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Database: PDB
Entry: 5XM1
LinkDB: 5XM1
Original site: 5XM1 
HEADER    STRUCTURAL PROTEIN/DNA                  12-MAY-17   5XM1              
TITLE     THE MOUSE NUCLEOSOME STRUCTURE CONTAINING H2A, H2B TYPE3-A, H3MM7, AND
TITLE    2 H4                                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3MM7;                                             
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 TYPE 1-B;                                      
COMPND  11 CHAIN: C, G;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HISTONE H2B TYPE 3-A;                                      
COMPND  15 CHAIN: D, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: DNA (146-MER);                                             
COMPND  19 CHAIN: I, J;                                                         
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PH3MM7;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: HIST1H4A, HIST1H4B, H4-53, HIST1H4C, H4-12, HIST1H4D,          
SOURCE  15 HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4M,          
SOURCE  16 HIST2H4A, HIST2H4, HIST4H4;                                          
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);                                
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PH4;                                      
SOURCE  22 MOL_ID: 3;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  24 ORGANISM_COMMON: MOUSE;                                              
SOURCE  25 ORGANISM_TAXID: 10090;                                               
SOURCE  26 GENE: HIST1H2AB;                                                     
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  31 EXPRESSION_SYSTEM_PLASMID: PH2A;                                     
SOURCE  32 MOL_ID: 4;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  34 ORGANISM_COMMON: MOUSE;                                              
SOURCE  35 ORGANISM_TAXID: 10090;                                               
SOURCE  36 GENE: HIST3H2BA;                                                     
SOURCE  37 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  39 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  40 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  41 EXPRESSION_SYSTEM_PLASMID: PH2B;                                     
SOURCE  42 MOL_ID: 5;                                                           
SOURCE  43 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5ALPHA;                        
SOURCE  46 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE  47 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE  48 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  49 EXPRESSION_SYSTEM_PLASMID: PGEM-T(EASY)                              
KEYWDS    NUCLEOSOME, CHROMATIN, DNA-PROTEIN COMPLEX, STRUCTURAL PROTEIN-DNA    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.TAGUCHI,N.HORIKOSHI,H.KURUMIZAKA                                    
REVDAT   2   20-MAR-19 5XM1    1       JRNL                                     
REVDAT   1   07-MAR-18 5XM1    0                                                
JRNL        AUTH   A.HARADA,K.MAEHARA,Y.ONO,H.TAGUCHI,K.YOSHIOKA,Y.KITAJIMA,    
JRNL        AUTH 2 Y.XIE,Y.SATO,T.IWASAKI,J.NOGAMI,S.OKADA,T.KOMATSU,Y.SEMBA,   
JRNL        AUTH 3 T.TAKEMOTO,H.KIMURA,H.KURUMIZAKA,Y.OHKAWA                    
JRNL        TITL   HISTONE H3.3 SUB-VARIANT H3MM7 IS REQUIRED FOR NORMAL        
JRNL        TITL 2 SKELETAL MUSCLE REGENERATION.                                
JRNL        REF    NAT COMMUN                    V.   9  1400 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29643389                                                     
JRNL        DOI    10.1038/S41467-018-03845-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.160                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26553                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1902                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.8765 -  8.2807    0.99     1936   150  0.1713 0.2080        
REMARK   3     2  8.2807 -  6.5871    0.99     1850   140  0.1843 0.2284        
REMARK   3     3  6.5871 -  5.7587    1.00     1846   142  0.2221 0.2882        
REMARK   3     4  5.7587 -  5.2341    0.99     1804   145  0.2095 0.2571        
REMARK   3     5  5.2341 -  4.8600    0.99     1805   139  0.1937 0.2461        
REMARK   3     6  4.8600 -  4.5741    0.99     1787   130  0.1867 0.2377        
REMARK   3     7  4.5741 -  4.3455    0.98     1781   142  0.1929 0.2526        
REMARK   3     8  4.3455 -  4.1567    0.97     1765   130  0.1999 0.2602        
REMARK   3     9  4.1567 -  3.9969    0.96     1721   135  0.2114 0.2672        
REMARK   3    10  3.9969 -  3.8591    0.95     1727   136  0.2212 0.3046        
REMARK   3    11  3.8591 -  3.7386    0.95     1699   130  0.2321 0.2951        
REMARK   3    12  3.7386 -  3.6319    0.93     1656   138  0.2376 0.3165        
REMARK   3    13  3.6319 -  3.5363    0.92     1651   123  0.2271 0.2980        
REMARK   3    14  3.5363 -  3.4501    0.90     1623   122  0.2528 0.3182        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 91.24                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 112.2                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          12728                                  
REMARK   3   ANGLE     :  1.247          18444                                  
REMARK   3   CHIRALITY :  0.061           2097                                  
REMARK   3   PLANARITY :  0.008           1325                                  
REMARK   3   DIHEDRAL  : 26.901           6639                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN B AND RESSEQ 25:101)                 
REMARK   3     SELECTION          : (CHAIN F AND RESSEQ 25:101)                 
REMARK   3     ATOM PAIRS NUMBER  : 738                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN H AND (RESSEQ 34:81 OR RESSEQ        
