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Database: PDB
Entry: 2CV5
LinkDB: 2CV5
Original site: 2CV5 
HEADER    STRUCTURAL PROTEIN/DNA                  31-MAY-05   2CV5              
TITLE     CRYSTAL STRUCTURE OF HUMAN NUCLEOSOME CORE PARTICLE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (146-MER);                                             
COMPND   3 CHAIN: I, J;                                                         
COMPND   4 SYNONYM: PALINDROMIC 146-BP HUMAN A-SATELLITE DNA;                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HISTONE H3.1;                                              
COMPND   8 CHAIN: A, E;                                                         
COMPND   9 SYNONYM: HISTONE H3;                                                 
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HISTONE H4;                                                
COMPND  13 CHAIN: B, F;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: HISTONE H2A.A;                                             
COMPND  17 CHAIN: C, G;                                                         
COMPND  18 SYNONYM: HISTONE H2A;                                                
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: HISTONE H2B K;                                             
COMPND  22 CHAIN: D, H;                                                         
COMPND  23 SYNONYM: HISTONE H2B, HIRA-INTERACTING PROTEIN 1;                    
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   5 ORGANISM_COMMON: HUMAN;                                              
SOURCE   6 ORGANISM_TAXID: 9606;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  26 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE  27 MOL_ID: 5;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  34 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    HUMAN NUCLEOSOME STRUCTURE, X-RAY CRYSTALLOGRAPHY,                    
KEYWDS   2 SUPERCOILED DNA PATH, METAL BINDING SITE, STRUCTURAL                 
KEYWDS   3 PROTEIN/DNA COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TSUNAKA,N.KAJIMURA,S.TATE,K.MORIKAWA                                
REVDAT   2   24-FEB-09 2CV5    1       VERSN                                    
REVDAT   1   28-JUN-05 2CV5    0                                                
JRNL        AUTH   Y.TSUNAKA,N.KAJIMURA,S.TATE,K.MORIKAWA                       
JRNL        TITL   ALTERATION OF THE NUCLEOSOMAL DNA PATH IN THE                
JRNL        TITL 2 CRYSTAL STRUCTURE OF A HUMAN NUCLEOSOME CORE                 
JRNL        TITL 3 PARTICLE                                                     
JRNL        REF    NUCLEIC ACIDS RES.            V.  33  3424 2005              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   15951514                                                     
JRNL        DOI    10.1093/NAR/GKI663                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 61552                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 6241                            
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            : 6048                                    
REMARK   3   NUCLEIC ACID ATOMS       : 5980                                    
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 430                                     
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: NULL                                      
REMARK   4                                                                      
REMARK   4 2CV5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024655.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61700                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MANGANESE (II) ION, CHLORIDE ION,        
REMARK 280  H2O                                                                 
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       49.78200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.71250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.71250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.78200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.18500            
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     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     LYS A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     ALA A   135                                                      
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     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     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     MET D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLU D    -1                                                      
REMARK 465     PRO D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     PRO D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     LYS D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     LYS D    12                                                      
REMARK 465     LYS D    13                                                      
REMARK 465     ALA D    14                                                      
REMARK 465     VAL D    15                                                      
REMARK 465     THR D    16                                                      
REMARK 465     LYS D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     GLN D    19                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     ASP D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     LYS D    25                                                      
REMARK 465     ARG D    26                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     THR E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     GLY E    13                                                      
REMARK 465     LYS E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     PRO E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     LEU E    20                                                      
REMARK 465     ALA E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     LYS E    23                                                      
