GenomeNet

Database: PDB
Entry: 6PWF
LinkDB: 6PWF
Original site: 6PWF 
HEADER    STRUCTURAL PROTEIN/DNA                  22-JUL-19   6PWF              
TITLE     CRYO-EM STRUCTURE OF THE ATPASE DOMAIN OF CHROMATIN REMODELING FACTOR 
TITLE    2 ISWI BOUND TO THE NUCLEOSOME                                         
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;                                                     
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: CHROMATIN REMODELING FACTOR ISWI;                          
COMPND  27 CHAIN: K;                                                            
COMPND  28 FRAGMENT: UNP RESIDUES 77-134,167-722;                               
COMPND  29 SYNONYM: COMPLEX ATPASE-LIKE PROTEIN;                                
COMPND  30 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;                                        
SOURCE  62 MOL_ID: 7;                                                           
SOURCE  63 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM;                        
SOURCE  64 ORGANISM_TAXID: 209285;                                              
SOURCE  65 GENE: CTHT_0046320;                                                  
SOURCE  66 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  67 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOSOME, DNA-BINDING PROTEIN, ATP-DEPENDENT CHROMATIN REMODELER,   
KEYWDS   2 ISWI, STRUCTURAL PROTEIN-DNA COMPLEX                                 
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.CHITTORI,S.SUBRAMANIAM                                              
REVDAT   4   04-DEC-19 6PWF    1       REMARK                                   
REVDAT   3   02-OCT-19 6PWF    1       JRNL                                     
REVDAT   2   28-AUG-19 6PWF    1       JRNL                                     
REVDAT   1   21-AUG-19 6PWF    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.    4.07 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)  : 4.070                          
REMARK   3   NUMBER OF PARTICLES               : 32529                          
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 6PWF 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_1000241416.                                   
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                 : COMPLEX OF THE ATPASE DOMAIN OF   
REMARK 245                                    ISWI BOUND TO THE NUCLEOSOME;     
REMARK 245                                    NUCLEOSOME; ATPASE DOMAIN OF      
REMARK 245                                    ISWI                              
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: UNDECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K                                     
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     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   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     ARG D    28                                                      
REMARK 465     LYS D    29                                                      
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     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 465      DT I    73                                                      
REMARK 465      DA J   -73                                                      
REMARK 465     MET K    83                                                      
REMARK 465     ALA K    84                                                      
REMARK 465     HIS K    85                                                      
REMARK 465     HIS K    86                                                      
REMARK 465     HIS K    87                                                      
REMARK 465     HIS K    88                                                      
REMARK 465     HIS K    89                                                      
REMARK 465     HIS K    90                                                      
REMARK 465     GLY K    91                                                      
REMARK 465     HIS K    92                                                      
REMARK 465     HIS K    93                                                      
REMARK 465     HIS K    94                                                      
REMARK 465     GLU K    95                                                      
REMARK 465     ASN K    96                                                      
REMARK 465     LEU K    97                                                      
REMARK 465     TYR K    98                                                      
REMARK 465     PHE K    99                                                      
REMARK 465     GLN K   100                                                      
REMARK 465     GLY K   101                                                      
REMARK 465     SER K   102                                                      
REMARK 465     SER K   103                                                      
REMARK 465     SER K   104                                                      
REMARK 465     GLY K   105                                                      
REMARK 465     LYS K   106                                                      
REMARK 465     LYS K   107                                                      
REMARK 465     HIS K   108                                                      
REMARK 465     ASP K   109                                                      
REMARK 465     ARG K   110                                                      
REMARK 465     LEU K   111                                                      
REMARK 465     GLY K   112                                                      
