,W.M.CLEMONS JR.,M.J.TARRY,A.P.CARTER,          
AUTHOR   2 V.RAMAKRISHNAN                                                       
REVDAT   2   24-FEB-09 1IBL    1       VERSN                                    
REVDAT   1   04-MAY-01 1IBL    0                                                
JRNL        AUTH   J.M.OGLE,D.E.BRODERSEN,W.M.CLEMONS JR.,M.J.TARRY,            
JRNL        AUTH 2 A.P.CARTER,V.RAMAKRISHNAN                                    
JRNL        TITL   RECOGNITION OF COGNATE TRANSFER RNA BY THE 30S               
JRNL        TITL 2 RIBOSOMAL SUBUNIT.                                           
JRNL        REF    SCIENCE                       V. 292   897 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11340196                                                     
JRNL        DOI    10.1126/SCIENCE.1060612                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.T.WIMBERLY,D.E.BRODERSEN,W.M.CLEMONS JR.,                  
REMARK   1  AUTH 2 R.MORGAN-WARREN,A.P.CARTER,C.VONRHEIN,T.HARTSCH,             
REMARK   1  AUTH 3 V.RAMAKRISHNAN                                               
REMARK   1  TITL   STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT                       
REMARK   1  REF    NATURE                        V. 407   327 2000              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/35030006                                             
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.P.CARTER,W.M.CLEMONS JR.,D.E.BRODERSEN,                    
REMARK   1  AUTH 2 B.T.WIMBERLY,R.MORGAN-WARREN,V.RAMAKRISHNAN                  
REMARK   1  TITL   FUNCTIONAL INSIGHTS FROM THE STRUCTURE OF THE 30S            
REMARK   1  TITL 2 RIBOSOMAL SUBUNIT AND ITS INTERACTIONS WITH                  
REMARK   1  TITL 3 ANTIBIOTICS                                                  
REMARK   1  REF    NATURE                        V. 407   340 2000              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/35030019                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : PROTEINS: ENGH & HUBER, RNA: PARKINSON AT       
REMARK   3                      AL.                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 316.23                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 228284                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11526                           
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.22                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 18748                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3234                       
REMARK   3   BIN FREE R VALUE                    : 0.3712                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.27                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1043                         
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            : 19197                                   
REMARK   3   NUCLEIC ACID ATOMS       : 32904                                   
REMARK   3   HETEROGEN ATOMS          : 169                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.32                          
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.21                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.38                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.54                            
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        : 0.34                                                 
REMARK   3   BSOL        : 300.00                                               
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA-MULTI-ENDO.PARAM                       
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PAR_LIGAND.PAR                                 
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA-MULTI-ENDO.TOP                         
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : PAR_LIGAND.TOP                                 
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IBL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013130.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 90.0                               
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 9                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99187                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 240896                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 316.230                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 4.860                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.51                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.57800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, AMMONIUM CHLORIDE, POTASSIUM        
REMARK 280  CHLORIDE, MAGNESIUM ACETATE, SODIUM CACODYLATE, PH 6.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP AT 277K, PH 6.50                            
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       87.94250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      200.40000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      200.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.97125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      200.40000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      200.40000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      131.91375            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      200.40000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      200.40000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.97125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      200.40000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      200.40000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      131.91375            
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       87.94250            
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: 24-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X, Y, Z, B, C, D, E, F,            
REMARK 350                    AND CHAINS: G, H, I, J, K, L, M, N, O,            
REMARK 350                    AND CHAINS: P, Q, R, S, T, V                      
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       U A     0                                                      
REMARK 465       U A     1                                                      
REMARK 465       U A     2                                                      
REMARK 465       G A     3                                                      
REMARK 465       U A     4                                                      
REMARK 465       C A  1535                                                      
REMARK 465       C A  1536                                                      
REMARK 465       U A  1537                                                      
REMARK 465       C A  1538                                                      
REMARK 465       C A  1539                                                      
REMARK 465       U A  1540                                                      
REMARK 465       U A  1541                                                      
REMARK 465       U A  1542                                                      
REMARK 465       C A  1543                                                      
REMARK 465       U A  1544                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     ALA B   242                                                      
REMARK 465     GLU B   243                                                      
REMARK 465     ALA B   244                                                      
REMARK 465     THR B   245                                                      
REMARK 465     GLU B   246                                                      
REMARK 465     THR B   247                                                      
REMARK 465     PRO B   248                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     GLY B   250                                                      
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     MET C     1                                                      
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     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PRO E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     GLU E   155                                                      
REMARK 465     ALA E   156                                                      
REMARK 465     HIS E   157                                                      
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 G     1                                                      
REMARK 465     MET I     1                                                      
REMARK 465     MET J     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     MET K     1                                                      
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     LYS K     7                                                      
REMARK 465     LYS K     8                                                      
REMARK 465     LYS K     9                                                      
REMARK 465     VAL K    10                                                      
REMARK 465     MET L     1                                                      
REMARK 465     VAL L     2                                                      
REMARK 465     ALA L     3                                                      
REMARK 465     LEU L     4                                                      
REMARK 465     ALA L   129                                                      
REMARK 465     LYS L   130                                                      
REMARK 465     THR L   131                                                      
REMARK 465     ALA L   132                                                      
REMARK 465     ALA L   133                                                      
REMARK 465     LYS L   134                                                      
REMARK 465     LYS L   135                                                      
REMARK 465     MET M     1                                                      
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     MET N     1                                                      
REMARK 465     MET O     1                                                      
REMARK 465     ALA P    84                                                      
REMARK 465     ARG P    85                                                      
REMARK 465     GLU P    86                                                      
REMARK 465     GLY P    87                                                      
REMARK 465     ALA P    88                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     MET R     1                                                      
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     LYS R     7                                                      
REMARK 465     PRO R     8                                                      
REMARK 465     LYS R     9                                                      
REMARK 465     LYS R    10                                                      
REMARK 465     GLU R    11                                                      
REMARK 465     ALA R    12                                                      
REMARK 465     GLN R    13                                                      
REMARK 465     ARG R    14                                                      
REMARK 465     ARG R    15                                                      
REMARK 465     MET S     1                                                      
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     MET T     1                                                      
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 V    26                                                      
REMARK 465     LYS V    27                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470       U A   5    P    OP1  OP2                                       
REMARK 470     THR J 100    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OP1  G   A   254     O    LYS Q    67              2.04            
REMARK 500   O    LYS L    28     N    ALA L    30              2.09            
REMARK 500   OP1  U   A  1330     O    TYR M    23              2.11            
REMARK 500   O2'  G   A  1182     OP2  A   A  1183              2.14            
REMARK 500   O    VAL J    49     O    ARG J    60              2.15            
REMARK 500   O    ILE C    14     N    ARG C    16              2.16            
REMARK 500   OP1  G   A   521     O    GLU L    73              2.18            
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   CD   ARG J    79     CD   ARG J    79     8665     2.14            
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    VAL D 198   C     ASN D 199   N      -0.191                       
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      C A  48   C2' -  C3' -  O3' ANGL. DEV. =  11.3 DEGREES          
REMARK 500      A A  60   C2' -  C3' -  O3' ANGL. DEV. =  10.5 DEGREES          
REMARK 500      G A 129A  C2' -  C3' -  O3' ANGL. DEV. =  10.8 DEGREES          
REMARK 500      G A 181   C2' -  C3' -  O3' ANGL. DEV. =  12.2 DEGREES          
REMARK 500      A A 197   C2' -  C3' -  O3' ANGL. DEV. =  10.4 DEGREES          
REMARK 500      A A 243   C2' -  C3' -  O3' ANGL. DEV. =  16.7 DEGREES          
REMARK 500      G A 281   C2' -  C3' -  O3' ANGL. DEV. =  16.4 DEGREES          
REMARK 500      C A 328   C2' -  C3' -  O3' ANGL. DEV. =  12.0 DEGREES          
REMARK 500      A A 353   C5' -  C4' -  O4' ANGL. DEV. =  -8.1 DEGREES          
REMARK 500      C A 366   C2' -  C3' -  O3' ANGL. DEV. =  14.3 DEGREES          
REMARK 500      C A 372   C2' -  C3' -  O3' ANGL. DEV. =  11.8 DEGREES          
REMARK 500      A A 460   N9  -  C1' -  C2' ANGL. DEV. =   8.1 DEGREES          
REMARK 500      G A 481   C5' -  C4' -  C3' ANGL. DEV. =  -9.9 DEGREES          
REMARK 500      G A 484   C2' -  C3' -  O3' ANGL. DEV. =  15.1 DEGREES          
REMARK 500      A A 559   C2' -  C3' -  O3' ANGL. DEV. =  10.1 DEGREES          
REMARK 500      A A 687   C2' -  C3' -  O3' ANGL. DEV. =  14.3 DEGREES          
REMARK 500      A A 913   C2' -  C3' -  O3' ANGL. DEV. =  10.0 DEGREES          
REMARK 500      A A 965   C2' -  C3' -  O3' ANGL. DEV. =  12.3 DEGREES          
REMARK 500      A A1299   N9  -  C1' -  C2' ANGL. DEV. =   7.9 DEGREES          
REMARK 500      U A1302   C2' -  C3' -  O3' ANGL. DEV. =  14.8 DEGREES          
REMARK 500      A A1346   C2' -  C3' -  O3' ANGL. DEV. =  11.5 DEGREES          
REMARK 500      U A1498   C2' -  C3' -  O3' ANGL. DEV. =  17.9 DEGREES          
REMARK 500      A A1502   N9  -  C1' -  C2' ANGL. DEV. =   9.3 DEGREES          
REMARK 500      U A1528   C4' -  C3' -  O3' ANGL. DEV. =  12.8 DEGREES          
REMARK 500      U A1528   C2' -  C3' -  O3' ANGL. DEV. =  13.6 DEGREES          
REMARK 500    CYS D  12   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B   8     -109.82   -174.52                                   
REMARK 500    GLU B   9      105.47     60.80                                   
REMARK 500    LEU B  10      -62.75    -90.95                                   
REMARK 500    LEU B  11       68.89    -67.89                                   
REMARK 500    ALA B  13        4.87    -60.40                                   
REMARK 500    VAL B  15     -131.16   -169.13                                   
REMARK 500    HIS B  16      -75.46     42.45                                   
REMARK 500    PHE B  17      -74.58     21.76                                   
REMARK 500    GLU B  20      117.24     59.53                                   
REMARK 500    ARG B  21     -177.59    -56.16                                   
REMARK 500    ARG B  23       -5.92    174.47                                   
REMARK 500    TRP B  24     -134.70     -9.73                                   
REMARK 500    ASN B  25      114.09   -166.94                                   
REMARK 500    PHE B  28        6.86    -68.23                                   
REMARK 500    TYR B  31       17.05    -69.61                                   
REMARK 500    ILE B  39      129.22     64.58                                   
REMARK 500    ILE B  42      139.57    -36.66                                   
REMARK 500    MET B  48      -72.75    -51.68                                   
REMARK 500    GLU B  59      -72.87    -51.34                                   
REMARK 500    ASP B  60      -34.24    -32.10                                   
REMARK 500    MET B  63       39.98    -70.77                                   
REMARK 500    ARG B  64        5.18   -153.28                                   
REMARK 500    LYS B  74      107.29    -47.83                                   
REMARK 500    LYS B  75      -16.69    -47.51                                   
REMARK 500    ALA B  77       16.32   -156.08                                   
REMARK 500    GLN B  78       44.34    -70.99                                   
REMARK 500    ASP B  79      -56.06   -161.87                                   
REMARK 500    MET B  83      -89.81    -69.79                                   
REMARK 500    ALA B  88     -169.50   -105.49                                   
REMARK 500    MET B  90      154.56    -46.34                                   
REMARK 500    GLN B  95      -96.28    -60.23                                   
REMARK 500    THR B 107      -62.67    -93.64                                   
REMARK 500    HIS B 113        8.58    -61.43                                   
REMARK 500    ALA B 120      -72.61    -67.97                                   
REMARK 500    LEU B 121      -39.02    -37.56                                   
REMARK 500    ALA B 123      -20.02   -178.00                                   
REMARK 500    ARG B 130      140.84     71.13                                   
REMARK 500    PRO B 131      159.52    -49.47                                   
REMARK 500    GLN B 135       37.86    -73.56                                   
REMARK 500    VAL B 136      -40.14   -159.34                                   
REMARK 500    LEU B 149       36.16    -85.06                                   
REMARK 500    ALA B 177      -74.76    -51.89                                   
REMARK 500    ARG B 178      -65.78    -29.70                                   
REMARK 500    PHE B 181        9.93     56.64                                   
REMARK 500    ALA B 188      144.47    -22.50                                   
REMARK 500    THR B 190      -34.10    -26.99                                   
REMARK 500    ASP B 195      -23.68    -35.21                                   
