GenomeNet

Database: PDB
Entry: 4QLC
LinkDB: 4QLC
Original site: 4QLC 
HEADER    CHROMATIN BINDING PROTEIN/DNA           11-JUN-14   4QLC              
TITLE     CRYSTAL STRUCTURE OF CHROMATOSOME AT 3.5 ANGSTROM RESOLUTION          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (167-MER);                                             
COMPND   3 CHAIN: I;                                                            
COMPND   4 FRAGMENT: 167BP WIDOM 601 DNA;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (167-MER);                                             
COMPND   8 CHAIN: J;                                                            
COMPND   9 FRAGMENT: 167BP WIDOM 601 DNA;                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HISTONE H3;                                                
COMPND  13 CHAIN: A, E;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: HISTONE H4;                                                
COMPND  17 CHAIN: B, F;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: HISTONE H2A;                                               
COMPND  21 CHAIN: C, G;                                                         
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: HISTONE H2B;                                               
COMPND  25 CHAIN: D, H;                                                         
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 MOL_ID: 7;                                                           
COMPND  28 MOLECULE: H5;                                                        
COMPND  29 CHAIN: U;                                                            
COMPND  30 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: DNA;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 GENE: DNA;                                                           
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  15 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  16 ORGANISM_TAXID: 7227;                                                
SOURCE  17 STRAIN: 7227;                                                        
SOURCE  18 GENE: CG31613, CG33803, CG33806, CG33809, CG33812, CG33815, CG33818, 
SOURCE  19 CG33821, CG33824, CG33827, CG33830, CG33833, CG33836, CG33839,       
SOURCE  20 CG33842, CG33845, CG33848, CG33851, CG33854, CG33857, CG33860,       
SOURCE  21 CG33863, CG33866, H3_DROME, HIS3, HIS3:CG31613, HIS3:CG33803,        
SOURCE  22 HIS3:CG33806, HIS3:CG33809, HIS3:CG33812, HIS3:CG33815,              
SOURCE  23 HIS3:CG33818, HIS3:CG33821, HIS3:CG33824, HIS3:CG33827,              
SOURCE  24 HIS3:CG33830, HIS3:CG33833, HIS3:CG33836, HIS3:CG33839,              
SOURCE  25 HIS3:CG33842, HIS3:CG33845, HIS3:CG33848, HIS3:CG33851,              
SOURCE  26 HIS3:CG33854, HIS3:CG33857, HIS3:CG33860, HIS3:CG33863,              
SOURCE  27 HIS3:CG33866;                                                        
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  30 EXPRESSION_SYSTEM_STRAIN: 562;                                       
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  33 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  34 ORGANISM_TAXID: 7227;                                                
SOURCE  35 STRAIN: 7227;                                                        
SOURCE  36 GENE: CG31611, CG3379, CG33869, CG33871, CG33873, CG33875, CG33877,  
SOURCE  37 CG33879, CG33881, CG33883, CG33885, CG33887, CG33889, CG33891,       
SOURCE  38 CG33893, CG33895, CG33897, CG33899, CG33901, CG33903, CG33905,       
SOURCE  39 CG33907, CG33909, H4, H4R, H4_DROME, HIS4, HIS4:CG31611,             
SOURCE  40 HIS4:CG33869, HIS4:CG33871, HIS4:CG33873, HIS4:CG33875,              
SOURCE  41 HIS4:CG33877, HIS4:CG33879, HIS4:CG33881, HIS4:CG33883,              
SOURCE  42 HIS4:CG33885, HIS4:CG33887, HIS4:CG33889, HIS4:CG33891,              
SOURCE  43 HIS4:CG33893, HIS4:CG33895, HIS4:CG33897, HIS4:CG33899,              
SOURCE  44 HIS4:CG33901, HIS4:CG33903, HIS4:CG33905, HIS4:CG33907,              
SOURCE  45 HIS4:CG33909, HIS4R;                                                 
SOURCE  46 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  47 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  48 EXPRESSION_SYSTEM_STRAIN: 562;                                       
SOURCE  49 MOL_ID: 5;                                                           
SOURCE  50 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  51 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  52 ORGANISM_TAXID: 7227;                                                
SOURCE  53 STRAIN: 7227;                                                        
SOURCE  54 GENE: CG31618, CG33808, CG33814, CG33817, CG33820, CG33823, CG33826, 
SOURCE  55 CG33829, CG33832, CG33835, CG33838, CG33841, CG33844, CG33847,       
SOURCE  56 CG33850, CG33862, CG33865, H2A, H2A_DROME, HIS2A, HIS2A:CG31618,     
SOURCE  57 HIS2A:CG33808, HIS2A:CG33814, HIS2A:CG33817, HIS2A:CG33820,          
SOURCE  58 HIS2A:CG33823, HIS2A:CG33826, HIS2A:CG33829, HIS2A:CG33832,          
SOURCE  59 HIS2A:CG33835, HIS2A:CG33838, HIS2A:CG33841, HIS2A:CG33844,          
SOURCE  60 HIS2A:CG33847, HIS2A:CG33850, HIS2A:CG33862, HIS2A:CG33865;          
SOURCE  61 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  62 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  63 EXPRESSION_SYSTEM_STRAIN: 562;                                       
SOURCE  64 MOL_ID: 6;                                                           
SOURCE  65 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  66 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  67 ORGANISM_TAXID: 7227;                                                
