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Database: PDB
Entry: 6PWE
LinkDB: 6PWE
Original site: 6PWE 
HEADER    STRUCTURAL PROTEIN/DNA                  22-JUL-19   6PWE              
TITLE     CRYO-EM STRUCTURE OF NUCLEOSOME CORE PARTICLE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3;                                                
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H4;                                                
COMPND   7 CHAIN: B, F;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HISTONE H2A;                                               
COMPND  11 CHAIN: C, G;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HISTONE H2B;                                               
COMPND  15 CHAIN: D, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: DNA (147-MER);                                             
COMPND  19 CHAIN: I;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: DNA (147-MER);                                             
COMPND  23 CHAIN: J;                                                            
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: HIS3, HIS3:CG31613, CG31613, HIS3:CG33803, CG33803,            
SOURCE   6 HIS3:CG33806, CG33806, HIS3:CG33809, CG33809, HIS3:CG33812, CG33812, 
SOURCE   7 HIS3:CG33815, CG33815, HIS3:CG33818, CG33818, HIS3:CG33821, CG33821, 
SOURCE   8 HIS3:CG33824, CG33824, HIS3:CG33827, CG33827, HIS3:CG33830, CG33830, 
SOURCE   9 HIS3:CG33833, CG33833, HIS3:CG33836, CG33836, HIS3:CG33839, CG33839, 
SOURCE  10 HIS3:CG33842, CG33842, HIS3:CG33845, CG33845, HIS3:CG33848, CG33848, 
SOURCE  11 HIS3:CG33851, CG33851, HIS3:CG33854, CG33854, HIS3:CG33857, CG33857, 
SOURCE  12 HIS3:CG33860, CG33860, HIS3:CG33863, CG33863, HIS3:CG33866, CG33866; 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 2;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  17 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  18 ORGANISM_TAXID: 7227;                                                
SOURCE  19 GENE: HIS4R, BCDNA:RH52884, CG3379, DMEL\CG3379, FBTR0082962, H4R,   
SOURCE  20 HIS4-88CD, HIS4R, CG3379, DMEL_CG3379;                               
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  25 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  26 ORGANISM_TAXID: 7227;                                                
SOURCE  27 GENE: HIS2A, H2A, HIS2A:CG31618, CG31618, HIS2A:CG33808, CG33808,    
SOURCE  28 HIS2A:CG33814, CG33814, HIS2A:CG33817, CG33817, HIS2A:CG33820,       
SOURCE  29 CG33820, HIS2A:CG33823, CG33823, HIS2A:CG33826, CG33826,             
SOURCE  30 HIS2A:CG33829, CG33829, HIS2A:CG33832, CG33832, HIS2A:CG33835,       
SOURCE  31 CG33835, HIS2A:CG33838, CG33838, HIS2A:CG33841, CG33841,             
SOURCE  32 HIS2A:CG33844, CG33844, HIS2A:CG33847, CG33847, HIS2A:CG33850,       
SOURCE  33 CG33850, HIS2A:CG33862, CG33862, HIS2A:CG33865, CG33865;             
SOURCE  34 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  36 MOL_ID: 4;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  38 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  39 ORGANISM_TAXID: 7227;                                                
SOURCE  40 GENE: HIS2B, HIS2B:CG17949, CG17949, HIS2B:CG33868, CG33868,         
SOURCE  41 HIS2B:CG33870, CG33870, HIS2B:CG33872, CG33872, HIS2B:CG33874,       
SOURCE  42 CG33874, HIS2B:CG33876, CG33876, HIS2B:CG33878, CG33878,             
SOURCE  43 HIS2B:CG33880, CG33880, HIS2B:CG33882, CG33882, HIS2B:CG33884,       
SOURCE  44 CG33884, HIS2B:CG33886, CG33886, HIS2B:CG33888, CG33888,             
SOURCE  45 HIS2B:CG33890, CG33890, HIS2B:CG33892, CG33892, HIS2B:CG33894,       
SOURCE  46 CG33894, HIS2B:CG33896, CG33896, HIS2B:CG33898, CG33898,             
SOURCE  47 HIS2B:CG33900, CG33900, HIS2B:CG33902, CG33902, HIS2B:CG33904,       
SOURCE  48 CG33904, HIS2B:CG33906, CG33906, HIS2B:CG33908, CG33908,             
SOURCE  49 HIS2B:CG33910, CG33910;                                              
SOURCE  50 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  51 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  52 MOL_ID: 5;                                                           
SOURCE  53 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  54 ORGANISM_TAXID: 32630;                                               
SOURCE  55 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  56 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  57 MOL_ID: 6;                                                           
SOURCE  58 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  59 ORGANISM_TAXID: 32630;                                               
