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Database: PDB
Entry: 2PYO
LinkDB: 2PYO
Original site: 2PYO 
HEADER    STRUCTURAL PROTEIN/DNA                  16-MAY-07   2PYO              
TITLE     DROSOPHILA NUCLEOSOME CORE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (147-MER);                                             
COMPND   3 CHAIN: I;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DNA (147-MER);                                             
COMPND   7 CHAIN: J;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HISTONE H3;                                                
COMPND  11 CHAIN: A, E;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HISTONE H4;                                                
COMPND  15 CHAIN: B, F;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: HISTONE H2A;                                               
COMPND  19 CHAIN: C, G;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: HISTONE H2B;                                               
COMPND  23 CHAIN: D, H;                                                         
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  15 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  16 ORGANISM_TAXID: 7227;                                                
SOURCE  17 GENE: HIS3;                                                          
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  22 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  23 ORGANISM_TAXID: 7227;                                                
SOURCE  24 GENE: HIS4, H4;                                                      
SOURCE  25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  27 MOL_ID: 5;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  29 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  30 ORGANISM_TAXID: 7227;                                                
SOURCE  31 GENE: HIS2A, H2A;                                                    
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  34 MOL_ID: 6;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  36 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  37 ORGANISM_TAXID: 7227;                                                
SOURCE  38 GENE: HIS2B;                                                         
SOURCE  39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOSOME CORE, HISTONE FOLD, STRUCTURAL PROTEIN/DNA                 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.CLAPIER,C.PETOSA,C.W.MUELLER                                      
REVDAT   3   24-FEB-09 2PYO    1       VERSN                                    
REVDAT   2   04-MAR-08 2PYO    1       JRNL                                     
REVDAT   1   06-NOV-07 2PYO    0                                                
JRNL        AUTH   C.R.CLAPIER,S.CHAKRAVARTHY,C.PETOSA,                         
JRNL        AUTH 2 C.FERNANDEZ-TORNERO,K.LUGER,C.W.MULLER                       
JRNL        TITL   STRUCTURE OF THE DROSOPHILA NUCLEOSOME CORE                  
JRNL        TITL 2 PARTICLE HIGHLIGHTS EVOLUTIONARY CONSTRAINTS ON              
JRNL        TITL 3 THE H2A-H2B HISTONE DIMER.                                   
JRNL        REF    PROTEINS                      V.  71     1 2007              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17957772                                                     
JRNL        DOI    10.1002/PROT.21720                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 500.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 75234                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3798                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 6021                                    
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.49700                                             
REMARK   3    B22 (A**2) : -5.89000                                             
REMARK   3    B33 (A**2) : 11.38700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 50.66                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042931.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
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   (%): 53.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION WAS CARRIED OUT BY       
REMARK 280  EQUILIBRATING A DROPLET CONTAINING 3 MG/ML NUCLEOSOME CORE          
REMARK 280  PARTICLE, 80-85 MM MNCL2, 50-80 MM KCL AND 20 MM POTASSIUM          
REMARK 280  CACODYLATE (PH 6.0) AGAINST A RESERVOIR SOLUTION CONTAINING OF      
REMARK 280  40-42.5 MM MNCL2, 25-40 MM KCL AND 20 MM POTASSIUM CACODYLATE       
REMARK 280  (PH 6.0). , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       53.01500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.71000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.02000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.71000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.01500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.02000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THERE IS ONE NUCLEOSOME IN THE ASYMMETRIC UNIT,              
REMARK 300 CONSISTING OF TWO COPIES EACH OF HISTONES H2A, H2B, H3 AND H4        
REMARK 300 PLUS DOUBLE-STRANDED DNA.                                            
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, C, D, E, F, G, H          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     LYS A    36                                                      
REMARK 465     THR B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     VAL C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     LYS C    12                                                      
REMARK 465     PRO D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     LYS D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     GLN D    16                                                      
REMARK 465     LYS D    17                                                      
REMARK 465     ASN D    18                                                      
REMARK 465     ILE D    19                                                      
REMARK 465     THR D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     ASP D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     LYS D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     THR E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     GLY E    13                                                      
REMARK 465     LYS E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     PRO E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     LEU E    20                                                      
REMARK 465     ALA E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     LYS E    23                                                      
REMARK 465     ALA E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     ARG E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     PRO E    30                                                      
REMARK 465     ALA E    31                                                      
REMARK 465     THR E    32                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     VAL E    35                                                      
REMARK 465     LYS E    36                                                      