SOURCE  68 STRAIN: 7227;                                                        
SOURCE  69 GENE: CG17949, CG33868, CG33870, CG33872, CG33874, CG33876, CG33878, 
SOURCE  70 CG33880, CG33882, CG33884, CG33886, CG33888, CG33890, CG33892,       
SOURCE  71 CG33894, CG33896, CG33898, CG33900, CG33902, CG33904, CG33906,       
SOURCE  72 CG33908, CG33910, H2B_DROME, HIS2B, HIS2B:CG17949, HIS2B:CG33868,    
SOURCE  73 HIS2B:CG33870, HIS2B:CG33872, HIS2B:CG33874, HIS2B:CG33876,          
SOURCE  74 HIS2B:CG33878, HIS2B:CG33880, HIS2B:CG33882, HIS2B:CG33884,          
SOURCE  75 HIS2B:CG33886, HIS2B:CG33888, HIS2B:CG33890, HIS2B:CG33892,          
SOURCE  76 HIS2B:CG33894, HIS2B:CG33896, HIS2B:CG33898, HIS2B:CG33900,          
SOURCE  77 HIS2B:CG33902, HIS2B:CG33904, HIS2B:CG33906, HIS2B:CG33908,          
SOURCE  78 HIS2B:CG33910;                                                       
SOURCE  79 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  80 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  81 EXPRESSION_SYSTEM_STRAIN: 562;                                       
SOURCE  82 MOL_ID: 7;                                                           
SOURCE  83 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  84 ORGANISM_TAXID: 9031;                                                
SOURCE  85 STRAIN: 9031;                                                        
SOURCE  86 GENE: H5_CHICK;                                                      
SOURCE  87 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  88 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  89 EXPRESSION_SYSTEM_STRAIN: 562                                        
KEYWDS    NUCLEOSOME CORE PARTICLE, HISTONE FOLD, CHROMOSOME, CHROMATIN, GLOBAL 
KEYWDS   2 HISTONE H5, GH5, NCP167, REGULATION, SEGREGATION, CHROMATOSOME, GH1, 
KEYWDS   3 LIKER HISTONE H5, LINKER DNA, PROTEIN-DNA COMPLEXES, DNA BINDING     
KEYWDS   4 PROTEIN-DNA COMPLEX, CHROMATIN BINDING PROTEIN-DNA COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.JIANG,B.R.ZHOU,T.S.XIAO,Y.W.BAI                                   
REVDAT   4   22-NOV-17 4QLC    1       REMARK                                   
REVDAT   3   12-AUG-15 4QLC    1       JRNL                                     
REVDAT   2   29-JUL-15 4QLC    1       JRNL   REMARK                            
REVDAT   1   22-JUL-15 4QLC    0                                                
JRNL        AUTH   B.R.ZHOU,J.JIANG,H.FENG,R.GHIRLANDO,T.S.XIAO,Y.BAI           
JRNL        TITL   STRUCTURAL MECHANISMS OF NUCLEOSOME RECOGNITION BY LINKER    
JRNL        TITL 2 HISTONES.                                                    
JRNL        REF    MOL.CELL                      V.PL 1     2 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26212454                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.06.025                                 
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 87833                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4443                            
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 43.6930 -  9.4824    0.90     3991   209  0.1486 0.1354        
REMARK   3     2  9.4824 -  7.5390    0.93     4143   221  0.1579 0.1608        
REMARK   3     3  7.5390 -  6.5897    0.93     4156   222  0.2007 0.2159        
REMARK   3     4  6.5897 -  5.9889    0.94     4178   221  0.2196 0.2543        
REMARK   3     5  5.9889 -  5.5605    0.94     4190   217  0.2283 0.2711        
REMARK   3     6  5.5605 -  5.2332    0.94     4159   218  0.2163 0.2320        
REMARK   3     7  5.2332 -  4.9715    0.94     4204   217  0.2190 0.2339        
REMARK   3     8  4.9715 -  4.7554    0.94     4154   222  0.2161 0.2531        
REMARK   3     9  4.7554 -  4.5725    0.94     4164   220  0.2219 0.2511        
REMARK   3    10  4.5725 -  4.4149    0.94     4195   217  0.2230 0.2952        
REMARK   3    11  4.4149 -  4.2770    0.94     4201   221  0.2226 0.2729        
REMARK   3    12  4.2770 -  4.1548    0.94     4171   220  0.2422 0.2715        
REMARK   3    13  4.1548 -  4.0455    0.94     4223   225  0.2421 0.2621        
REMARK   3    14  4.0455 -  3.9469    0.94     4220   225  0.2577 0.3179        
REMARK   3    15  3.9469 -  3.8572    0.94     4150   216  0.2621 0.3172        
REMARK   3    16  3.8572 -  3.7752    0.94     4218   223  0.2759 0.3239        
REMARK   3    17  3.7752 -  3.6997    0.94     4193   218  0.2825 0.3084        
REMARK   3    18  3.6997 -  3.6299    0.94     4201   216  0.2842 0.3634        
REMARK   3    19  3.6299 -  3.5651    0.94     4191   225  0.2894 0.3345        
REMARK   3    20  3.5651 -  3.5047    0.93     4128   213  0.3003 0.3074        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 91.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 137.1                          
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      :  0.004          14280                                  
REMARK   3   ANGLE     :  0.757          20705                                  
REMARK   3   CHIRALITY :  0.033           2341                                  
REMARK   3   PLANARITY :  0.004           1471                                  
REMARK   3   DIHEDRAL  : 26.823           5889                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : NULL                                        
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : NULL                                        
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : NULL                                        
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ZERO OCCUPANCY ATOMS REPRESENT ATOMS      