REMARK   3                          83:85 OR RESSEQ 87:123))                    
REMARK   3     SELECTION          : (CHAIN D AND (RESSEQ 34:81 OR RESSEQ        
REMARK   3                          83:85 OR RESSEQ 87:123))                    
REMARK   3     ATOM PAIRS NUMBER  : 752                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESSEQ 38:52 OR RESSEQ        
REMARK   3                          54:77 OR (RESID 78 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG   
REMARK   3                          OR NAME CD1 OR NAME CE1 OR NAME CZ )) OR    
REMARK   3                          RESSEQ 79:80 OR (RESID 81 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME OD2)) OR RESSEQ 82:83 OR    
REMARK   3                          (RESID 84 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD1 OR NAME CE1 OR NAME CZ )) OR RESSEQ     
REMARK   3                          85:134))                                    
REMARK   3     SELECTION          : (CHAIN E AND (RESSEQ 38:52 OR RESSEQ        
REMARK   3                          54:77 OR (RESID 78 AND (NAME N OR NAME CA   
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG   
REMARK   3                          OR NAME CD1 OR NAME CE1 OR NAME CZ )) OR    
REMARK   3                          RESSEQ 79:80 OR (RESID 81 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME OD2)) OR RESSEQ 82:83 OR    
REMARK   3                          (RESID 84 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD1 OR NAME CE1 OR NAME CZ )) OR RESSEQ     
REMARK   3                          85:134))                                    
REMARK   3     ATOM PAIRS NUMBER  : 902                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN G AND (RESSEQ 16:38 OR (RESID 39     
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB OR NAME CG OR NAME CD1 OR      
REMARK   3                          NAME CE1 OR NAME CZ OR NAME OH )) OR        
REMARK   3                          RESSEQ 40:89 OR (RESID 90 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME OD2)) OR RESSEQ 91:117))    
REMARK   3     SELECTION          : (CHAIN C AND (RESSEQ 16:38 OR (RESID 39     
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB OR NAME CG OR NAME CD1 OR      
REMARK   3                          NAME CE1 OR NAME CZ OR NAME OH )) OR        
REMARK   3                          RESSEQ 40:89 OR (RESID 90 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB OR   
REMARK   3                          NAME CG OR NAME OD2)) OR RESSEQ 91:117))    
REMARK   3     ATOM PAIRS NUMBER  : 950                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5XM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003757.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-1A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 704W, HKL                 
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28747                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.1                                          
REMARK 200 STARTING MODEL: 3AV2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CACODYLATE, POTASSIUM          
REMARK 280  CHLORIDE, MANGANESE CHLORIDE, PH 6.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 293.0K                                            
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       52.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.10450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.69000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.10450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.69000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 55660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 72320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -399.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
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     SER A    31                                                      
REMARK 465     ILE 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     ALA A   135                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
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     ASP B    24                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     HIS C    -1                                                      
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     GLN C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     ARG C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     LYS C   119                                                      
REMARK 465     THR C   120                                                      
REMARK 465     GLU C   121                                                      
REMARK 465     SER C   122                                                      
REMARK 465     HIS C   123                                                      
REMARK 465     HIS C   124                                                      
REMARK 465     LYS C   125                                                      
REMARK 465     ALA C   126                                                      
REMARK 465     LYS C   127                                                      
REMARK 465     GLY C   128                                                      
REMARK 465     LYS C   129                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     PRO D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     LYS D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     LYS D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     ILE D    18                                                      
REMARK 465     THR D    19                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     ALA D    21                                                      
REMARK 465     GLN D    22                                                      
