GenomeNet

Database: PDB
Entry: 4X23
LinkDB: 4X23
Original site: 4X23 
HEADER    STRUCTURAL PROTEIN/DNA                  25-NOV-14   4X23              
TITLE     CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE       
TITLE    2 PARTICLE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (147-MER);                                             
COMPND   3 CHAIN: I, S;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: 147 BP WIDOM 601 DNA FRAGMENT (+ STRAND);             
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (147-MER);                                             
COMPND   8 CHAIN: J, T;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: 147 BP WIDOM 601 DNA FRAGMENT (- STRAND);             
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HISTONE H3;                                                
COMPND  13 CHAIN: A, E, K, O;                                                   
COMPND  14 FRAGMENT: UNP RESIDUES 41-133;                                       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: HISTONE H4;                                                
COMPND  18 CHAIN: B, F, L, P;                                                   
COMPND  19 FRAGMENT: UNP RESIDUES 25-103;                                       
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: HISTONE H2A;                                               
COMPND  23 CHAIN: C, G, M, Q;                                                   
COMPND  24 FRAGMENT: UNP RESIDUES 16-117;                                       
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MOL_ID: 6;                                                           
COMPND  27 MOLECULE: HISTONE H2B;                                               
COMPND  28 CHAIN: D, H, N, R;                                                   
COMPND  29 FRAGMENT: UNP RESIDUES 33-122;                                       
COMPND  30 ENGINEERED: YES;                                                     
COMPND  31 MOL_ID: 7;                                                           
COMPND  32 MOLECULE: CENP-C;                                                    
COMPND  33 CHAIN: V, U, X, W;                                                   
COMPND  34 FRAGMENT: UNP RESIDUES 710-734;                                      
COMPND  35 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  13 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  14 ORGANISM_TAXID: 7227;                                                
SOURCE  15 GENE: HIS3;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 4;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  20 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  21 ORGANISM_TAXID: 7227;                                                
SOURCE  22 GENE: HIS4;                                                          
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  27 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  28 ORGANISM_TAXID: 7227;                                                
SOURCE  29 GENE: HIS2A;                                                         
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  32 MOL_ID: 6;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  34 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  35 ORGANISM_TAXID: 7227;                                                
SOURCE  36 GENE: HIS2B;                                                         
SOURCE  37 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  39 MOL_ID: 7;                                                           
SOURCE  40 SYNTHETIC: YES;                                                      
SOURCE  41 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  42 ORGANISM_COMMON: RAT;                                                
SOURCE  43 ORGANISM_TAXID: 10116                                                
KEYWDS    NUCLEOSOME CORE PARTICLE, WIDOM 601 DNA FRAGMMENT, HISTONE FOLD,      
KEYWDS   2 CENP-C COMPLEX, SEGREGATION, CHROMOSOME CENTROMERE, KINETOCHORE      
KEYWDS   3 ASSEMBLY, CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK (CCAN)          
KEYWDS   4 PROTEINS, STRUCTURAL PROTEIN-DNA COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.JIANG                                                             
REVDAT   4   22-NOV-17 4X23    1       REMARK                                   
REVDAT   3   13-JUL-16 4X23    1       REMARK                                   
REVDAT   2   24-DEC-14 4X23    1       REMARK                                   
REVDAT   1   10-DEC-14 4X23    0                                                
SPRSDE     10-DEC-14 4X23      4INM                                             
JRNL        AUTH   H.KATO,J.S.JIANG,B.R.ZHOU,M.ROZENDAAL,H.FENG,R.GHIRLANDO,    
JRNL        AUTH 2 T.S.XIAO,A.F.STRAIGHT,Y.BAI                                  
JRNL        TITL   A CONSERVED MECHANISM FOR CENTROMERIC NUCLEOSOME RECOGNITION 
JRNL        TITL 2 BY CENTROMERE PROTEIN CENP-C.                                