REMARK 500    PRO B 202       95.94    -65.87                                   
REMARK 500    ASN B 204       99.96    -51.39                                   
REMARK 500    ALA B 207      112.70     85.37                                   
REMARK 500    ARG B 226       30.41    -98.64                                   
REMARK 500    PRO B 232      154.06    -39.16                                   
REMARK 500    TYR B 236       -9.24    -59.05                                   
REMARK 500    ASN C   3     -142.01   -146.08                                   
REMARK 500    LYS C   4      118.93     73.30                                   
REMARK 500    PRO C   7      -13.38    -46.79                                   
REMARK 500    LEU C  12      -34.84    -39.35                                   
REMARK 500    ILE C  14     -147.78   -131.79                                   
REMARK 500    THR C  15       42.34      6.92                                   
REMARK 500    ARG C  16      145.39    161.68                                   
REMARK 500    TRP C  18      159.89    -48.27                                   
REMARK 500    SER C  20       82.35   -177.10                                   
REMARK 500    ARG C  21       76.18   -100.19                                   
REMARK 500    LYS C  26      -32.74    -26.52                                   
REMARK 500    TYR C  29      -50.64    -28.31                                   
REMARK 500    ARG C  30        5.84    -68.76                                   
REMARK 500    ILE C  39      -80.45    -64.36                                   
REMARK 500    ARG C  40       -9.79    -52.28                                   
REMARK 500    LEU C  43       -4.34    -57.74                                   
REMARK 500    LYS C  45       11.12    -65.56                                   
REMARK 500    GLU C  46      -81.28   -127.74                                   
REMARK 500    LEU C  47       18.67    -58.94                                   
REMARK 500    ALA C  53      -93.55    -88.47                                   
REMARK 500    ALA C  60       59.78   -164.09                                   
REMARK 500    ALA C  61       97.68     70.06                                   
REMARK 500    ASP C  62       -7.19     61.09                                   
REMARK 500    THR C  67       57.65    -65.97                                   
REMARK 500    LYS C  72       69.66   -119.69                                   
REMARK 500    GLU C  82      -95.11    -62.12                                   
REMARK 500    ILE C  84       40.24    -62.58                                   
REMARK 500    ARG C  85      -51.56   -149.30                                   
REMARK 500    LEU C  94      -73.95    -73.09                                   
REMARK 500    LYS C  97        3.60   -150.42                                   
REMARK 500    ASN C  98      101.26     45.17                                   
REMARK 500    ALA C 100     -163.63    -56.05                                   
REMARK 500    LEU C 101       54.93   -175.78                                   
REMARK 500    ASN C 102      172.80    -57.96                                   
REMARK 500    ASN C 108      108.18     64.73                                   
REMARK 500    ARG C 119      -72.78    -50.71                                   
REMARK 500    ARG C 127       50.13     80.26                                   
REMARK 500    ALA C 146      121.04     65.51                                   
REMARK 500    LYS C 150      139.13   -171.17                                   
REMARK 500    SER C 154     -137.24    -77.80                                   
REMARK 500    ARG C 156       21.01     93.53                                   
REMARK 500    ARG C 164     -151.49   -135.80                                   
REMARK 500    THR C 165      116.19   -175.61                                   
REMARK 500    TRP C 167     -120.30   -103.91                                   
REMARK 500    ALA C 168      119.11     88.09                                   
REMARK 500    ARG C 172      126.22    -37.06                                   
REMARK 500    ARG C 179      -24.75    178.05                                   
REMARK 500    ASN C 181      118.09     85.97                                   
REMARK 500    ALA C 189       88.72    175.98                                   
REMARK 500    GLU C 206      -76.14   -167.70                                   
REMARK 500    ARG D   3       95.59    -41.55                                   
REMARK 500    TYR D   4      -87.82     49.25                                   
REMARK 500    ILE D   5      121.62     68.10                                   
REMARK 500    PRO D   7      126.99    -33.61                                   
REMARK 500    LYS D  22       -5.16   -162.57                                   
REMARK 500    ARG D  25      -48.94     78.31                                   
REMARK 500    PRO D  29       62.85     -6.60                                   
REMARK 500    LYS D  30       -3.56   -166.18                                   
REMARK 500    CYS D  31       -0.41    -56.34                                   
REMARK 500    ALA D  32      -46.19     76.55                                   
REMARK 500    ARG D  35       97.72     65.14                                   
REMARK 500    ARG D  36       45.04    119.31                                   
REMARK 500    PRO D  37        4.66    -69.82                                   
REMARK 500    PRO D  39      157.20    -49.05                                   
REMARK 500    GLN D  42       -8.08    -45.72                                   
REMARK 500    VAL D  88       92.74    -47.64                                   
REMARK 500    ASP D 134       35.17    -98.73                                   
REMARK 500    SER D 137        4.60    -69.43                                   
REMARK 500    GLU D 150      -65.84    -19.75                                   
REMARK 500    ASN D 154       75.79   -113.94                                   
REMARK 500    ASN D 161      -71.42    -62.69                                   
REMARK 500    ALA D 164      -19.00    -42.71                                   
REMARK 500    PRO D 172        5.58    -66.22                                   
REMARK 500    ASP D 177       70.90   -151.25                                   
REMARK 500    SER D 208      -82.78    -86.96                                   
REMARK 500    PRO E  70       82.19    -69.28                                   
REMARK 500    ASN E  73      -11.00     66.15                                   
REMARK 500    HIS E  78     -170.07    162.15                                   
REMARK 500    ARG E 107      -80.68    -51.58                                   
REMARK 500    ALA E 108      -35.90    -27.24                                   
REMARK 500    ASN F  11      112.51    -34.99                                   
REMARK 500    PRO F  12       13.82    -69.09                                   
REMARK 500    LYS F  39      145.12    -37.03                                   
REMARK 500    LYS F  54      -16.73     67.73                                   
REMARK 500    LEU F  98      143.56    -36.71                                   
REMARK 500    ALA G   7      129.75    -20.34                                   
REMARK 500    ASP G  33       19.71     57.66                                   
REMARK 500    ASN G  37      -77.27    -59.40                                   
REMARK 500    GLU G  52       -7.04    -52.09                                   
REMARK 500    LYS G  63      -82.24    -37.17                                   
REMARK 500    GLN G  64      -39.92    -36.67                                   
REMARK 500    ALA G 100      -70.06    -52.72                                   
REMARK 500    ASN G 109       19.02    -67.67                                   
REMARK 500    ARG G 111      158.30    -49.90                                   
REMARK 500    ALA G 134      -70.78    -55.58                                   
REMARK 500    GLU G 146      -63.19     66.72                                   
REMARK 500    ALA G 147        2.33    -62.07                                   
REMARK 500    ASN G 148       13.29   -142.08                                   
REMARK 500    ARG G 155      -27.91    -36.78                                   
REMARK 500    ASN H  15      -70.35    -46.75                                   
REMARK 500    SER H  23     -159.85   -115.91                                   
REMARK 500    THR H  24      133.38    167.31                                   
REMARK 500    SER H  29      136.40   -175.75                                   
REMARK 500    ARG H  30      -71.20    -34.05                                   
REMARK 500    TYR H  58     -169.26   -110.92                                   
REMARK 500    ASP H  73       76.03     51.67                                   
REMARK 500    PRO H  76      161.99    -48.82                                   
REMARK 500    ILE H  86      -78.93   -116.56                                   
REMARK 500    ARG H  91       68.77    136.95                                   
REMARK 500    ARG H 104       67.43     63.71                                   
REMARK 500    ARG H 105       30.66     33.38                                   
REMARK 500    LEU H 127        2.64    -65.54                                   
REMARK 500    VAL H 137      129.17   -176.70                                   
REMARK 500    THR I   7      -91.21    -94.83                                   
REMARK 500    LYS I  11       67.16     34.55                                   
REMARK 500    GLN I  38       92.87    -50.21                                   
REMARK 500    VAL I  41      -69.30     -7.97                                   
REMARK 500    ALA I  43      -59.10    -18.84                                   
REMARK 500    ALA I  45      -52.52    -25.38                                   
REMARK 500    ALA I  46      -18.52    -37.30                                   
REMARK 500    LEU I  56      -46.18     74.13                                   
REMARK 500    ARG I  58       -7.24   -176.04                                   
REMARK 500    TYR I  88     -114.12    -65.26                                   
REMARK 500    ALA I  94      -47.87    -16.97                                   
REMARK 500    ASP I 105      106.68    -32.94                                   
REMARK 500    HIS I 117      -42.87    -19.02                                   
REMARK 500    ALA I 119      -81.23     74.96                                   
REMARK 500    LYS I 127       43.22     28.37                                   
REMARK 500    ILE J   4       75.74   -155.55                                   
REMARK 500    THR J  15       -3.77    -57.76                                   
REMARK 500    LEU J  16      -74.25   -117.38                                   
REMARK 500    ASP J  17      -53.00    -24.49                                   
REMARK 500    ILE J  23       29.12    -67.23                                   
REMARK 500    VAL J  24      -61.90   -122.24                                   
REMARK 500    ALA J  26       20.26    -71.62                                   
REMARK 500    ALA J  27        8.81   -168.88                                   
REMARK 500    ALA J  32      -87.03    -56.61                                   
REMARK 500    GLN J  33       15.47   -171.77                                   
REMARK 500    VAL J  34      176.08     65.23                                   
REMARK 500    LEU J  40      125.02     68.46                                   
REMARK 500    PHE J  54      115.15     49.02                                   
REMARK 500    LYS J  55     -164.01     47.51                                   
REMARK 500    HIS J  56       51.39     71.89                                   
REMARK 500    SER J  59      -85.07    -90.63                                   
REMARK 500    ARG J  60      -81.18     86.10                                   
REMARK 500    GLU J  61      137.92     63.66                                   
REMARK 500    LEU J  71      -61.36   -126.46                                   
REMARK 500    VAL J  72      -90.63     64.76                                   
REMARK 500    ASP J  73      101.81     64.76                                   
REMARK 500    ASN J  76       64.62     87.49                                   
REMARK 500    ASN J  78       54.33   -105.12                                   
REMARK 500    ARG J  79      -72.02     52.10                                   
REMARK 500    LEU J  85      -80.06    -77.91                                   
REMARK 500    MET J  86      -84.00     37.76                                   
REMARK 500    THR J  87       83.46   -153.63                                   
REMARK 500    LEU J  90      -58.32   -146.67                                   
REMARK 500    ARG K  12       40.46   -144.30                                   
REMARK 500    GLN K  13      113.42     16.88                                   
REMARK 500    ALA K  15      -82.20     49.61                                   
REMARK 500    HIS K  22       76.96   -111.07                                   
REMARK 500    ASN K  27      149.62    166.81                                   
REMARK 500    PRO K  35      -22.35    -26.54                                   
REMARK 500    ILE K  48     -154.06    -87.97                                   
REMARK 500    TYR K  50      128.51    -37.02                                   
REMARK 500    THR K  57      141.63    -33.73                                   
REMARK 500    ALA K  69      -77.14    -62.22                                   
REMARK 500    LYS K  70      -71.87    -30.74                                   
REMARK 500    LYS K  71      -39.81    -37.42                                   
REMARK 500    GLN K  78       29.81   -177.20                                   
REMARK 500    SER K  79      130.98    179.36                                   
REMARK 500    THR K  87       79.39   -119.95                                   
REMARK 500    ARG K  91      -83.33    -50.66                                   
REMARK 500    LEU K 103      140.91    -36.12                                   
REMARK 500    HIS K 116       31.19    -84.54                                   
REMARK 500    ASN K 117       81.38     87.17                                   
REMARK 500    LYS K 127       -2.28     79.80                                   
REMARK 500    VAL L  24       66.82   -155.29                                   
REMARK 500    ALA L  26        3.11    -67.58                                   
REMARK 500    LEU L  27      150.67     55.06                                   
REMARK 500    ALA L  30      146.03    -20.48                                   
REMARK 500    LYS L  46     -140.08   -112.05                                   
REMARK 500    LYS L  47      -88.44     11.85                                   
REMARK 500    ALA L  51     -169.97    165.59                                   
REMARK 500    SER L  62       35.66    -89.21                                   
REMARK 500    GLU L  73      -85.13    -56.70                                   
REMARK 500    HIS L  75     -151.45   -124.19                                   
REMARK 500    ASN L  76       46.73   -164.24                                   
REMARK 500    GLU L  79      -17.55    -41.89                                   
REMARK 500    TYR L 105     -128.71     76.03                                   
REMARK 500    VAL L 110      107.72    -18.77                                   
REMARK 500    ASP L 112      -10.61     67.75                                   
REMARK 500    LYS L 115      -93.74    -97.06                                   
REMARK 500    SER L 116       36.30    -70.81                                   
REMARK 500    ARG M   3       56.39     18.03                                   
REMARK 500    ILE M   4     -106.67    -77.61                                   
REMARK 500    ALA M   5      171.81    -51.57                                   
REMARK 500    VAL M   7       50.67     38.88                                   
REMARK 500    ILE M   9       68.18    175.23                                   
REMARK 500    ASN M  12      -12.52     76.29                                   
REMARK 500    TYR M  21       -8.12    -48.37                                   
REMARK 500    TYR M  23      -98.54    -48.76                                   
REMARK 500    LYS M  27      -71.85     21.15                                   
REMARK 500    ALA M  28      -81.67    -52.60                                   
REMARK 500    LYS M  36       26.43    -66.07                                   
REMARK 500    THR M  63      -30.62    138.71                                   
REMARK 500    GLU M  67     -127.03     18.75                                   
REMARK 500    ARG M  80      -75.52    -60.75                                   
REMARK 500    CYS M  86      119.56     36.71                                   
REMARK 500    ARG M  93      -72.96    -63.88                                   
REMARK 500    ASN M 106     -152.13     48.19                                   
REMARK 500    THR M 109       10.30    -60.50                                   
REMARK 500    ARG M 110      -14.72   -148.19                                   
REMARK 500    LYS N  11      100.38    -48.04                                   
REMARK 500    THR N  13      108.73    -53.90                                   
REMARK 500    LYS N  15      -30.11    106.16                                   
REMARK 500    ARG N  19        7.16    -52.60                                   
REMARK 500    ARG N  23      143.09     64.25                                   
REMARK 500    VAL N  25       38.76    -87.24                                   
REMARK 500    ARG N  26      -63.58   -165.92                                   
REMARK 500    ALA N  30      -79.51    -74.71                                   
REMARK 500    SER N  32      -17.57    114.31                                   
REMARK 500    ARG N  35      -59.06   -123.07                                   
REMARK 500    PHE N  36       33.71    -61.78                                   
REMARK 500    PHE N  37      -32.23   -167.88                                   
REMARK 500    GLN N  52        4.26    -66.47                                   
REMARK 500    ALA O  16      128.23    -35.15                                   
REMARK 500    PHE O  18      161.71    176.20                                   
REMARK 500    ASP O  21       99.34    -65.27                                   
REMARK 500    ARG O  63      -76.32    -72.71                                   
REMARK 500    ARG O  64      -37.39    -34.68                                   