REMARK 465     GLU K   113                                                      
REMARK 465     ASN K   114                                                      
REMARK 465     LYS K   115                                                      
REMARK 465     GLU K   116                                                      
REMARK 465     ASP K   117                                                      
REMARK 465     ASP K   118                                                      
REMARK 465     THR K   119                                                      
REMARK 465     LEU K   120                                                      
REMARK 465     ARG K   121                                                      
REMARK 465     ARG K   122                                                      
REMARK 465     PHE K   123                                                      
REMARK 465     ARG K   124                                                      
REMARK 465     TYR K   125                                                      
REMARK 465     LEU K   126                                                      
REMARK 465     LEU K   127                                                      
REMARK 465     GLY K   128                                                      
REMARK 465     LEU K   129                                                      
REMARK 465     THR K   130                                                      
REMARK 465     ASP K   131                                                      
REMARK 465     LEU K   132                                                      
REMARK 465     PHE K   133                                                      
REMARK 465     ARG K   134                                                      
REMARK 465     HIS K   135                                                      
REMARK 465     PHE K   136                                                      
REMARK 465     ILE K   137                                                      
REMARK 465     GLU K   138                                                      
REMARK 465     THR K   139                                                      
REMARK 465     ASN K   140                                                      
REMARK 465     PRO K   141                                                      
REMARK 465     ASN K   142                                                      
REMARK 465     PRO K   143                                                      
REMARK 465     LYS K   144                                                      
REMARK 465     ILE K   145                                                      
REMARK 465     ARG K   146                                                      
REMARK 465     GLU K   147                                                      
REMARK 465     ILE K   148                                                      
REMARK 465     MET K   149                                                      
REMARK 465     ALA K   150                                                      
REMARK 465     GLU K   151                                                      
REMARK 465     ILE K   152                                                      
REMARK 465     ASP K   153                                                      
REMARK 465     ARG K   154                                                      
REMARK 465     GLN K   155                                                      
REMARK 465     ASN K   156                                                      
REMARK 465     ALA K   157                                                      
REMARK 465     GLU K   158                                                      
REMARK 465     GLU K   159                                                      
REMARK 465     ALA K   160                                                      
REMARK 465     LYS K   161                                                      
REMARK 465     LYS K   162                                                      
REMARK 465     GLY K   163                                                      
REMARK 465     SER K   164                                                      
REMARK 465     SER K   165                                                      
REMARK 465     GLY K   166                                                      
REMARK 465     GLY K   167                                                      
REMARK 465     GLY K   168                                                      
REMARK 465     SER K   169                                                      
REMARK 465     ALA K   170                                                      
REMARK 465     GLU K   171                                                      
REMARK 465     THR K   172                                                      
REMARK 465     VAL K   173                                                      
REMARK 465     ASP K   437                                                      
REMARK 465     ALA K   438                                                      
REMARK 465     VAL K   439                                                      
REMARK 465     ASN K   440                                                      
REMARK 465     GLY K   441                                                      
REMARK 465     ALA K   442                                                      
REMARK 465     GLY K   443                                                      
REMARK 465     GLY K   444                                                      
REMARK 465     LYS K   445                                                      
REMARK 465     ARG K   446                                                      
REMARK 465     GLU K   447                                                      
