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Database: PDB
Entry: 1U35
LinkDB: 1U35
Original site: 1U35 
HEADER    STRUCTURAL PROTEIN/DNA                  20-JUL-04   1U35              
TITLE     CRYSTAL STRUCTURE OF THE NUCLEOSOME CORE PARTICLE                     
TITLE    2 CONTAINING THE HISTONE DOMAIN OF MACROH2A                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-SATELLITE DNA;                                       
COMPND   3 CHAIN: I, J;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H3.1;                                              
COMPND   7 CHAIN: A, E;                                                         
COMPND   8 SYNONYM: H3/A, H3/C, H3/D, H3/F, H3/H, H3/I, H3/J, H3/K,             
COMPND   9 H3/L;                                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HIST1H4I PROTEIN;                                          
COMPND  13 CHAIN: B, F;                                                         
COMPND  14 SYNONYM: MEMBER Y ISOFORM 1, HISTONE MACROH2A1.2, HISTONE            
COMPND  15 MACROH2A1.1;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: H2A HISTONE FAMILY;                                        
COMPND  19 CHAIN: C, G;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: HISTONE 3, H2BA;                                           
COMPND  23 CHAIN: D, H;                                                         
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5-ALPHA;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC19;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: H3FA, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL;          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21-DE3-PLYSS;                            
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  23 ORGANISM_TAXID: 10090;                                               
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: BL21-DE3-PLYSS;                            
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  29 MOL_ID: 4;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  35 EXPRESSION_SYSTEM_STRAIN: BL21-DE3-PLYSS;                            
SOURCE  36 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  37 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  38 MOL_ID: 5;                                                           
SOURCE  39 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  40 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  41 ORGANISM_TAXID: 10090;                                               
SOURCE  42 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  43 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  44 EXPRESSION_SYSTEM_STRAIN: BL21-DE3-PLYSS;                            
SOURCE  45 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  46 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    NUCLEOSOME, NCP, HISTONE FOLD, HISTONE VARIANT, MACROH2A,             
KEYWDS   2 STRUCTURAL PROTEIN/DNA COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHAKRAVARTHY,S.K.GUNDIMELLA,C.CARON,P.Y.PERCHE,                     
AUTHOR   2 J.R.PEHRSON,S.KHOCHBIN,K.LUGER                                       
REVDAT   4   24-FEB-09 1U35    1       VERSN                                    
REVDAT   3   24-JAN-06 1U35    1       DBREF                                    
REVDAT   2   06-DEC-05 1U35    1       REMARK                                   
REVDAT   1   27-SEP-05 1U35    0                                                
JRNL        AUTH   S.CHAKRAVARTHY,S.K.GUNDIMELLA,C.CARON,P.Y.PERCHE,            
JRNL        AUTH 2 J.R.PEHRSON,S.KHOCHBIN,K.LUGER                               
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE HISTONE VARIANT           
JRNL        TITL 2 MACROH2A.                                                    
JRNL        REF    MOL.CELL.BIOL.                V.  25  7616 2005              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   16107708                                                     
JRNL        DOI    10.1128/MCB.25.17.7616-7624.2005                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 39783                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2004                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6009                                    
REMARK   3   NUCLEIC ACID ATOMS       : 5939                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THERE ARE CLOSE CONTACTS BETWEEN          
REMARK   3  A217 AND T218 IN CHAIN J, BETWEEN T74 AND C75 IN CHAIN I.           