REMARK 465     LYS D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     ASP D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     LYS D    28                                                      
REMARK 465     ARG D    29                                                      
REMARK 465     LYS D    30                                                      
REMARK 465     LYS D   125                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     HIS E    -1                                                      
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     SER E    31                                                      
REMARK 465     ILE 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     GLY F    -3                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     HIS F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     SER 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     GLY G    -3                                                      
REMARK 465     SER G    -2                                                      
REMARK 465     HIS G    -1                                                      
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     GLN G     6                                                      
REMARK 465     GLY G     7                                                      
REMARK 465     GLY G     8                                                      
REMARK 465     LYS G     9                                                      
REMARK 465     ALA G    10                                                      
REMARK 465     ARG G    11                                                      
REMARK 465     ALA G    12                                                      
REMARK 465     LYS G    13                                                      
REMARK 465     ALA G    14                                                      
REMARK 465     LYS G   119                                                      
REMARK 465     THR G   120                                                      
REMARK 465     GLU G   121                                                      
REMARK 465     SER G   122                                                      
REMARK 465     HIS G   123                                                      
REMARK 465     HIS G   124                                                      
REMARK 465     LYS G   125                                                      
REMARK 465     ALA G   126                                                      
REMARK 465     LYS G   127                                                      
REMARK 465     GLY G   128                                                      
REMARK 465     LYS G   129                                                      
REMARK 465     GLY H    -3                                                      
REMARK 465     SER H    -2                                                      
REMARK 465     HIS H    -1                                                      
REMARK 465     MET H     0                                                      
REMARK 465     PRO H     1                                                      
REMARK 465     GLU H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     ARG H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     PRO H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     PRO H    10                                                      
REMARK 465     LYS H    11                                                      
REMARK 465     LYS H    12                                                      
REMARK 465     GLY H    13                                                      
REMARK 465     SER H    14                                                      
REMARK 465     LYS H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     ALA H    17                                                      
REMARK 465     ILE H    18                                                      
REMARK 465     THR H    19                                                      
REMARK 465     LYS H    20                                                      
REMARK 465     ALA H    21                                                      
REMARK 465     GLN H    22                                                      
REMARK 465     LYS H    23                                                      
REMARK 465     LYS H    24                                                      
REMARK 465     ASP H    25                                                      
REMARK 465     GLY H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     LYS H    28                                                      
REMARK 465     ARG H    29                                                      
REMARK 465     LYS H    30                                                      
REMARK 465     ARG H    31                                                      
REMARK 465     GLY H    32                                                      
REMARK 465     ARG H    33                                                      
REMARK 465     LYS H   125                                                      
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   N2    DG I   125     O2    DT J   169              2.03            
REMARK 500   N6    DA I    11     O4    DT J   282              2.16            
REMARK 500   NH1  ARG C    32     OP1   DA I    29              2.18            
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   OE2  GLU C    56     NH2  ARG F    23     3544     2.15            
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    ASP E  77   CB    ASP E  77   CG      0.190                       
REMARK 500     DA I   4   O3'    DA I   4   C3'    -0.043                       
REMARK 500     DG I  40   O3'    DG I  40   C3'    -0.041                       
REMARK 500     DC I  89   O3'    DC I  89   C3'    -0.051                       
REMARK 500     DA J 163   O3'    DA J 163   C3'    -0.042                       