REMARK 465     THR F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     LYS F    12                                                      
REMARK 465     GLY F    13                                                      
REMARK 465     GLY F    14                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     LYS G     5                                                      
REMARK 465     GLY G     6                                                      
REMARK 465     GLY G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     VAL G     9                                                      
REMARK 465     LYS G    10                                                      
REMARK 465     GLU G   120                                                      
REMARK 465     PRO H     1                                                      
REMARK 465     PRO H     2                                                      
REMARK 465     LYS H     3                                                      
REMARK 465     THR H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     GLY H     6                                                      
REMARK 465     LYS H     7                                                      
REMARK 465     ALA H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     LYS H    10                                                      
REMARK 465     LYS H    11                                                      
REMARK 465     ALA H    12                                                      
REMARK 465     GLY H    13                                                      
REMARK 465     LYS H    14                                                      
REMARK 465     ALA H    15                                                      
REMARK 465     GLN H    16                                                      
REMARK 465     LYS H    17                                                      
REMARK 465     ASN H    18                                                      
REMARK 465     ILE H    19                                                      
REMARK 465     THR H    20                                                      
REMARK 465     LYS H    21                                                      
REMARK 465     THR H    22                                                      
REMARK 465     ASP H    23                                                      
REMARK 465     LYS H    24                                                      
REMARK 465     LYS H    25                                                      
REMARK 465     LYS H    26                                                      
REMARK 465     LYS H    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     ARG B  23    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS C 117    CB   CG   CD   CE   NZ                              
REMARK 470     LYS C 118    CB   CG   CD   CE   NZ                              
REMARK 470     THR C 119    CB   OG1  CG2                                       
REMARK 470     GLU C 120    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS G 118    CB   CG   CD   CE   NZ                              
REMARK 470     THR G 119    CB   OG1  CG2                                       
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     DT I  67   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG B  95       50.48   -113.26                                   
REMARK 500    THR B  96      131.63    -35.65                                   
REMARK 500    LYS C  14      109.92   -177.81                                   
REMARK 500    PRO C  25       98.98    -64.04                                   
REMARK 500    LYS C 117      179.09    149.42                                   
REMARK 500    THR C 119     -106.91     60.89                                   
REMARK 500    LYS D  29      113.64     66.78                                   
REMARK 500    PRO E  38      154.54    -46.27                                   
REMARK 500    LYS E 115       32.47     70.31                                   
REMARK 500    HIS F  18       59.10     31.17                                   
REMARK 500    ARG F  95       51.55   -109.42                                   
REMARK 500    SER G  15      151.19    -49.07                                   
REMARK 500    PRO G  25       88.26    -65.66                                   
REMARK 500    ASN G 109      119.04   -166.25                                   
REMARK 500    PRO G 116      140.42    -39.99                                   
REMARK 500    LYS G 117       79.93     66.10                                   
REMARK 500    LYS G 118     -110.03     77.78                                   
REMARK 500    LYS H  29      101.24   -165.06                                   
REMARK 500    SER H 120       38.50    -68.98                                   
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     DG I  -6         0.07    SIDE_CHAIN                              
REMARK 500     DG J  -6         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                              MN E1002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  77   OD1                                                    
REMARK 620 2 HOH E1029   O    81.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1007                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1008                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1010                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1011                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1012                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1013                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1001                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1003                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1004                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1005                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1009                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1014                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1017                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1016                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1002                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1018                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1015                 
DBREF  2PYO I  -73    73  PDB    2PYO     2PYO             1    147             
DBREF  2PYO J  -73    73  PDB    2PYO     2PYO             1    147             
DBREF  2PYO A    1   135  UNP    P02299   H3_DROME         2    136             
DBREF  2PYO B    1   102  UNP    P84040   H4_DROME         2    103             
DBREF  2PYO C    1   120  UNP    P84051   H2A_DROME        2    121             
DBREF  2PYO D    1   122  UNP    P02283   H2B_DROME        2    123             
DBREF  2PYO E    1   135  UNP    P02299   H3_DROME         2    136             
DBREF  2PYO F    1   102  UNP    P84040   H4_DROME         2    103             
DBREF  2PYO G    1   120  UNP    P84051   H2A_DROME        2    121             
DBREF  2PYO H    1   122  UNP    P02283   H2B_DROME        2    123             
SEQRES   1 I  147   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 I  147   DT  DG  DC  DA  DG  DA  DT  DA  DC  DT  DA  DC  DC          