REMARK   4                                                                      
REMARK   4 1U35 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023185.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43366                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.150                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1AOI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CHLORIDE, MANGANESE            
REMARK 280  CHLORIDE, POTASSIUM CACODYLATE, PH 6.0, VAPOR DIFFUSION,            
REMARK 280  SITTING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       52.75250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.99450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.79900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.99450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.75250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.79900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, C, D, E, F, G, H          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465      DT I    74A                                                     
REMARK 465      DA J   217A                                                     
REMARK 465     MET A   400                                                      
REMARK 465     ALA A   401                                                      
REMARK 465     ARG A   402                                                      
REMARK 465     THR A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     GLN A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     ARG A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     GLY A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     LYS A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     ARG A   417                                                      
REMARK 465     LYS A   418                                                      
REMARK 465     GLN A   419                                                      
REMARK 465     LEU A   420                                                      
REMARK 465     ALA A   421                                                      
REMARK 465     THR A   422                                                      
REMARK 465     LYS A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     ALA A   425                                                      
REMARK 465     ARG A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     ALA A   429                                                      
REMARK 465     PRO A   430                                                      
REMARK 465     ALA A   431                                                      
REMARK 465     THR A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     GLY A   434                                                      
REMARK 465     VAL A   435                                                      
REMARK 465     LYS A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     MET B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     VAL B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     MET C   803                                                      
REMARK 465     SER C   804                                                      
REMARK 465     SER C   805                                                      
REMARK 465     ARG C   806                                                      
REMARK 465     GLY C   807                                                      
REMARK 465     GLY C   808                                                      
REMARK 465     LYS C   809                                                      
REMARK 465     LYS C   810                                                      
REMARK 465     LYS C   811                                                      
REMARK 465     SER C   812                                                      
REMARK 465     THR C   813                                                      
REMARK 465     ARG C   920                                                      
REMARK 465     GLY C   921                                                      
REMARK 465     SER C   922                                                      
REMARK 465     MET D  1197                                                      
REMARK 465     PRO D  1198                                                      
REMARK 465     GLU D  1199                                                      
REMARK 465     PRO D  1200                                                      
REMARK 465     SER D  1201                                                      
REMARK 465     ARG D  1202                                                      
REMARK 465     SER D  1203                                                      
REMARK 465     THR D  1204                                                      
REMARK 465     PRO D  1205                                                      
REMARK 465     ALA D  1206                                                      
REMARK 465     PRO D  1207                                                      
REMARK 465     LYS D  1208                                                      
REMARK 465     LYS D  1209                                                      
REMARK 465     GLY D  1210                                                      
REMARK 465     SER D  1211                                                      
REMARK 465     LYS D  1212                                                      
REMARK 465     LYS D  1213                                                      
REMARK 465     ALA D  1214                                                      
REMARK 465     ILE D  1215                                                      
REMARK 465     THR D  1216                                                      