REMARK 500     DA J 175   O3'    DA J 175   C3'    -0.041                       
REMARK 500     DG J 186   O3'    DG J 186   C3'    -0.042                       
REMARK 500     DC J 195   O3'    DC J 195   C3'    -0.058                       
REMARK 500     DT J 266   O3'    DT J 266   C3'    -0.044                       
REMARK 500     DG J 267   O3'    DG J 267   C3'    -0.040                       
REMARK 500     DG J 284   O3'    DG J 284   C3'    -0.050                       
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    ASP E  77   CB  -  CG  -  OD1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    LEU E  82   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500     DA I   1   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT I   8   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC I  12   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DG I  18   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT I  20   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT I  21   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC I  22   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA I  28   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA I  29   O4' -  C1' -  N9  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DA I  35   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT I  37   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT I  37   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DG I  39   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA I  57   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DG I  68   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA I  83   O5' -  P   -  OP2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500     DA I  85   O4' -  C1' -  N9  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DG I  87   O4' -  C1' -  N9  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DT I  93   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG I  94   O4' -  C1' -  N9  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DA I 102   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT I 117   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DA I 124   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DG I 125   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC I 129   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DG I 134   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DT I 143   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DA I 145   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC J 162   O4' -  C4' -  C3' ANGL. DEV. =  -3.3 DEGREES          
REMARK 500     DT J 169   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA J 203   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DG J 204   C3' -  C2' -  C1' ANGL. DEV. =  -5.4 DEGREES          
REMARK 500     DG J 204   O4' -  C1' -  N9  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DA J 223   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DA J 241   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DG J 243   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT J 258   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DG J 271   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT J 274   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG J 280   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT J 282   O4' -  C1' -  N1  ANGL. DEV. =   3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  81       71.10     40.24                                   
REMARK 500    THR B  96      124.99    -29.66                                   
REMARK 500    ASN C 110      108.76   -163.91                                   
REMARK 500    GLU D 105      -52.98     59.23                                   
REMARK 500    ASP E  81       69.60     26.67                                   
REMARK 500    ARG E 134      -36.20   -137.51                                   
REMARK 500    THR F  96      122.73    -31.94                                   
REMARK 500    ASN G 110      109.07   -163.08                                   
REMARK 500    PRO H 103       88.69    -69.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5XM1 A   -3   135  PDB    5XM1     5XM1            -3    135             
DBREF  5XM1 B    0   102  UNP    P62806   H4_MOUSE         1    103             
DBREF  5XM1 C    0   129  UNP    C0HKE1   H2A1B_MOUSE      1    130             
DBREF  5XM1 D    0   125  UNP    Q9D2U9   H2B3A_MOUSE      1    126             
DBREF  5XM1 E   -3   135  PDB    5XM1     5XM1            -3    135             
DBREF  5XM1 F    0   102  UNP    P62806   H4_MOUSE         1    103             
DBREF  5XM1 G    0   129  UNP    C0HKE1   H2A1B_MOUSE      1    130             
DBREF  5XM1 H    0   125  UNP    Q9D2U9   H2B3A_MOUSE      1    126             
DBREF  5XM1 I    1   146  PDB    5XM1     5XM1             1    146             
DBREF  5XM1 J  147   292  PDB    5XM1     5XM1           147    292             
SEQADV 5XM1 GLY B   -3  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 SER B   -2  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 HIS B   -1  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 GLY C   -3  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 SER C   -2  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 HIS C   -1  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 GLY D   -3  UNP  Q9D2U9              EXPRESSION TAG                 
SEQADV 5XM1 SER D   -2  UNP  Q9D2U9              EXPRESSION TAG                 
SEQADV 5XM1 HIS D   -1  UNP  Q9D2U9              EXPRESSION TAG                 
SEQADV 5XM1 GLY F   -3  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 SER F   -2  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 HIS F   -1  UNP  P62806              EXPRESSION TAG                 
SEQADV 5XM1 GLY G   -3  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 SER G   -2  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 HIS G   -1  UNP  C0HKE1              EXPRESSION TAG                 