REMARK   3  FOR WHICH NO ELECTRON DENSITY OBSERVED                              
REMARK   4                                                                      
REMARK   4 4QLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086199.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 274                                
REMARK 200  PH                             : 3.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45664                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.393                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
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) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4INM, 1HST                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MM CITRIC ACID, 0.1MM POTASSIUM      
REMARK 280  CHLORIDE, AND 10% MPD, PH 3.75, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.19333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.59667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.89500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.29833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       76.49167            
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: UNDECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: UNDECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 61600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 82790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -380.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, C, D, E, F, G, H,         
REMARK 350                    AND CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465      DT I   167                                                      
REMARK 465      DT J   167                                                      
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     THR B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     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     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     VAL C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     LYS C    12                                                      
REMARK 465     ALA C    13                                                      
REMARK 465     LYS C   118                                                      
REMARK 465     THR C   119                                                      
REMARK 465     GLU C   120                                                      
REMARK 465     LYS C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     ALA C   123                                                      
REMARK 465     PRO D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     LYS D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     GLN D    16                                                      
REMARK 465     LYS D    17                                                      
REMARK 465     ASN D    18                                                      
REMARK 465     ILE D    19                                                      
REMARK 465     THR D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     ASP D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     LYS D    25                                                      
REMARK 465     LYS D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     ARG D    28                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     THR E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     GLY E    13                                                      
REMARK 465     LYS E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     PRO E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     LEU E    20                                                      
REMARK 465     ALA E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     LYS E    23                                                      
REMARK 465     ALA E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     ARG E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     PRO E    30                                                      
REMARK 465     ALA E    31                                                      
REMARK 465     THR E    32                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     VAL E    35                                                      
REMARK 465     LYS E    36                                                      
REMARK 465     LYS E    37                                                      
REMARK 465     THR F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     LYS F    12                                                      
REMARK 465     GLY F    13                                                      
REMARK 465     GLY F    14                                                      
REMARK 465     ALA F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     ARG F    17                                                      
REMARK 465     HIS F    18                                                      
REMARK 465     ARG F    19                                                      
REMARK 465     LYS F    20                                                      
REMARK 465     VAL F    21                                                      
REMARK 465     LEU F    22                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     LYS G     5                                                      
REMARK 465     GLY G     6                                                      
REMARK 465     GLY G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     VAL G     9                                                      