REMARK 465     ALA E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     ARG E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     PRO E    30                                                      
REMARK 465     ALA E    31                                                      
REMARK 465     THR E    32                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     VAL E    35                                                      
REMARK 465     LYS E    36                                                      
REMARK 465     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     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     MET H    -3                                                      
REMARK 465     PRO H    -2                                                      
REMARK 465     GLU H    -1                                                      
REMARK 465     PRO H     0                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     LYS H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     PRO H     5                                                      
REMARK 465     ALA H     6                                                      
REMARK 465     PRO H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     LYS H     9                                                      
REMARK 465     GLY H    10                                                      
REMARK 465     SER H    11                                                      
REMARK 465     LYS H    12                                                      
REMARK 465     LYS H    13                                                      
REMARK 465     ALA H    14                                                      
REMARK 465     VAL H    15                                                      
REMARK 465     THR H    16                                                      
REMARK 465     LYS H    17                                                      
REMARK 465     ALA H    18                                                      
REMARK 465     GLN H    19                                                      
REMARK 465     LYS H    20                                                      
REMARK 465     LYS H    21                                                      
REMARK 465     ASP H    22                                                      
REMARK 465     GLY H    23                                                      
REMARK 465     LYS H    24                                                      
REMARK 465     LYS H    25                                                      
REMARK 465     ARG H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     LYS H   122                                                      
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     DG I  87   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DA J 213   O4' -  C1' -  N9  ANGL. DEV. =   1.8 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  77        1.93    -67.98                                   
REMARK 500    ASP A  81       58.95     29.57                                   
REMARK 500    ASN C 110      104.82   -167.04                                   
REMARK 500    ARG D  28      -54.67   -137.42                                   
REMARK 500    SER D  29       71.76     68.77                                   
REMARK 500    HIS D  46       85.41   -150.86                                   
REMARK 500    ARG E 134       39.71   -152.94                                   
REMARK 500    ARG F  19      -96.71     55.32                                   
REMARK 500    PRO G  26       95.30    -69.23                                   
REMARK 500    ASN G 110      121.43   -176.04                                   
REMARK 500    PRO G 117     -162.15    -69.47                                   
REMARK 500    SER H  29      -87.48    -64.32                                   
REMARK 500    ARG H  30      -86.14     46.59                                   
REMARK 500    HIS H  46       75.19   -153.12                                   
REMARK 500    SER H 120      -97.68    -58.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D1008  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL D  45   O                                                      
REMARK 620 2 HOH D1026   O    93.0                                              
REMARK 620 3 ASP E  77   OD1  89.8  85.6                                        
REMARK 620 4 HOH E2048   O   174.5  88.3  95.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN I1004  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH I1039   O                                                      
REMARK 620 2  DG I  68   O6   93.3                                              
REMARK 620 3 HOH J1081   O   126.5 109.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN J1001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH J1043   O                                                      
REMARK 620 2 HOH J1046   O   146.1                                              
REMARK 620 3  DG J 185   N7   72.0  80.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN J1002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH J1071   O                                                      
REMARK 620 2 HOH J1041   O    71.9                                              
REMARK 620 3 HOH J1044   O    90.3 159.8                                        
REMARK 620 4  DG J 267   N7   98.6  91.7  81.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1004                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1005                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1006                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1007                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1008                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1009                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 2001                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 2002                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 2003                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2004                 