REMARK 465     SER K   448                                                      
REMARK 465     LYS K   449                                                      
REMARK 465     GLY K   641                                                      
REMARK 465     ARG K   642                                                      
REMARK 465     ALA K   643                                                      
REMARK 465     GLN K   644                                                      
REMARK 465     ILE K   645                                                      
REMARK 465     ALA K   646                                                      
REMARK 465     THR K   647                                                      
REMARK 465     LYS K   648                                                      
REMARK 465     ALA K   649                                                      
REMARK 465     ALA K   650                                                      
REMARK 465     ALA K   651                                                      
REMARK 465     ASN K   652                                                      
REMARK 465     LYS K   653                                                      
REMARK 465     GLU K   654                                                      
REMARK 465     GLU K   655                                                      
REMARK 465     LEU K   656                                                      
REMARK 465     LEU K   657                                                      
REMARK 465     SER K   658                                                      
REMARK 465     MET K   659                                                      
REMARK 465     ILE K   660                                                      
REMARK 465     GLN K   661                                                      
REMARK 465     HIS K   662                                                      
REMARK 465     GLY K   663                                                      
REMARK 465     ALA K   664                                                      
REMARK 465     GLU K   665                                                      
REMARK 465     LYS K   666                                                      
REMARK 465     VAL K   667                                                      
REMARK 465     PHE K   668                                                      
REMARK 465     GLN K   669                                                      
REMARK 465     THR K   670                                                      
REMARK 465     LYS K   671                                                      
REMARK 465     GLY K   672                                                      
REMARK 465     ALA K   673                                                      
REMARK 465     PHE K   674                                                      
REMARK 465     GLY K   675                                                      
REMARK 465     LEU K   676                                                      
REMARK 465     MET K   677                                                      
REMARK 465     ALA K   678                                                      
REMARK 465     GLU K   679                                                      
REMARK 465     LYS K   680                                                      
REMARK 465     GLY K   681                                                      
REMARK 465     ALA K   682                                                      
REMARK 465     ASN K   683                                                      
REMARK 465     LEU K   684                                                      
REMARK 465     ASP K   685                                                      
REMARK 465     ASP K   686                                                      
REMARK 465     ASP K   687                                                      
REMARK 465     ASP K   688                                                      
REMARK 465     ILE K   689                                                      
REMARK 465     ASP K   690                                                      
REMARK 465     ALA K   691                                                      
REMARK 465     ILE K   692                                                      
REMARK 465     LEU K   693                                                      
REMARK 465     LYS K   694                                                      
REMARK 465     ALA K   695                                                      
REMARK 465     GLY K   696                                                      
REMARK 465     GLU K   697                                                      
REMARK 465     GLU K   698                                                      
REMARK 465     ARG K   699                                                      
REMARK 465     THR K   700                                                      
REMARK 465     ARG K   701                                                      
REMARK 465     GLU K   702                                                      
REMARK 465     LEU K   703                                                      
REMARK 465     ASN K   704                                                      
REMARK 465     ALA K   705                                                      
REMARK 465     LYS K   706                                                      
REMARK 465     TYR K   707                                                      
REMARK 465     GLU K   708                                                      
REMARK 465     LYS K   709                                                      