JRNL        REF    SCIENCE                       V. 340  1110 2013              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   23723239                                                     
JRNL        DOI    10.1126/SCIENCE.1235532                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1690)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 48623                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.780                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1838                            
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 49.5482 -  8.2181    1.00     3833   150  0.1593 0.2019        
REMARK   3     2  8.2181 -  6.5277    1.00     3651   145  0.2255 0.2718        
REMARK   3     3  6.5277 -  5.7039    1.00     3638   142  0.2671 0.3533        
REMARK   3     4  5.7039 -  5.1830    1.00     3595   141  0.2771 0.3426        
REMARK   3     5  5.1830 -  4.8118    1.00     3618   142  0.2448 0.2605        
REMARK   3     6  4.8118 -  4.5283    1.00     3564   140  0.2403 0.2486        
REMARK   3     7  4.5283 -  4.3017    1.00     3574   141  0.2449 0.2784        
REMARK   3     8  4.3017 -  4.1145    1.00     3564   140  0.2710 0.3522        
REMARK   3     9  4.1145 -  3.9562    1.00     3572   140  0.2904 0.3269        
REMARK   3    10  3.9562 -  3.8197    1.00     3540   139  0.3038 0.4004        
REMARK   3    11  3.8197 -  3.7003    1.00     3554   140  0.3159 0.3877        
REMARK   3    12  3.7003 -  3.5946    1.00     3545   140  0.3313 0.3636        
REMARK   3    13  3.5946 -  3.5000    1.00     3537   138  0.3500 0.4249        
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)     : 0.590            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 122.9                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 157.6                          
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      :  0.003          25588                                  
REMARK   3   ANGLE     :  0.559          37074                                  
REMARK   3   CHIRALITY :  0.022           4220                                  
REMARK   3   PLANARITY :  0.002           2672                                  
REMARK   3   DIHEDRAL  : 26.071          10504                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: CNS 1.3 WAS USED FOR LOW RESOLUTION       
REMARK   3  REFINEMENT                                                          
REMARK   4                                                                      
REMARK   4 4X23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204912.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-12; 22-JUN-12               
REMARK 200  TEMPERATURE           (KELVIN) : 274; 274                           
REMARK 200  PH                             : 7.4 - 7.6                          
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; NSLS                          
REMARK 200  BEAMLINE                       : 23-ID-D; X29A                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033; 1.075                       
REMARK 200  MONOCHROMATOR                  : GRAPHITE; GRAPHITE                 
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, HKL-2000, SCALEPACK           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48623                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2PYO, 3MVD                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPD, 40MM SODIUM CACODYLATE, 24MM    
REMARK 280  SPERMINE TETRA-HCL, 80MM SODIUM CHLORIDE, 20MM MAGNESIUM            
REMARK 280  CHLORIDE; RESERVIOR 35% MPD. PH 7.5, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 294K                                              
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       51.49700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.42300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       88.05100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.42300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.49700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       88.05100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, C, D, E, F, G, H,         
REMARK 350                    AND CHAINS: V, U                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, K, L, M, N, O, P, Q, R,         
REMARK 350                    AND CHAINS: X, W                                  
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      DA I     1                                                      
REMARK 465      DT J   147                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     LEU A   137                                                      
REMARK 465     PRO V   710                                                      
REMARK 465     ASN V   711                                                      
REMARK 465     GLN V   734                                                      
REMARK 465     PRO U   710                                                      
REMARK 465     ASN U   711                                                      
REMARK 465     VAL U   712                                                      
REMARK 465     ARG U   713                                                      
REMARK 465     ARG U   714                                                      
REMARK 465     SER U   715                                                      
REMARK 465     LYS U   721                                                      
REMARK 465     PRO U   722                                                      
REMARK 465     LEU U   723                                                      
REMARK 465     GLU U   724                                                      
REMARK 465     TYR U   725                                                      