REMARK 465     LYS D  1217                                                      
REMARK 465     ALA D  1218                                                      
REMARK 465     GLN D  1219                                                      
REMARK 465     LYS D  1220                                                      
REMARK 465     LYS D  1221                                                      
REMARK 465     ASP D  1222                                                      
REMARK 465     GLY D  1223                                                      
REMARK 465     LYS D  1224                                                      
REMARK 465     LYS D  1225                                                      
REMARK 465     ARG D  1226                                                      
REMARK 465     LYS D  1227                                                      
REMARK 465     ARG D  1228                                                      
REMARK 465     GLY D  1229                                                      
REMARK 465     MET E   600                                                      
REMARK 465     ALA E   601                                                      
REMARK 465     ARG E   602                                                      
REMARK 465     THR E   603                                                      
REMARK 465     LYS E   604                                                      
REMARK 465     GLN E   605                                                      
REMARK 465     THR E   606                                                      
REMARK 465     ALA E   607                                                      
REMARK 465     ARG E   608                                                      
REMARK 465     LYS E   609                                                      
REMARK 465     SER E   610                                                      
REMARK 465     THR E   611                                                      
REMARK 465     GLY E   612                                                      
REMARK 465     GLY E   613                                                      
REMARK 465     LYS E   614                                                      
REMARK 465     ALA E   615                                                      
REMARK 465     PRO E   616                                                      
REMARK 465     ARG E   617                                                      
REMARK 465     LYS E   618                                                      
REMARK 465     GLN E   619                                                      
REMARK 465     LEU E   620                                                      
REMARK 465     ALA E   621                                                      
REMARK 465     THR E   622                                                      
REMARK 465     LYS E   623                                                      
REMARK 465     ALA E   624                                                      
REMARK 465     ALA E   625                                                      
REMARK 465     ARG E   626                                                      
REMARK 465     LYS E   627                                                      
REMARK 465     SER E   628                                                      
REMARK 465     ALA E   629                                                      
REMARK 465     PRO E   630                                                      
REMARK 465     ALA E   631                                                      
REMARK 465     THR E   632                                                      
REMARK 465     GLY E   633                                                      
REMARK 465     GLY E   634                                                      
REMARK 465     VAL E   635                                                      
REMARK 465     LYS E   636                                                      
REMARK 465     LYS E   637                                                      
REMARK 465     MET F   200                                                      
REMARK 465     SER F   201                                                      
REMARK 465     GLY F   202                                                      
REMARK 465     ARG F   203                                                      
REMARK 465     GLY F   204                                                      
REMARK 465     LYS F   205                                                      
REMARK 465     GLY F   206                                                      
REMARK 465     GLY F   207                                                      
REMARK 465     LYS F   208                                                      
REMARK 465     GLY F   209                                                      
REMARK 465     LEU F   210                                                      
REMARK 465     GLY F   211                                                      
REMARK 465     LYS F   212                                                      
REMARK 465     GLY F   213                                                      
REMARK 465     GLY F   214                                                      
REMARK 465     ALA F   215                                                      
REMARK 465     LYS F   216                                                      
REMARK 465     ARG F   217                                                      
REMARK 465     HIS F   218                                                      
REMARK 465     ARG F   219                                                      
REMARK 465     MET G  1003                                                      
REMARK 465     SER G  1004                                                      
