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Database: PDB
Entry: 2NQB
LinkDB: 2NQB
Original site: 2NQB 
HEADER    STRUCTURAL PROTEIN/DNA                  30-OCT-06   2NQB              
TITLE     DROSOPHILA NUCLEOSOME STRUCTURE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-SATELLITE DNA;                                       
COMPND   3 CHAIN: I, J;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H3;                                                
COMPND   7 CHAIN: A, E;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HISTONE H4;                                                
COMPND  11 CHAIN: B, F;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HISTONE H2A;                                               
COMPND  15 CHAIN: C, G;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: HISTONE H2B;                                               
COMPND  19 CHAIN: D, H;                                                         
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HIS3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  10 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  11 ORGANISM_TAXID: 7227;                                                
SOURCE  12 GENE: HIS4;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  17 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  18 ORGANISM_TAXID: 7227;                                                
SOURCE  19 GENE: HIS2A;                                                         
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  24 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  25 ORGANISM_TAXID: 7227;                                                
SOURCE  26 GENE: HIS2B;                                                         
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  31 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  32 ORGANISM_TAXID: 7227;                                                
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOSOME, NCP, CHROMATIN, HISTONE, STRUCTURAL PROTEIN/DNA           
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.LUGER,S.CHAKRAVARTHY                                                
REVDAT   2   24-FEB-09 2NQB    1       VERSN                                    
REVDAT   1   11-SEP-07 2NQB    0                                                
JRNL        AUTH   S.CHAKRAVARTHY,K.LUGER                                       
JRNL        TITL   COMPARATIVE ANALYSIS OF NUCLEOSOME STRUCTURES FROM           
JRNL        TITL 2 DIFFERENT SPECIES.                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.00                          
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)   (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 91209                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2267                            
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            : 6050                                    
REMARK   3   NUCLEIC ACID ATOMS       : 5980                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 264                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.47300                                             
REMARK   3    B22 (A**2) : 5.93400                                              
REMARK   3    B33 (A**2) : -2.46100                                             
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.96                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : 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 2NQB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040172.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93949                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1AOI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CONSTITUENTS OF THE CRYSTALLIZATION      
REMARK 280  BUFFER: POTASSIUM CHLORIDE, MANGANESE CHLORIDE, AND POTASSIUM       
REMARK 280  CACODYLATE., PH 6.0, VAPOR DIFFUSION, SITTING DROP,                 
REMARK 280  TEMPERATURE 292K                                                    
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       53.07150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.02250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.79050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.02250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.07150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.79050            
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: EACH NUCLEOSOME HAS TWO COPIES EACH OF HISTONES H2A,         
REMARK 300 H2B, H3 AND H4, AND A 146 BASE PAIRS LONG PALINDROMIC STRAND OF      
REMARK 300 DNA DERIVED FROM HUMAN ALPHA-SATELLITE SEQUENCE.                     
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   401                                                      
REMARK 465     ARG A   402                                                      
REMARK 465     THR A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     GLN A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     ARG A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     LYS A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     ARG A   417                                                      
REMARK 465     LYS A   418                                                      
REMARK 465     GLN A   419                                                      
REMARK 465     LEU A   420                                                      
REMARK 465     ALA A   421                                                      
REMARK 465     THR A   422                                                      
REMARK 465     LYS A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     ALA A   425                                                      
REMARK 465     ARG A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     ALA A   429                                                      
REMARK 465     PRO A   430                                                      
REMARK 465     ALA A   431                                                      
REMARK 465     THR A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     GLY A   434                                                      
REMARK 465     VAL A   435                                                      
REMARK 465     LYS A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ILE B     0                                                      
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     SER C   802                                                      
REMARK 465     GLY C   803                                                      
REMARK 465     ARG C   804                                                      