REMARK 465     TRP U   726                                                      
REMARK 465     ARG U   727                                                      
REMARK 465     GLY U   728                                                      
REMARK 465     GLU U   729                                                      
REMARK 465     ARG U   730                                                      
REMARK 465     ILE U   731                                                      
REMARK 465     ASP U   732                                                      
REMARK 465     TYR U   733                                                      
REMARK 465     GLN U   734                                                      
REMARK 465      DA S     1                                                      
REMARK 465      DT T   147                                                      
REMARK 465     GLY K   135                                                      
REMARK 465     GLY K   136                                                      
REMARK 465     LEU K   137                                                      
REMARK 465     SER R   120                                                      
REMARK 465     SER R   121                                                      
REMARK 465     PRO X   710                                                      
REMARK 465     ASN X   711                                                      
REMARK 465     VAL X   712                                                      
REMARK 465     GLN X   734                                                      
REMARK 465     PRO W   710                                                      
REMARK 465     ASN W   711                                                      
REMARK 465     VAL W   712                                                      
REMARK 465     ARG W   713                                                      
REMARK 465     ARG W   714                                                      
REMARK 465     ILE W   718                                                      
REMARK 465     ARG W   719                                                      
REMARK 465     LEU W   720                                                      
REMARK 465     LYS W   721                                                      
REMARK 465     PRO W   722                                                      
REMARK 465     LEU W   723                                                      
REMARK 465     GLU W   724                                                      
REMARK 465     TYR W   725                                                      
REMARK 465     TRP W   726                                                      
REMARK 465     ARG W   727                                                      
REMARK 465     GLY W   728                                                      
REMARK 465     GLU W   729                                                      
REMARK 465     ARG W   730                                                      
REMARK 465     ILE W   731                                                      
REMARK 465     ASP W   732                                                      
REMARK 465     TYR W   733                                                      
REMARK 465     GLN W   734                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     GLU G  55    CG   CD   OE1  OE2                                  
REMARK 470     ASN U 716    CG   OD1  ND2                                       
REMARK 470     LEU U 720    CG   CD1  CD2                                       
REMARK 470     ARG K  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP K 106    CG   OD1  OD2                                       
REMARK 470     LEU K 109    CG   CD1  CD2                                       
REMARK 470     GLU K 134    CG   CD   OE1  OE2                                  
REMARK 470     ARG O  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE G   29   CG1  CG2  CD1                                       
REMARK 480     LEU G   33   CG   CD1  CD2                                       
REMARK 480     LEU G   50   CG   CD1  CD2                                       
REMARK 480     MET G   54   CG   SD   CE                                        
REMARK 480     ILE H   86   CG1  CG2  CD1                                       
REMARK 480     ILE M   29   CG1  CG2  CD1                                       
REMARK 480     LEU M   33   CG   CD1  CD2                                       
REMARK 480     LEU M   50   CG   CD1  CD2                                       
REMARK 480     MET M   54   CG   SD   CE                                        
REMARK 480     ILE N   86   CG1  CG2  CD1                                       
REMARK 480     ILE Q   29   CG1  CG2  CD1                                       
REMARK 480     LEU Q   33   CG   CD1  CD2                                       
REMARK 480     LEU Q   50   CD1  CD2                                            
REMARK 480     MET Q   54   CG   SD   CE                                        
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    TYR A  41     -152.27    -91.59                                   
REMARK 500    PRO A  43       93.45    -61.31                                   
REMARK 500    ASP A  81       70.30     55.15                                   
REMARK 500    LYS B  44      -61.45    -99.44                                   
REMARK 500    GLN B  93       38.08   -149.83                                   
REMARK 500    ARG B  95       48.27   -107.93                                   
REMARK 500    LEU C  96       34.35    -96.67                                   
REMARK 500    PRO C 108      102.71    -59.79                                   
REMARK 500    HIS D  46       87.36   -157.25                                   