SOURCE  60 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  61 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOSOME, HISTONE, DNA, DNA-BINDING PROTEIN, STRUCTURAL PROTEIN-DNA 
KEYWDS   2 COMPLEX                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.CHITTORI,S.SUBRAMANIAM                                              
REVDAT   4   04-DEC-19 6PWE    1       REMARK                                   
REVDAT   3   02-OCT-19 6PWE    1       JRNL                                     
REVDAT   2   28-AUG-19 6PWE    1       JRNL                                     
REVDAT   1   21-AUG-19 6PWE    0                                                
JRNL        AUTH   S.CHITTORI,J.HONG,Y.BAI,S.SUBRAMANIAM                        
JRNL        TITL   STRUCTURE OF THE PRIMED STATE OF THE ATPASE DOMAIN OF        
JRNL        TITL 2 CHROMATIN REMODELING FACTOR ISWI BOUND TO THE NUCLEOSOME.    
JRNL        REF    NUCLEIC ACIDS RES.            V.  47  9400 2019              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   31402386                                                     
JRNL        DOI    10.1093/NAR/GKZ670                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.950                          
REMARK   3   NUMBER OF PARTICLES               : 52917                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6PWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241415.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : NUCLEOSOME CORE PARTICLE          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : UNSPECIFIED                       
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 39.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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     MET A     0                                                      
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     LYS A    37                                                      
REMARK 465     ARG A   134                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     MET 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     LEU B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     MET C     0                                                      
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     ALA C    13                                                      
REMARK 465     LYS C   117                                                      
REMARK 465     LYS C   118                                                      
REMARK 465     THR C   119                                                      
REMARK 465     GLU C   120                                                      
REMARK 465     LYS C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     ALA C   123                                                      
REMARK 465     MET D     0                                                      
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     LYS D   122                                                      
REMARK 465     MET E     0                                                      
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     LYS E    37                                                      
REMARK 465     ARG E   134                                                      
REMARK 465     ALA E   135                                                      
REMARK 465     MET F     0                                                      
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     ALA F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     ARG F    17                                                      
REMARK 465     HIS F    18                                                      
REMARK 465     ARG F    19                                                      
REMARK 465     LYS F    20                                                      
REMARK 465     VAL F    21                                                      
REMARK 465     LEU F    22                                                      
REMARK 465     ARG F    23                                                      
REMARK 465     MET G     0                                                      
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     GLY G    11                                                      
REMARK 465     LYS G    12                                                      
REMARK 465     ALA G    13                                                      
REMARK 465     LYS G   117                                                      
REMARK 465     LYS G   118                                                      
REMARK 465     THR G   119                                                      
REMARK 465     GLU G   120                                                      