SEQRES   3 I  147   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 I  147   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 I  147   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 I  147   DC  DA  DG  DC  DT  DG  DG  DA  DA  DT  DC  DC  DA          
SEQRES   7 I  147   DG  DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT          
SEQRES   8 I  147   DT  DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG          
SEQRES   9 I  147   DT  DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC          
SEQRES  10 I  147   DT  DT  DT  DT  DG  DG  DT  DA  DG  DT  DA  DT  DC          
SEQRES  11 I  147   DT  DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT          
SEQRES  12 I  147   DT  DG  DA  DT                                              
SEQRES   1 J  147   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 J  147   DT  DG  DC  DA  DG  DA  DT  DA  DC  DT  DA  DC  DC          
SEQRES   3 J  147   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 J  147   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 J  147   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 J  147   DC  DA  DG  DC  DT  DG  DG  DA  DT  DT  DC  DC  DA          
SEQRES   7 J  147   DG  DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT          
SEQRES   8 J  147   DT  DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG          
SEQRES   9 J  147   DT  DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC          
SEQRES  10 J  147   DT  DT  DT  DT  DG  DG  DT  DA  DG  DT  DA  DT  DC          
SEQRES  11 J  147   DT  DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT          
SEQRES  12 J  147   DT  DG  DA  DT                                              
SEQRES   1 A  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 A  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 A  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 A  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 A  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 A  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 A  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 A  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   9 A  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 A  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 A  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 B  102  THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 B  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 B  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 B  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 B  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 B  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 B  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 B  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 C  120  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 C  120  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 C  120  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 C  120  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 C  120  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 C  120  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 C  120  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 C  120  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 C  120  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 C  120  LYS THR GLU                                                  
SEQRES   1 D  122  PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY          
SEQRES   2 D  122  LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS          
SEQRES   3 D  122  LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR          
SEQRES   4 D  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 D  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 D  122  ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA          
SEQRES   7 D  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 D  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 D  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 D  122  TYR THR SER SER LYS                                          
SEQRES   1 E  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 E  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 E  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 E  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 E  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 E  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 E  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 E  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   9 E  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 E  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 E  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 F  102  THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 F  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 F  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 F  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 F  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 F  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 F  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 F  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 G  120  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 G  120  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 G  120  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 G  120  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 G  120  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 G  120  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 G  120  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 G  120  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 G  120  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 G  120  LYS THR GLU                                                  
SEQRES   1 H  122  PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY          
SEQRES   2 H  122  LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS          
SEQRES   3 H  122  LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR          
SEQRES   4 H  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 H  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 H  122  ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA          
SEQRES   7 H  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 H  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 H  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 H  122  TYR THR SER SER LYS                                          
HET     MN  I1006       1                                                       
HET     MN  I1007       1                                                       
HET     MN  I1008       1                                                       
HET     MN  I1010       1                                                       
HET     MN  I1011       1                                                       
HET     MN  I1012       1                                                       
HET     MN  I1013       1                                                       
HET     MN  J1001       1                                                       
HET     MN  J1003       1                                                       
HET     MN  J1004       1                                                       