REMARK 465     GLY C   805                                                      
REMARK 465     LYS C   806                                                      
REMARK 465     GLY C   807                                                      
REMARK 465     GLY C   808                                                      
REMARK 465     LYS C   809                                                      
REMARK 465     VAL C   810                                                      
REMARK 465     LYS C   811                                                      
REMARK 465     GLY C   812                                                      
REMARK 465     LYS C   813                                                      
REMARK 465     THR C   920                                                      
REMARK 465     GLU C   921                                                      
REMARK 465     LYS C   922                                                      
REMARK 465     LYS C   923                                                      
REMARK 465     ALA C   924                                                      
REMARK 465     ILE D  1200                                                      
REMARK 465     PRO D  1201                                                      
REMARK 465     PRO D  1202                                                      
REMARK 465     LYS D  1203                                                      
REMARK 465     THR D  1204                                                      
REMARK 465     SER D  1205                                                      
REMARK 465     GLY D  1206                                                      
REMARK 465     LYS D  1207                                                      
REMARK 465     ALA D  1208                                                      
REMARK 465     ALA D  1209                                                      
REMARK 465     LYS D  1210                                                      
REMARK 465     LYS D  1211                                                      
REMARK 465     ALA D  1212                                                      
REMARK 465     GLY D  1213                                                      
REMARK 465     LYS D  1214                                                      
REMARK 465     ALA D  1215                                                      
REMARK 465     GLN D  1216                                                      
REMARK 465     LYS D  1217                                                      
REMARK 465     ASN D  1218                                                      
REMARK 465     ILE D  1219                                                      
REMARK 465     THR D  1220                                                      
REMARK 465     LYS D  1221                                                      
REMARK 465     THR D  1222                                                      
REMARK 465     ASP D  1223                                                      
REMARK 465     LYS D  1224                                                      
REMARK 465     LYS D  1225                                                      
REMARK 465     LYS D  1226                                                      
REMARK 465     LYS D  1227                                                      
REMARK 465     ALA E   601                                                      
REMARK 465     ARG E   602                                                      
REMARK 465     THR E   603                                                      
REMARK 465     LYS E   604                                                      
REMARK 465     GLN E   605                                                      
REMARK 465     THR E   606                                                      
REMARK 465     ALA E   607                                                      
REMARK 465     ARG E   608                                                      
REMARK 465     LYS E   609                                                      
REMARK 465     SER E   610                                                      
REMARK 465     THR E   611                                                      
REMARK 465     GLY E   612                                                      
REMARK 465     GLY E   613                                                      
REMARK 465     LYS E   614                                                      
REMARK 465     ALA E   615                                                      
REMARK 465     PRO E   616                                                      
REMARK 465     ARG E   617                                                      
REMARK 465     LYS E   618                                                      
REMARK 465     GLN E   619                                                      
REMARK 465     LEU E   620                                                      
REMARK 465     ALA E   621                                                      
REMARK 465     THR E   622                                                      
REMARK 465     LYS E   623                                                      
REMARK 465     ALA E   624                                                      
REMARK 465     ALA E   625                                                      
REMARK 465     ARG E   626                                                      
REMARK 465     LYS E   627                                                      
REMARK 465     SER E   628                                                      
REMARK 465     ALA E   629                                                      
REMARK 465     PRO E   630                                                      
REMARK 465     ALA E   631                                                      
REMARK 465     THR E   632                                                      
REMARK 465     GLY E   633                                                      
REMARK 465     GLY E   634                                                      
REMARK 465     VAL E   635                                                      
REMARK 465     LYS E   636                                                      
REMARK 465     LYS E   637                                                      
REMARK 465     ILE F   200                                                      
REMARK 465     THR F   201                                                      
REMARK 465     GLY F   202                                                      
REMARK 465     ARG F   203                                                      