REMARK 465     LYS G   121                                                      
REMARK 465     LYS G   122                                                      
REMARK 465     ALA G   123                                                      
REMARK 465     MET H     0                                                      
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 465     LYS H   122                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DA I -55   O3'    DA I -55   C3'    -0.036                       
REMARK 500     DG I  27   O3'    DG I  27   C3'    -0.043                       
REMARK 500     DG I  38   O3'    DG I  38   C3'    -0.046                       
REMARK 500     DA J  16   O3'    DA J  16   C3'    -0.041                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT I -57   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC I -52   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC I -25   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT I  22   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DC J -27   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA J  -9   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC J  -4   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DA J  59   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA J  63   O4' -  C1' -  N9  ANGL. DEV. =   2.0 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    ASP A  81       63.78     60.14                                   
REMARK 500    PRO A 121        0.47    -64.16                                   
REMARK 500    VAL B  65      -53.34   -122.69                                   
REMARK 500    ARG C  34      -30.38   -131.94                                   
REMARK 500    GLN C 103       47.51     38.54                                   
REMARK 500    LYS D  31      178.82    167.23                                   
REMARK 500    GLU D 102       -7.46     71.62                                   
REMARK 500    LYS E  56      -30.01   -130.74                                   
REMARK 500    ASP E  81       63.78     60.19                                   
REMARK 500    PRO E 121        0.54    -64.23                                   
REMARK 500    VAL F  65      -53.29   -122.75                                   
REMARK 500    ARG G  34      -30.48   -131.85                                   
REMARK 500    GLN G 103       47.61     38.45                                   
REMARK 500    LYS H  31      178.83    167.25                                   
REMARK 500    GLU H 102       -7.47     71.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS D   29     ARG D   30                 -127.05                    
REMARK 500 ARG D   30     LYS D   31                  140.19                    
REMARK 500 LYS H   29     ARG H   30                 -127.10                    
REMARK 500 ARG H   30     LYS H   31                  140.22                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-20506   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF NUCLEOSOME CORE PARTICLE                        
REMARK 900 RELATED ID: EMD-20507   RELATED DB: EMDB                             
DBREF  6PWE A    0   135  UNP    P02299   H3_DROME         1    136             
DBREF1 6PWE B    0   102  UNP                  A0A0B4KFZ9_DROME                 
DBREF2 6PWE B     A0A0B4KFZ9                          1         103             
DBREF  6PWE C    0   123  UNP    P84051   H2A_DROME        1    124             
DBREF  6PWE D    0   122  UNP    P02283   H2B_DROME        1    123             
DBREF  6PWE E    0   135  UNP    P02299   H3_DROME         1    136             
DBREF1 6PWE F    0   102  UNP                  A0A0B4KFZ9_DROME                 
DBREF2 6PWE F     A0A0B4KFZ9                          1         103             
DBREF  6PWE G    0   123  UNP    P84051   H2A_DROME        1    124             
DBREF  6PWE H    0   122  UNP    P02283   H2B_DROME        1    123             
DBREF  6PWE I  -73    73  PDB    6PWE     6PWE           -73     73             
DBREF  6PWE J  -73    73  PDB    6PWE     6PWE           -73     73             
SEQRES   1 A  136  MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY          
SEQRES   2 A  136  GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA          
SEQRES   3 A  136  ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO          
SEQRES   4 A  136  HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE          
SEQRES   5 A  136  ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS          
SEQRES   6 A  136  LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP          
SEQRES   7 A  136  PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET          