REMARK 500    PRO D 100      -84.47    -41.86                                   
REMARK 500    SER D 120      -96.64   -101.78                                   
REMARK 500    TYR E  41     -150.08    -88.87                                   
REMARK 500    PRO E  43       94.58    -60.26                                   
REMARK 500    ASP E  81       70.72     55.79                                   
REMARK 500    LYS F  44      -61.86    -99.44                                   
REMARK 500    GLN F  93       37.66   -149.38                                   
REMARK 500    ARG F  95       49.42   -107.72                                   
REMARK 500    LEU G  96       34.04    -96.91                                   
REMARK 500    GLN G 103       43.44     37.22                                   
REMARK 500    HIS H  46       89.42   -158.99                                   
REMARK 500    GLU H 102      -25.92     64.13                                   
REMARK 500    ARG V 713     -152.29   -125.45                                   
REMARK 500    ARG V 717     -162.58   -129.80                                   
REMARK 500    LEU V 720      -96.99   -125.65                                   
REMARK 500    LEU V 723       -9.19     67.90                                   
REMARK 500    GLU V 724     -161.43     58.34                                   
REMARK 500    TYR V 725     -143.50   -179.02                                   
REMARK 500    TRP V 726      -13.76     42.40                                   
REMARK 500    ARG V 727      -34.28   -154.41                                   
REMARK 500    ARG U 717     -160.47    -73.76                                   
REMARK 500    TYR K  41       41.98    -92.76                                   
REMARK 500    PRO K  43       92.48    -62.16                                   
REMARK 500    ASP K  81       70.79     55.67                                   
REMARK 500    LYS L  44      -61.40    -99.62                                   
REMARK 500    GLN L  93       38.07   -149.58                                   
REMARK 500    ARG L  95       47.76   -108.45                                   
REMARK 500    LEU M  96       33.76    -96.88                                   
REMARK 500    GLN M 103       43.59     37.52                                   
REMARK 500    HIS N  46       88.22   -157.50                                   
REMARK 500    GLU N 102      -30.33     68.73                                   
REMARK 500    SER N 120     -161.04   -101.57                                   
REMARK 500    PRO O  43       94.55    -60.83                                   
REMARK 500    ASP O  81       70.59     55.44                                   
REMARK 500    LYS P  44      -62.06    -98.84                                   
REMARK 500    GLN P  93       37.79   -148.53                                   
REMARK 500    ARG P  95       48.38   -108.14                                   
REMARK 500    LEU Q  96       33.21    -97.08                                   
REMARK 500    GLN Q 103       44.02     37.51                                   
REMARK 500    HIS R  46       88.74   -158.25                                   
REMARK 500    LEU X 720      -99.12   -127.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4INM   RELATED DB: PDB                                   
REMARK 900 DNA SEQUENCES HAD ERRORS IN 4INM. DNA SEQUENCES ARE CORRECTED AND    
REMARK 900 COORDINATES ARE UPDATED IN THIS ENTRY.                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DISCREPANCY AT THE C-TERM OF H3 SEQUENCES (CHAINS A,E,K,O) IS A  
REMARK 999 RESULT OF CHIMERIC CENP-A, I.E. THE LAST THREE RESIDUES OF H3 (-ERA) 
REMARK 999 TO THE LAST SIX RESIDUES OF CENP-A (-IEGGLG)                         
DBREF  4X23 I    1   147  PDB    4X23     4X23             1    147             
DBREF  4X23 J    1   147  PDB    4X23     4X23             1    147             
DBREF  4X23 A   40   132  UNP    P02299   H3_DROME        41    133             
DBREF  4X23 B   24   102  UNP    P84040   H4_DROME        25    103             
DBREF  4X23 C   15   116  UNP    P84051   H2A_DROME       16    117             
DBREF  4X23 D   32   121  UNP    P02283   H2B_DROME       33    122             
DBREF  4X23 E   40   132  UNP    P02299   H3_DROME        41    133             
DBREF  4X23 F   24   102  UNP    P84040   H4_DROME        25    103             
DBREF  4X23 G   15   116  UNP    P84051   H2A_DROME       16    117             
DBREF  4X23 H   32   121  UNP    P02283   H2B_DROME       33    122             
DBREF  4X23 V  710   734  UNP    Q66LH7   Q66LH7_RAT     710    734             
DBREF  4X23 U  710   734  UNP    Q66LH7   Q66LH7_RAT     710    734             
DBREF  4X23 S    1   147  PDB    4X23     4X23             1    147             
DBREF  4X23 T    1   147  PDB    4X23     4X23             1    147             
DBREF  4X23 K   40   132  UNP    P02299   H3_DROME        41    133             
DBREF  4X23 L   24   102  UNP    P84040   H4_DROME        25    103             
DBREF  4X23 M   15   116  UNP    P84051   H2A_DROME       16    117             
DBREF  4X23 N   32   121  UNP    P02283   H2B_DROME       33    122             
DBREF  4X23 O   40   132  UNP    P02299   H3_DROME        41    133             
DBREF  4X23 P   24   102  UNP    P84040   H4_DROME        25    103             
DBREF  4X23 Q   15   116  UNP    P84051   H2A_DROME       16    117             
DBREF  4X23 R   32   121  UNP    P02283   H2B_DROME       33    122             
DBREF  4X23 X  710   734  UNP    Q66LH7   Q66LH7_RAT     710    734             
DBREF  4X23 W  710   734  UNP    Q66LH7   Q66LH7_RAT     710    734             