DBREF  2CV5 A    0   135  UNP    P68431   H31_HUMAN        0    135             
DBREF  2CV5 B    0   102  UNP    P62805   H4_HUMAN         0    102             
DBREF  2CV5 C    0   129  UNP    P28001   H2AA_HUMAN       0    129             
DBREF  2CV5 D   -3   122  UNP    O60814   H2BK_HUMAN       0    125             
DBREF  2CV5 E    0   135  UNP    P68431   H31_HUMAN        0    135             
DBREF  2CV5 F    0   102  UNP    P62805   H4_HUMAN         0    102             
DBREF  2CV5 G    0   129  UNP    P28001   H2AA_HUMAN       0    129             
DBREF  2CV5 H   -3   122  UNP    O60814   H2BK_HUMAN       0    125             
DBREF  2CV5 I    1   146  PDB    2CV5     2CV5             1    146             
DBREF  2CV5 J  147   292  PDB    2CV5     2CV5           147    292             
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                                                  
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  130  MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA          
SEQRES   2 C  130  LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE          
SEQRES   3 C  130  PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN          
SEQRES   4 C  130  TYR SER GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU          
SEQRES   5 C  130  ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU          
SEQRES   6 C  130  LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG          
SEQRES   7 C  130  ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP          
SEQRES   8 C  130  GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA          
SEQRES   9 C  130  GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU          
SEQRES  10 C  130  PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS          
SEQRES   1 D  126  MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS          
SEQRES   2 D  126  GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP          
SEQRES   3 D  126  GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER          
SEQRES   4 D  126  VAL 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 GLY 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 ILE 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 ALA 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  130  MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA          
SEQRES   2 G  130  LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE          
SEQRES   3 G  130  PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN          
SEQRES   4 G  130  TYR SER GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU          
SEQRES   5 G  130  ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU          
SEQRES   6 G  130  LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG          
SEQRES   7 G  130  ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP          
SEQRES   8 G  130  GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA          
SEQRES   9 G  130  GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU          
SEQRES  10 G  130  PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS          
SEQRES   1 H  126  MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS          
SEQRES   2 H  126  GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP          
SEQRES   3 H  126  GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER          
SEQRES   4 H  126  VAL 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 GLY 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 ILE 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 ALA LYS                          
HET     MN  J1001       1                                                       
HET     MN  J1002       1                                                       
HET     MN  J1003       1                                                       
HET     MN  I1004       1                                                       
HET     MN  I1005       1                                                       
HET     MN  J1006       1                                                       
HET     MN  I1007       1                                                       
HET     MN  D1008       1                                                       
HET     MN  J1009       1                                                       
HET     CL  C2001       1                                                       
HET     CL  G2002       1                                                       
HET     CL  E2003       1                                                       
HET     CL  A2004       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      CL CHLORIDE ION                                                     
FORMUL  11   MN    9(MN 2+)                                                     
FORMUL  20   CL    4(CL 1-)                                                     
FORMUL  24  HOH   *430(H2 O)                                                    
HELIX    1   1 GLY A   44  SER A   57  1                                  14    
HELIX    2   2 ARG A   63  ASP A   77  1                                  15    
HELIX    3   3 GLN A   85  ALA A  114  1                                  30    
HELIX    4   4 MET A  120  ARG A  131  1                                  12    
HELIX    5   5 ASN B   25  ILE B   29  5                                   5    
HELIX    6   6 THR B   30  GLY B   41  1                                  12    
HELIX    7   7 LEU B   49  ALA B   76  1                                  28    
HELIX    8   8 THR B   82  GLN B   93  1                                  12    
HELIX    9   9 THR C   16  GLY C   22  1                                   7    
HELIX   10  10 PRO C   26  LYS C   36  1                                  11    
HELIX   11  11 ALA C   45  ASN C   73  1                                  29    
HELIX   12  12 ILE C   79  ASN C   89  1                                  11    
HELIX   13  13 ASP C   90  LEU C   97  1                                   8    
HELIX   14  14 GLN C  112  LEU C  116  5                                   5    
HELIX   15  15 TYR D   34  HIS D   46  1                                  13    