REMARK 465     GLY F   204                                                      
REMARK 465     LYS F   205                                                      
REMARK 465     GLY F   206                                                      
REMARK 465     GLY F   207                                                      
REMARK 465     LYS F   208                                                      
REMARK 465     GLY F   209                                                      
REMARK 465     LEU F   210                                                      
REMARK 465     GLY F   211                                                      
REMARK 465     LYS F   212                                                      
REMARK 465     GLY F   213                                                      
REMARK 465     GLY F   214                                                      
REMARK 465     ALA F   215                                                      
REMARK 465     LYS F   216                                                      
REMARK 465     SER G  1002                                                      
REMARK 465     GLY G  1003                                                      
REMARK 465     ARG G  1004                                                      
REMARK 465     GLY G  1005                                                      
REMARK 465     LYS G  1006                                                      
REMARK 465     GLY G  1007                                                      
REMARK 465     GLY G  1008                                                      
REMARK 465     LYS G  1009                                                      
REMARK 465     VAL G  1010                                                      
REMARK 465     LYS G  1011                                                      
REMARK 465     GLY G  1012                                                      
REMARK 465     LYS G  1013                                                      
REMARK 465     LYS G  1119                                                      
REMARK 465     THR G  1120                                                      
REMARK 465     GLU G  1121                                                      
REMARK 465     LYS G  1122                                                      
REMARK 465     LYS G  1123                                                      
REMARK 465     ALA G  1124                                                      
REMARK 465     ILE H  1400                                                      
REMARK 465     PRO H  1401                                                      
REMARK 465     PRO H  1402                                                      
REMARK 465     LYS H  1403                                                      
REMARK 465     THR H  1404                                                      
REMARK 465     SER H  1405                                                      
REMARK 465     GLY H  1406                                                      
REMARK 465     LYS H  1407                                                      
REMARK 465     ALA H  1408                                                      
REMARK 465     ALA H  1409                                                      
REMARK 465     LYS H  1410                                                      
REMARK 465     LYS H  1411                                                      
REMARK 465     ALA H  1412                                                      
REMARK 465     GLY H  1413                                                      
REMARK 465     LYS H  1414                                                      
REMARK 465     ALA H  1415                                                      
REMARK 465     GLN H  1416                                                      
REMARK 465     LYS H  1417                                                      
REMARK 465     ASN H  1418                                                      
REMARK 465     ILE H  1419                                                      
REMARK 465     THR H  1420                                                      
REMARK 465     LYS H  1421                                                      
REMARK 465     THR H  1422                                                      
REMARK 465     ASP H  1423                                                      
REMARK 465     LYS H  1424                                                      
REMARK 465     LYS H  1425                                                      
REMARK 465     LYS H  1426                                                      
REMARK 465     LYS H  1427                                                      
REMARK 465     ARG H  1428                                                      
REMARK 465     LYS H  1522                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH I   322     O    HOH I   516              1.24            
REMARK 500   O    HOH G   363     O    HOH G   518              1.26            
REMARK 500   O3'  DA  I    28     O    HOH I   522              1.63            
REMARK 500   CB   ARG F   292     O    HOH F   517              1.65            
REMARK 500   C5'  DT  J   166     O    HOH J   529              1.65            
REMARK 500   O    HOH J   364     O    HOH J   521              1.71            
REMARK 500   N    VAL F   265     O    HOH F   531              1.78            
REMARK 500   O4'  DT  J   166     O    HOH J   529              1.81            
REMARK 500   O5'  DT  J   166     O    HOH J   529              1.86            
REMARK 500   O    HOH C   499     O    HOH D   362              1.90            
REMARK 500   O    LEU F   262     O    HOH F   531              1.94            
REMARK 500   N4   DC  J   149     O    HOH J   587              1.97            
REMARK 500   N7   DG  I   100     O    HOH I   516              2.02            
REMARK 500   CG   ARG F   292     O    HOH F   517              2.05            
REMARK 500   N3   DA  I    55     O    HOH I   565              2.06            
REMARK 500   C4'  DT  J   166     O    HOH J   529              2.06            
REMARK 500   O    PHE F   261     O    HOH F   531              2.10            
REMARK 500   O    HOH I   471     O    HOH J   364              2.13            
REMARK 500   NH1  ARG C   881     O    HOH C   478              2.14            
REMARK 500   O    HOH J   364     O    HOH J   465              2.18            
REMARK 500   C4   DA  I    55     O    HOH I   565              2.18            
REMARK 500   N3   DG  I    58     O    HOH I   525              2.18            
REMARK 500   OD1  ASP E   677     O    HOH E   736              2.18            