SEQADV 5XM1 GLY H   -3  UNP  Q9D2U9              EXPRESSION TAG                 
SEQADV 5XM1 SER H   -2  UNP  Q9D2U9              EXPRESSION TAG                 
SEQADV 5XM1 HIS H   -1  UNP  Q9D2U9              EXPRESSION TAG                 
SEQRES   1 A  139  GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS          
SEQRES   2 A  139  SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR          
SEQRES   3 A  139  LYS ALA ALA ARG LYS SER ALA PRO SER ILE GLY GLY VAL          
SEQRES   4 A  139  LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU          
SEQRES   5 A  139  ARG GLU ILE ARG ARG TYR GLN LYS ALA THR GLU LEU LEU          
SEQRES   6 A  139  ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE          
SEQRES   7 A  139  ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER ALA          
SEQRES   8 A  139  ALA ILE GLY ALA LEU GLN GLU ALA SER GLU ALA TYR LEU          
SEQRES   9 A  139  VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS          
SEQRES  10 A  139  ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU          
SEQRES  11 A  139  ALA ARG ARG ILE ARG GLY GLU ARG ALA                          
SEQRES   1 B  106  GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY          
SEQRES   2 B  106  LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU          
SEQRES   3 B  106  ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG          
SEQRES   4 B  106  ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY          
SEQRES   5 B  106  LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE          
SEQRES   6 B  106  LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU          
SEQRES   7 B  106  HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL          
SEQRES   8 B  106  TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE          
SEQRES   9 B  106  GLY GLY                                                      
SEQRES   1 C  133  GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS          
SEQRES   2 C  133  ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY          
SEQRES   3 C  133  LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG          
SEQRES   4 C  133  LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO          
SEQRES   5 C  133  VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU          
SEQRES   6 C  133  ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS          
SEQRES   7 C  133  LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE          
SEQRES   8 C  133  ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL          
SEQRES   9 C  133  THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA          
SEQRES  10 C  133  VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA          
SEQRES  11 C  133  LYS GLY LYS                                                  
SEQRES   1 D  129  GLY SER HIS MET PRO GLU PRO SER ARG SER THR PRO ALA          
SEQRES   2 D  129  PRO LYS LYS GLY SER LYS LYS ALA ILE THR LYS ALA GLN          
SEQRES   3 D  129  LYS LYS ASP GLY LYS LYS ARG LYS ARG GLY ARG LYS GLU          
SEQRES   4 D  129  SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL          
SEQRES   5 D  129  HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE          
SEQRES   6 D  129  MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA          
SEQRES   7 D  129  SER GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER          
SEQRES   8 D  129  THR ILE THR SER ARG GLU VAL GLN THR ALA VAL ARG LEU          
SEQRES   9 D  129  LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU          
SEQRES  10 D  129  GLY THR LYS ALA VAL THR LYS TYR THR SER SER LYS              
SEQRES   1 E  139  GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS          
SEQRES   2 E  139  SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR          
SEQRES   3 E  139  LYS ALA ALA ARG LYS SER ALA PRO SER ILE GLY GLY VAL          
SEQRES   4 E  139  LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU          
SEQRES   5 E  139  ARG GLU ILE ARG ARG TYR GLN LYS ALA THR GLU LEU LEU          
SEQRES   6 E  139  ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE          
SEQRES   7 E  139  ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER ALA          
SEQRES   8 E  139  ALA ILE GLY ALA LEU GLN GLU ALA SER GLU ALA TYR LEU          
SEQRES   9 E  139  VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS          
SEQRES  10 E  139  ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU          
SEQRES  11 E  139  ALA ARG ARG ILE ARG GLY GLU ARG ALA                          
SEQRES   1 F  106  GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY          
SEQRES   2 F  106  LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU          
SEQRES   3 F  106  ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG          
SEQRES   4 F  106  ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY          
SEQRES   5 F  106  LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE          
SEQRES   6 F  106  LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU          
SEQRES   7 F  106  HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL          
SEQRES   8 F  106  TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE          
SEQRES   9 F  106  GLY GLY                                                      
SEQRES   1 G  133  GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS          
SEQRES   2 G  133  ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY          
SEQRES   3 G  133  LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG          
SEQRES   4 G  133  LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO          
SEQRES   5 G  133  VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU          
SEQRES   6 G  133  ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS          
SEQRES   7 G  133  LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE          
SEQRES   8 G  133  ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL          