REMARK 500    GLU O  73      -59.59   -121.17                                   
REMARK 500    PRO O  75      -24.40    -39.87                                   
REMARK 500    LEU O  85      -94.51    -78.22                                   
REMARK 500    PHE P   9      -22.48   -142.94                                   
REMARK 500    ALA P  24      -36.54    -35.37                                   
REMARK 500    LYS P  43       61.95     34.22                                   
REMARK 500    ASP P  47       57.24   -110.64                                   
REMARK 500    SER Q  12      117.98    176.85                                   
REMARK 500    LYS Q  17       26.71     49.63                                   
REMARK 500    LYS Q  34      135.43    -30.34                                   
REMARK 500    GLU Q  49       55.70     29.97                                   
REMARK 500    PRO Q  64      129.99    -37.57                                   
REMARK 500    SER Q  66     -173.72    178.32                                   
REMARK 500    ARG Q  68      -33.79     66.17                                   
REMARK 500    ARG Q  75     -144.10   -162.37                                   
REMARK 500    ARG Q  81       74.84    173.83                                   
REMARK 500    TYR Q  95      -75.54    -55.96                                   
REMARK 500    GLN Q  96      -37.21    -27.82                                   
REMARK 500    SER Q  97      -91.65    -65.57                                   
REMARK 500    LEU Q  98       63.85    -32.83                                   
REMARK 500    SER Q  99      -89.20   -123.76                                   
REMARK 500    LYS Q 104     -145.49   -101.37                                   
REMARK 500    SER R  17       80.83     62.04                                   
REMARK 500    ARG R  18       53.62   -145.18                                   
REMARK 500    LYS R  19     -123.24   -129.17                                   
REMARK 500    VAL R  22      -12.79    -48.80                                   
REMARK 500    LEU R  26      171.21    160.40                                   
REMARK 500    ASN R  36       62.57    -68.09                                   
REMARK 500    LEU R  58     -165.69    -56.54                                   
REMARK 500    ARG R  87     -145.81     77.80                                   
REMARK 500    LEU S   5      -70.24   -152.36                                   
REMARK 500    LYS S   6     -105.66    140.63                                   
REMARK 500    VAL S   9      152.51    -38.41                                   
REMARK 500    HIS S  14      -91.94    -22.74                                   
REMARK 500    LEU S  16      -76.92    -57.51                                   
REMARK 500    GLU S  17        1.60    -62.08                                   
REMARK 500    LEU S  22      -36.54    -36.80                                   
REMARK 500    LYS S  28     -163.11   -118.79                                   
REMARK 500    LEU S  30      124.69     69.94                                   
REMARK 500    GLU S  43        5.25    -57.25                                   
REMARK 500    VAL S  67     -100.11    -61.96                                   
REMARK 500    HIS S  83      -44.35    133.39                                   
REMARK 500    ASN T   9       88.61     69.79                                   
REMARK 500    SER T  11      -14.03    -49.37                                   
REMARK 500    LYS T  38      -73.90    -48.53                                   
REMARK 500    LYS T  39      -62.58    -19.84                                   
REMARK 500    GLU T  50      -81.66    -33.46                                   
REMARK 500    SER T  70       47.26    -94.68                                   
REMARK 500    LEU T  72      -48.84   -137.63                                   
REMARK 500    HIS T  73     -154.29     37.56                                   
REMARK 500    LYS T  74     -153.16     39.86                                   
REMARK 500    ARG T  86      -88.54    -65.19                                   
REMARK 500    LYS T  87      -37.84    -36.62                                   
REMARK 500    ALA T  94       33.91   -149.02                                   
REMARK 500    ALA T  95       42.06     79.10                                   
REMARK 500    ALA T  97       90.83     77.82                                   
REMARK 500    PRO T  98       74.28    -25.21                                   
REMARK 500    LYS V   3      -19.70    -46.26                                   
REMARK 500    ARG V   9      -83.91    -51.68                                   
REMARK 500    THR V  17     -166.84    -72.71                                   
REMARK 500    ARG V  22       71.58    176.76                                   
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      C A  19         0.07    SIDE_CHAIN                              
REMARK 500      G A  77         0.06    SIDE_CHAIN                              
REMARK 500      U A 190L        0.07    SIDE_CHAIN                              
REMARK 500      A A 197         0.07    SIDE_CHAIN                              
REMARK 500      A A 250         0.07    SIDE_CHAIN                              
REMARK 500      G A 251         0.05    SIDE_CHAIN                              
REMARK 500      C A 290         0.06    SIDE_CHAIN                              
REMARK 500      U A 368         0.07    SIDE_CHAIN                              
REMARK 500      G A 380         0.07    SIDE_CHAIN                              
REMARK 500      U A 387         0.08    SIDE_CHAIN                              
REMARK 500      U A 495         0.06    SIDE_CHAIN                              
REMARK 500      C A 528         0.06    SIDE_CHAIN                              
REMARK 500      U A 561         0.08    SIDE_CHAIN                              
REMARK 500      G A 587         0.07    SIDE_CHAIN                              
REMARK 500      G A 664         0.06    SIDE_CHAIN                              
REMARK 500      G A 682         0.05    SIDE_CHAIN                              
REMARK 500      G A 691         0.05    SIDE_CHAIN                              
REMARK 500      G A 724         0.06    SIDE_CHAIN                              
REMARK 500      G A 727         0.09    SIDE_CHAIN                              
REMARK 500      A A 733         0.05    SIDE_CHAIN                              
REMARK 500      A A 759         0.07    SIDE_CHAIN                              
REMARK 500      C A 879         0.08    SIDE_CHAIN                              
REMARK 500      G A 898         0.08    SIDE_CHAIN                              
REMARK 500      U A1073         0.08    SIDE_CHAIN                              
REMARK 500      G A1077         0.08    SIDE_CHAIN                              
REMARK 500      G A1185         0.06    SIDE_CHAIN                              
REMARK 500      G A1300         0.05    SIDE_CHAIN                              
REMARK 500      U A1341         0.07    SIDE_CHAIN                              
REMARK 500      U A1390         0.07    SIDE_CHAIN                              
REMARK 500      G A1405         0.05    SIDE_CHAIN                              
REMARK 500      U A1414         0.08    SIDE_CHAIN                              
REMARK 500      G A1454         0.06    SIDE_CHAIN                              
REMARK 500      A A1492         0.06    SIDE_CHAIN                              
REMARK 500      A A1519         0.07    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 A 210  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 604   O6                                                     
REMARK 620 2   U A 605   O4   63.7                                              
REMARK 620 3   G A 633   O6   79.1  75.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 214  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 548   OP1                                                    
REMARK 620 2   A A 547   OP1 103.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1546  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 944   OP1                                                    
REMARK 620 2   G A 945   OP2  85.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1548  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A  22   O6                                                     
REMARK 620 2   G A  21   O6   86.7                                              
REMARK 620 3   U A  12   O4   75.3  88.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1551  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 749   OP2                                                    
REMARK 620 2   G A 750   OP2 120.2                                              
REMARK 620 3   C A 749   OP1  55.6  75.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1558  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 509   O3'                                                    
REMARK 620 2   A A 509   OP2  65.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1562  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 596   OP2                                                    
REMARK 620 2   G A 597   OP2  92.1                                              
REMARK 620 3   G A 595   O3'  54.2 111.9                                        
REMARK 620 4   U A 598   O4  169.0  84.8 136.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1563  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 869   N7                                                     
REMARK 620 2   G A 858   N7   61.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1565  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 911   O4                                                     
REMARK 620 2   G A 886   O6   78.1                                              
REMARK 620 3   G A 885   O6  101.3  71.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1570  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A1199   OP1                                                    
REMARK 620 2   U A1199   OP2  55.5                                              
REMARK 620 3   A A 964   OP1  73.4 128.9                                        
REMARK 620 N                    1     2                                         
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 A 979   O3'                                                    
REMARK 620 2   C A 980   OP1  72.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1573  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A1054   OP2                                                    
REMARK 620 2   G A1053   O2'  99.6                                              
REMARK 620 3   C A1054   OP1  63.1  64.9                                        
REMARK 620 4   G A1197   OP1  80.4 101.3  45.4                                  
REMARK 620 5   G A1053   O3'  50.9  48.8  50.6  94.8                            
REMARK 620 N                    1     2     3     4                             
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   C A1054   OP1                                                    
REMARK 620 2   U A1196   O3'  97.3                                              
REMARK 620 3   C A1054   O5'  51.4 101.9                                        
REMARK 620 4   G A1197   OP1  49.4  66.8  96.3                                  
REMARK 620 5   G A1198   OP2  66.2 129.0 102.6  66.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1575  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 558   OP1                                                    
REMARK 620 2   G A 299   O6  139.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1577  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 574   OP2                                                    
REMARK 620 2   A A 573   OP2  69.7                                              
REMARK 620 3   A A 572   OP2 161.2  92.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1580  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1079   O6                                                     
REMARK 620 2   C A 866   OP1 162.2                                              
REMARK 620 3   A A 865   O3' 111.3  52.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1581  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1068   OP1                                                    
REMARK 620 2   G A1094   OP1 101.9                                              
REMARK 620 3   A A1067   O3'  56.2  94.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1582  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A1095   OP2                                                    
REMARK 620 2   G A1108   O6   78.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1585  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1511   O6                                                     
REMARK 620 2   U A1512   O4   74.2                                              
REMARK 620 3   G A1523   O6   74.0  74.6                                        
REMARK 620 4   U A1510   O4   78.8 125.8 139.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1586  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1499   O3'                                                    
REMARK 620 2   G A1521   OP1  91.5                                              
REMARK 620 3   G A1508   OP1 115.4 136.5                                        
REMARK 620 4   A A1500   OP1  53.2 136.1  62.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1587  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1505   OP2                                                    
REMARK 620 2   A A1499   OP2 108.9                                              
REMARK 620 3   A A1500   OP2  77.5 106.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1588  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1508   OP1                                                    
REMARK 620 2   A A1500   OP1  81.2                                              
REMARK 620 3   G A1505   OP1 166.4  87.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1591  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 183   OP2                                                    
REMARK 620 2   U A 182   OP1  85.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1592  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 117   OP2                                                    
REMARK 620 2   A A 116   OP2  83.2                                              
REMARK 620 3   G A 289   OP2 139.1  81.9                                        
REMARK 620 4   A A 116   OP1  94.2  53.4 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1594  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 372   O2                                                     
REMARK 620 2   U A 387   O4   85.7                                              
REMARK 620 3   C A 372   O2'  82.8  86.9                                        
REMARK 620 4   U A 375   O4   75.7 126.6 137.6                                  
REMARK 620 5   G A 376   O6  109.0  81.3 162.4  59.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1596  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 794   OP2                                                    
REMARK 620 2   A A 782   OP1 167.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1597  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1058   O6                                                     
REMARK 620 2   U A1199   O4   72.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1598  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A1303   OP2                                                    
REMARK 620 2   G A1304   OP2 104.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1599  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 565   OP2                                                    
REMARK 620 2   G A 567   OP2  84.3                                              
REMARK 620 3   A A 563   O2'  88.1  90.6                                        
REMARK 620 4   C A 564   OP2  92.8 177.1  89.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 529   N7                                                     
REMARK 620 2   C A 518   N3   78.2                                              
REMARK 620 3 PRO L  48   O   156.9  93.9                                        
REMARK 620 4   G A 529   O6   63.5  88.0  94.8                                  
REMARK 620 5 ASN L  49   ND2 102.2 165.1  79.9  79.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 235   N4                                                     
REMARK 620 2   C A 121   O2   88.5                                              
REMARK 620 3   G A 124   O6  171.3  83.4                                        
REMARK 620 4   C A 121   N3   78.7  46.8  97.9                                  
REMARK 620 5   U A 125   O4  112.6 115.2  68.5 160.1                            
REMARK 620 6   G A 126   O6   58.3 138.5 127.2 133.1  64.7                      
REMARK 620 7   G A 236   O6  112.4 151.1  76.3 115.8  76.2  70.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1606  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 175   OP2                                                    
REMARK 620 2   C A 174   OP1  67.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 109   OP1                                                    
REMARK 620 2   G A 331   OP2 130.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1608  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A  98   O4                                                     
REMARK 620 2   G A  70   O6   72.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1609  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 105   O6                                                     
REMARK 620 2   G A  61   O6   70.5                                              
REMARK 620 3   U A  62   O4   74.5  79.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1613  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO L  48   O                                                      
REMARK 620 2   C A 518   O2   82.7                                              
REMARK 620 3   C A 518   N3   92.6  44.5                                        
REMARK 620 4   U Z   3   O2' 117.2 142.9 100.8                                  
REMARK 620 5   G A 530   O6  172.0  90.1  84.6  70.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1614  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 831   O4                                                     
REMARK 620 2   G A 855   O6   83.6                                              
REMARK 620 3   C A 856   N4  130.2  67.0                                        