SEQADV 4X23 ILE A  133  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLU A  134  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY A  135  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY A  136  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 LEU A  137  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 ILE E  133  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLU E  134  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY E  135  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY E  136  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 LEU E  137  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 ILE K  133  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLU K  134  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY K  135  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY K  136  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 LEU K  137  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 ILE O  133  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLU O  134  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY O  135  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 GLY O  136  UNP  P02299              EXPRESSION TAG                 
SEQADV 4X23 LEU O  137  UNP  P02299              EXPRESSION TAG                 
SEQRES   1 I  147   DA  DT  DC  DG  DA  DG  DA  DA  DT  DC  DC  DC  DG          
SEQRES   2 I  147   DG  DT  DG  DC  DC  DG  DA  DG  DG  DC  DC  DG  DC          
SEQRES   3 I  147   DT  DC  DA  DA  DT  DT  DG  DG  DT  DC  DG  DT  DA          
SEQRES   4 I  147   DG  DA  DC  DA  DG  DC  DT  DC  DT  DA  DG  DC  DA          
SEQRES   5 I  147   DC  DC  DG  DC  DT  DT  DA  DA  DA  DC  DG  DC  DA          
SEQRES   6 I  147   DC  DG  DT  DA  DC  DG  DC  DG  DC  DT  DG  DT  DC          
SEQRES   7 I  147   DC  DC  DC  DC  DG  DC  DG  DT  DT  DT  DT  DA  DA          
SEQRES   8 I  147   DC  DC  DG  DC  DC  DA  DA  DG  DG  DG  DG  DA  DT          
SEQRES   9 I  147   DT  DA  DC  DT  DC  DC  DC  DT  DA  DG  DT  DC  DT          
SEQRES  10 I  147   DC  DC  DA  DG  DG  DC  DA  DC  DG  DT  DG  DT  DC          
SEQRES  11 I  147   DA  DG  DA  DT  DA  DT  DA  DT  DA  DC  DA  DT  DC          
SEQRES  12 I  147   DC  DG  DA  DT                                              
SEQRES   1 J  147   DA  DT  DC  DG  DG  DA  DT  DG  DT  DA  DT  DA  DT          
SEQRES   2 J  147   DA  DT  DC  DT  DG  DA  DC  DA  DC  DG  DT  DG  DC          
SEQRES   3 J  147   DC  DT  DG  DG  DA  DG  DA  DC  DT  DA  DG  DG  DG          
SEQRES   4 J  147   DA  DG  DT  DA  DA  DT  DC  DC  DC  DC  DT  DT  DG          
SEQRES   5 J  147   DG  DC  DG  DG  DT  DT  DA  DA  DA  DA  DC  DG  DC          
SEQRES   6 J  147   DG  DG  DG  DG  DG  DA  DC  DA  DG  DC  DG  DC  DG          
SEQRES   7 J  147   DT  DA  DC  DG  DT  DG  DC  DG  DT  DT  DT  DA  DA          
SEQRES   8 J  147   DG  DC  DG  DG  DT  DG  DC  DT  DA  DG  DA  DG  DC          
SEQRES   9 J  147   DT  DG  DT  DC  DT  DA  DC  DG  DA  DC  DC  DA  DA          
SEQRES  10 J  147   DT  DT  DG  DA  DG  DC  DG  DG  DC  DC  DT  DC  DG          
SEQRES  11 J  147   DG  DC  DA  DC  DC  DG  DG  DG  DA  DT  DT  DC  DT          
SEQRES  12 J  147   DC  DG  DA  DT                                              
SEQRES   1 A   98  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   2 A   98  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   3 A   98  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   4 A   98  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   5 A   98  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   6 A   98  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES   7 A   98  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES   8 A   98  ARG GLY ILE GLU GLY GLY LEU                                  
SEQRES   1 B   79  ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG          
SEQRES   2 B   79  LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU          
SEQRES   3 B   79  ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU          
SEQRES   4 B   79  GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS          
SEQRES   5 B   79  ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR          
SEQRES   6 B   79  ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY          
SEQRES   7 B   79  GLY                                                          
SEQRES   1 C  102  SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL GLY          
SEQRES   2 C  102  ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU          
SEQRES   3 C  102  ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL          
SEQRES   4 C  102  MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA GLY          
SEQRES   5 C  102  ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO          
SEQRES   6 C  102  ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU LEU          
SEQRES   7 C  102  ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY GLY          
SEQRES   8 C  102  VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO                  
SEQRES   1 D   90  GLU SER TYR ALA ILE TYR ILE TYR LYS VAL LEU LYS GLN          
SEQRES   2 D   90  VAL HIS PRO ASP THR GLY ILE SER SER LYS ALA MET SER          
SEQRES   3 D   90  ILE MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE          
SEQRES   4 D   90  ALA ALA GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG          
SEQRES   5 D   90  SER THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG          
SEQRES   6 D   90  LEU LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER          
SEQRES   7 D   90  GLU GLY THR LYS ALA VAL THR LYS TYR THR SER SER              
SEQRES   1 E   98  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   2 E   98  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   3 E   98  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   4 E   98  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   5 E   98  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   6 E   98  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES   7 E   98  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES   8 E   98  ARG GLY ILE GLU GLY GLY LEU                                  