SEQRES   8 A  136  ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU          
SEQRES   9 A  136  PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG          
SEQRES  10 A  136  VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG          
SEQRES  11 A  136  ILE ARG GLY GLU ARG ALA                                      
SEQRES   1 B  103  MET 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  124  MET SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS          
SEQRES   2 C  124  ALA LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO          
SEQRES   3 C  124  VAL GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR          
SEQRES   4 C  124  ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA          
SEQRES   5 C  124  ALA VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU          
SEQRES   6 C  124  ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE          
SEQRES   7 C  124  ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU          
SEQRES   8 C  124  GLU LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN          
SEQRES   9 C  124  GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO          
SEQRES  10 C  124  LYS LYS THR GLU LYS LYS ALA                                  
SEQRES   1 D  123  MET 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 LYS 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  136  MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY          
SEQRES   2 E  136  GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA          
SEQRES   3 E  136  ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO          
SEQRES   4 E  136  HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE          
SEQRES   5 E  136  ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS          
SEQRES   6 E  136  LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP          
SEQRES   7 E  136  PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET          
SEQRES   8 E  136  ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU          
SEQRES   9 E  136  PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG          
SEQRES  10 E  136  VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG          
SEQRES  11 E  136  ILE ARG GLY GLU ARG ALA                                      
SEQRES   1 F  103  MET 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  124  MET SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS          
SEQRES   2 G  124  ALA LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO          
SEQRES   3 G  124  VAL GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR          
SEQRES   4 G  124  ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA          
SEQRES   5 G  124  ALA VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU          
SEQRES   6 G  124  ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE          
SEQRES   7 G  124  ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU          
SEQRES   8 G  124  GLU LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN          
SEQRES   9 G  124  GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO          
SEQRES  10 G  124  LYS LYS THR GLU LYS LYS ALA                                  
SEQRES   1 H  123  MET 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 LYS 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                                      
SEQRES   1 I  147   DA  DT  DC  DG  DG  DA  DT  DG  DT  DA  DT  DA  DT          
SEQRES   2 I  147   DA  DT  DC  DT  DG  DA  DC  DA  DC  DG  DT  DG  DC          
SEQRES   3 I  147   DC  DT  DG  DG  DA  DG  DA  DC  DT  DA  DG  DG  DG          
SEQRES   4 I  147   DA  DG  DT  DA  DA  DT  DC  DC  DC  DC  DT  DT  DG          
SEQRES   5 I  147   DG  DC  DG  DG  DT  DT  DA  DA  DA  DA  DC  DG  DC          
SEQRES   6 I  147   DG  DG  DG  DG  DG  DA  DC  DA  DG  DC  DG  DC  DG          
SEQRES   7 I  147   DT  DA  DC  DG  DT  DG  DC  DG  DT  DT  DT  DA  DA          
SEQRES   8 I  147   DG  DC  DG  DG  DT  DG  DC  DT  DA  DG  DA  DG  DC          
SEQRES   9 I  147   DT  DG  DT  DC  DT  DA  DC  DG  DA  DC  DC  DA  DA          
SEQRES  10 I  147   DT  DT  DG  DA  DG  DC  DG  DG  DC  DC  DT  DC  DG          
SEQRES  11 I  147   DG  DC  DA  DC  DC  DG  DG  DG  DA  DT  DT  DC  DT          
SEQRES  12 I  147   DC  DG  DA  DT                                              
SEQRES   1 J  147   DA  DT  DC  DG  DA  DG  DA  DA  DT  DC  DC  DC  DG          
SEQRES   2 J  147   DG  DT  DG  DC  DC  DG  DA  DG  DG  DC  DC  DG  DC          
SEQRES   3 J  147   DT  DC  DA  DA  DT  DT  DG  DG  DT  DC  DG  DT  DA          
SEQRES   4 J  147   DG  DA  DC  DA  DG  DC  DT  DC  DT  DA  DG  DC  DA          