REMARK 620 4   G A 830   O6   78.5  98.2  67.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1622  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A1090   O4                                                     
REMARK 620 2   U A1095   O4   77.4                                              
REMARK 620 3   G A1094   OP2 130.9  66.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1624  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 182   OP1                                                    
REMARK 620 2   G A 183   N7   92.9                                              
REMARK 620 3   G A 181   O2'  90.4  92.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1625  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1238   OP2                                                    
REMARK 620 2   C A1335   O2   74.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1632  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 533   OP1                                                    
REMARK 620 2   U A 516   O4  137.8                                              
REMARK 620 3   A A 532   O3'  53.7 130.2                                        
REMARK 620 4   A A 533   OP2  65.5  87.7  50.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1633  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A1049   OP1                                                    
REMARK 620 2 ALA N   2   O    83.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1634  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A1052   O4                                                     
REMARK 620 2   C A1200   O2   73.3                                              
REMARK 620 3   G A1207   O6   75.4 130.8                                        
REMARK 620 4   G A1206   O6   81.7  82.8  55.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1635  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 921   O4                                                     
REMARK 620 2   U A1393   O4  167.2                                              
REMARK 620 3   G A 922   O6   92.6  76.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1637  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A 924   N4                                                     
REMARK 620 2   U A1390   O4  106.6                                              
REMARK 620 3   G A 925   O6   70.1 121.8                                        
REMARK 620 4   G A 927   O6  132.8  79.8  67.5                                  
REMARK 620 5   U A1391   O4   66.1  65.8  60.2  75.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1638  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A 920   O4                                                     
REMARK 620 2   G A  15   O6   71.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1640  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  MG A1641  MG                                                      
REMARK 620 2   G A1415   O6   71.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1641  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1416   N7                                                     
REMARK 620 2   G A1416   O6   71.4                                              
REMARK 620 3   G A1417   O6   83.9  96.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1642  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 416   O6                                                     
REMARK 620 2  MG A1643  MG   116.8                                              
REMARK 620 3   U A 427   O4   54.6  81.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1644  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 785   O6                                                     
REMARK 620 2   G A 786   O6   85.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1646  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 592   O6                                                     
REMARK 620 2   G A 593   O6   69.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1648  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 937   N1                                                     
REMARK 620 2 ALA G   2   N   120.5                                              
REMARK 620 3   A A1377   N3  129.0  94.7                                        
REMARK 620 4   A A1377   O2'  99.5 113.8  97.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1650  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A 116   OP2                                                    
REMARK 620 2   G A 289   OP2  63.3                                              
REMARK 620 3   G A 289   O4' 154.1  99.1                                        
REMARK 620 4   G A 117   O6  150.4 143.8  53.3                                  
REMARK 620 5   G A 115   O2'  60.6 109.7 114.2 103.7                            
REMARK 620 6   G A 117   N7   89.5 116.8 116.0  68.1 101.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1655  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A  48   OP2                                                    
REMARK 620 2   G A 115   OP1  72.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1656  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A 357   O6                                                     
REMARK 620 2   C A 352   O2   71.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 215  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D  89   OG1                                                    
REMARK 620 2 GLY D  87   O    99.5                                              
REMARK 620 3 LYS D  85   O   163.2  88.2                                        
REMARK 620 4 SER D  83   O   100.6 159.4  71.2                                  
REMARK 620 5 ALA D  82   O    81.9 109.6  81.5  68.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 306  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  26   SG                                                     
REMARK 620 2 CYS D   9   SG  152.4                                              
REMARK 620 3 CYS D  31   SG   73.0 123.9                                        
REMARK 620 4 CYS D  12   SG   90.1 110.6  88.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 422  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS J  57   NZ                                                     
REMARK 620 2   C A 972   OP1  95.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 449  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG J  60   NH2                                                    
REMARK 620 2   G A 973   OP1 129.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 307  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  27   SG                                                     
REMARK 620 2 CYS N  43   SG  145.1                                              
REMARK 620 3 CYS N  24   SG   73.6  86.0                                        
REMARK 620 4 CYS N  40   SG   73.3  75.5  79.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAR A 1545                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1546                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1547                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1548                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1549                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1550                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1551                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1552                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1553                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1555                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1556                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1557                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1558                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1559                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1561                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1562                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1563                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 71                   
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1565                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1566                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1567                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1568                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 210                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 86                   
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1570                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1571                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1573                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1574                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1575                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1576                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1577                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1578                 
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1579                 
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1580                 
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1581                 
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1582                 
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1583                 
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1585                 
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1586                 
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1587                 
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1588                 
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1589                 
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1590                 
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1591                 
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1592                 
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1593                 
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1594                 
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1596                 
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1597                 
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1598                 
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1599                 
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 210                  
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 211                  
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 214                  
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 215                  
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1601                 
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1602                 
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1603                 
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1604                 
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1605                 
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1606                 
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1607                 
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1608                 
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1609                 
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1613                 
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1614                 
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1615                 
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1616                 
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1617                 
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1618                 
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1619                 
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1620                 
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1621                 
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1622                 
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1623                 
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1624                 
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1625                 
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1626                 
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1629                 
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1630                 
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1631                 
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1632                 
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 422                  
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1633                 
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1634                 
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1635                 
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1637                 
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1638                 
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1640                 
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1641                 
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1642                 
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1643                 
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1644                 
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 441                  
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1645                 
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1646                 
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1647                 
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1648                 
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1649                 
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1650                 
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 449                  
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1652                 
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1653                 
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1654                 
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1655                 
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1656                 
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1657                 
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 456                  
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 306                  
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 307                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FJF   RELATED DB: PDB                                   
REMARK 900 NATIVE STRUCTURE OF THE 30S PARTICLE                                 
REMARK 900 RELATED ID: 1FJG   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 30S PARTICLE IN COMPLEX WITH THE                    
REMARK 900 ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN AND PAROMOMYCIN              
REMARK 900 RELATED ID: 1IBK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 30S PARTICLE IN COMPLEX WITH P-SITE                 
REMARK 900 MESSENGER RNA FRAGMENT AND WITH THE ANTIBIOTIC PAROMOMYCIN           
REMARK 900 RELATED ID: 1IBM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE 30S PARTICLE IN COMPLEX WITH MESSENGER RNA          
REMARK 900 FRAGMENT AND COGNATE TRANSFER RNA ANTICODON STEM-LOOP BOUND          
REMARK 900 TO THE A SITE                                                        
DBREF  1IBL A    0  1544  GB     155076   M26924         646   2167             
DBREF  1IBL B    1   256  EMBL   13446664 CAC35061         1    256             
DBREF  1IBL C    1   239  EMBL   13446666 CAC35062         1    239             
DBREF  1IBL D    1   209  UNP    P80373   RS4_THETH        1    209             
DBREF  1IBL E    1   162  UNP    P27152   RS5_THETH        1    162             
DBREF  1IBL F    1   101  UNP    P23370   RS6_THETH        1    101             
DBREF  1IBL G    1   156  UNP    P17291   RS7_THETH        1    156             
DBREF  1IBL H    1   138  UNP    P24319   RS8_THETH        1    138             
DBREF  1IBL I    1   128  EMBL   13446668 CAC35063         1    128             
DBREF  1IBL J    1   105  UNP    P80375   RS10_THETH       1    105             
DBREF  1IBL K    1   129  GB     4519421  BAA75547         1    129             
DBREF  1IBL L    1   135  UNP    P17293   RS12_THETH       1    135             
DBREF  1IBL M    1   126  GB     4519420  BAA75546         1    126             
DBREF  1IBL N    1    61  UNP    P24320   RS14_THETH       1     61             
DBREF  1IBL O    1    89  UNP    P80378   RS15_THETH       1     89             
DBREF  1IBL P    1    88  GB     12056104 CAC21226         1     88             
DBREF  1IBL Q    1   105  EMBL   673503   CAA85419         1    105             
DBREF  1IBL R    1    88  GB     6739549  AAF27297         1     88             
DBREF  1IBL S    1    93  UNP    P80381   RS19_THETH       1     93             
DBREF  1IBL T    1   106  GB     11125386 CAC15067         1    106             
DBREF  1IBL V    2    27  UNP    P32193   RSHX_THETH       1     26             
DBREF  1IBL X    1     6  PDB    1IBL     1IBL             1      6             
DBREF  1IBL Y   28    42  PDB    1IBL     1IBL            28     42             
DBREF  1IBL Z    1     4  PDB    1IBL     1IBL             1      4             
SEQADV 1IBL     P       GB   12056104  PHE    18 CONFLICT/DELETION              
SEQADV 1IBL     P       GB   12056104  HIS    19 CONFLICT/DELETION              
SEQADV 1IBL     P       GB   12056104  TYR    20 CONFLICT/DELETION              
SEQRES   1 A 1522    U   U   U   G   U   U   G   G   A   G   A   G   U          
SEQRES   2 A 1522    U   U   G   A   U   C   C   U   G   G   C   U   C          
SEQRES   3 A 1522    A   G   G   G   U   G   A   A   C   G   C   U   G          
SEQRES   4 A 1522    G   C   G   G   C   G   U   G   C   C   U   A   A          
SEQRES   5 A 1522    G   A   C   A   U   G   C   A   A   G   U   C   G          
SEQRES   6 A 1522    U   G   C   G   G   G   C   C   G   C   G   G   G          
SEQRES   7 A 1522    G   U   U   U   U   A   C   U   C   C   G   U   G          
SEQRES   8 A 1522    G   U   C   A   G   C   G   G   C   G   G   A   C          
SEQRES   9 A 1522    G   G   G   U   G   A   G   U   A   A   C   G   C          
SEQRES  10 A 1522    G   U   G   G   G   U   G   A   C   C   U   A   C          