SEQRES   1 F   79  ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG          
SEQRES   2 F   79  LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU          
SEQRES   3 F   79  ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU          
SEQRES   4 F   79  GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS          
SEQRES   5 F   79  ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR          
SEQRES   6 F   79  ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY          
SEQRES   7 F   79  GLY                                                          
SEQRES   1 G  102  SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL GLY          
SEQRES   2 G  102  ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU          
SEQRES   3 G  102  ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL          
SEQRES   4 G  102  MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA GLY          
SEQRES   5 G  102  ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO          
SEQRES   6 G  102  ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU LEU          
SEQRES   7 G  102  ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY GLY          
SEQRES   8 G  102  VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO                  
SEQRES   1 H   90  GLU SER TYR ALA ILE TYR ILE TYR LYS VAL LEU LYS GLN          
SEQRES   2 H   90  VAL HIS PRO ASP THR GLY ILE SER SER LYS ALA MET SER          
SEQRES   3 H   90  ILE MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE          
SEQRES   4 H   90  ALA ALA GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG          
SEQRES   5 H   90  SER THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG          
SEQRES   6 H   90  LEU LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER          
SEQRES   7 H   90  GLU GLY THR LYS ALA VAL THR LYS TYR THR SER SER              
SEQRES   1 V   25  PRO ASN VAL ARG ARG SER ASN ARG ILE ARG LEU LYS PRO          
SEQRES   2 V   25  LEU GLU TYR TRP ARG GLY GLU ARG ILE ASP TYR GLN              
SEQRES   1 U   25  PRO ASN VAL ARG ARG SER ASN ARG ILE ARG LEU LYS PRO          
SEQRES   2 U   25  LEU GLU TYR TRP ARG GLY GLU ARG ILE ASP TYR GLN              
SEQRES   1 S  147   DA  DT  DC  DG  DA  DG  DA  DA  DT  DC  DC  DC  DG          
SEQRES   2 S  147   DG  DT  DG  DC  DC  DG  DA  DG  DG  DC  DC  DG  DC          
SEQRES   3 S  147   DT  DC  DA  DA  DT  DT  DG  DG  DT  DC  DG  DT  DA          
SEQRES   4 S  147   DG  DA  DC  DA  DG  DC  DT  DC  DT  DA  DG  DC  DA          
SEQRES   5 S  147   DC  DC  DG  DC  DT  DT  DA  DA  DA  DC  DG  DC  DA          
SEQRES   6 S  147   DC  DG  DT  DA  DC  DG  DC  DG  DC  DT  DG  DT  DC          
SEQRES   7 S  147   DC  DC  DC  DC  DG  DC  DG  DT  DT  DT  DT  DA  DA          
SEQRES   8 S  147   DC  DC  DG  DC  DC  DA  DA  DG  DG  DG  DG  DA  DT          
SEQRES   9 S  147   DT  DA  DC  DT  DC  DC  DC  DT  DA  DG  DT  DC  DT          
SEQRES  10 S  147   DC  DC  DA  DG  DG  DC  DA  DC  DG  DT  DG  DT  DC          
SEQRES  11 S  147   DA  DG  DA  DT  DA  DT  DA  DT  DA  DC  DA  DT  DC          
SEQRES  12 S  147   DC  DG  DA  DT                                              
SEQRES   1 T  147   DA  DT  DC  DG  DG  DA  DT  DG  DT  DA  DT  DA  DT          
SEQRES   2 T  147   DA  DT  DC  DT  DG  DA  DC  DA  DC  DG  DT  DG  DC          
SEQRES   3 T  147   DC  DT  DG  DG  DA  DG  DA  DC  DT  DA  DG  DG  DG          
SEQRES   4 T  147   DA  DG  DT  DA  DA  DT  DC  DC  DC  DC  DT  DT  DG          
SEQRES   5 T  147   DG  DC  DG  DG  DT  DT  DA  DA  DA  DA  DC  DG  DC          
SEQRES   6 T  147   DG  DG  DG  DG  DG  DA  DC  DA  DG  DC  DG  DC  DG          
SEQRES   7 T  147   DT  DA  DC  DG  DT  DG  DC  DG  DT  DT  DT  DA  DA          
SEQRES   8 T  147   DG  DC  DG  DG  DT  DG  DC  DT  DA  DG  DA  DG  DC          
SEQRES   9 T  147   DT  DG  DT  DC  DT  DA  DC  DG  DA  DC  DC  DA  DA          
SEQRES  10 T  147   DT  DT  DG  DA  DG  DC  DG  DG  DC  DC  DT  DC  DG          
SEQRES  11 T  147   DG  DC  DA  DC  DC  DG  DG  DG  DA  DT  DT  DC  DT          
SEQRES  12 T  147   DC  DG  DA  DT                                              
SEQRES   1 K   98  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   2 K   98  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   3 K   98  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   4 K   98  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   5 K   98  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   6 K   98  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES   7 K   98  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES   8 K   98  ARG GLY ILE GLU GLY GLY LEU                                  
SEQRES   1 L   79  ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG          
SEQRES   2 L   79  LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU          
SEQRES   3 L   79  ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU          
SEQRES   4 L   79  GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS          
SEQRES   5 L   79  ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR          
SEQRES   6 L   79  ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY          
SEQRES   7 L   79  GLY                                                          
SEQRES   1 M  102  SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL GLY          
SEQRES   2 M  102  ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU          
SEQRES   3 M  102  ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL          
SEQRES   4 M  102  MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA GLY          
SEQRES   5 M  102  ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO          
SEQRES   6 M  102  ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU LEU          