REMARK 465     SER G  1005                                                      
REMARK 465     ARG G  1006                                                      
REMARK 465     GLY G  1007                                                      
REMARK 465     GLY G  1008                                                      
REMARK 465     LYS G  1009                                                      
REMARK 465     LYS G  1010                                                      
REMARK 465     LYS G  1011                                                      
REMARK 465     SER G  1012                                                      
REMARK 465     THR G  1013                                                      
REMARK 465     ARG G  1120                                                      
REMARK 465     GLY G  1121                                                      
REMARK 465     SER G  1122                                                      
REMARK 465     MET H  1397                                                      
REMARK 465     PRO H  1398                                                      
REMARK 465     GLU H  1399                                                      
REMARK 465     PRO H  1400                                                      
REMARK 465     SER H  1401                                                      
REMARK 465     ARG H  1402                                                      
REMARK 465     SER H  1403                                                      
REMARK 465     THR H  1404                                                      
REMARK 465     PRO H  1405                                                      
REMARK 465     ALA H  1406                                                      
REMARK 465     PRO H  1407                                                      
REMARK 465     LYS H  1408                                                      
REMARK 465     LYS H  1409                                                      
REMARK 465     GLY H  1410                                                      
REMARK 465     SER H  1411                                                      
REMARK 465     LYS H  1412                                                      
REMARK 465     LYS H  1413                                                      
REMARK 465     ALA H  1414                                                      
REMARK 465     ILE H  1415                                                      
REMARK 465     THR H  1416                                                      
REMARK 465     LYS H  1417                                                      
REMARK 465     ALA H  1418                                                      
REMARK 465     GLN H  1419                                                      
REMARK 465     LYS H  1420                                                      
REMARK 465     LYS H  1421                                                      
REMARK 465     ASP H  1422                                                      
REMARK 465     GLY H  1423                                                      
REMARK 465     LYS H  1424                                                      
REMARK 465     LYS H  1425                                                      
REMARK 465     ARG H  1426                                                      
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   O3'  DA  I    73     P    DT  I    74              1.60            
REMARK 500   O3'  DG  J   216     P    DA  J   217              1.60            
REMARK 500   O    HOH D   301     O    HOH D   337              1.98            
REMARK 500   O    VAL D  1245     O    HOH D   301              2.02            
REMARK 500   O    HOH D   301     O    HOH D   338              2.15            
REMARK 500   OP1  DA  I    29     NH1  ARG C   832              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP E   677     O    HOH D   301     3745     1.96            
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    LYS C 840   CE    LYS C 840   NZ      0.186                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 477        7.03    -57.01                                   
REMARK 500    ASP A 481       83.94     44.67                                   
REMARK 500    ARG A 534      136.28      6.87                                   
REMARK 500    ILE B  26      -66.06    156.35                                   
REMARK 500    PHE B 100       21.90   -140.82                                   
REMARK 500    PRO C 826       93.31    -66.38                                   
REMARK 500    LYS C 835      -70.56    -65.89                                   
REMARK 500    LYS C 836      -20.81    -36.72                                   
REMARK 500    LYS C 840      -58.03    151.67                                   
REMARK 500    ASN C 910      112.63    179.80                                   
REMARK 500    LYS C 918     -161.17     74.22                                   
REMARK 500    SER D1320       -8.67    176.47                                   
REMARK 500    ARG E 640      121.09   -172.28                                   
REMARK 500    THR E 658       -0.84   -142.05                                   
REMARK 500    ARG E 734       80.33    -34.75                                   
REMARK 500    VAL F 221      103.14     62.72                                   
REMARK 500    PHE F 300      -11.83   -142.43                                   
REMARK 500    PRO G1026       70.35    -54.32                                   
REMARK 500    HIS G1038       61.75   -115.65                                   
REMARK 500    ALA G1047      -70.73    -45.45                                   
REMARK 500    HIS G1112      150.53    -46.19                                   