SEQRES  11 A 1522    C   C   G   G   A   A   G   A   G   G   G   G   G          
SEQRES  12 A 1522    A   C   A   A   C   C   C   G   G   G   G   A   A          
SEQRES  13 A 1522    A   C   U   C   G   G   G   C   U   A   A   U   C          
SEQRES  14 A 1522    C   C   C   C   A   U   G   U   G   G   A   C   C          
SEQRES  15 A 1522    C   G   C   C   C   C   U   U   G   G   G   G   U          
SEQRES  16 A 1522    G   U   G   U   C   C   A   A   A   G   G   G   C          
SEQRES  17 A 1522    U   U   U   G   C   C   C   G   C   U   U   C   C          
SEQRES  18 A 1522    G   G   A   U   G   G   G   C   C   C   G   C   G          
SEQRES  19 A 1522    U   C   C   C   A   U   C   A   G   C   U   A   G          
SEQRES  20 A 1522    U   U   G   G   U   G   G   G   G   U   A   A   U          
SEQRES  21 A 1522    G   G   C   C   C   A   C   C   A   A   G   G   C          
SEQRES  22 A 1522    G   A   C   G   A   C   G   G   G   U   A   G   C          
SEQRES  23 A 1522    C   G   G   U   C   U   G   A   G   A   G   G   A          
SEQRES  24 A 1522    U   G   G   C   C   G   G   C   C   A   C   A   G          
SEQRES  25 A 1522    G   G   G   C   A   C   U   G   A   G   A   C   A          
SEQRES  26 A 1522    C   G   G   G   C   C   C   C   A   C   U   C   C          
SEQRES  27 A 1522    U   A   C   G   G   G   A   G   G   C   A   G   C          
SEQRES  28 A 1522    A   G   U   U   A   G   G   A   A   U   C   U   U          
SEQRES  29 A 1522    C   C   G   C   A   A   U   G   G   G   C   G   C          
SEQRES  30 A 1522    A   A   G   C   C   U   G   A   C   G   G   A   G          
SEQRES  31 A 1522    C   G   A   C   G   C   C   G   C   U   U   G   G          
SEQRES  32 A 1522    A   G   G   A   A   G   A   A   G   C   C   C   U          
SEQRES  33 A 1522    U   C   G   G   G   G   U   G   U   A   A   A   C          
SEQRES  34 A 1522    U   C   C   U   G   A   A   C   C   C   G   G   G          
SEQRES  35 A 1522    A   C   G   A   A   A   C   C   C   C   C   G   A          
SEQRES  36 A 1522    C   G   A   G   G   G   G   A   C   U   G   A   C          
SEQRES  37 A 1522    G   G   U   A   C   C   G   G   G   G   U   A   A          
SEQRES  38 A 1522    U   A   G   C   G   C   C   G   G   C   C   A   A          
SEQRES  39 A 1522    C   U   C   C   G   U   G   C   C   A   G   C   A          
SEQRES  40 A 1522    G   C   C   G   C   G   G   U   A   A   U   A   C          
SEQRES  41 A 1522    G   G   A   G   G   G   C   G   C   G   A   G   C          
SEQRES  42 A 1522    G   U   U   A   C   C   C   G   G   A   U   U   C          
SEQRES  43 A 1522    A   C   U   G   G   G   C   G   U   A   A   A   G          
SEQRES  44 A 1522    G   G   C   G   U   G   U   A   G   G   C   G   G          
SEQRES  45 A 1522    C   C   U   G   G   G   G   C   G   U   C   C   C          
SEQRES  46 A 1522    A   U   G   U   G   A   A   A   G   A   C   C   A          
SEQRES  47 A 1522    C   G   G   C   U   C   A   A   C   C   G   U   G          
SEQRES  48 A 1522    G   G   G   G   A   G   C   G   U   G   G   G   A          
SEQRES  49 A 1522    U   A   C   G   C   U   C   A   G   G   C   U   A          
SEQRES  50 A 1522    G   A   C   G   G   U   G   G   G   A   G   A   G          
SEQRES  51 A 1522    G   G   U   G   G   U   G   G   A   A   U   U   C          
SEQRES  52 A 1522    C   C   G   G   A   G   U   A   G   C   G   G   U          
SEQRES  53 A 1522    G   A   A   A   U   G   C   G   C   A   G   A   U          
SEQRES  54 A 1522    A   C   C   G   G   G   A   G   G   A   A   C   G          
SEQRES  55 A 1522    C   C   G   A   U   G   G   C   G   A   A   G   G          
SEQRES  56 A 1522    C   A   G   C   C   A   C   C   U   G   G   U   C          
SEQRES  57 A 1522    C   A   C   C   C   G   U   G   A   C   G   C   U          
SEQRES  58 A 1522    G   A   G   G   C   G   C   G   A   A   A   G   C          
SEQRES  59 A 1522    G   U   G   G   G   G   A   G   C   A   A   A   C          
SEQRES  60 A 1522    C   G   G   A   U   U   A   G   A   U   A   C   C          
SEQRES  61 A 1522    C   G   G   G   U   A   G   U   C   C   A   C   G          
SEQRES  62 A 1522    C   C   C   U   A   A   A   C   G   A   U   G   C          
SEQRES  63 A 1522    G   C   G   C   U   A   G   G   U   C   U   C   U          
SEQRES  64 A 1522    G   G   G   U   C   U   C   C   U   G   G   G   G          
SEQRES  65 A 1522    G   C   C   G   A   A   G   C   U   A   A   C   G          
SEQRES  66 A 1522    C   G   U   U   A   A   G   C   G   C   G   C   C          
SEQRES  67 A 1522    G   C   C   U   G   G   G   G   A   G   U   A   C          
SEQRES  68 A 1522    G   G   C   C   G   C   A   A   G   G   C   U   G          
SEQRES  69 A 1522    A   A   A   C   U   C   A   A   A   G   G   A   A          
SEQRES  70 A 1522    U   U   G   A   C   G   G   G   G   G   C   C   C          
SEQRES  71 A 1522    G   C   A   C   A   A   G   C   G   G   U   G   G          
SEQRES  72 A 1522    A   G   C   A   U   G   U   G   G   U   U   U   A          
SEQRES  73 A 1522    A   U   U   C   G   A   A   G   C   A   A   C   G          
SEQRES  74 A 1522    C   G   A   A   G   A   A   C   C   U   U   A   C          
SEQRES  75 A 1522    C   A   G   G   C   C   U   U   G   A   C   A   U          
SEQRES  76 A 1522    G   C   U   A   G   G   G   A   A   C   C   C   G          
SEQRES  77 A 1522    G   G   U   G   A   A   A   G   C   C   U   G   G          
SEQRES  78 A 1522    G   G   U   G   C   C   C   C   G   C   G   A   G          
SEQRES  79 A 1522    G   G   G   A   G   C   C   C   U   A   G   C   A          
SEQRES  80 A 1522    C   A   G   G   U   G   C   U   G   C   A   U   G          
SEQRES  81 A 1522    G   C   C   G   U   C   G   U   C   A   G   C   U          
SEQRES  82 A 1522    C   G   U   G   C   C   G   U   G   A   G   G   U          
SEQRES  83 A 1522    G   U   U   G   G   G   U   U   A   A   G   U   C          
SEQRES  84 A 1522    C   C   G   C   A   A   C   G   A   G   C   G   C          
SEQRES  85 A 1522    A   A   C   C   C   C   C   G   C   C   G   U   U          
SEQRES  86 A 1522    A   G   U   U   G   C   C   A   G   C   G   G   U          
SEQRES  87 A 1522    U   C   G   G   C   C   G   G   G   C   A   C   U          
SEQRES  88 A 1522    C   U   A   A   C   G   G   G   A   C   U   G   C          
SEQRES  89 A 1522    C   C   G   C   G   A   A   A   G   C   G   G   G          
SEQRES  90 A 1522    A   G   G   A   A   G   G   A   G   G   G   G   A          
SEQRES  91 A 1522    C   G   A   C   G   U   C   U   G   G   U   C   A          
SEQRES  92 A 1522    G   C   A   U   G   G   C   C   C   U   U   A   C          
SEQRES  93 A 1522    G   G   C   C   U   G   G   G   C   G   A   C   A          
SEQRES  94 A 1522    C   A   C   G   U   G   C   U   A   C   A   A   U          
SEQRES  95 A 1522    G   C   C   C   A   C   U   A   C   A   A   A   G          
SEQRES  96 A 1522    C   G   A   U   G   C   C   A   C   C   C   G   G          
SEQRES  97 A 1522    C   A   A   C   G   G   G   G   A   G   C   U   A          
SEQRES  98 A 1522    A   U   C   G   C   A   A   A   A   A   G   G   U          
SEQRES  99 A 1522    G   G   G   C   C   C   A   G   U   U   C   G   G          
SEQRES 100 A 1522    A   U   U   G   G   G   G   U   C   U   G   C   A          
SEQRES 101 A 1522    A   C   C   C   G   A   C   C   C   C   A   U   G          
SEQRES 102 A 1522    A   A   G   C   C   G   G   A   A   U   C   G   C          
SEQRES 103 A 1522    U   A   G   U   A   A   U   C   G   C   G   G   A          
SEQRES 104 A 1522    U   C   A   G   C   C   A   U   G   C   C   G   C          
SEQRES 105 A 1522    G   G   U   G   A   A   U   A   C   G   U   U   C          
SEQRES 106 A 1522    C   C   G   G   G   C   C   U   U   G   U   A   C          
SEQRES 107 A 1522    A   C   A   C   C   G   C   C   C   G   U   C   A          
SEQRES 108 A 1522    C   G   C   C   A   U   G   G   G   A   G   C   G          
SEQRES 109 A 1522    G   G   C   U   C   U   A   C   C   C   G   A   A          
SEQRES 110 A 1522    G   U   C   G   C   C   G   G   G   A   G   C   C          
SEQRES 111 A 1522    U   A   C   G   G   G   C   A   G   G   C   G   C          
SEQRES 112 A 1522    C   G   A   G   G   G   U   A   G   G   G   C   C          
SEQRES 113 A 1522    C   G   U   G   A   C   U   G   G   G   G   C   G          
SEQRES 114 A 1522    A   A   G   U   C   G   U   A   A   C   A   A   G          
SEQRES 115 A 1522    G   U   A   G   C   U   G   U   A   C   C   G   G          
SEQRES 116 A 1522    A   A   G   G   U   G   C   G   G   C   U   G   G          
SEQRES 117 A 1522    A   U   C   A   C   C   U   C   C   U   U   U   C          
SEQRES 118 A 1522    U                                                          
SEQRES   1 X    6    C   U   U   U   C   U                                      
SEQRES   1 Y   15    G   G   G   A   U   U   G   A   A   A   A   U   C          
SEQRES   2 Y   15    C   C                                                      
SEQRES   1 Z    4    U   U   U   U                                              
SEQRES   1 B  256  MET PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA          
SEQRES   2 B  256  GLY VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO          
SEQRES   3 B  256  LYS PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE          
SEQRES   4 B  256  HIS ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU          
SEQRES   5 B  256  ARG THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY          
SEQRES   6 B  256  GLY THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN          
SEQRES   7 B  256  ASP ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO          
SEQRES   8 B  256  TYR VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN          
SEQRES   9 B  256  PHE LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU          
SEQRES  10 B  256  LEU GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG          
SEQRES  11 B  256  PRO LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU          
SEQRES  12 B  256  ARG LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS          
SEQRES  13 B  256  ARG LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS          
SEQRES  14 B  256  GLU ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE          
SEQRES  15 B  256  PRO VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP          
SEQRES  16 B  256  LEU VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE          
SEQRES  17 B  256  ARG SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU          
SEQRES  18 B  256  ILE ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO          
SEQRES  19 B  256  SER TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR          
SEQRES  20 B  256  PRO GLU GLY GLU SER GLU VAL GLU ALA                          
SEQRES   1 C  239  MET GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY          
SEQRES   2 C  239  ILE THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS          
SEQRES   3 C  239  LYS GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE          
SEQRES   4 C  239  ARG GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU          
SEQRES   5 C  239  ALA ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA          
SEQRES   6 C  239  VAL THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY          
SEQRES   7 C  239  ARG GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU          
SEQRES   8 C  239  ALA LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN          
SEQRES   9 C  239  GLU VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA          
SEQRES  10 C  239  GLN ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL          
SEQRES  11 C  239  ARG ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU          
SEQRES  12 C  239  SER GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG          
SEQRES  13 C  239  ILE GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA          
SEQRES  14 C  239  GLN GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE          
SEQRES  15 C  239  ASP TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL          
SEQRES  16 C  239  LEU GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE          
SEQRES  17 C  239  GLY GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS          
SEQRES  18 C  239  ALA GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG          
SEQRES  19 C  239  VAL LYS LYS GLU GLU                                          
SEQRES   1 D  209  MET GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG          
SEQRES   2 D  209  ARG GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS          
SEQRES   3 D  209  TYR SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO          
SEQRES   4 D  209  PRO GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER          
SEQRES   5 D  209  ASP TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG          
SEQRES   6 D  209  ARG ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU          
SEQRES   7 D  209  PHE GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER          
SEQRES   8 D  209  VAL PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL          
SEQRES   9 D  209  VAL TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA          
SEQRES  10 D  209  ARG GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY          
SEQRES  11 D  209  ARG ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY          
SEQRES  12 D  209  ASP GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU          
SEQRES  13 D  209  LEU ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS          
SEQRES  14 D  209  VAL GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS          
SEQRES  15 D  209  GLY LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA          
SEQRES  16 D  209  LEU PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER          
SEQRES  17 D  209  ARG                                                          
SEQRES   1 E  162  MET PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE          
SEQRES   2 E  162  ARG ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE          
SEQRES   3 E  162  ARG PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY          
SEQRES   4 E  162  ARG VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO          
SEQRES   5 E  162  LEU ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN          
SEQRES   6 E  162  MET VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS          
SEQRES   7 E  162  GLU ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU          
SEQRES   8 E  162  LYS PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA          
SEQRES   9 E  162  VAL PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP          
SEQRES  10 E  162  ILE LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN          
SEQRES  11 E  162  ILE ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG          
SEQRES  12 E  162  THR LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA          
SEQRES  13 E  162  HIS 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  156  MET ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN          
SEQRES   2 G  156  PRO ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE          
SEQRES   3 G  156  ILE ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA          
SEQRES   4 G  156  ALA ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU          
SEQRES   5 G  156  LYS THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA          
SEQRES   6 G  156  VAL GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG          
SEQRES   7 G  156  ARG VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL          
SEQRES   8 G  156  SER PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU          
SEQRES   9 G  156  VAL GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA          
SEQRES  10 G  156  VAL ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY          
SEQRES  11 G  156  LYS GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG          
SEQRES  12 G  156  MET 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 ASP VAL          
SEQRES   3 H  138  PRO ALA SER ARG PHE LYS GLU GLU ILE LEU ARG ILE LEU          
SEQRES   4 H  138  ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL ASP          
SEQRES   5 H  138  VAL ASP GLY LYS PRO TYR LEU ARG VAL TYR 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 HIS HIS ILE ARG ARG ILE SER LYS 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 SER 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  105  MET PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS          
SEQRES   2 J  105  LYS THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA          
SEQRES   3 J  105  ALA ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO          
SEQRES   4 J  105  LEU PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY          
SEQRES   5 J  105  PRO PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU          
SEQRES   6 J  105  ARG THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN          
SEQRES   7 J  105  ARG LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO          
SEQRES   8 J  105  THR GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY          
SEQRES   9 J  105  ARG                                                          
SEQRES   1 K  129  MET ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN          
SEQRES   2 K  129  VAL ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN          
SEQRES   3 K  129  ASN THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO          
SEQRES   4 K  129  ILE THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY          
SEQRES   5 K  129  SER ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA          
SEQRES   6 K  129  LEU ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN          
SEQRES   7 K  129  SER VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG          
SEQRES   8 K  129  GLU GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN          
SEQRES   9 K  129  VAL LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN          
SEQRES  10 K  129  GLY CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER              
SEQRES   1 L  135  MET VAL ALA LEU PRO THR ILE ASN GLN LEU VAL ARG LYS          
SEQRES   2 L  135  GLY ARG GLU LYS VAL ARG LYS LYS SER LYS VAL PRO ALA          
SEQRES   3 L  135  LEU LYS GLY ALA PRO PHE ARG ARG GLY VAL CYS THR VAL          
SEQRES   4 L  135  VAL ARG THR VAL THR PRO LYS LYS PRO ASN SER ALA LEU          
SEQRES   5 L  135  ARG LYS VAL ALA LYS VAL ARG LEU THR SER GLY TYR GLU          
SEQRES   6 L  135  VAL THR ALA TYR ILE PRO GLY GLU GLY HIS ASN LEU GLN          
SEQRES   7 L  135  GLU HIS SER VAL VAL LEU ILE ARG GLY GLY ARG VAL LYS          
SEQRES   8 L  135  ASP LEU PRO GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL          
SEQRES   9 L  135  TYR ASP ALA ALA GLY VAL LYS ASP ARG LYS LYS SER ARG          
SEQRES  10 L  135  SER LYS TYR GLY THR LYS LYS PRO LYS GLU ALA ALA LYS          