REMARK 465     LEU K   710                                                      
REMARK 465     GLY K   711                                                      
REMARK 465     ILE K   712                                                      
REMARK 465     ASP K   713                                                      
REMARK 465     ASP K   714                                                      
REMARK 465     LEU K   715                                                      
REMARK 465     GLN K   716                                                      
REMARK 465     LYS K   717                                                      
REMARK 465     PHE K   718                                                      
REMARK 465     THR K   719                                                      
REMARK 465     SER K   720                                                      
REMARK 465     GLU K   721                                                      
REMARK 465     SER K   722                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     ARG B  17    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B  18    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     VAL B  21    CG1  CG2                                            
REMARK 470     LEU B  22    CG   CD1  CD2                                       
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE K 174    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG K 175    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU K 176    CG   CD   OE1  OE2                                  
REMARK 470     SER K 177    OG                                                  
REMARK 470     PHE K 180    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE K 181    CG1  CG2  CD1                                       
REMARK 470     LYS K 182    CG   CD   CE   NZ                                   
REMARK 470     THR K 184    OG1  CG2                                            
REMARK 470     MET K 185    CG   SD   CE                                        
REMARK 470     ASP K 187    CG   OD1  OD2                                       
REMARK 470     TYR K 188    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN K 189    CG   CD   OE1  NE2                                  
REMARK 470     ILE K 190    CG1  CG2  CD1                                       
REMARK 470     LEU K 193    CG   CD1  CD2                                       
REMARK 470     ASN K 194    CG   OD1  ND2                                       
REMARK 470     TRP K 195    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K 195    CZ3  CH2                                            
REMARK 470     LEU K 196    CG   CD1  CD2                                       
REMARK 470     ILE K 197    CG1  CG2  CD1                                       
REMARK 470     LEU K 199    CG   CD1  CD2                                       
REMARK 470     HIS K 200    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN K 202    CG   OD1  ND2                                       
REMARK 470     ILE K 204    CG1  CG2  CD1                                       
REMARK 470     SER K 205    OG                                                  
REMARK 470     GLU K 211    CG   CD   OE1  OE2                                  
REMARK 470     THR K 217    OG1  CG2                                            
REMARK 470     LEU K 218    CG   CD1  CD2                                       
REMARK 470     LEU K 227    CG   CD1  CD2                                       
REMARK 470     HIS K 229    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE K 230    CG1  CG2  CD1                                       
REMARK 470     GLN K 231    CG   CD   OE1  NE2                                  
REMARK 470     GLU K 252    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 254    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 255    CG   CD   CE   NZ                                   
REMARK 470     ASP K 259    CG   OD1  OD2                                       
REMARK 470     LYS K 269    CG   CD   CE   NZ                                   
REMARK 470     GLU K 270    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 271    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 293    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 322    CG   CD   OE1  OE2                                  
REMARK 470     MET K 331    CG   SD   CE                                        
REMARK 470     ARG K 335    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN K 336    CG   OD1  ND2                                       
REMARK 470     ARG K 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K 346    CG   CD   OE1  NE2                                  
REMARK 470     ASN K 347    CG   OD1  ND2                                       
REMARK 470     ASN K 348    CG   OD1  ND2                                       
REMARK 470     LEU K 349    CG   CD1  CD2                                       
REMARK 470     GLU K 351    CG   CD   OE1  OE2                                  
REMARK 470     ASN K 357    CG   OD1  ND2                                       
REMARK 470     ASP K 362    CG   OD1  OD2                                       
REMARK 470     VAL K 363    CG1  CG2                                            
REMARK 470     PHE K 364    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP K 366    CG   OD1  OD2                                       
REMARK 470     SER K 367    OG                                                  
REMARK 470     ASP K 368    CG   OD1  OD2                                       
REMARK 470     PHE K 370    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN K 372    CG   CD   OE1  NE2                                  