SEQRES   7 M  102  ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY GLY          
SEQRES   8 M  102  VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO                  
SEQRES   1 N   90  GLU SER TYR ALA ILE TYR ILE TYR LYS VAL LEU LYS GLN          
SEQRES   2 N   90  VAL HIS PRO ASP THR GLY ILE SER SER LYS ALA MET SER          
SEQRES   3 N   90  ILE MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE          
SEQRES   4 N   90  ALA ALA GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG          
SEQRES   5 N   90  SER THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG          
SEQRES   6 N   90  LEU LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER          
SEQRES   7 N   90  GLU GLY THR LYS ALA VAL THR LYS TYR THR SER SER              
SEQRES   1 O   98  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   2 O   98  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   3 O   98  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   4 O   98  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   5 O   98  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   6 O   98  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES   7 O   98  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES   8 O   98  ARG GLY ILE GLU GLY GLY LEU                                  
SEQRES   1 P   79  ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG          
SEQRES   2 P   79  LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU          
SEQRES   3 P   79  ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU          
SEQRES   4 P   79  GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS          
SEQRES   5 P   79  ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR          
SEQRES   6 P   79  ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY          
SEQRES   7 P   79  GLY                                                          
SEQRES   1 Q  102  SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL GLY          
SEQRES   2 Q  102  ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA GLU          
SEQRES   3 Q  102  ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA VAL          
SEQRES   4 Q  102  MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA GLY          
SEQRES   5 Q  102  ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE PRO          
SEQRES   6 Q  102  ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU LEU          
SEQRES   7 Q  102  ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY GLY          
SEQRES   8 Q  102  VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO                  
SEQRES   1 R   90  GLU SER TYR ALA ILE TYR ILE TYR LYS VAL LEU LYS GLN          
SEQRES   2 R   90  VAL HIS PRO ASP THR GLY ILE SER SER LYS ALA MET SER          
SEQRES   3 R   90  ILE MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE          
SEQRES   4 R   90  ALA ALA GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG          
SEQRES   5 R   90  SER THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG          
SEQRES   6 R   90  LEU LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER          
SEQRES   7 R   90  GLU GLY THR LYS ALA VAL THR LYS TYR THR SER SER              
SEQRES   1 X   25  PRO ASN VAL ARG ARG SER ASN ARG ILE ARG LEU LYS PRO          
SEQRES   2 X   25  LEU GLU TYR TRP ARG GLY GLU ARG ILE ASP TYR GLN              
SEQRES   1 W   25  PRO ASN VAL ARG ARG SER ASN ARG ILE ARG LEU LYS PRO          
SEQRES   2 W   25  LEU GLU TYR TRP ARG GLY GLU ARG ILE ASP TYR GLN              
HELIX    1 AA1 GLY A   44  LYS A   56  1                                  13    
HELIX    2 AA2 ARG A   63  ASP A   77  1                                  15    
HELIX    3 AA3 GLN A   85  ALA A  114  1                                  30    
HELIX    4 AA4 MET A  120  GLY A  132  1                                  13    
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  ARG B   92  1                                  11    
HELIX    9 AA9 PRO C   25  GLY C   36  1                                  12    
HELIX   10 AB1 GLY C   45  ASP C   71  1                                  27    
HELIX   11 AB2 ILE C   78  ARG C   87  1                                  10    
HELIX   12 AB3 ASP C   89  LEU C   96  1                                   8    
HELIX   13 AB4 GLN C  111  LEU C  115  5                                   5    
HELIX   14 AB5 TYR D   34  HIS D   46  1                                  13    
HELIX   15 AB6 SER D   52  ASN D   81  1                                  30    
HELIX   16 AB7 THR D   87  LEU D   99  1                                  13    
HELIX   17 AB8 GLY D  101  TYR D  118  1                                  18    
HELIX   18 AB9 GLY E   44  LYS E   56  1                                  13    
HELIX   19 AC1 ARG E   63  LYS E   79  1                                  17    
HELIX   20 AC2 GLN E   85  ALA E  114  1                                  30    
HELIX   21 AC3 MET E  120  GLY E  132  1                                  13    
HELIX   22 AC4 ASN F   25  ILE F   29  5                                   5    
HELIX   23 AC5 THR F   30  GLY F   41  1                                  12    
HELIX   24 AC6 LEU F   49  ALA F   76  1                                  28    
HELIX   25 AC7 THR F   82  ARG F   92  1                                  11    
HELIX   26 AC8 PRO G   25  GLY G   36  1                                  12    
HELIX   27 AC9 GLY G   45  ASP G   71  1                                  27    
HELIX   28 AD1 ILE G   78  ARG G   87  1                                  10    
HELIX   29 AD2 ASP G   89  LEU G   96  1                                   8    
HELIX   30 AD3 GLN G  111  LEU G  115  5                                   5    
HELIX   31 AD4 TYR H   34  HIS H   46  1                                  13    