REMARK 465     LYS G    10                                                      
REMARK 465     GLY G    11                                                      
REMARK 465     LYS G    12                                                      
REMARK 465     LYS G   117                                                      
REMARK 465     LYS G   118                                                      
REMARK 465     THR G   119                                                      
REMARK 465     GLU G   120                                                      
REMARK 465     LYS G   121                                                      
REMARK 465     LYS G   122                                                      
REMARK 465     ALA G   123                                                      
REMARK 465     PRO H     1                                                      
REMARK 465     PRO H     2                                                      
REMARK 465     LYS H     3                                                      
REMARK 465     THR H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     GLY H     6                                                      
REMARK 465     LYS H     7                                                      
REMARK 465     ALA H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     LYS H    10                                                      
REMARK 465     LYS H    11                                                      
REMARK 465     ALA H    12                                                      
REMARK 465     GLY H    13                                                      
REMARK 465     LYS H    14                                                      
REMARK 465     ALA H    15                                                      
REMARK 465     GLN H    16                                                      
REMARK 465     LYS H    17                                                      
REMARK 465     ASN H    18                                                      
REMARK 465     ILE H    19                                                      
REMARK 465     THR H    20                                                      
REMARK 465     LYS H    21                                                      
REMARK 465     THR H    22                                                      
REMARK 465     ASP H    23                                                      
REMARK 465     LYS H    24                                                      
REMARK 465     LYS H    25                                                      
REMARK 465     LYS H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     LYS H   122                                                      
REMARK 465     SER U    98                                                      
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     TYR H   80   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     TYR H   80   OH                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER U    41     O    GLY U    44              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT I  48   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DA I  49   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC I  64   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA I  69   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DA I  69   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC I  72   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DA I 113   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA J   1   O4' -  C1' -  N9  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG J  78   O4' -  C4' -  C3' ANGL. DEV. =  -2.8 DEGREES          
REMARK 500     DT J  99   O4' -  C1' -  N1  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DA J 100   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DC J 108   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  41     -148.37     56.29                                   
REMARK 500    HIS D  46       84.27   -152.02                                   
REMARK 500    TYR E  41     -146.35     54.31                                   
REMARK 500    PHE F 100       -4.77   -149.12                                   
REMARK 500    ARG U  42      -79.63    -63.16                                   
REMARK 500    THR U  84      -70.41   -122.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DC I  64         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     CIT G   202                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT G 202                 
DBREF  4QLC A    1   135  UNP    P02299   H3_DROME         2    136             
DBREF  4QLC B    1   102  UNP    P84040   H4_DROME         2    103             
DBREF  4QLC C    1   123  UNP    P84051   H2A_DROME        2    124             
DBREF  4QLC D    1   122  UNP    P02283   H2B_DROME        2    123             
DBREF  4QLC E    1   135  UNP    P02299   H3_DROME         2    136             
DBREF  4QLC F    1   102  UNP    P84040   H4_DROME         2    103             
DBREF  4QLC G    1   123  UNP    P84051   H2A_DROME        2    124             
DBREF  4QLC H    1   122  UNP    P02283   H2B_DROME        2    123             
DBREF  4QLC U   22    98  UNP    P02259   H5_CHICK        23     99             
DBREF  4QLC I    1   167  PDB    4QLC     4QLC             1    167             
DBREF  4QLC J    1   167  PDB    4QLC     4QLC             1    167             
SEQRES   1 I  167   DA  DC  DT  DG  DG  DC  DC  DG  DC  DC  DC  DT  DG          
SEQRES   2 I  167   DG  DA  DG  DA  DA  DT  DC  DC  DC  DG  DG  DT  DG          