REMARK 470     TRP K 373    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K 373    CZ3  CH2                                            
REMARK 470     ARG K 375    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K 377    CG   CD   OE1  NE2                                  
REMARK 470     ASP K 378    CG   OD1  OD2                                       
REMARK 470     ARG K 379    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K 381    CG   CD   OE1  NE2                                  
REMARK 470     ASP K 382    CG   OD1  OD2                                       
REMARK 470     GLN K 383    CG   CD   OE1  NE2                                  
REMARK 470     VAL K 384    CG1  CG2                                            
REMARK 470     GLN K 386    CG   CD   OE1  NE2                                  
REMARK 470     LEU K 388    CG   CD1  CD2                                       
REMARK 470     ARG K 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL K 391    CG1  CG2                                            
REMARK 470     LEU K 392    CG   CD1  CD2                                       
REMARK 470     ARG K 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K 399    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 401    CG   CD   CE   NZ                                   
REMARK 470     ASP K 403    CG   OD1  OD2                                       
REMARK 470     GLU K 405    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 406    CG   CD   CE   NZ                                   
REMARK 470     SER K 407    OG                                                  
REMARK 470     LYS K 411    CG   CD   CE   NZ                                   
REMARK 470     LYS K 412    CG   CD   CE   NZ                                   
REMARK 470     GLU K 413    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 422    CG   CD   OE1  OE2                                  
REMARK 470     GLN K 424    CG   CD   OE1  NE2                                  
REMARK 470     LYS K 426    CG   CD   CE   NZ                                   
REMARK 470     LYS K 429    CG   CD   CE   NZ                                   
REMARK 470     LYS K 430    CG   CD   CE   NZ                                   
REMARK 470     LEU K 432    CG   CD1  CD2                                       
REMARK 470     GLU K 433    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 434    CG   CD   CE   NZ                                   
REMARK 470     ASP K 435    CG   OD1  OD2                                       
REMARK 470     ILE K 436    CG1  CG2  CD1                                       
REMARK 470     GLN K 458    CG   CD   OE1  NE2                                  
REMARK 470     HIS K 465    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU K 470    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 473    CG   CD   OE1  OE2                                  
REMARK 470     ASP K 481    CG   OD1  OD2                                       
REMARK 470     HIS K 483    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU K 484    CG   CD1  CD2                                       
REMARK 470     ASP K 495    CG   OD1  OD2                                       
REMARK 470     LEU K 498    CG   CD1  CD2                                       
REMARK 470     ASP K 519    CG   OD1  OD2                                       
REMARK 470     ASP K 549    CG   OD1  OD2                                       
REMARK 470     GLU K 550    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 558    CG   CD   CE   NZ                                   
REMARK 470     ARG K 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN K 573    CG   OD1  ND2                                       
REMARK 470     ASP K 586    CG   OD1  OD2                                       
REMARK 470     LEU K 593    CG   CD1  CD2                                       
REMARK 470     GLN K 594    CG   CD   OE1  NE2                                  
REMARK 470     ILE K 602    CG1  CG2  CD1                                       
REMARK 470     THR K 605    OG1  CG2                                            
REMARK 470     LYS K 606    CG   CD   CE   NZ                                   
REMARK 470     GLN K 607    CG   CD   OE1  NE2                                  
REMARK 470     GLU K 625    CG   CD   OE1  OE2                                  
REMARK 470     ARG K 632    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU K 633    CG   CD1  CD2                                       
REMARK 470     GLN K 639    CG   CD   OE1  NE2                                  
REMARK 470     GLN K 640    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OP1   DA J    23     ND2  ASN K   588              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC J  -4   O3'    DC J  -4   C3'    -0.042                       
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     DA I -60   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DG I -44   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DG I -44   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA I -31   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC I  -2   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DT I  14   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC I  19   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT I  25   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DA J -31   O4' -  C4' -  C3' ANGL. DEV. =  -2.9 DEGREES          
REMARK 500     DT J -26   C3' -  C2' -  C1' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DT J -26   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC J -10   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG J  26   C3' -  C2' -  C1' ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DA J  63   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN B  93       30.48    -90.81                                   