HELIX   32 AD5 SER H   52  ASN H   81  1                                  30    
HELIX   33 AD6 THR H   87  LEU H   99  1                                  13    
HELIX   34 AD7 GLU H  102  SER H  121  1                                  20    
HELIX   35 AD8 GLY K   44  LYS K   56  1                                  13    
HELIX   36 AD9 ARG K   63  LYS K   79  1                                  17    
HELIX   37 AE1 GLN K   85  ALA K  114  1                                  30    
HELIX   38 AE2 MET K  120  GLY K  132  1                                  13    
HELIX   39 AE3 ASN L   25  ILE L   29  5                                   5    
HELIX   40 AE4 THR L   30  GLY L   41  1                                  12    
HELIX   41 AE5 LEU L   49  ALA L   76  1                                  28    
HELIX   42 AE6 THR L   82  ARG L   92  1                                  11    
HELIX   43 AE7 PRO M   25  GLY M   36  1                                  12    
HELIX   44 AE8 GLY M   45  ASP M   71  1                                  27    
HELIX   45 AE9 ILE M   78  ARG M   87  1                                  10    
HELIX   46 AF1 ASP M   89  LEU M   96  1                                   8    
HELIX   47 AF2 GLN M  111  LEU M  115  5                                   5    
HELIX   48 AF3 TYR N   34  HIS N   46  1                                  13    
HELIX   49 AF4 SER N   52  ASN N   81  1                                  30    
HELIX   50 AF5 THR N   87  LEU N   99  1                                  13    
HELIX   51 AF6 GLU N  102  TYR N  118  1                                  17    
HELIX   52 AF7 GLY O   44  LYS O   56  1                                  13    
HELIX   53 AF8 ARG O   63  LYS O   79  1                                  17    
HELIX   54 AF9 GLN O   85  ALA O  114  1                                  30    
HELIX   55 AG1 MET O  120  GLY O  132  1                                  13    
HELIX   56 AG2 ASN P   25  ILE P   29  5                                   5    
HELIX   57 AG3 THR P   30  GLY P   41  1                                  12    
HELIX   58 AG4 LEU P   49  ALA P   76  1                                  28    
HELIX   59 AG5 THR P   82  ARG P   92  1                                  11    
HELIX   60 AG6 PRO Q   25  GLY Q   36  1                                  12    
HELIX   61 AG7 GLY Q   45  ASP Q   71  1                                  27    
HELIX   62 AG8 ILE Q   78  ARG Q   87  1                                  10    
HELIX   63 AG9 ASP Q   89  LEU Q   96  1                                   8    
HELIX   64 AH1 GLN Q  111  LEU Q  115  5                                   5    
HELIX   65 AH2 TYR R   34  HIS R   46  1                                  13    
HELIX   66 AH3 SER R   52  ASN R   81  1                                  30    
HELIX   67 AH4 THR R   87  LEU R   99  1                                  13    
HELIX   68 AH5 PRO R  100  TYR R  118  1                                  19    
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 THR B  96  TYR B  98  0                                        
SHEET    2 AA3 2 VAL G  99  ILE G 101  1  O  THR G 100   N  THR B  96           
SHEET    1 AA4 2 ARG C  41  VAL C  42  0                                        
SHEET    2 AA4 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  41           
SHEET    1 AA5 2 ARG C  76  ILE C  77  0                                        
SHEET    2 AA5 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  77           
SHEET    1 AA6 2 THR C 100  ILE C 101  0                                        
SHEET    2 AA6 2 LEU F  97  TYR F  98  1  O  TYR F  98   N  THR C 100           
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  41  VAL G  42  0                                        
SHEET    2 AA9 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  41           
SHEET    1 AB1 2 ARG G  76  ILE G  77  0                                        
SHEET    2 AB1 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  77           
SHEET    1 AB2 2 ARG K  83  PHE K  84  0                                        
SHEET    2 AB2 2 THR L  80  VAL L  81  1  O  VAL L  81   N  ARG K  83           
SHEET    1 AB3 2 THR K 118  ILE K 119  0                                        
SHEET    2 AB3 2 ARG L  45  ILE L  46  1  O  ARG L  45   N  ILE K 119           
SHEET    1 AB4 2 LEU L  97  TYR L  98  0                                        
SHEET    2 AB4 2 THR Q 100  ILE Q 101  1  O  THR Q 100   N  TYR L  98           
SHEET    1 AB5 2 ARG M  41  VAL M  42  0                                        
SHEET    2 AB5 2 THR N  85  ILE N  86  1  O  ILE N  86   N  ARG M  41           
SHEET    1 AB6 2 ARG M  76  ILE M  77  0                                        
SHEET    2 AB6 2 GLY N  50  ILE N  51  1  O  GLY N  50   N  ILE M  77           
SHEET    1 AB7 2 THR M 100  ILE M 101  0                                        
SHEET    2 AB7 2 LEU P  97  TYR P  98  1  O  TYR P  98   N  THR M 100           
SHEET    1 AB8 2 ARG O  83  PHE O  84  0                                        
SHEET    2 AB8 2 THR P  80  VAL P  81  1  O  VAL P  81   N  ARG O  83           
SHEET    1 AB9 2 THR O 118  ILE O 119  0                                        
SHEET    2 AB9 2 ARG P  45  ILE P  46  1  O  ARG P  45   N  ILE O 119           
SHEET    1 AC1 2 ARG Q  41  VAL Q  42  0                                        
SHEET    2 AC1 2 THR R  85  ILE R  86  1  O  ILE R  86   N  ARG Q  41           
SHEET    1 AC2 2 ARG Q  76  ILE Q  77  0                                        
SHEET    2 AC2 2 GLY R  50  ILE R  51  1  O  GLY R  50   N  ILE Q  77           
CRYST1  102.994  176.102  208.846  90.00  90.00  90.00 P 21 21 21   16          
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      0.009709  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005679  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system