SEQRES   3 I  167   DC  DC  DG  DA  DG  DG  DC  DC  DG  DC  DT  DC  DA          
SEQRES   4 I  167   DA  DT  DT  DG  DG  DT  DC  DG  DT  DA  DG  DA  DC          
SEQRES   5 I  167   DA  DG  DC  DT  DC  DT  DA  DG  DC  DA  DC  DC  DG          
SEQRES   6 I  167   DC  DT  DT  DA  DA  DA  DC  DG  DC  DA  DC  DG  DT          
SEQRES   7 I  167   DA  DC  DG  DC  DG  DC  DT  DG  DT  DC  DC  DC  DC          
SEQRES   8 I  167   DC  DG  DC  DG  DT  DT  DT  DT  DA  DA  DC  DC  DG          
SEQRES   9 I  167   DC  DC  DA  DA  DG  DG  DG  DG  DA  DT  DT  DA  DC          
SEQRES  10 I  167   DT  DC  DC  DC  DT  DA  DG  DT  DC  DT  DC  DC  DA          
SEQRES  11 I  167   DG  DG  DC  DA  DC  DG  DT  DG  DT  DC  DA  DG  DA          
SEQRES  12 I  167   DT  DA  DT  DA  DT  DA  DC  DA  DT  DC  DC  DT  DG          
SEQRES  13 I  167   DT  DG  DC  DA  DT  DG  DT  DA  DA  DG  DT                  
SEQRES   1 J  167   DA  DC  DT  DT  DA  DC  DA  DT  DG  DC  DA  DC  DA          
SEQRES   2 J  167   DG  DG  DA  DT  DG  DT  DA  DT  DA  DT  DA  DT  DC          
SEQRES   3 J  167   DT  DG  DA  DC  DA  DC  DG  DT  DG  DC  DC  DT  DG          
SEQRES   4 J  167   DG  DA  DG  DA  DC  DT  DA  DG  DG  DG  DA  DG  DT          
SEQRES   5 J  167   DA  DA  DT  DC  DC  DC  DC  DT  DT  DG  DG  DC  DG          
SEQRES   6 J  167   DG  DT  DT  DA  DA  DA  DA  DC  DG  DC  DG  DG  DG          
SEQRES   7 J  167   DG  DG  DA  DC  DA  DG  DC  DG  DC  DG  DT  DA  DC          
SEQRES   8 J  167   DG  DT  DG  DC  DG  DT  DT  DT  DA  DA  DG  DC  DG          
SEQRES   9 J  167   DG  DT  DG  DC  DT  DA  DG  DA  DG  DC  DT  DG  DT          
SEQRES  10 J  167   DC  DT  DA  DC  DG  DA  DC  DC  DA  DA  DT  DT  DG          
SEQRES  11 J  167   DA  DG  DC  DG  DG  DC  DC  DT  DC  DG  DG  DC  DA          
SEQRES  12 J  167   DC  DC  DG  DG  DG  DA  DT  DT  DC  DT  DC  DC  DA          
SEQRES  13 J  167   DG  DG  DG  DC  DG  DG  DC  DC  DA  DG  DT                  
SEQRES   1 A  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 A  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 A  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 A  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 A  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 A  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 A  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 A  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   9 A  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 A  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 A  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 B  102  THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 B  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 B  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 B  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 B  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 B  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 B  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 B  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 C  123  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 C  123  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 C  123  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 C  123  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 C  123  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 C  123  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 C  123  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 C  123  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 C  123  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 C  123  LYS THR GLU LYS LYS ALA                                      
SEQRES   1 D  122  PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY          
SEQRES   2 D  122  LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS          
SEQRES   3 D  122  LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR          
SEQRES   4 D  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 D  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 D  122  ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA          
SEQRES   7 D  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 D  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 D  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 D  122  TYR THR SER SER LYS                                          
SEQRES   1 E  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 E  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 E  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 E  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 E  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 E  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 E  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 E  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE          
SEQRES   9 E  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 E  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 E  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 F  102  THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 F  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 F  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 F  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 F  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 F  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 F  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 F  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 G  123  SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA          