REMARK 500    LEU C  22     -169.58   -127.50                                   
REMARK 500    GLN F  27        1.45    -66.24                                   
REMARK 500    SER F  47     -167.62    -79.27                                   
REMARK 500    GLN G 103       36.12     39.90                                   
REMARK 500    PRO G 116     -175.71    -69.98                                   
REMARK 500    LYS H  31      -14.04     72.05                                   
REMARK 500    THR H  49     -168.99   -128.62                                   
REMARK 500    GLU H 102       -2.76     68.38                                   
REMARK 500    ALA H 114       30.76    -96.34                                   
REMARK 500    LYS K 182     -158.89    -81.00                                   
REMARK 500    THR K 184       70.58     58.08                                   
REMARK 500    ILE K 230      -60.72    -95.47                                   
REMARK 500    ASP K 284       57.12    -96.25                                   
REMARK 500    GLU K 308      -62.58    -94.76                                   
REMARK 500    SER K 323     -165.02    -79.22                                   
REMARK 500    THR K 341     -166.71   -123.35                                   
REMARK 500    LEU K 349       -9.88     72.91                                   
REMARK 500    PRO K 361       20.02    -78.51                                   
REMARK 500    PHE K 370       31.00    -87.47                                   
REMARK 500    PHE K 374      -32.60   -131.13                                   
REMARK 500    GLN K 377       97.97    -69.16                                   
REMARK 500    VAL K 384      -60.33   -125.28                                   
REMARK 500    LYS K 406       29.53     46.90                                   
REMARK 500    MET K 420     -167.01    -78.69                                   
REMARK 500    LEU K 453       70.02     60.65                                   
REMARK 500    MET K 514       73.72     63.37                                   
REMARK 500    SER K 556     -165.77    -78.16                                   
REMARK 500    TYR K 583      -65.47    -93.69                                   
REMARK 500    ARG K 612      148.54   -171.81                                   
REMARK 500    THR K 615     -164.69    -79.19                                   
REMARK 500    ASN K 617        6.00     59.74                                   
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 H   31     GLU H   32                  146.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-20507   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF THE ATPASE DOMAIN OF CHROMATIN REMODELING       
REMARK 900 FACTOR ISWI BOUND TO THE NUCLEOSOME                                  
REMARK 900 RELATED ID: EMD-20506   RELATED DB: EMDB                             
DBREF  6PWF A    0   135  UNP    P02299   H3_DROME         1    136             
DBREF1 6PWF B    0   102  UNP                  A0A0B4KFZ9_DROME                 
DBREF2 6PWF B     A0A0B4KFZ9                          1         103             
DBREF  6PWF C    0   123  UNP    P84051   H2A_DROME        1    124             
DBREF  6PWF D    0   122  UNP    P02283   H2B_DROME        1    123             
DBREF  6PWF E    0   135  UNP    P02299   H3_DROME         1    136             
DBREF1 6PWF F    0   102  UNP                  A0A0B4KFZ9_DROME                 
DBREF2 6PWF F     A0A0B4KFZ9                          1         103             
DBREF  6PWF G    0   123  UNP    P84051   H2A_DROME        1    124             
DBREF  6PWF H    0   122  UNP    P02283   H2B_DROME        1    123             
DBREF  6PWF I  -73    73  PDB    6PWF     6PWF           -73     73             
DBREF  6PWF J  -73    73  PDB    6PWF     6PWF           -73     73             
DBREF  6PWF K  105   162  UNP    G0S9L5   G0S9L5_CHATD    77    134             
DBREF  6PWF K  167   722  UNP    G0S9L5   G0S9L5_CHATD   167    722             
SEQADV 6PWF MET K   83  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF ALA K   84  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   85  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   86  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   87  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   88  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   89  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   90  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF GLY K   91  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   92  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   93  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF HIS K   94  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF GLU K   95  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF ASN K   96  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF LEU K   97  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF TYR K   98  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF PHE K   99  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF GLN K  100  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF GLY K  101  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF SER K  102  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF SER K  103  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF SER K  104  UNP  G0S9L5              EXPRESSION TAG                 
SEQADV 6PWF GLY K  163  UNP  G0S9L5              LINKER                         
SEQADV 6PWF SER K  164  UNP  G0S9L5              LINKER                         