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  23      173.37    178.25                                   
REMARK 500    ARG B  95       52.72   -117.41                                   
REMARK 500    PRO C 826       92.62    -64.12                                   
REMARK 500    ASN C 910      114.02   -164.44                                   
REMARK 500    LYS C 918     -153.66     42.37                                   
REMARK 500    ARG E 734       16.14   -178.12                                   
REMARK 500    ARG F 219     -138.95     18.75                                   
REMARK 500    LYS F 220       75.04    144.06                                   
REMARK 500    VAL F 221      124.53    -18.29                                   
REMARK 500    ASP F 224       43.60     37.16                                   
REMARK 500    ARG F 295       66.87   -108.57                                   
REMARK 500    PRO G1026       94.27    -66.66                                   
REMARK 500    ASN G1110      112.06   -163.86                                   
REMARK 500    ARG H1430      170.93    -26.99                                   
REMARK 500    LYS H1431      103.85    178.36                                   
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 131         0.05    SIDE_CHAIN                              
REMARK 500     DG J 214         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AOI   RELATED DB: PDB                                   
REMARK 900 XENOPUS NUCLEOSOME STRUCTURE                                         
REMARK 900 RELATED ID: 1ID3   RELATED DB: PDB                                   
REMARK 900 YEAST NUCLEOSOME STRUCTURE                                           
REMARK 900 RELATED ID: 2CV5   RELATED DB: PDB                                   
REMARK 900 HUMAN NUCLEOSOME STRUCTURE                                           
DBREF  2NQB A  401   535  UNP    P02299   H3_DROME         1    135             
DBREF  2NQB E  601   735  UNP    P02299   H3_DROME         1    135             
DBREF  2NQB B    1   102  UNP    P84040   H4_DROME         1    102             
DBREF  2NQB F  201   302  UNP    P84040   H4_DROME         1    102             
DBREF  2NQB C  802   924  UNP    P84051   H2A_DROME        1    123             
DBREF  2NQB G 1002  1124  UNP    P84051   H2A_DROME        1    123             
DBREF  2NQB D 1200  1322  UNP    P02283   H2B_DROME        1    123             
DBREF  2NQB H 1400  1522  UNP    P02283   H2B_DROME        1    123             
DBREF  2NQB I    1   146  PDB    2NQB     2NQB             1    146             
DBREF  2NQB J  147   292  PDB    2NQB     2NQB           147    292             
SEQADV 2NQB ILE B    0  UNP  P84040              EXPRESSION TAG                 
SEQADV 2NQB ILE F  200  UNP  P84040              EXPRESSION TAG                 
SEQADV 2NQB ILE D 1200  UNP  P02283              EXPRESSION TAG                 
SEQADV 2NQB THR D 1240  UNP  P02283    LYS    40 ENGINEERED                     
SEQADV 2NQB ILE H 1400  UNP  P02283              EXPRESSION TAG                 
SEQADV 2NQB THR H 1440  UNP  P02283    LYS    40 ENGINEERED                     
SEQRES   1 I  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 I  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 I  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 I  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 I  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 I  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 I  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 I  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 I  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 I  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 I  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 I  146   DG  DA  DT                                                  
SEQRES   1 J  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 J  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 J  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 J  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 J  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 J  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 J  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 J  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 J  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 J  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 J  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 J  146   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  103  ILE THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS          
SEQRES   2 B  103  GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN          
SEQRES   3 B  103  ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA          
SEQRES   4 B  103  ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR          
SEQRES   5 B  103  GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN          
SEQRES   6 B  103  VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS          
SEQRES   7 B  103  ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU          
SEQRES   8 B  103  LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY              
SEQRES   1 C  123  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 C  123  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 C  123  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 C  123  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 C  123  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 C  123  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 C  123  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 C  123  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 C  123  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 C  123  LYS THR GLU LYS LYS ALA                                      
SEQRES   1 D  123  ILE PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA          
SEQRES   2 D  123  GLY LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS          
SEQRES   3 D  123  LYS LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE          
SEQRES   4 D  123  TYR THR VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE          
SEQRES   5 D  123  SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN          
SEQRES   6 D  123  ASP ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU          
SEQRES   7 D  123  ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU          
SEQRES   8 D  123  ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU          
SEQRES   9 D  123  ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR          