SEQRES  11 L  135  THR ALA ALA LYS LYS                                          
SEQRES   1 M  126  MET ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS          
SEQRES   2 M  126  ARG VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY          
SEQRES   3 M  126  LYS ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE          
SEQRES   4 M  126  ASN PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU          
SEQRES   5 M  126  VAL VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS          
SEQRES   6 M  126  LEU GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE          
SEQRES   7 M  126  LYS ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG          
SEQRES   8 M  126  HIS ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG          
SEQRES   9 M  126  THR ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL          
SEQRES  10 M  126  ALA GLY LYS LYS LYS ALA PRO ARG LYS                          
SEQRES   1 N   61  MET ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR          
SEQRES   2 N   61  PRO LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG          
SEQRES   3 N   61  CYS GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU          
SEQRES   4 N   61  CYS ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN          
SEQRES   5 N   61  LEU PRO GLY VAL ARG LYS ALA SER TRP                          
SEQRES   1 O   89  MET PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN          
SEQRES   2 O   89  GLU PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU          
SEQRES   3 O   89  VAL GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU          
SEQRES   4 O   89  SER GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER          
SEQRES   5 O   89  HIS ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG          
SEQRES   6 O   89  LEU LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR          
SEQRES   7 O   89  ARG 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  105  MET PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP          
SEQRES   2 Q  105  LYS MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN          
SEQRES   3 Q  105  PHE PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER          
SEQRES   4 Q  105  LYS LYS TYR LEU ALA HIS ASP PRO GLU GLU LYS TYR LYS          
SEQRES   5 Q  105  LEU GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE          
SEQRES   6 Q  105  SER LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU          
SEQRES   7 Q  105  SER GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG          
SEQRES   8 Q  105  ARG GLN ASN TYR GLN SER LEU SER LYS ARG GLY GLY LYS          
SEQRES   9 Q  105  ALA                                                          
SEQRES   1 R   88  MET SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN          
SEQRES   2 R   88  ARG ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU          
SEQRES   3 R   88  GLY GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL          
SEQRES   4 R   88  LEU LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO          
SEQRES   5 R   88  ARG ARG ARG THR GLY LEU SER GLY LYS GLU GLN ARG ILE          
SEQRES   6 R   88  LEU ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU          
SEQRES   7 R   88  LEU PRO PHE THR GLU LYS LEU VAL ARG LYS                      
SEQRES   1 S   93  MET PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP          
SEQRES   2 S   93  HIS LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY          
SEQRES   3 S   93  GLU LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR          
SEQRES   4 S   93  ILE VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR          
SEQRES   5 S   93  ASN GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN          
SEQRES   6 S   93  MET VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG          
SEQRES   7 S   93  THR TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS          
SEQRES   8 S   93  LYS LYS                                                      
SEQRES   1 T  106  MET ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU          
SEQRES   2 T  106  LYS ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN          
SEQRES   3 T  106  LYS ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS          
SEQRES   4 T  106  ALA ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA          
SEQRES   5 T  106  LEU LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS          
SEQRES   6 T  106  ALA ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA          
SEQRES   7 T  106  ARG ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU          
SEQRES   8 T  106  LEU GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU          
SEQRES   9 T  106  SER ALA                                                      
SEQRES   1 V   26  GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP          
SEQRES   2 V   26  ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS LYS          
HET    PAR  A1545      42                                                       
HET     MG  A1546       1                                                       
HET     MG  A1547       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  A  71       1                                                       
HET     MG  A1565       1                                                       
HET     MG  A1566       1                                                       
HET     MG  A1567       1                                                       
HET     MG  A1568       1                                                       
HET     MG  A1569       1                                                       
HET     MG  D 210       1                                                       
HET     MG  A  86       1                                                       
HET     MG  A  87       1                                                       
HET     MG  A1570       1                                                       
HET     MG  A1571       1                                                       
HET     MG  A1572       1                                                       
HET     MG  A1573       1                                                       
HET     MG  A1574       1                                                       
HET     MG  A1575       1                                                       
HET     MG  A1576       1                                                       
HET     MG  A1577       1                                                       
HET     MG  A1578       1                                                       
HET     MG  A1579       1                                                       
HET     MG  A1580       1                                                       
HET     MG  A1581       1                                                       
HET     MG  A1582       1                                                       
HET     MG  A1583       1                                                       
HET     MG  A1584       1                                                       
HET     MG  A1585       1                                                       
HET     MG  A1586       1                                                       
HET     MG  A1587       1                                                       
HET     MG  A1588       1                                                       
HET     MG  A1589       1                                                       
HET     MG  A1590       1                                                       
HET     MG  A1591       1                                                       
HET     MG  A1592       1                                                       
HET     MG  A1593       1                                                       
HET     MG  A1594       1                                                       
HET     MG  A1595       1                                                       
HET     MG  A1596       1                                                       
HET     MG  A1597       1                                                       
HET     MG  A1598       1                                                       
HET     MG  A1599       1                                                       
HET     MG  A 210       1                                                       
HET     MG  A 211       1                                                       
HET     MG  A 213       1                                                       
HET     MG  A 214       1                                                       
HET     MG  D 215       1                                                       
HET     MG  A1600       1                                                       
HET     MG  A1601       1                                                       
HET     MG  A1602       1                                                       
HET     MG  A1603       1                                                       
HET     MG  A1604       1                                                       
HET     MG  A1605       1                                                       
HET     MG  A1606       1                                                       
HET     MG  A1607       1                                                       
HET     MG  A1608       1                                                       
HET     MG  A1609       1                                                       
HET     MG  A1610       1                                                       
HET     MG  A1611       1                                                       
HET     MG  A1612       1                                                       
HET     MG  A1613       1                                                       
HET     MG  A1614       1                                                       
HET     MG  A1615       1                                                       
HET     MG  A1616       1                                                       
HET     MG  A1617       1                                                       
HET     MG  A1618       1                                                       
HET     MG  A1619       1                                                       
HET     MG  A1620       1                                                       
HET     MG  A1621       1                                                       
HET     MG  A1622       1                                                       
HET     MG  A1623       1                                                       
HET     MG  A1624       1                                                       
HET     MG  A1625       1                                                       
HET     MG  A1626       1                                                       
HET     MG  A1627       1                                                       
HET     MG  A1628       1                                                       
HET     MG  A1629       1                                                       
HET     MG  A1630       1                                                       
HET     MG  A1631       1                                                       
HET     MG  A1632       1                                                       
HET     MG  J 422       1                                                       
HET     MG  A1633       1                                                       
HET     MG  A1634       1                                                       
HET     MG  A1635       1                                                       
HET     MG  A1636       1                                                       
HET     MG  A1637       1                                                       
HET     MG  A1638       1                                                       
HET     MG  A1639       1                                                       
HET     MG  A1640       1                                                       
HET     MG  A1641       1                                                       
HET     MG  A1642       1                                                       
HET     MG  A1643       1                                                       
HET     MG  A1644       1                                                       
HET     MG  A 441       1                                                       
HET     MG  A1645       1                                                       
HET     MG  A1646       1                                                       
HET     MG  A1647       1                                                       
HET     MG  A1648       1                                                       
HET     MG  A1649       1                                                       
HET     MG  A1650       1                                                       
HET     MG  A1651       1                                                       
HET     MG  J 449       1                                                       
HET     MG  A1652       1                                                       
HET     MG  A1653       1                                                       
HET     MG  A1654       1                                                       
HET     MG  A1655       1                                                       
HET     MG  A1656       1                                                       
HET     MG  A1657       1                                                       
HET     MG  Y 456       1                                                       
HET     ZN  D 306       1                                                       
HET     ZN  N 307       1                                                       
HETNAM     PAR PAROMOMYCIN                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETSYN     PAR PAROMOMYCIN I, AMMINOSIDIN, CATENULIN, CRESTOMYCIN,              
HETSYN   2 PAR  MONOMYCIN A, NEOMYCIN E                                         
FORMUL  25  PAR    C23 H45 N5 O14                                               
FORMUL  26   MG    125(MG 2+)                                                   
FORMUL  15   ZN    2(ZN 2+)                                                     
HELIX    1   1 ASN B   25  TYR B   31  5                                   7    
HELIX    2   2 ASP B   43  GLY B   65  1                                  23    
HELIX    3   3 LYS B   74  GLN B   76  5                                   3    
HELIX    4   4 ALA B   77  ALA B   88  1                                  12    
HELIX    5   5 ASN B  104  PHE B  122  1                                  19    
HELIX    6   6 PRO B  131  LEU B  149  1                                  19    
HELIX    7   7 GLU B  170  LEU B  180  1                                  11    
HELIX    8   8 ASP B  193  VAL B  197  5                                   5    
HELIX    9   9 ALA B  207  GLN B  224  1                                  18    
HELIX   10  10 SER B  235  GLN B  240  1                                   6    
HELIX   11  11 ILE C    8  LEU C   12  5                                   5    
HELIX   12  12 GLN C   28  GLU C   44  1                                  17    
HELIX   13  13 LYS C   72  GLY C   78  1                                   7    
HELIX   14  14 GLU C   82  ALA C   92  1                                  11    
HELIX   15  15 ASN C  108  LEU C  111  5                                   4    
HELIX   16  16 SER C  112  ARG C  127  1                                  16    
HELIX   17  17 ALA C  129  SER C  144  1                                  16    
HELIX   18  18 ARG C  156  ALA C  160  5                                   5    
HELIX   19  19 ARG D   10  GLY D   16  1                                   7    
HELIX   20  20 GLY D   23  SER D   28  5                                   6    
HELIX   21  21 CYS D   31  ARG D   35  5                                   5    
HELIX   22  22 SER D   52  TYR D   68  1                                  17    
HELIX   23  23 SER D   71  LYS D   85  1                                  15    
HELIX   24  24 VAL D   88  SER D   99  1                                  12    
HELIX   25  25 ARG D  100  LEU D  108  1                                   9    
HELIX   26  26 SER D  113  HIS D  123  1                                  11    
HELIX   27  27 GLU D  150  ASN D  154  5                                   5    
HELIX   28  28 LEU D  155  MET D  165  1                                  11    
HELIX   29  29 ASN D  199  TYR D  207  1                                   9    
HELIX   30  30 GLU E   50  ARG E   64  1                                  15    
HELIX   31  31 GLY E  103  ALA E  113  1                                  11    
HELIX   32  32 ASN E  127  LEU E  142  1                                  16    
HELIX   33  33 THR E  144  LYS E  153  1                                  10    
HELIX   34  34 ASP F   15  TYR F   33  1                                  19    
HELIX   35  35 PRO F   68  ASP F   70  5                                   3    
HELIX   36  36 ARG F   71  ARG F   80  1                                  10    
HELIX   37  37 ASP G   20  MET G   31  1                                  12    
HELIX   38  38 LYS G   35  GLN G   51  1                                  17    
HELIX   39  39 GLU G   57  LYS G   70  1                                  14    
HELIX   40  40 SER G   92  ASN G  109  1                                  18    
HELIX   41  41 ARG G  115  GLY G  130  1                                  16    
HELIX   42  42 LYS G  131  ALA G  145  1                                  15    
HELIX   43  43 ASN G  148  HIS G  153  5                                   6    
HELIX   44  44 ASP H    4  VAL H   19  1                                  16    
HELIX   45  45 SER H   29  GLU H   42  1                                  14    
HELIX   46  46 ARG H  102  LEU H  107  5                                   6    
HELIX   47  47 ASP H  121  LEU H  127  1                                   7    
HELIX   48  48 PHE I   33  PHE I   37  1                                   5    
HELIX   49  49 LEU I   40  ALA I   46  5                                   7    
HELIX   50  50 LEU I   47  ASP I   54  1                                   8    
HELIX   51  51 GLY I   69  ASN I   89  1                                  21    
HELIX   52  52 TYR I   92  LYS I   97  1                                   6    
HELIX   53  53 ASP J   12  GLY J   31  1                                  20    
HELIX   54  54 ARG J   79  THR J   87  1                                   9    
HELIX   55  55 GLY K   52  THR K   57  5                                   6    
HELIX   56  56 PRO K   58  ALA K   74  1                                  17    
HELIX   57  57 GLY K   90  ALA K  100  1                                  11    