SEQADV 6PWF SER K  165  UNP  G0S9L5              LINKER                         
SEQADV 6PWF GLY K  166  UNP  G0S9L5              LINKER                         
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                                              
SEQRES   1 K  640  MET ALA HIS HIS HIS HIS HIS HIS GLY HIS HIS HIS GLU          
SEQRES   2 K  640  ASN LEU TYR PHE GLN GLY SER SER SER GLY LYS LYS HIS          
SEQRES   3 K  640  ASP ARG LEU GLY GLU ASN LYS GLU ASP ASP THR LEU ARG          
SEQRES   4 K  640  ARG PHE ARG TYR LEU LEU GLY LEU THR ASP LEU PHE ARG          
SEQRES   5 K  640  HIS PHE ILE GLU THR ASN PRO ASN PRO LYS ILE ARG GLU          
SEQRES   6 K  640  ILE MET ALA GLU ILE ASP ARG GLN ASN ALA GLU GLU ALA          
SEQRES   7 K  640  LYS LYS GLY SER SER GLY GLY GLY SER ALA GLU THR VAL          
SEQRES   8 K  640  PHE ARG GLU SER PRO PRO PHE ILE LYS GLY THR MET ARG          
SEQRES   9 K  640  ASP TYR GLN ILE ALA GLY LEU ASN TRP LEU ILE SER LEU          
SEQRES  10 K  640  HIS GLU ASN GLY ILE SER GLY ILE LEU ALA ASP GLU MET          
SEQRES  11 K  640  GLY LEU GLY LYS THR LEU GLN THR ILE SER PHE LEU GLY          
SEQRES  12 K  640  TYR LEU ARG HIS ILE GLN GLY ILE THR GLY PRO HIS LEU          
SEQRES  13 K  640  VAL ALA VAL PRO LYS SER THR LEU ASP ASN TRP LYS ARG          
SEQRES  14 K  640  GLU PHE GLU LYS TRP THR PRO ASP VAL ASN VAL LEU VAL          
SEQRES  15 K  640  LEU GLN GLY ALA LYS GLU GLU ARG HIS GLN LEU ILE ASN          
SEQRES  16 K  640  ASP ARG LEU ILE ASP GLU ASP PHE ASP VAL CYS ILE THR          
SEQRES  17 K  640  SER TYR GLU MET ILE LEU ARG GLU LYS ALA HIS LEU LYS          
SEQRES  18 K  640  LYS PHE ALA TRP GLU TYR ILE ILE ILE ASP GLU ALA HIS          
SEQRES  19 K  640  ARG ILE LYS ASN GLU GLU SER SER LEU SER GLN VAL ILE          
SEQRES  20 K  640  ARG MET PHE SER SER ARG ASN ARG LEU LEU ILE THR GLY          
SEQRES  21 K  640  THR PRO LEU GLN ASN ASN LEU HIS GLU LEU TRP ALA LEU          
SEQRES  22 K  640  LEU ASN PHE LEU LEU PRO ASP VAL PHE GLY ASP SER ASP          
SEQRES  23 K  640  ALA PHE ASP GLN TRP PHE ARG GLY GLN ASP ARG ASP GLN          
SEQRES  24 K  640  ASP GLN VAL VAL GLN GLN LEU HIS ARG VAL LEU ARG PRO          
SEQRES  25 K  640  PHE LEU LEU ARG ARG VAL LYS SER ASP VAL GLU LYS SER          
SEQRES  26 K  640  LEU LEU PRO LYS LYS GLU ILE ASN VAL TYR ILE GLY MET          
SEQRES  27 K  640  SER GLU MET GLN VAL LYS TRP TYR LYS LYS ILE LEU GLU          
SEQRES  28 K  640  LYS ASP ILE ASP ALA VAL ASN GLY ALA GLY GLY LYS ARG          
SEQRES  29 K  640  GLU SER LYS THR ARG LEU LEU ASN ILE VAL MET GLN LEU          
SEQRES  30 K  640  ARG LYS CYS CYS ASN HIS PRO TYR LEU PHE GLU GLY ALA          
SEQRES  31 K  640  GLU PRO GLY PRO PRO TYR THR THR ASP GLU HIS LEU ILE          
SEQRES  32 K  640  TYR ASN SER GLY LYS MET ILE VAL LEU ASP LYS LEU LEU          
SEQRES  33 K  640  LYS ARG LEU GLN SER GLN GLY SER ARG VAL LEU ILE PHE          
SEQRES  34 K  640  SER GLN MET SER ARG LEU LEU ASP ILE LEU GLU ASP TYR          
SEQRES  35 K  640  CYS VAL PHE ARG GLY TYR LYS TYR CYS ARG ILE ASP GLY          
SEQRES  36 K  640  GLY THR ALA HIS GLU ASP ARG ILE ALA ALA ILE ASP GLU          
SEQRES  37 K  640  TYR ASN ARG PRO GLY SER ASP LYS PHE ILE PHE LEU LEU          
SEQRES  38 K  640  THR THR ARG ALA GLY GLY LEU GLY ILE ASN LEU THR THR          
SEQRES  39 K  640  ALA ASP THR VAL ILE LEU TYR ASP SER ASP TRP ASN PRO          
SEQRES  40 K  640  GLN ALA ASP LEU GLN ALA MET ASP ARG ALA HIS ARG ILE          
SEQRES  41 K  640  GLY GLN THR LYS GLN VAL VAL VAL TYR ARG PHE VAL THR          
SEQRES  42 K  640  ASP ASN ALA ILE GLU GLU LYS VAL LEU GLU ARG ALA ALA          
SEQRES  43 K  640  GLN LYS LEU ARG LEU ASP GLN LEU VAL ILE GLN GLN GLY          
SEQRES  44 K  640  ARG ALA GLN ILE ALA THR LYS ALA ALA ALA ASN LYS GLU          
SEQRES  45 K  640  GLU LEU LEU SER MET ILE GLN HIS GLY ALA GLU LYS VAL          
SEQRES  46 K  640  PHE GLN THR LYS GLY ALA PHE GLY LEU MET ALA GLU LYS          
SEQRES  47 K  640  GLY ALA ASN LEU ASP ASP ASP ASP ILE ASP ALA ILE LEU          
SEQRES  48 K  640  LYS ALA GLY GLU GLU ARG THR ARG GLU LEU ASN ALA LYS          
SEQRES  49 K  640  TYR GLU LYS LEU GLY ILE ASP ASP LEU GLN LYS PHE THR          
SEQRES  50 K  640  SER GLU SER                                                  
HELIX    1 AA1 GLU A   50  GLN A   55  1                                   6    
HELIX    2 AA2 ARG A   63  ALA A   75  1                                  13    
HELIX    3 AA3 GLN A   76  PHE A   78  5                                   3    
HELIX    4 AA4 ALA A   88  ILE A  112  1                                  25    
HELIX    5 AA5 HIS A  113  LYS A  115  5                                   3    
HELIX    6 AA6 MET A  120  GLU A  133  1                                  14    
HELIX    7 AA7 ASN B   25  ILE B   29  5                                   5    
HELIX    8 AA8 LYS B   31  GLY B   41  1                                  11    
HELIX    9 AA9 LEU B   49  LEU B   62  1                                  14    
HELIX   10 AB1 ILE B   66  ALA B   76  1                                  11    
HELIX   11 AB2 THR B   82  GLN B   93  1                                  12    
HELIX   12 AB3 ARG C   28  LYS C   35  1                                   8    
HELIX   13 AB4 GLY C   45  ASN C   67  1                                  23    
HELIX   14 AB5 ALA C   68  ARG C   70  5                                   3    
HELIX   15 AB6 ILE C   78  ARG C   87  1                                  10    
HELIX   16 AB7 GLU C   91  LEU C   96  1                                   6    
HELIX   17 AB8 TYR D   37  HIS D   46  1                                  10    
HELIX   18 AB9 SER D   53  SER D   61  1                                   9    
HELIX   19 AC1 ILE D   66  ASN D   81  1                                  16    