SEQRES   2 G  123  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   3 G  123  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   4 G  123  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   5 G  123  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   6 G  123  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   7 G  123  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   8 G  123  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   9 G  123  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES  10 G  123  LYS THR GLU LYS LYS ALA                                      
SEQRES   1 H  122  PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY          
SEQRES   2 H  122  LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS          
SEQRES   3 H  122  LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR          
SEQRES   4 H  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 H  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 H  122  ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA          
SEQRES   7 H  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 H  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 H  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 H  122  TYR THR SER SER LYS                                          
SEQRES   1 U   77  SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA          
SEQRES   2 U   77  ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG          
SEQRES   3 U   77  GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL          
SEQRES   4 U   77  GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG          
SEQRES   5 U   77  ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY          
SEQRES   6 U   77  VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS SER              
HET    CIT  A 201      13                                                       
HET    CIT  G 201      13                                                       
HET    CIT  G 202      13                                                       
HETNAM     CIT CITRIC ACID                                                      
FORMUL  12  CIT    3(C6 H8 O7)                                                  
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  GLY A  132  1                                  13    
HELIX    5   5 ASN B   25  ILE B   29  5                                   5    
HELIX    6   6 THR B   30  GLY B   42  1                                  13    
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 SER C   15  ALA C   20  1                                   6    
HELIX   10  10 PRO C   25  LYS C   35  1                                  11    
HELIX   11  11 ALA C   44  ASN C   72  1                                  29    
HELIX   12  12 ILE C   78  ASP C   89  1                                  12    
HELIX   13  13 ASP C   89  LEU C   96  1                                   8    
HELIX   14  14 GLN C  111  LEU C  115  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  SER E   57  1                                  14    
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  GLY E  132  1                                  13    
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 SER G   15  ALA G   20  1                                   6    
HELIX   28  28 PRO G   25  LYS G   35  1                                  11    
HELIX   29  29 ALA G   44  ASP G   71  1                                  28    
HELIX   30  30 ILE G   78  ASN G   88  1                                  11    
HELIX   31  31 ASP G   89  LEU G   96  1                                   8    
HELIX   32  32 GLN G  111  LEU G  115  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  SER H  120  1                                  21    
HELIX   37  37 THR U   27  ALA U   38  1                                  12    
HELIX   38  38 ARG U   47  TYR U   58  1                                  12    
HELIX   39  39 ASN U   63  ALA U   78  1                                  16    
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  99  ILE G 101  1  O  THR G 100   N  THR B  96           
SHEET    1   D 2 ARG C  41  VAL C  42  0                                        
SHEET    2   D 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  41           
SHEET    1   E 2 ARG C  76  ILE C  77  0                                        
SHEET    2   E 2 GLY D  50  ILE D  51  1  O  GLY D  50   N  ILE C  77           
SHEET    1   F 2 VAL C  99  ILE C 101  0                                        
SHEET    2   F 2 THR F  96  TYR F  98  1  O  THR F  96   N  THR C 100           
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  41  VAL G  42  0                                        
SHEET    2   I 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  41           
SHEET    1   J 2 ARG G  76  ILE G  77  0                                        
SHEET    2   J 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  77           
SHEET    1   K 3 SER U  45  SER U  46  0                                        
SHEET    2   K 3 GLY U  91  LEU U  95 -1  O  PHE U  93   N  SER U  45           
SHEET    3   K 3 LEU U  81  GLY U  86 -1  N  LYS U  82   O  ARG U  94           
SITE     1 AC1  2 ARG A 129  ARG A 134                                          
SITE     1 AC2  2 GLU G  60  GLU G  63                                          
SITE     1 AC3  2 LYS A  64  GLN G 103                                          
CRYST1  262.870  262.870   91.790  90.00  90.00 120.00 P 65         12          
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      0.003804  0.002196  0.000000        0.00000                         
SCALE2      0.000000  0.004393  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010894        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system