HELIX   58  58 LYS K  122  ARG K  126  5                                   5    
HELIX   59  59 THR L    6  GLY L   14  1                                   9    
HELIX   60  60 PRO L  125  ALA L  128  4                                   4    
HELIX   61  61 ARG M   14  LEU M   19  1                                   6    
HELIX   62  62 THR M   20  ILE M   22  5                                   3    
HELIX   63  63 GLY M   26  LYS M   36  1                                  11    
HELIX   64  64 THR M   49  TRP M   64  1                                  16    
HELIX   65  65 LEU M   66  LEU M   81  1                                  16    
HELIX   66  66 MET M   82  ILE M   84  5                                   3    
HELIX   67  67 CYS M   86  GLY M   95  1                                  10    
HELIX   68  68 ALA M  107  GLY M  112  1                                   6    
HELIX   69  69 PHE N   16  ALA N   20  5                                   5    
HELIX   70  70 CYS N   40  GLY N   51  1                                  12    
HELIX   71  71 THR O    4  ALA O   16  1                                  13    
HELIX   72  72 SER O   24  LEU O   43  1                                  20    
HELIX   73  73 ASP O   49  ASP O   74  1                                  26    
HELIX   74  74 ASP O   74  LEU O   85  1                                  12    
HELIX   75  75 ASP P   52  VAL P   62  1                                  11    
HELIX   76  76 THR P   67  ALA P   77  1                                  11    
HELIX   77  77 ARG Q   81  GLN Q   96  1                                  16    
HELIX   78  78 ASN R   36  LYS R   41  1                                   6    
HELIX   79  79 PRO R   52  GLY R   57  1                                   6    
HELIX   80  80 SER R   59  LEU R   76  1                                  18    
HELIX   81  81 ASP S   12  LYS S   25  1                                  14    
HELIX   82  82 VAL S   41  VAL S   45  5                                   5    
HELIX   83  83 LEU T   13  GLY T   47  1                                  35    
HELIX   84  84 LYS T   48  ALA T   67  1                                  20    
HELIX   85  85 HIS T   73  GLY T   96  1                                  24    
HELIX   86  86 THR V    8  GLY V   16  1                                   9    
SHEET    1   A 5 TYR B  92  VAL B  93  0                                        
SHEET    2   A 5 ILE B  68  VAL B  71  1  O  PHE B  70   N  VAL B  93           
SHEET    3   A 5 ALA B 161  VAL B 164  1  O  ALA B 161   N  LEU B  69           
SHEET    4   A 5 VAL B 184  ALA B 188  1  N  ILE B 185   O  ILE B 162           
SHEET    5   A 5 TYR B 199  PRO B 202  1  N  TYR B 199   O  VAL B 184           
SHEET    1   B 3 ARG C  54  ASP C  56  0                                        
SHEET    2   B 3 THR C  67  VAL C  70 -1  N  THR C  67   O  ASP C  56           
SHEET    3   B 3 VAL C 103  GLU C 105  1  O  GLN C 104   N  VAL C  70           
SHEET    1   C 4 ALA C 169  GLY C 171  0                                        
SHEET    2   C 4 GLY C 148  VAL C 153 -1  N  ALA C 149   O  GLN C 170           
SHEET    3   C 4 VAL C 198  PHE C 203 -1  N  LYS C 199   O  ILE C 152           
SHEET    4   C 4 ILE C 182  ALA C 187 -1  N  ASP C 183   O  ILE C 202           
SHEET    1   D 2 ILE D 126  VAL D 128  0                                        
SHEET    2   D 2 ILE D 146  VAL D 148 -1  O  ALA D 147   N  THR D 127           
SHEET    1   E 2 LEU D 174  ASP D 177  0                                        
SHEET    2   E 2 LYS D 182  PHE D 185 -1  O  LYS D 182   N  ASP D 177           
SHEET    1   F 4 GLU E   7  ARG E  14  0                                        
SHEET    2   F 4 PHE E  28  GLY E  35 -1  N  GLY E  29   O  ARG E  14           
SHEET    3   F 4 ARG E  40  ALA E  48 -1  O  GLY E  42   N  VAL E  34           
SHEET    4   F 4 MET E  66  GLU E  68 -1  N  VAL E  67   O  VAL E  41           
SHEET    1   G 2 MET E  19  GLN E  20  0                                        
SHEET    2   G 2 GLY E  23  ARG E  24 -1  N  GLY E  23   O  GLN E  20           
SHEET    1   H 4 ILE E  80  PHE E  84  0                                        
SHEET    2   H 4 SER E  87  PRO E  93 -1  O  SER E  87   N  PHE E  84           
SHEET    3   H 4 ILE E 118  GLY E 124 -1  N  LEU E 119   O  LYS E  92           
SHEET    4   H 4 VAL E 100  ILE E 101  1  N  ILE E 101   O  ILE E 118           
SHEET    1   I 4 VAL F  85  LYS F  92  0                                        
SHEET    2   I 4 ARG F   2  LEU F  10 -1  O  GLU F   5   N  VAL F  91           
SHEET    3   I 4 ASP F  55  PHE F  60 -1  O  TYR F  59   N  LEU F  10           
SHEET    4   I 4 GLY F  44  ILE F  52 -1  O  GLY F  44   N  PHE F  60           
SHEET    1   J 4 VAL F  85  LYS F  92  0                                        
SHEET    2   J 4 ARG F   2  LEU F  10 -1  O  GLU F   5   N  VAL F  91           
SHEET    3   J 4 TYR F  63  MET F  67 -1  O  TYR F  63   N  VAL F   6           
SHEET    4   J 4 LYS F  39  VAL F  40 -1  O  LYS F  39   N  GLN F  64           
SHEET    1   K 2 MET G  73  ARG G  76  0                                        
SHEET    2   K 2 VAL G  87  GLU G  90 -1  O  VAL G  87   N  ARG G  76           
SHEET    1   L 2 ARG G  79  VAL G  80  0                                        
SHEET    2   L 2 ALA G  83  ASN G  84 -1  O  ALA G  83   N  VAL G  80           
SHEET    1   M 3 ASP H  25  PRO H  27  0                                        
SHEET    2   M 3 LYS H  56  TYR H  62 -1  N  LEU H  59   O  VAL H  26           
SHEET    3   M 3 GLY H  47  VAL H  53 -1  O  GLY H  47   N  TYR H  62           
SHEET    1   N 4 GLY H 117  THR H 120  0                                        
SHEET    2   N 4 ILE H 109  THR H 114 -1  N  LEU H 112   O  LEU H 119           
SHEET    3   N 4 GLY H 131  TRP H 138 -1  N  GLU H 132   O  SER H 113           
SHEET    4   N 4 HIS H  82  ARG H  85 -1  O  HIS H  82   N  TRP H 138           
SHEET    1   O 4 GLY H 117  THR H 120  0                                        
SHEET    2   O 4 ILE H 109  THR H 114 -1  N  LEU H 112   O  LEU H 119           
SHEET    3   O 4 GLY H 131  TRP H 138 -1  N  GLU H 132   O  SER H 113           
SHEET    4   O 4 TYR H  94  VAL H  95 -1  N  VAL H  95   O  GLY H 131           
SHEET    1   P 5 TYR I   4  GLY I   6  0                                        
SHEET    2   P 5 VAL I  14  PRO I  21 -1  N  VAL I  17   O  GLY I   6           
SHEET    3   P 5 PHE I  59  ARG I  66 -1  N  ASP I  60   O  ARG I  20           
SHEET    4   P 5 VAL I  26  VAL I  28  1  O  THR I  27   N  ILE I  63           
SHEET    5   P 5 GLN I  31  ASP I  32 -1  O  GLN I  31   N  VAL I  28           
SHEET    1   Q 2 ARG J   5  ILE J   6  0                                        
SHEET    2   Q 2 ILE J  98  LYS J  99 -1  N  LYS J  99   O  ARG J   5           
SHEET    1   R 4 ARG J  43  THR J  48  0                                        
SHEET    2   R 4 HIS J  62  ASN J  69 -1  N  PHE J  63   O  PHE J  47           
SHEET    3   R 4 ARG J   9  GLY J  10 -1  O  GLY J  10   N  HIS J  68           
SHEET    4   R 4 VAL J  94  GLU J  95 -1  N  GLU J  95   O  ARG J   9           
SHEET    1   S 3 ARG J  43  THR J  48  0                                        
SHEET    2   S 3 HIS J  62  ASN J  69 -1  N  PHE J  63   O  PHE J  47           
SHEET    3   S 3 VAL N  56  LYS N  58 -1  O  ARG N  57   N  GLU J  64           
SHEET    1   T 5 PRO K  39  SER K  44  0                                        
SHEET    2   T 5 ILE K  29  THR K  33 -1  O  VAL K  30   N  SER K  43           
SHEET    3   T 5 SER K  16  HIS K  22 -1  O  ARG K  18   N  THR K  33           
SHEET    4   T 5 SER K  79  ARG K  85  1  O  SER K  79   N  GLY K  17           
SHEET    5   T 5 GLN K 104  ASP K 110  1  O  GLN K 104   N  VAL K  80           
SHEET    1   U 4 VAL L  83  ILE L  85  0                                        
SHEET    2   U 4 ARG L  33  VAL L  39 -1  O  ARG L  33   N  ILE L  85           
SHEET    3   U 4 ARG L  53  LEU L  60 -1  N  LYS L  57   O  VAL L  39           
SHEET    4   U 4 THR L  42  VAL L  43 -1  N  VAL L  43   O  ARG L  53           
SHEET    1   V 5 VAL L  83  ILE L  85  0                                        
SHEET    2   V 5 ARG L  33  VAL L  39 -1  O  ARG L  33   N  ILE L  85           
SHEET    3   V 5 ARG L  53  LEU L  60 -1  N  LYS L  57   O  VAL L  39           
SHEET    4   V 5 GLU L  65  TYR L  69 -1  O  VAL L  66   N  VAL L  58           
SHEET    5   V 5 TYR L  98  HIS L  99  1  O  TYR L  98   N  TYR L  69           
SHEET    1   W 5 LEU P  49  LYS P  50  0                                        
SHEET    2   W 5 GLU P  34  TYR P  39 -1  N  TYR P  38   O  LYS P  50           
SHEET    3   W 5 TYR P  17  ASP P  23 -1  O  TYR P  17   N  TYR P  39           
SHEET    4   W 5 VAL P   2  ARG P   8 -1  N  LYS P   3   O  THR P  22           
SHEET    5   W 5 GLN P  65  PRO P  66  1  N  GLN P  65   O  VAL P   2           
SHEET    1   X 6 VAL Q   5  SER Q  12  0                                        
SHEET    2   X 6 THR Q  18  PRO Q  28 -1  N  THR Q  20   O  SER Q  12           
SHEET    3   X 6 VAL Q  35  HIS Q  45 -1  N  ILE Q  36   O  PHE Q  27           
SHEET    4   X 6 LYS Q  69  GLU Q  78  1  O  PHE Q  71   N  HIS Q  45           
SHEET    5   X 6 VAL Q  56  SER Q  66 -1  O  VAL Q  56   N  VAL Q  77           
SHEET    6   X 6 VAL Q   5  SER Q  12 -1  O  LEU Q   6   N  ILE Q  59           
SHEET    1   Y 3 ILE S  31  THR S  33  0                                        
SHEET    2   Y 3 THR S  48  TYR S  52  1  O  THR S  48   N  ILE S  31           
SHEET    3   Y 3 HIS S  57  TYR S  61 -1  N  VAL S  58   O  VAL S  51           
SSBOND   1 CYS D   26    CYS D   31                          1555   1555  2.78  
SSBOND   2 CYS N   24    CYS N   27                          1555   1555  2.99  
SSBOND   3 CYS N   40    CYS N   43                          1555   1555  2.97  
LINK        MG    MG A  71                 OP2   A A 860     1555   1555  2.61  
LINK        MG    MG A  86                 OP2   G A 588     1555   1555  2.11  
LINK        MG    MG A 210                 O6    G A 604     1555   1555  2.85  
LINK        MG    MG A 210                 O4    U A 605     1555   1555  3.01  
LINK        MG    MG A 210                 O6    G A 633     1555   1555  3.06  
LINK        MG    MG A 214                 OP1   G A 548     1555   1555  3.07  
LINK        MG    MG A 214                 OP1   A A 547     1555   1555  2.44  
LINK        MG    MG A 441                 O6    G A 853     1555   1555  2.41  
LINK        MG    MG A1546                 OP1   G A 944     1555   1555  2.10  
LINK        MG    MG A1546                 OP2   G A 945     1555   1555  2.51  
LINK        MG    MG A1547                 OP1   G A1224     1555   1555  1.82  
LINK        MG    MG A1548                 O6    G A  22     1555   1555  2.57  
LINK        MG    MG A1548                 O6    G A  21     1555   1555  3.07  
LINK        MG    MG A1548                 O4    U A  12     1555   1555  2.82  
LINK        MG    MG A1551                 OP2   C A 749     1555   1555  2.15  
LINK        MG    MG A1551                 OP2   G A 750     1555   1555  1.92  
LINK        MG    MG A1551                 OP1   C A 749     1555   1555  3.07  
LINK        MG    MG A1552                 OP2   A A 766     1555   1555  2.08  
LINK        MG    MG A1553                 OP2   A A 768     1555   1555  2.29  
LINK        MG    MG A1555                 O6    G A 800     1555   1555  3.10  
LINK        MG    MG A1556                 OP1   C A 578     1555   1555  2.80  
LINK        MG    MG A1558                 O3'   A A 509     1555   1555  2.89  
LINK        MG    MG A1558                 OP2   A A 509     1555   1555  2.14  
LINK        MG    MG A1559                 OP2   U A 560     1555   1555  2.73  
LINK        MG    MG A1561                 OP1   G A  21     1555   1555  1.98  
LINK        MG    MG A1562                 OP2   C A 596     1555   1555  2.40  
LINK        MG    MG A1562                 OP2   G A 597     1555   1555  2.64  
LINK        MG    MG A1562                 O3'   G A 595     1555   1555  3.00  
LINK        MG    MG A1562                 O4    U A 598     1555   1555  2.88  
LINK        MG    MG A1563                 N7    G A 869     1555   1555  2.93  
LINK        MG    MG A1563                 N7    G A 858     1555   1555  2.95  
LINK        MG    MG A1565                 O4    U A 911     1555   1555  3.01  
LINK        MG    MG A1565                 O6    G A 886     1555   1555  2.53  
LINK        MG    MG A1565                 O6    G A 885     1555   1555  3.02  
LINK        MG    MG A1566                 OP2   A A 937     1555   1555  2.53  
LINK        MG    MG A1567                 OP1   C A 934     1555   1555  2.24  
LINK        MG    MG A1568                 O6    G A1370     1555   1555  2.26  
LINK        MG    MG A1570                 OP1   U A1199     1555   1555  2.30  
LINK        MG    MG A1570                 OP2   U A1199     1555   1555  3.05  
LINK        MG    MG A1570                 OP1   A A 964     1555   1555  2.32  
LINK        MG    MG A1571                 O3'   C A 979     1555   1555  2.07  
LINK        MG    MG A1571                 OP1   C A 980     1555   1555  2.15  
LINK        MG    MG A1573                 OP2   C A1054     1555   1555  2.61  
LINK        MG    MG A1573                 O2'   G A1053     1555   1555  2.93  
LINK        MG    MG A1573                 OP1   C A1054     1555   1555  2.24  
LINK        MG    MG A1573                 OP1   G A1197     1555   1555  3.09  
LINK        MG    MG A1573                 O3'   G A1053     1555   1555  3.13  
LINK        MG    MG A1574                 OP1   C A1054     1555   1555  2.83  
LINK        MG    MG A1574                 O3'   U A1196     1555   1555  2.20  
LINK        MG    MG A1574                 O5'   C A1054     1555   1555  2.94  
LINK        MG    MG A1574                 OP1   G A1197     1555   1555  2.32  
LINK        MG    MG A1574                 OP2   G A1198     1555   1555  2.09  
LINK        MG    MG A1575                 OP1   G A 558     1555   1555  2.21  
LINK        MG    MG A1575                 O6    G A 299     1555   1555  1.98  
LINK        MG    MG A1576                 N7    G A 324     1555   1555  2.42  
LINK        MG    MG A1577                 OP2   A A 574     1555   1555  1.99  
LINK        MG    MG A1577                 OP2   A A 573     1555   1555  2.28  
LINK        MG    MG A1577                 OP2   A A 572     1555   1555  2.41  
LINK        MG    MG A1579                 OP2   A A1110     1555   1555  1.99  
LINK        MG    MG A1580                 O6    G A1079     1555   1555  2.58  
LINK        MG    MG A1580                 OP1   C A 866     1555   1555  2.87  
LINK        MG    MG A1580                 O3'   A A 865     1555   1555  2.81  
LINK        MG    MG A1581                 OP1   G A1068     1555   1555  2.86  
LINK        MG    MG A1581                 OP1   G A1094     1555   1555  2.20  
LINK        MG    MG A1581                 O3'   A A1067     1555   1555  2.34  
LINK        MG    MG A1582                 OP2   U A1095     1555   1555  2.13  
LINK        MG    MG A1582                 O6    G A1108     1555   1555  2.39  
LINK        MG    MG A1585                 O6    G A1511     1555   1555  2.54  
LINK        MG    MG A1585                 O4    U A1512     1555   1555  2.77  
LINK        MG    MG A1585                 O6    G A1523     1555   1555  2.61  
LINK        MG    MG A1585                 O4    U A1510     1555   1555  3.04  
LINK        MG    MG A1586                 O3'   A A1499     1555   1555  2.94  
LINK        MG    MG A1586                 OP1   G A1521     1555   1555  3.02  
LINK        MG    MG A1586                 OP1   G A1508     1555   1555  2.59  
LINK        MG    MG A1586                 OP1   A A1500     1555   1555  2.64  
LINK        MG    MG A1587                 OP2   G A1505     1555   1555  2.24  
LINK        MG    MG A1587                 OP2   A A1499     1555   1555  2.38  
LINK        MG    MG A1587                 OP2   A A1500     1555   1555  1.95  
LINK        MG    MG A1588                 OP1   G A1508     1555   1555  2.07  
LINK        MG    MG A1588                 OP1   A A1500     1555   1555  2.10  
LINK        MG    MG A1588                 OP1   G A1505     1555   1555  2.30  
LINK        MG    MG A1589                 O6    G A 168     1555   1555  2.90  
LINK        MG    MG A1590                 OP2   A A 195     1555   1555  2.15  
LINK        MG    MG A1591                 OP2   G A 183     1555   1555  2.55  
LINK        MG    MG A1591                 OP1   U A 182     1555   1555  2.55  
LINK        MG    MG A1592                 OP2   G A 117     1555   1555  2.23  
LINK        MG    MG A1592                 OP2   A A 116     1555   1555  2.51  
LINK        MG    MG A1592                 OP2   G A 289     1555   1555  2.01  
LINK        MG    MG A1592                 OP1   A A 116     1555   1555  3.05  
LINK        MG    MG A1593                 OP2   C A 352     1555   1555  2.12  
LINK        MG    MG A1594                 O2    C A 372     1555   1555  2.21  
LINK        MG    MG A1594                 O4    U A 387     1555   1555  2.66  
LINK        MG    MG A1594                 O2'   C A 372     1555   1555  2.92  
LINK        MG    MG A1594                 O4    U A 375     1555   1555  2.91  
LINK        MG    MG A1594                 O6    G A 376     1555   1555  2.86  
LINK        MG    MG A1596                 OP2   A A 794     1555   1555  2.53  
LINK        MG    MG A1596                 OP1   A A 782     1555   1555  2.07  
LINK        MG    MG A1597                 O6    G A1058     1555   1555  3.09  
LINK        MG    MG A1597                 O4    U A1199     1555   1555  2.38  
LINK        MG    MG A1598                 OP2   C A1303     1555   1555  2.98  
LINK        MG    MG A1598                 OP2   G A1304     1555   1555  2.45  
LINK        MG    MG A1599                 OP2   U A 565     1555   1555  2.88  
LINK        MG    MG A1599                 OP2   G A 567     1555   1555  2.70  
LINK        MG    MG A1599                 O2'   A A 563     1555   1555  2.60  
LINK        MG    MG A1599                 OP2   C A 564     1555   1555  2.40  
LINK        MG    MG A1603                 OP1   C A 504     1555   1555  2.41  
LINK        MG    MG A1604                 N7    G A 529     1555   1555  3.05  
LINK        MG    MG A1604                 N3    C A 518     1555   1555  3.09  
LINK        MG    MG A1604                 O   PRO L  48     1555   1555  2.98  
LINK        MG    MG A1604                 O6    G A 529     1555   1555  2.78  
LINK        MG    MG A1604                 ND2 ASN L  49     1555   1555  2.66  
LINK        MG    MG A1605                 N4    C A 235     1555   1555  3.05  
LINK        MG    MG A1605                 O2    C A 121     1555   1555  2.98  