REMARK 500    ALA G1117      -77.97    -37.77                                   
REMARK 500    LYS G1118      -79.89    178.55                                   
REMARK 500    ASP H1448       53.00   -114.96                                   
REMARK 500    LYS H1482       48.77     32.49                                   
REMARK 500    SER H1520       41.04    -64.92                                   
REMARK 500    SER H1521      -80.02   -163.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DA I  67         0.06    SIDE_CHAIN                              
REMARK 500     DC I  88         0.07    SIDE_CHAIN                              
REMARK 500     DA J 212         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AOI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NUCLEOSOME CONTAINING NON-VARINAT               
REMARK 900 HISTONES FROM XENOPUS LAEVIS.                                        
REMARK 900 RELATED ID: 1F66   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NUCLEOSOME CONTAINING THE HISTONE               
REMARK 900 VARINAT H2A.Z.                                                       
DBREF  1U35 A  400   535  UNP    P68433   H31_MOUSE        0    135             
DBREF  1U35 E  600   735  UNP    P68433   H31_MOUSE        0    135             
DBREF  1U35 B    0   102  UNP    Q5T006   Q5T006_MOUSE    10    112             
DBREF  1U35 F  200   302  UNP    Q5T006   Q5T006_MOUSE    10    112             
DBREF  1U35 C  803   922  UNP    O75367   H2AY_HUMAN       1    120             
DBREF  1U35 G 1003  1122  UNP    O75367   H2AY_HUMAN       1    120             
DBREF  1U35 D 1197  1322  UNP    Q9D2U9   Q9D2U9_MOUSE     1    126             
DBREF  1U35 H 1397  1522  UNP    Q9D2U9   Q9D2U9_MOUSE     1    126             
DBREF  1U35 I    1   145  PDB    1U35     1U35             1    145             
DBREF  1U35 J  146   290  PDB    1U35     1U35           146    290             
SEQADV 1U35 VAL C  867  UNP  O75367    GLY    65 ENGINEERED                     
SEQADV 1U35 VAL G 1067  UNP  O75367    GLY    65 ENGINEERED                     
SEQRES   1 I  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 I  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 I  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 I  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 I  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 I  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 I  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 I  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 I  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 I  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 I  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 I  146   DG  DA  DT                                                  
SEQRES   1 J  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 J  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 J  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 J  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 J  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 J  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 J  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 J  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 J  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 J  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 J  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 J  146   DG  DA  DT                                                  
SEQRES   1 A  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 CYS 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 SER 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  120  MET SER SER ARG GLY GLY LYS LYS LYS SER THR LYS THR          
SEQRES   2 C  120  SER ARG SER ALA LYS ALA GLY VAL ILE PHE PRO VAL GLY          
SEQRES   3 C  120  ARG MET LEU ARG TYR ILE LYS LYS GLY HIS PRO LYS TYR          
SEQRES   4 C  120  ARG ILE GLY VAL GLY ALA PRO VAL TYR MET ALA ALA VAL          
SEQRES   5 C  120  LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU ALA VAL          
SEQRES   6 C  120  ASN ALA ALA ARG ASP ASN LYS LYS GLY ARG VAL THR PRO          
SEQRES   7 C  120  ARG HIS ILE LEU LEU ALA VAL ALA ASN ASP GLU GLU LEU          
SEQRES   8 C  120  ASN GLN LEU LEU LYS GLY VAL THR ILE ALA SER GLY GLY          
SEQRES   9 C  120  VAL LEU PRO ASN ILE HIS PRO GLU LEU LEU ALA LYS LYS          
SEQRES  10 C  120  ARG GLY SER                                                  
SEQRES   1 D  126  MET PRO GLU PRO SER ARG SER THR PRO ALA PRO LYS LYS          
SEQRES   2 D  126  GLY SER LYS LYS ALA ILE THR LYS ALA GLN LYS LYS ASP          
SEQRES   3 D  126  GLY LYS LYS ARG LYS ARG GLY ARG LYS GLU SER TYR SER          
SEQRES   4 D  126  ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP          
SEQRES   5 D  126  THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER          
SEQRES   6 D  126  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA SER GLU ALA          
SEQRES   7 D  126  SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR          
SEQRES   8 D  126  SER ARG GLU VAL GLN THR ALA VAL ARG LEU LEU LEU PRO          
SEQRES   9 D  126  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS          
SEQRES  10 D  126  ALA VAL THR 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 CYS 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 SER 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  120  MET SER SER ARG GLY GLY LYS LYS LYS SER THR LYS THR          
SEQRES   2 G  120  SER ARG SER ALA LYS ALA GLY VAL ILE PHE PRO VAL GLY          
SEQRES   3 G  120  ARG MET LEU ARG TYR ILE LYS LYS GLY HIS PRO LYS TYR          
SEQRES   4 G  120  ARG ILE GLY VAL GLY ALA PRO VAL TYR MET ALA ALA VAL          
SEQRES   5 G  120  LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU ALA VAL          