HET     MN  J1005       1                                                       
HET     MN  J1009       1                                                       
HET     MN  J1014       1                                                       
HET     CL  A1017       1                                                       
HET     CL  D1016       1                                                       
HET     MN  E1002       1                                                       
HET     CL  E1018       1                                                       
HET     CL  H1015       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      CL CHLORIDE ION                                                     
FORMUL  11   MN    14(MN 2+)                                                    
FORMUL  24   CL    4(CL 1-)                                                     
FORMUL  29  HOH   *88(H2 O)                                                     
HELIX    1   1 GLY A   44  SER A   57  1                                  14    
HELIX    2   2 ARG A   63  ASP A   77  1                                  15    
HELIX    3   3 GLN A   85  ALA A  114  1                                  30    
HELIX    4   4 MET A  120  ARG A  131  1                                  12    
HELIX    5   5 ASN B   25  ILE B   29  5                                   5    
HELIX    6   6 THR B   30  GLY B   41  1                                  12    
HELIX    7   7 LEU B   49  ALA B   76  1                                  28    
HELIX    8   8 THR B   82  GLN B   93  1                                  12    
HELIX    9   9 SER C   15  GLY C   21  1                                   7    
HELIX   10  10 PRO C   25  GLY C   36  1                                  12    
HELIX   11  11 ALA C   44  ASN C   72  1                                  29    
HELIX   12  12 ILE C   78  ASP C   89  1                                  12    
HELIX   13  13 ASP C   89  LEU C   96  1                                   8    
HELIX   14  14 GLN C  111  LEU C  115  5                                   5    
HELIX   15  15 TYR D   34  HIS D   46  1                                  13    
HELIX   16  16 SER D   52  ASN D   81  1                                  30    
HELIX   17  17 THR D   87  LEU D   99  1                                  13    
HELIX   18  18 PRO D  100  SER D  120  1                                  21    
HELIX   19  19 GLY E   44  SER E   57  1                                  14    
HELIX   20  20 ARG E   63  ASP E   77  1                                  15    
HELIX   21  21 GLN E   85  ALA E  114  1                                  30    
HELIX   22  22 MET E  120  ARG E  131  1                                  12    
HELIX   23  23 ASP F   24  ILE F   29  5                                   6    
HELIX   24  24 THR F   30  GLY F   41  1                                  12    
HELIX   25  25 LEU F   49  ALA F   76  1                                  28    
HELIX   26  26 THR F   82  ARG F   92  1                                  11    
HELIX   27  27 SER G   15  GLY G   21  1                                   7    
HELIX   28  28 PRO G   25  LYS G   35  1                                  11    
HELIX   29  29 ALA G   44  ASP G   71  1                                  28    
HELIX   30  30 ILE G   78  ASP G   89  1                                  12    
HELIX   31  31 ASP G   89  LEU G   96  1                                   8    
HELIX   32  32 GLN G  111  LEU G  115  5                                   5    
HELIX   33  33 TYR H   34  HIS H   46  1                                  13    
HELIX   34  34 SER H   52  ASN H   81  1                                  30    
HELIX   35  35 THR H   87  LEU H   99  1                                  13    
HELIX   36  36 PRO H  100  SER H  120  1                                  21    
SHEET    1   A 2 ARG A  83  PHE A  84  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A  83           
SHEET    1   B 2 THR A 118  ILE A 119  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1   C 2 LEU B  97  TYR B  98  0                                        
SHEET    2   C 2 THR G 100  ILE G 101  1  O  THR G 100   N  TYR B  98           
SHEET    1   D 2 ARG C  41  VAL C  42  0                                        
SHEET    2   D 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  41           
SHEET    1   E 2 ARG C  76  ILE C  77  0                                        
SHEET    2   E 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  77           
SHEET    1   F 2 THR C 100  ILE C 101  0                                        
SHEET    2   F 2 LEU F  97  TYR F  98  1  O  TYR F  98   N  THR C 100           
SHEET    1   G 2 ARG E  83  PHE E  84  0                                        
SHEET    2   G 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1   H 2 THR E 118  ILE E 119  0                                        
SHEET    2   H 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1   I 2 ARG G  41  VAL G  42  0                                        
SHEET    2   I 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  41           
SHEET    1   J 2 ARG G  76  ILE G  77  0                                        
SHEET    2   J 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  77           
LINK         O6   DG I -34                MN    MN I1013     1555   1555  2.26  
LINK         O6   DG J -34                MN    MN J1009     1555   1555  2.36  
LINK         OD1 ASP E  77                MN    MN E1002     1555   1555  2.10  
LINK        MN    MN E1002                 O   HOH E1029     1555   1555  2.33  
SITE     1 AC1  1  DG I  48                                                     
SITE     1 AC2  1  DG I  61                                                     
SITE     1 AC3  1  DG I  27                                                     
SITE     1 AC4  2  DG I   5   DG J  -6                                          
SITE     1 AC5  2  DG I  -3   DG I  -2                                          
SITE     1 AC6  2  DG I -35   DG I -34                                          
SITE     1 AC7  1  DG J  61                                                     
SITE     1 AC8  2  DT I  67   DG J  27                                          
SITE     1 AC9  1  DG J  -3                                                     
SITE     1 BC1  1  DG J  48                                                     
SITE     1 BC2  2  DG J -35   DG J -34                                          
SITE     1 BC3  2  DG I  -6   DG J   5                                          
SITE     1 BC4  2 PRO A 121  LYS A 122                                          
SITE     1 BC5  3 GLY C  45  THR D  87  SER D  88                               
SITE     1 BC6  3 VAL D  45  ASP E  77  HOH E1029                               
SITE     1 BC7  3 MET E 120  PRO E 121  LYS E 122                               
SITE     1 BC8  4 GLY G  45  ALA G  46  THR H  87  SER H  88                    
CRYST1  106.030  182.040  109.420  90.00  90.00  90.00 P 21 21 21    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      0.009431  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005493  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009139        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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