SEQRES   5 J  147   DC  DC  DG  DC  DT  DT  DA  DA  DA  DC  DG  DC  DA          
SEQRES   6 J  147   DC  DG  DT  DA  DC  DG  DC  DG  DC  DT  DG  DT  DC          
SEQRES   7 J  147   DC  DC  DC  DC  DG  DC  DG  DT  DT  DT  DT  DA  DA          
SEQRES   8 J  147   DC  DC  DG  DC  DC  DA  DA  DG  DG  DG  DG  DA  DT          
SEQRES   9 J  147   DT  DA  DC  DT  DC  DC  DC  DT  DA  DG  DT  DC  DT          
SEQRES  10 J  147   DC  DC  DA  DG  DG  DC  DA  DC  DG  DT  DG  DT  DC          
SEQRES  11 J  147   DA  DG  DA  DT  DA  DT  DA  DT  DA  DC  DA  DT  DC          
SEQRES  12 J  147   DC  DG  DA  DT                                              
HELIX    1 AA1 VAL A   46  GLU A   50  5                                   5    
HELIX    2 AA2 LYS A   64  ALA A   75  1                                  12    
HELIX    3 AA3 ALA A   88  GLU A  105  1                                  18    
HELIX    4 AA4 ASN A  108  HIS A  113  1                                   6    
HELIX    5 AA5 MET A  120  ARG A  128  1                                   9    
HELIX    6 AA6 ASP B   24  ILE B   29  5                                   6    
HELIX    7 AA7 THR B   30  ARG B   39  1                                  10    
HELIX    8 AA8 LEU B   49  GLU B   63  1                                  15    
HELIX    9 AA9 ILE B   66  ALA B   76  1                                  11    
HELIX   10 AB1 THR B   82  GLN B   93  1                                  12    
HELIX   11 AB2 ARG C   16  GLY C   21  1                                   6    
HELIX   12 AB3 ARG C   28  LEU C   33  1                                   6    
HELIX   13 AB4 GLY C   45  ASN C   72  1                                  28    
HELIX   14 AB5 ILE C   78  ASN C   88  1                                  11    
HELIX   15 AB6 ASP C   89  LYS C   94  1                                   6    
HELIX   16 AB7 TYR D   34  LYS D   43  1                                  10    
HELIX   17 AB8 LYS D   54  TYR D   80  1                                  27    
HELIX   18 AB9 THR D   87  ALA D   94  1                                   8    
HELIX   19 AC1 LEU D  103  LYS D  117  1                                  15    
HELIX   20 AC2 VAL E   46  GLU E   50  5                                   5    
HELIX   21 AC3 LYS E   64  ALA E   75  1                                  12    
HELIX   22 AC4 ALA E   88  GLU E  105  1                                  18    
HELIX   23 AC5 ASN E  108  HIS E  113  1                                   6    
HELIX   24 AC6 MET E  120  ARG E  128  1                                   9    
HELIX   25 AC7 ASP F   24  ILE F   29  5                                   6    
HELIX   26 AC8 THR F   30  ARG F   39  1                                  10    
HELIX   27 AC9 LEU F   49  GLU F   63  1                                  15    
HELIX   28 AD1 ILE F   66  ALA F   76  1                                  11    
HELIX   29 AD2 THR F   82  GLN F   93  1                                  12    
HELIX   30 AD3 ARG G   16  GLY G   21  1                                   6    
HELIX   31 AD4 ARG G   28  LEU G   33  1                                   6    
HELIX   32 AD5 GLY G   45  ASN G   72  1                                  28    
HELIX   33 AD6 ILE G   78  ASN G   88  1                                  11    
HELIX   34 AD7 ASP G   89  LYS G   94  1                                   6    
HELIX   35 AD8 TYR H   34  LYS H   43  1                                  10    
HELIX   36 AD9 LYS H   54  TYR H   80  1                                  27    
HELIX   37 AE1 THR H   87  ALA H   94  1                                   8    
HELIX   38 AE2 LEU H  103  LYS H  117  1                                  15    
SHEET    1 AA1 2 THR A 118  ILE A 119  0                                        
SHEET    2 AA1 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1 AA2 2 ARG C  41  VAL C  42  0                                        
SHEET    2 AA2 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  41           
SHEET    1 AA3 2 ARG C  76  ILE C  77  0                                        
SHEET    2 AA3 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  77           
SHEET    1 AA4 2 THR E 118  ILE E 119  0                                        
SHEET    2 AA4 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1 AA5 2 ARG G  41  VAL G  42  0                                        
SHEET    2 AA5 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  41           
SHEET    1 AA6 2 ARG G  76  ILE G  77  0                                        
SHEET    2 AA6 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  77           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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