SEQRES   9 G  133  THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA          
SEQRES  10 G  133  VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA          
SEQRES  11 G  133  LYS GLY LYS                                                  
SEQRES   1 H  129  GLY SER HIS MET PRO GLU PRO SER ARG SER THR PRO ALA          
SEQRES   2 H  129  PRO LYS LYS GLY SER LYS LYS ALA ILE THR LYS ALA GLN          
SEQRES   3 H  129  LYS LYS ASP GLY LYS LYS ARG LYS ARG GLY ARG LYS GLU          
SEQRES   4 H  129  SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL          
SEQRES   5 H  129  HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE          
SEQRES   6 H  129  MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA          
SEQRES   7 H  129  SER GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER          
SEQRES   8 H  129  THR ILE THR SER ARG GLU VAL GLN THR ALA VAL ARG LEU          
SEQRES   9 H  129  LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU          
SEQRES  10 H  129  GLY THR LYS ALA VAL THR LYS TYR THR SER SER LYS              
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  DT  DG  DA  DA  DT  DT  DC  DA  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  DT  DG  DA  DA  DT  DT  DC  DA  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                                                  
HELIX    1 AA1 GLY A   44  ALA A   57  1                                  14    
HELIX    2 AA2 ARG A   63  GLN A   76  1                                  14    
HELIX    3 AA3 GLN A   85  ALA A  114  1                                  30    
HELIX    4 AA4 MET A  120  ARG A  131  1                                  12    
HELIX    5 AA5 ASN B   25  ILE B   29  5                                   5    
HELIX    6 AA6 THR B   30  GLY B   41  1                                  12    
HELIX    7 AA7 LEU B   49  ALA B   76  1                                  28    
HELIX    8 AA8 THR B   82  GLN B   93  1                                  12    
HELIX    9 AA9 THR C   16  ALA C   21  1                                   6    
HELIX   10 AB1 PRO C   26  LYS C   36  1                                  11    
HELIX   11 AB2 GLY C   46  ASN C   73  1                                  28    
HELIX   12 AB3 ILE C   79  ASP C   90  1                                  12    
HELIX   13 AB4 ASP C   90  LEU C   97  1                                   8    
HELIX   14 AB5 GLN C  112  LEU C  116  5                                   5    
HELIX   15 AB6 TYR D   37  HIS D   49  1                                  13    
HELIX   16 AB7 SER D   55  ASN D   84  1                                  30    
HELIX   17 AB8 THR D   90  LEU D  102  1                                  13    
HELIX   18 AB9 GLU D  105  THR D  122  1                                  18    
HELIX   19 AC1 GLY E   44  ALA E   57  1                                  14    
HELIX   20 AC2 ARG E   63  ASP E   77  1                                  15    
HELIX   21 AC3 GLN E   85  ALA E  114  1                                  30    
HELIX   22 AC4 MET E  120  GLY E  132  1                                  13    
HELIX   23 AC5 ASN F   25  ILE F   29  5                                   5    
HELIX   24 AC6 THR F   30  GLY F   41  1                                  12    
HELIX   25 AC7 LEU F   49  ALA F   76  1                                  28    
HELIX   26 AC8 THR F   82  GLN F   93  1                                  12    
HELIX   27 AC9 THR G   16  GLY G   22  1                                   7    
HELIX   28 AD1 PRO G   26  LYS G   36  1                                  11    
HELIX   29 AD2 GLY G   46  ASN G   73  1                                  28    
HELIX   30 AD3 ILE G   79  ASP G   90  1                                  12    
HELIX   31 AD4 ASP G   90  LEU G   97  1                                   8    
HELIX   32 AD5 GLN G  112  LEU G  116  5                                   5    
HELIX   33 AD6 TYR H   37  HIS H   49  1                                  13    
HELIX   34 AD7 SER H   55  ASN H   84  1                                  30    
HELIX   35 AD8 THR H   90  LEU H  102  1                                  13    
HELIX   36 AD9 GLU H  105  SER H  124  1                                  20    
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 LEU B  97  TYR B  98  0                                        
SHEET    2 AA3 2 THR G 101  ILE G 102  1  O  THR G 101   N  TYR B  98           
SHEET    1 AA4 2 ARG C  42  VAL C  43  0                                        
SHEET    2 AA4 2 THR D  88  ILE D  89  1  O  ILE D  89   N  ARG C  42           
SHEET    1 AA5 2 ARG C  77  ILE C  78  0                                        
SHEET    2 AA5 2 GLY D  53  ILE D  54  1  O  GLY D  53   N  ILE C  78           
SHEET    1 AA6 2 THR C 101  ILE C 102  0                                        
SHEET    2 AA6 2 LEU F  97  TYR F  98  1  O  TYR F  98   N  THR C 101           
SHEET    1 AA7 2 ARG E  83  PHE E  84  0                                        
SHEET    2 AA7 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1 AA8 2 THR E 118  ILE E 119  0                                        
SHEET    2 AA8 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1 AA9 2 ARG G  42  VAL G  43  0                                        
SHEET    2 AA9 2 THR H  88  ILE H  89  1  O  ILE H  89   N  ARG G  42           
SHEET    1 AB1 2 ARG G  77  ILE G  78  0                                        
SHEET    2 AB1 2 GLY H  53  ILE H  54  1  O  GLY H  53   N  ILE G  78           
CISPEP   1 ARG D   31    GLY D   32          0         0.73                     
CISPEP   2 GLY H  104    GLU H  105          0        17.61                     
CRYST1  105.550  109.380  176.209  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      0.009474  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009142  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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