SEQRES   6 G  120  ASN ALA ALA ARG ASP ASN LYS LYS GLY ARG VAL THR PRO          
SEQRES   7 G  120  ARG HIS ILE LEU LEU ALA VAL ALA ASN ASP GLU GLU LEU          
SEQRES   8 G  120  ASN GLN LEU LEU LYS GLY VAL THR ILE ALA SER GLY GLY          
SEQRES   9 G  120  VAL LEU PRO ASN ILE HIS PRO GLU LEU LEU ALA LYS LYS          
SEQRES  10 G  120  ARG GLY SER                                                  
SEQRES   1 H  126  MET PRO GLU PRO SER ARG SER THR PRO ALA PRO LYS LYS          
SEQRES   2 H  126  GLY SER LYS LYS ALA ILE THR LYS ALA GLN LYS LYS ASP          
SEQRES   3 H  126  GLY LYS LYS ARG LYS ARG GLY ARG LYS GLU SER TYR SER          
SEQRES   4 H  126  ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP          
SEQRES   5 H  126  THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER          
SEQRES   6 H  126  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA SER GLU ALA          
SEQRES   7 H  126  SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR          
SEQRES   8 H  126  SER ARG GLU VAL GLN THR ALA VAL ARG LEU LEU LEU PRO          
SEQRES   9 H  126  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS          
SEQRES  10 H  126  ALA VAL THR LYS TYR THR SER SER LYS                          
FORMUL  11  HOH   *105(H2 O)                                                    
HELIX    1   1 GLY A  444  GLN A  455  1                                  12    
HELIX    2   2 ARG A  463  ASP A  477  1                                  15    
HELIX    3   3 GLN A  485  ALA A  514  1                                  30    
HELIX    4   4 MET A  520  GLY A  532  1                                  13    
HELIX    5   5 THR B   30  GLY B   41  1                                  12    
HELIX    6   6 LEU B   49  ALA B   76  1                                  28    
HELIX    7   7 THR B   82  GLN B   93  1                                  12    
HELIX    8   8 SER C  816  GLY C  822  1                                   7    
HELIX    9   9 PRO C  826  HIS C  838  1                                  13    
HELIX   10  10 GLY C  846  ASN C  873  1                                  28    
HELIX   11  11 THR C  879  ASP C  890  1                                  12    
HELIX   12  12 ASP C  890  LEU C  897  1                                   8    
HELIX   13  13 HIS C  912  LEU C  916  5                                   5    
HELIX   14  14 TYR D 1234  HIS D 1246  1                                  13    
HELIX   15  15 SER D 1252  ASN D 1281  1                                  30    
HELIX   16  16 THR D 1287  LEU D 1299  1                                  13    
HELIX   17  17 PRO D 1300  THR D 1319  1                                  20    
HELIX   18  18 GLY E  644  SER E  657  1                                  14    
HELIX   19  19 ARG E  663  ASP E  677  1                                  15    
HELIX   20  20 GLN E  685  ALA E  714  1                                  30    
HELIX   21  21 MET E  720  ARG E  731  1                                  12    
HELIX   22  22 ASP F  224  ILE F  229  5                                   6    
HELIX   23  23 THR F  230  GLY F  241  1                                  12    
HELIX   24  24 LEU F  249  ALA F  276  1                                  28    
HELIX   25  25 THR F  282  GLN F  293  1                                  12    
HELIX   26  26 SER G 1016  GLY G 1022  1                                   7    
HELIX   27  27 PRO G 1026  HIS G 1038  1                                  13    
HELIX   28  28 VAL G 1045  ASN G 1073  1                                  29    
HELIX   29  29 THR G 1079  ASP G 1090  1                                  12    
HELIX   30  30 ASP G 1090  LEU G 1097  1                                   8    
HELIX   31  31 TYR H 1434  GLN H 1444  1                                  11    
HELIX   32  32 SER H 1452  ASN H 1481  1                                  30    
HELIX   33  33 THR H 1487  LEU H 1499  1                                  13    
HELIX   34  34 PRO H 1500  SER H 1520  1                                  21    
SHEET    1   A 2 ARG A 483  PHE A 484  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A 483           
SHEET    1   B 2 THR A 518  ILE A 519  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 519           
SHEET    1   C 2 THR B  96  TYR B  98  0                                        
SHEET    2   C 2 VAL G1100  ILE G1102  1  O  THR G1101   N  TYR B  98           
SHEET    1   D 2 ARG C 842  ILE C 843  0                                        
SHEET    2   D 2 THR D1285  ILE D1286  1  O  ILE D1286   N  ARG C 842           
SHEET    1   E 2 ARG C 877  VAL C 878  0                                        
SHEET    2   E 2 GLY D1250  ILE D1251  1  O  GLY D1250   N  VAL C 878           
SHEET    1   F 2 VAL C 900  ILE C 902  0                                        
SHEET    2   F 2 THR F 296  TYR F 298  1  O  TYR F 298   N  THR C 901           
SHEET    1   G 2 ARG E 683  PHE E 684  0                                        
SHEET    2   G 2 THR F 280  VAL F 281  1  O  VAL F 281   N  ARG E 683           
SHEET    1   H 2 THR E 718  ILE E 719  0                                        
SHEET    2   H 2 ARG F 245  ILE F 246  1  O  ARG F 245   N  ILE E 719           
SHEET    1   I 2 ARG G1042  ILE G1043  0                                        
SHEET    2   I 2 THR H1485  ILE H1486  1  O  ILE H1486   N  ARG G1042           
SHEET    1   J 2 ARG G1077  VAL G1078  0                                        
SHEET    2   J 2 GLY H1450  ILE H1451  1  O  GLY H1450   N  VAL G1078           
CRYST1  105.505  109.598  175.989  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009478  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005682        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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