LINK        MG    MG A1605                 O6    G A 124     1555   1555  2.67  
LINK        MG    MG A1605                 N3    C A 121     1555   1555  2.67  
LINK        MG    MG A1605                 O4    U A 125     1555   1555  2.64  
LINK        MG    MG A1605                 O6    G A 126     1555   1555  3.07  
LINK        MG    MG A1605                 O6    G A 236     1555   1555  2.53  
LINK        MG    MG A1606                 OP2   C A 175     1555   1555  2.64  
LINK        MG    MG A1606                 OP1   C A 174     1555   1555  2.79  
LINK        MG    MG A1607                 OP1   A A 109     1555   1555  2.93  
LINK        MG    MG A1607                 OP2   G A 331     1555   1555  2.14  
LINK        MG    MG A1608                 O4    U A  98     1555   1555  2.45  
LINK        MG    MG A1608                 O6    G A  70     1555   1555  2.98  
LINK        MG    MG A1609                 O6    G A 105     1555   1555  2.59  
LINK        MG    MG A1609                 O6    G A  61     1555   1555  2.86  
LINK        MG    MG A1609                 O4    U A  62     1555   1555  2.56  
LINK        MG    MG A1613                 O   PRO L  48     1555   1555  3.05  
LINK        MG    MG A1613                 O2    C A 518     1555   1555  2.85  
LINK        MG    MG A1613                 N3    C A 518     1555   1555  3.09  
LINK        MG    MG A1613                 O2'   U Z   3     1555   1555  2.70  
LINK        MG    MG A1613                 O6    G A 530     1555   1555  2.74  
LINK        MG    MG A1614                 O4    U A 831     1555   1555  2.64  
LINK        MG    MG A1614                 O6    G A 855     1555   1555  2.61  
LINK        MG    MG A1614                 N4    C A 856     1555   1555  2.98  
LINK        MG    MG A1614                 O6    G A 830     1555   1555  2.29  
LINK        MG    MG A1616                 O6    G A 595     1555   1555  2.94  
LINK        MG    MG A1618                 O6    G A 887     1555   1555  3.09  
LINK        MG    MG A1620                 N7    G A1497     1555   1555  2.95  
LINK        MG    MG A1622                 O4    U A1090     1555   1555  3.05  
LINK        MG    MG A1622                 O4    U A1095     1555   1555  2.93  
LINK        MG    MG A1622                 OP2   G A1094     1555   1555  3.12  
LINK        MG    MG A1623                 O6    G A 284     1555   1555  3.11  
LINK        MG    MG A1624                 OP1   U A 182     1555   1555  2.58  
LINK        MG    MG A1624                 N7    G A 183     1555   1555  2.55  
LINK        MG    MG A1624                 O2'   G A 181     1555   1555  2.43  
LINK        MG    MG A1625                 OP2   A A1238     1555   1555  2.25  
LINK        MG    MG A1625                 O2    C A1335     1555   1555  2.96  
LINK        MG    MG A1626                 OP2   A A 608     1555   1555  2.30  
LINK        MG    MG A1629                 OP1   C A 328     1555   1555  2.49  
LINK        MG    MG A1630                 OP1   A A 315     1555   1555  2.47  
LINK        MG    MG A1632                 OP1   A A 533     1555   1555  2.11  
LINK        MG    MG A1632                 O4    U A 516     1555   1555  2.09  
LINK        MG    MG A1632                 O3'   A A 532     1555   1555  3.11  
LINK        MG    MG A1632                 OP2   A A 533     1555   1555  2.56  
LINK        MG    MG A1633                 OP1   U A1049     1555   1555  3.13  
LINK        MG    MG A1633                 O   ALA N   2     1555   1555  3.13  
LINK        MG    MG A1634                 O4    U A1052     1555   1555  2.70  
LINK        MG    MG A1634                 O2    C A1200     1555   1555  1.98  
LINK        MG    MG A1634                 O6    G A1207     1555   1555  3.11  
LINK        MG    MG A1634                 O6    G A1206     1555   1555  2.60  
LINK        MG    MG A1635                 O4    U A 921     1555   1555  2.87  
LINK        MG    MG A1635                 O4    U A1393     1555   1555  3.07  
LINK        MG    MG A1635                 O6    G A 922     1555   1555  2.57  
LINK        MG    MG A1637                 N4    C A 924     1555   1555  3.06  
LINK        MG    MG A1637                 O4    U A1390     1555   1555  2.56  
LINK        MG    MG A1637                 O6    G A 925     1555   1555  2.64  
LINK        MG    MG A1637                 O6    G A 927     1555   1555  2.68  
LINK        MG    MG A1637                 O4    U A1391     1555   1555  2.98  
LINK        MG    MG A1638                 O4    U A 920     1555   1555  2.66  
LINK        MG    MG A1638                 O6    G A  15     1555   1555  3.02  
LINK        MG    MG A1640                MG    MG A1641     1555   1555  2.98  
LINK        MG    MG A1640                 O6    G A1415     1555   1555  2.39  
LINK        MG    MG A1641                 N7    G A1416     1555   1555  2.86  
LINK        MG    MG A1641                 O6    G A1416     1555   1555  2.33  
LINK        MG    MG A1641                 O6    G A1417     1555   1555  3.14  
LINK        MG    MG A1642                 O6    G A 416     1555   1555  3.11  
LINK        MG    MG A1642                MG    MG A1643     1555   1555  3.13  
LINK        MG    MG A1642                 O4    U A 427     1555   1555  3.03  
LINK        MG    MG A1644                 O6    G A 785     1555   1555  2.66  
LINK        MG    MG A1644                 O6    G A 786     1555   1555  2.61  
LINK        MG    MG A1645                 O6    G A 838     1555   1555  2.86  
LINK        MG    MG A1646                 O6    G A 592     1555   1555  2.98  
LINK        MG    MG A1646                 O6    G A 593     1555   1555  2.64  
LINK        MG    MG A1647                 O6    G A 650     1555   1555  2.80  
LINK        MG    MG A1648                 N1    A A 937     1555   1555  2.66  
LINK        MG    MG A1648                 N   ALA G   2     1555   1555  2.80  
LINK        MG    MG A1648                 N3    A A1377     1555   1555  2.77  
LINK        MG    MG A1648                 O2'   A A1377     1555   1555  2.89  
LINK        MG    MG A1650                 OP2   A A 116     1555   1555  2.60  
LINK        MG    MG A1650                 OP2   G A 289     1555   1555  3.05  
LINK        MG    MG A1650                 O4'   G A 289     1555   1555  2.83  
LINK        MG    MG A1650                 O6    G A 117     1555   1555  2.77  
LINK        MG    MG A1650                 O2'   G A 115     1555   1555  2.10  
LINK        MG    MG A1650                 N7    G A 117     1555   1555  2.69  
LINK        MG    MG A1652                 N7    G A 362     1555   1555  3.08  
LINK        MG    MG A1654                 OP2   A A  53     1555   1555  2.18  
LINK        MG    MG A1655                 OP2   C A  48     1555   1555  2.82  
LINK        MG    MG A1655                 OP1   G A 115     1555   1555  3.00  
LINK        MG    MG A1656                 O6    G A 357     1555   1555  2.95  
LINK        MG    MG A1656                 O2    C A 352     1555   1555  3.09  
LINK        MG    MG D 215                 OG1 THR D  89     1555   1555  2.37  
LINK        MG    MG D 215                 O   GLY D  87     1555   1555  2.92  
LINK        MG    MG D 215                 O   LYS D  85     1555   1555  2.58  
LINK        MG    MG D 215                 O   SER D  83     1555   1555  2.57  
LINK        MG    MG D 215                 O   ALA D  82     1555   1555  2.68  
LINK        ZN    ZN D 306                 SG  CYS D  26     1555   1555  2.43  
LINK        ZN    ZN D 306                 SG  CYS D   9     1555   1555  2.08  
LINK        ZN    ZN D 306                 SG  CYS D  31     1555   1555  2.24  
LINK        MG    MG J 422                 NZ  LYS J  57     1555   1555  1.92  
LINK        MG    MG J 422                 OP1   C A 972     1555   1555  2.32  
LINK        MG    MG J 449                 NH2 ARG J  60     1555   1555  2.79  
LINK        MG    MG J 449                 OP1   G A 973     1555   1555  3.04  
LINK        ZN    ZN N 307                 SG  CYS N  27     1555   1555  2.29  
LINK        ZN    ZN N 307                 SG  CYS N  43     1555   1555  2.26  
LINK        ZN    ZN N 307                 SG  CYS N  24     1555   1555  2.67  
LINK        ZN    ZN N 307                 SG  CYS N  40     1555   1555  2.57  
LINK        MG    MG Y 456                 O6    G Y  30     1555   1555  2.28  
LINK         SG  CYS D  12                ZN    ZN D 306     1555   1555  2.89  
SITE     1 AC1 10   G A1405    U A1406    C A1407    A A1408                    
SITE     2 AC1 10   C A1490    G A1491    A A1492    A A1493                    
SITE     3 AC1 10   G A1494    U A1495                                          
SITE     1 AC2  2   G A 944    G A 945                                          
SITE     1 AC3  2   C A1223    G A1224                                          
SITE     1 AC4  5   G A  11    U A  12    G A  21    G A  22                    
SITE     2 AC4  5   C A  23                                                     
SITE     1 AC5  2   U A  14    U A  17                                          
SITE     1 AC6  2   G A 376    G A 377                                          
SITE     1 AC7  2   C A 749    G A 750                                          
SITE     1 AC8  1   A A 766                                                     
SITE     1 AC9  1   A A 768                                                     
SITE     1 BC1  2   A A 780    G A 800                                          
SITE     1 BC2  1   C A 578                                                     
SITE     1 BC3  1  MG A 441                                                     
SITE     1 BC4  2   A A 509    A A 510                                          
SITE     1 BC5  2   U A 560    C A 562                                          
SITE     1 BC6  1   G A  21                                                     
SITE     1 BC7  4   G A 595    C A 596    G A 597    U A 598                    
SITE     1 BC8  2   G A 858    G A 869                                          
SITE     1 BC9  1   A A 860                                                     
SITE     1 CC1  4   G A 885    G A 886    U A 911   MG A1618                    
SITE     1 CC2  1   A A 937                                                     
SITE     1 CC3  1   C A 934                                                     
SITE     1 CC4  1   G A1370                                                     
SITE     1 CC5  1 ARG D 141                                                     
SITE     1 CC6  2   G A 587    G A 588                                          
SITE     1 CC7  3   A A 964    G A1198    U A1199                               
SITE     1 CC8  3   C A 979    C A 980    G A1220                               
SITE     1 CC9  3   G A1053    C A1054    G A1197                               
SITE     1 DC1  4   C A1054    U A1196    G A1197    G A1198                    
SITE     1 DC2  5   G A 299    A A 300    G A 558    U A 560                    
SITE     2 DC2  5   G A 566                                                     
SITE     1 DC3  1   G A 324                                                     
SITE     1 DC4  3   A A 572    A A 573    A A 574                               
SITE     1 DC5  1   G A 898                                                     
SITE     1 DC6  2   A A1110    C A1189                                          
SITE     1 DC7  3   A A 865    C A 866    G A1079                               
SITE     1 DC8  4   A A1067    G A1068    G A1094    G A1387                    
SITE     1 DC9  2   U A1095    G A1108                                          
SITE     1 EC1  1   G A 286                                                     
SITE     1 EC2  5   U A1510    G A1511    U A1512    G A1523                    
SITE     2 EC2  5   C A1524                                                     
SITE     1 EC3  5   A A1499    A A1500    G A1508    G A1521                    
SITE     2 EC3  5  MG A1588                                                     
SITE     1 EC4  4   A A1499    A A1500    G A1504    G A1505                    
SITE     1 EC5  5   A A1500    G A1505    A A1507    G A1508                    
SITE     2 EC5  5  MG A1586                                                     
SITE     1 EC6  3   A A 151    G A 167    G A 168                               
SITE     1 EC7  1   A A 195                                                     
SITE     1 EC8  3   U A 182    G A 183   MG A1624                               
SITE     1 EC9  3   A A 116    G A 117    G A 289                               
SITE     1 FC1  1   C A 352                                                     
SITE     1 FC2  4   C A 372    U A 375    G A 376    U A 387                    
SITE     1 FC3  2   A A 782    A A 794                                          
SITE     1 FC4  5   G A1053    G A1058    C A1059    G A1198                    
SITE     2 FC4  5   U A1199                                                     
SITE     1 FC5  3   C A1242    C A1303    G A1304                               
SITE     1 FC6  4   A A 563    C A 564    U A 565    G A 567                    
SITE     1 FC7  4   G A 604    U A 605    G A 633    C A 634                    
SITE     1 FC8  3   G A 584    C A 756    U A 757                               
SITE     1 FC9  2   A A 547    G A 548                                          
SITE     1 GC1  5 ALA D  82  SER D  83  LYS D  85  GLY D  87                    
SITE     2 GC1  5 THR D  89                                                     
SITE     1 GC2  1   A A 431                                                     
SITE     1 GC3  2   A A 535    C A 536                                          
SITE     1 GC4  2   C A 504    G A 505                                          
SITE     1 GC5  4   C A 518    G A 529  PRO L  48  ASN L  49                    
SITE     1 GC6  7   C A 121    G A 124    U A 125    G A 126                    
SITE     2 GC6  7   C A 235    G A 236    C A 237                               
SITE     1 GC7  2   C A 174    C A 175                                          
SITE     1 GC8  3   A A 109    A A 329    G A 331                               
SITE     1 GC9  4   G A  69    G A  70    G A  97    U A  98                    
SITE     1 HC1  4   G A  61    U A  62    G A 105    C A 106                    
SITE     1 HC2  4   C A 518    G A 530  PRO L  48    U Z   3                    
SITE     1 HC3  4   G A 830    U A 831    G A 855    C A 856                    
SITE     1 HC4  3   G A 594    G A 595   MG A1646                               
SITE     1 HC5  1   G A 595                                                     
SITE     1 HC6  2   G A 637    G A 638                                          
SITE     1 HC7  3   G A 887    G A 888   MG A1565                               
SITE     1 HC8  1   G A1461                                                     
SITE     1 HC9  2   G A1497    U A1498                                          
SITE     1 IC1  1   G A 916                                                     
SITE     1 IC2  4   U A1090    U A1091    G A1094    U A1095                    
SITE     1 IC3  2   G A 284    G A 285                                          
SITE     1 IC4  4   G A 181    U A 182    G A 183   MG A1591                    
SITE     1 IC5  3   A A1238    A A1299    C A1335                               
SITE     1 IC6  1   A A 608                                                     
SITE     1 IC7  3   C A 328    A A 329    C A 330                               
SITE     1 IC8  1   A A 315                                                     
SITE     1 IC9  1   G A 476                                                     
SITE     1 JC1  4   U A 516    G A 517    A A 532    A A 533                    
SITE     1 JC2  2   C A 972  LYS J  57                                          
SITE     1 JC3  3   G A1048    U A1049  ALA N   2                               
SITE     1 JC4  5   U A1052    C A1200    U A1205    G A1206                    
SITE     2 JC4  5   G A1207                                                     
SITE     1 JC5  3   U A 921    G A 922    U A1393                               
SITE     1 JC6  5   C A 924    G A 925    G A 927    U A1390                    
SITE     2 JC6  5   U A1391                                                     
SITE     1 JC7  4   G A  15    A A  16    A A 919    U A 920                    
SITE     1 JC8  5   U A1414    G A1415    U A1485    G A1486                    
SITE     2 JC8  5  MG A1641                                                     
SITE     1 JC9  4   G A1415    G A1416    G A1417   MG A1640                    
SITE     1 KC1  4   G A 416    G A 426    U A 427   MG A1643                    
SITE     1 KC2  2   G A 426   MG A1642                                          
SITE     1 KC3  4   G A 785    G A 786    C A 796    C A 797                    
SITE     1 KC4  4   U A 833    G A 852    G A 853   MG A1557                    
SITE     1 KC5  3   G A 837    G A 838    C A 840                               
SITE     1 KC6  5   G A 592    G A 593    G A 594    U A 646                    
SITE     2 KC6  5  MG A1615                                                     
SITE     1 KC7  2   G A 649    G A 650                                          
SITE     1 KC8  5   A A 937    U A1345    A A1377    G A1379                    
SITE     2 KC8  5 ALA G   2                                                     
SITE     1 KC9  1   G A1385                                                     
SITE     1 LC1  5   G A 115    A A 116    G A 117    U A 118                    
SITE     2 LC1  5   G A 289                                                     
SITE     1 LC2  4   C A 972    G A 973  LYS J  57  ARG J  60                    
SITE     1 LC3  1   G A 362                                                     
SITE     1 LC4  2   G A  52    A A 360                                          
SITE     1 LC5  1   A A  53                                                     
SITE     1 LC6  2   C A  48    G A 115                                          
SITE     1 LC7  2   C A 352    G A 357                                          
SITE     1 LC8  1   G A  44                                                     
SITE     1 LC9  1   G Y  30                                                     
SITE     1 MC1  4 CYS D   9  CYS D  12  CYS D  26  CYS D  31                    
SITE     1 MC2  4 CYS N  24  CYS N  27  CYS N  40  CYS N  43                    
CRYST1  400.800  400.800  175.885  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      0.002495  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002495  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005686        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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