HELIX   16  16 SER D   52  ASN D   81  1                                  30    
HELIX   17  17 THR D   87  LEU D   99  1                                  13    
HELIX   18  18 PRO D  100  SER D  120  1                                  21    
HELIX   19  19 GLY E   44  LYS E   56  1                                  13    
HELIX   20  20 ARG E   63  ASP E   77  1                                  15    
HELIX   21  21 GLN E   85  ALA E  114  1                                  30    
HELIX   22  22 MET E  120  ARG E  131  1                                  12    
HELIX   23  23 ASP F   24  ILE F   29  5                                   6    
HELIX   24  24 THR F   30  GLY F   41  1                                  12    
HELIX   25  25 LEU F   49  ALA F   76  1                                  28    
HELIX   26  26 THR F   82  GLN F   93  1                                  12    
HELIX   27  27 THR G   16  ALA G   21  1                                   6    
HELIX   28  28 PRO G   26  GLY G   37  1                                  12    
HELIX   29  29 ALA G   45  ASP G   72  1                                  28    
HELIX   30  30 ILE G   79  ASP G   90  1                                  12    
HELIX   31  31 ASP G   90  LEU G   97  1                                   8    
HELIX   32  32 GLN G  112  LEU G  116  5                                   5    
HELIX   33  33 TYR H   34  HIS H   46  1                                  13    
HELIX   34  34 SER H   52  ASN H   81  1                                  30    
HELIX   35  35 THR H   87  LEU H   99  1                                  13    
HELIX   36  36 PRO H  100  ALA H  121  1                                  22    
SHEET    1   A 2 ARG A  83  PHE A  84  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A  83           
SHEET    1   B 2 THR A 118  ILE A 119  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1   C 2 THR B  96  TYR B  98  0                                        
SHEET    2   C 2 VAL G 100  ILE G 102  1  O  THR G 101   N  TYR B  98           
SHEET    1   D 2 ARG C  42  VAL C  43  0                                        
SHEET    2   D 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  42           
SHEET    1   E 2 ARG C  77  ILE C  78  0                                        
SHEET    2   E 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  78           
SHEET    1   F 2 VAL C 100  ILE C 102  0                                        
SHEET    2   F 2 THR F  96  TYR F  98  1  O  TYR F  98   N  THR C 101           
SHEET    1   G 2 ARG E  83  PHE E  84  0                                        
SHEET    2   G 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1   H 2 THR E 118  ILE E 119  0                                        
SHEET    2   H 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1   I 2 ARG G  42  VAL G  43  0                                        
SHEET    2   I 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  42           
SHEET    1   J 2 ARG G  77  ILE G  78  0                                        
SHEET    2   J 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  78           
LINK        MN    MN D1008                 O   VAL D  45     1555   1555  2.39  
LINK        MN    MN D1008                 O   HOH D1026     1555   1555  2.27  
LINK        MN    MN I1004                 O   HOH I1039     1555   1555  2.62  
LINK        MN    MN I1004                 O6   DG I  68     1555   1555  2.38  
LINK        MN    MN I1005                 N7   DG I 121     1555   1555  2.53  
LINK        MN    MN I1007                 O   HOH I1042     1555   1555  2.67  
LINK        MN    MN J1001                 O   HOH J1043     1555   1555  2.56  
LINK        MN    MN J1001                 O   HOH J1046     1555   1555  2.45  
LINK        MN    MN J1001                 N7   DG J 185     1555   1555  2.46  
LINK        MN    MN J1002                 O   HOH J1071     1555   1555  2.39  
LINK        MN    MN J1002                 O   HOH J1041     1555   1555  2.35  
LINK        MN    MN J1002                 O   HOH J1044     1555   1555  2.22  
LINK        MN    MN J1002                 N7   DG J 267     1555   1555  2.25  
LINK        MN    MN J1003                 N7   DG J 217     1555   1555  2.60  
LINK        MN    MN J1006                 N7   DG J 280     1555   1555  2.74  
LINK        MN    MN J1009                 O   HOH J1088     1555   1555  2.16  
LINK        MN    MN D1008                 OD1 ASP E  77     1555   3555  2.09  
LINK        MN    MN D1008                 O   HOH E2048     1555   3555  2.29  
LINK        MN    MN I1004                 O   HOH J1081     1555   4555  2.41  
CISPEP   1 LYS E   37    PRO E   38          0        -0.41                     
SITE     1 AC1  4  DG J 185   DG J 186  HOH J1043  HOH J1046                    
SITE     1 AC2  4  DG J 267  HOH J1041  HOH J1044  HOH J1071                    
SITE     1 AC3  2  DG J 217  HOH J1042                                          
SITE     1 AC4  3  DG I  68  HOH I1039  HOH J1081                               
SITE     1 AC5  1  DG I 121                                                     
SITE     1 AC6  1  DG J 280                                                     
SITE     1 AC7  2  DG I 134  HOH I1042                                          
SITE     1 AC8  4 VAL D  45  HOH D1026  ASP E  77  HOH E2048                    
SITE     1 AC9  3 HOH I1095  HOH J1087  HOH J1088                               
SITE     1 BC1  4 GLY C  46  ALA C  47  THR D  87  SER D  88                    
SITE     1 BC2  6 GLY G  44  ALA G  45  GLY G  46  ALA G  47                    
SITE     2 BC2  6 THR H  87  SER H  88                                          
SITE     1 BC3  2 PRO E 121  LYS E 122                                          
SITE     1 BC4  2 PRO A 121  LYS A 122                                          
CRYST1   99.564  108.370  169.425  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      0.010044  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009228  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005902        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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