SEQRES  10 D  123  LYS 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  103  ILE THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS          
SEQRES   2 F  103  GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN          
SEQRES   3 F  103  ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA          
SEQRES   4 F  103  ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR          
SEQRES   5 F  103  GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN          
SEQRES   6 F  103  VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS          
SEQRES   7 F  103  ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU          
SEQRES   8 F  103  LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY              
SEQRES   1 G  123  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 G  123  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 G  123  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 G  123  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 G  123  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 G  123  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 G  123  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 G  123  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 G  123  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 G  123  LYS THR GLU LYS LYS ALA                                      
SEQRES   1 H  123  ILE PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA          
SEQRES   2 H  123  GLY LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS          
SEQRES   3 H  123  LYS LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE          
SEQRES   4 H  123  TYR THR VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE          
SEQRES   5 H  123  SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN          
SEQRES   6 H  123  ASP ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU          
SEQRES   7 H  123  ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU          
SEQRES   8 H  123  ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU          
SEQRES   9 H  123  ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR          
SEQRES  10 H  123  LYS TYR THR SER SER LYS                                      
FORMUL  11  HOH   *264(H2 O)                                                    
HELIX    1   1 GLY A  444  SER A  457  1                                  14    
HELIX    2   2 ARG A  463  ASP A  477  1                                  15    
HELIX    3   3 GLN A  485  ALA A  514  1                                  30    
HELIX    4   4 MET A  520  ARG A  531  1                                  12    
HELIX    5   5 ASP B   24  ILE B   29  5                                   6    
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  816  GLY C  822  1                                   7    
HELIX   10  10 PRO C  826  GLY C  837  1                                  12    
HELIX   11  11 ALA C  845  ASN C  873  1                                  29    
HELIX   12  12 ILE C  879  ASN C  889  1                                  11    
HELIX   13  13 ASP C  890  LEU C  897  1                                   8    
HELIX   14  14 GLN C  912  LEU C  916  5                                   5    
HELIX   15  15 TYR D 1234  HIS D 1246  1                                  13    
HELIX   16  16 SER D 1252  ASN D 1281  1                                  30    
HELIX   17  17 THR D 1287  LEU D 1299  1                                  13    
HELIX   18  18 PRO D 1300  SER D 1321  1                                  22    
HELIX   19  19 GLY E  644  SER E  657  1                                  14    
HELIX   20  20 ARG E  663  LYS E  679  1                                  17    
HELIX   21  21 GLN E  685  ALA E  714  1                                  30    
HELIX   22  22 MET E  720  GLY E  732  1                                  13    
HELIX   23  23 ASP F  224  ILE F  229  5                                   6    
HELIX   24  24 THR F  230  GLY F  241  1                                  12    
HELIX   25  25 LEU F  249  ALA F  276  1                                  28    
HELIX   26  26 THR F  282  GLN F  293  1                                  12    
HELIX   27  27 SER G 1016  GLY G 1022  1                                   7    
HELIX   28  28 PRO G 1026  GLY G 1037  1                                  12    
HELIX   29  29 ALA G 1045  ASN G 1073  1                                  29    
HELIX   30  30 ILE G 1079  ASN G 1089  1                                  11    
HELIX   31  31 ASP G 1090  LEU G 1097  1                                   8    
HELIX   32  32 GLN G 1112  LEU G 1116  5                                   5    
HELIX   33  33 TYR H 1434  HIS H 1446  1                                  13    
HELIX   34  34 SER H 1452  ASN H 1481  1                                  30    
HELIX   35  35 THR H 1487  LEU H 1499  1                                  13    
HELIX   36  36 PRO H 1500  SER H 1520  1                                  21    
SHEET    1   A 2 ARG A 483  PHE A 484  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A 483           
SHEET    1   B 2 THR A 518  ILE A 519  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 519           
SHEET    1   C 2 LEU B  97  TYR B  98  0                                        
SHEET    2   C 2 THR G1101  ILE G1102  1  O  THR G1101   N  TYR B  98           
SHEET    1   D 2 ARG C 842  VAL C 843  0                                        
SHEET    2   D 2 THR D1285  ILE D1286  1  O  ILE D1286   N  ARG C 842           
SHEET    1   E 2 ARG C 877  ILE C 878  0                                        
SHEET    2   E 2 GLY D1250  ILE D1251  1  O  GLY D1250   N  ILE C 878           
SHEET    1   F 2 VAL C 900  ILE C 902  0                                        
SHEET    2   F 2 THR F 296  TYR F 298  1  O  TYR F 298   N  THR C 901           
SHEET    1   G 2 ARG E 683  PHE E 684  0                                        
SHEET    2   G 2 THR F 280  VAL F 281  1  O  VAL F 281   N  ARG E 683           
SHEET    1   H 2 THR E 718  ILE E 719  0                                        
SHEET    2   H 2 ARG F 245  ILE F 246  1  O  ARG F 245   N  ILE E 719           
SHEET    1   I 2 ARG G1042  VAL G1043  0                                        
SHEET    2   I 2 THR H1485  ILE H1486  1  O  ILE H1486   N  ARG G1042           
SHEET    1   J 2 ARG G1077  ILE G1078  0                                        
SHEET    2   J 2 GLY H1450  ILE H1451  1  O  GLY H1450   N  ILE G1078           
CRYST1  106.143  109.581  182.045  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      0.009421  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005493        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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