HELIX   20 AC2 SER D   88  LEU D   97  1                                  10    
HELIX   21 AC3 LEU D  103  THR D  119  1                                  17    
HELIX   22 AC4 GLU E   50  GLN E   55  1                                   6    
HELIX   23 AC5 ARG E   63  ALA E   75  1                                  13    
HELIX   24 AC6 GLN E   76  PHE E   78  5                                   3    
HELIX   25 AC7 ALA E   88  ILE E  112  1                                  25    
HELIX   26 AC8 HIS E  113  LYS E  115  5                                   3    
HELIX   27 AC9 MET E  120  GLU E  133  1                                  14    
HELIX   28 AD1 LYS F   31  GLY F   41  1                                  11    
HELIX   29 AD2 LEU F   49  THR F   54  1                                   6    
HELIX   30 AD3 THR F   54  LEU F   62  1                                   9    
HELIX   31 AD4 ILE F   66  ALA F   76  1                                  11    
HELIX   32 AD5 THR F   82  GLN F   93  1                                  12    
HELIX   33 AD6 ARG G   28  GLY G   36  1                                   9    
HELIX   34 AD7 ALA G   46  LEU G   57  1                                  12    
HELIX   35 AD8 GLU G   60  ALA G   65  1                                   6    
HELIX   36 AD9 GLY G   66  ALA G   68  5                                   3    
HELIX   37 AE1 ILE G   78  ASP G   89  1                                  12    
HELIX   38 AE2 GLU G   90  LEU G   96  1                                   7    
HELIX   39 AE3 ILE H   36  HIS H   46  1                                  11    
HELIX   40 AE4 SER H   52  LYS H   82  1                                  31    
HELIX   41 AE5 LEU H  103  THR H  112  1                                  10    
HELIX   42 AE6 THR H  112  SER H  120  1                                   9    
HELIX   43 AE7 ARG K  186  ALA K  191  1                                   6    
HELIX   44 AE8 LEU K  193  GLY K  203  1                                  11    
HELIX   45 AE9 THR K  217  GLY K  225  1                                   9    
HELIX   46 AF1 GLY K  225  ILE K  230  1                                   6    
HELIX   47 AF2 PRO K  242  SER K  244  5                                   3    
HELIX   48 AF3 THR K  245  THR K  257  1                                  13    
HELIX   49 AF4 ALA K  268  HIS K  273  1                                   6    
HELIX   50 AF5 HIS K  273  ASP K  278  1                                   6    
HELIX   51 AF6 SER K  291  ARG K  297  1                                   7    
HELIX   52 AF7 HIS K  316  ASN K  320  5                                   5    
HELIX   53 AF8 LEU K  325  ARG K  330  1                                   6    
HELIX   54 AF9 LEU K  349  LEU K  360  1                                  12    
HELIX   55 AG1 VAL K  363  ASP K  368  1                                   6    
HELIX   56 AG2 PHE K  370  PHE K  374  5                                   5    
HELIX   57 AG3 LEU K  388  ARG K  393  1                                   6    
HELIX   58 AG4 VAL K  400  VAL K  404  5                                   5    
HELIX   59 AG5 LYS K  430  ILE K  436  1                                   7    
HELIX   60 AG6 LEU K  453  ARG K  460  1                                   8    
HELIX   61 AG7 LYS K  490  LEU K  501  1                                  12    
HELIX   62 AG8 MET K  514  VAL K  526  1                                  13    
HELIX   63 AG9 ALA K  540  ASN K  552  1                                  13    
HELIX   64 AH1 GLN K  590  ALA K  595  1                                   6    
HELIX   65 AH2 MET K  596  ALA K  599  5                                   4    
HELIX   66 AH3 ILE K  619  LYS K  630  1                                  12    
HELIX   67 AH4 ASP K  634  GLN K  640  1                                   7    
SHEET    1 AA1 2 ARG A  83  PHE A  84  0                                        
SHEET    2 AA1 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A  83           
SHEET    1 AA2 2 THR A 118  ILE A 119  0                                        
SHEET    2 AA2 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1 AA3 2 ARG C  41  VAL C  42  0                                        
SHEET    2 AA3 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  41           
SHEET    1 AA4 2 ARG C  76  ILE C  77  0                                        
SHEET    2 AA4 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  77           
SHEET    1 AA5 2 ARG E  83  PHE E  84  0                                        
SHEET    2 AA5 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1 AA6 2 THR E 118  ILE E 119  0                                        
SHEET    2 AA6 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1 AA7 5 ILE K 207  ALA K 209  0                                        
SHEET    2 AA7 5 SER K 334  THR K 341  1  O  LEU K 339   N  LEU K 208           
SHEET    3 AA7 5 TRP K 307  ASP K 313  1  N  ILE K 312   O  ILE K 340           
SHEET    4 AA7 5 HIS K 237  ALA K 240  1  N  ALA K 240   O  ASP K 313           
SHEET    5 AA7 5 VAL K 287  THR K 290  1  O  CYS K 288   N  HIS K 237           
SHEET    1 AA8 5 TYR K 532  ARG K 534  0                                        
SHEET    2 AA8 5 ILE K 560  LEU K 562  1  O  ILE K 560   N  CYS K 533           
SHEET    3 AA8 5 VAL K 508  ILE K 510  1  N  VAL K 508   O  PHE K 561           
SHEET    4 AA8 5 THR K 579  ILE K 581  1  O  THR K 579   N  LEU K 509           
SHEET    5 AA8 5 VAL K 609  TYR K 611  1  O  VAL K 609   N  VAL K 580           
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                                                                             
DBGET integrated database retrieval system