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Database: PDB
Entry: 5WCU
LinkDB: 5WCU
Original site: 5WCU 
HEADER    CHROMATIN BINDING PROTEIN/DNA           02-JUL-17   5WCU              
TITLE     CRYSTAL STRUCTURE OF 167 BP NUCLEOSOME BOUND TO THE GLOBULAR DOMAIN OF
TITLE    2 LINKER HISTONE H5                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3;                                                
COMPND   3 CHAIN: A, E, K, O;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 39-136;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HISTONE H4;                                                
COMPND   8 CHAIN: B, F, L, P;                                                   
COMPND   9 FRAGMENT: UNP RESIDUES 22-103;                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: HISTONE H2A;                                               
COMPND  13 CHAIN: C, G, M, Q;                                                   
COMPND  14 FRAGMENT: UNP RESIDUES 15-118;                                       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: HISTONE H2B;                                               
COMPND  18 CHAIN: D, H, N, R;                                                   
COMPND  19 FRAGMENT: UNP RESIDUES 29-122;                                       
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: DNA (167-MER);                                             
COMPND  23 CHAIN: I, S;                                                         
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 6;                                                           
COMPND  26 MOLECULE: DNA (167-MER);                                             
COMPND  27 CHAIN: J, T;                                                         
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MOL_ID: 7;                                                           
COMPND  30 MOLECULE: HISTONE H5;                                                
COMPND  31 CHAIN: U, V;                                                         
COMPND  32 FRAGMENT: UNP RESIDUES 23-98;                                        
COMPND  33 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: HIS3, HIS3:CG31613, CG31613, HIS3:CG33803, CG33803,            
SOURCE   6 HIS3:CG33806, CG33806, HIS3:CG33809, CG33809, HIS3:CG33812, CG33812, 
SOURCE   7 HIS3:CG33815, CG33815, HIS3:CG33818, CG33818, HIS3:CG33821, CG33821, 
SOURCE   8 HIS3:CG33824, CG33824, HIS3:CG33827, CG33827, HIS3:CG33830, CG33830, 
SOURCE   9 HIS3:CG33833, CG33833, HIS3:CG33836, CG33836, HIS3:CG33839, CG33839, 
SOURCE  10 HIS3:CG33842, CG33842, HIS3:CG33845, CG33845, HIS3:CG33848, CG33848, 
SOURCE  11 HIS3:CG33851, CG33851, HIS3:CG33854, CG33854, HIS3:CG33857, CG33857, 
SOURCE  12 HIS3:CG33860, CG33860, HIS3:CG33863, CG33863, HIS3:CG33866, CG33866; 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 2;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  17 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  18 ORGANISM_TAXID: 7227;                                                
SOURCE  19 GENE: HIS4, H4, HIS4R, H4R, CG3379, HIS4:CG31611, CG31611,           
SOURCE  20 HIS4:CG33869, CG33869, HIS4:CG33871, CG33871, HIS4:CG33873, CG33873, 
SOURCE  21 HIS4:CG33875, CG33875, HIS4:CG33877, CG33877, HIS4:CG33879, CG33879, 
SOURCE  22 HIS4:CG33881, CG33881, HIS4:CG33883, CG33883, HIS4:CG33885, CG33885, 
SOURCE  23 HIS4:CG33887, CG33887, HIS4:CG33889, CG33889, HIS4:CG33891, CG33891, 
SOURCE  24 HIS4:CG33893, CG33893, HIS4:CG33895, CG33895, HIS4:CG33897, CG33897, 
SOURCE  25 HIS4:CG33899, CG33899, HIS4:CG33901, CG33901, HIS4:CG33903, CG33903, 
SOURCE  26 HIS4:CG33905, CG33905, HIS4:CG33907, CG33907, HIS4:CG33909, CG33909; 
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 MOL_ID: 3;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  31 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  32 ORGANISM_TAXID: 7227;                                                
SOURCE  33 GENE: HIS2A, H2A, HIS2A:CG31618, CG31618, HIS2A:CG33808, CG33808,    
SOURCE  34 HIS2A:CG33814, CG33814, HIS2A:CG33817, CG33817, HIS2A:CG33820,       
SOURCE  35 CG33820, HIS2A:CG33823, CG33823, HIS2A:CG33826, CG33826,             
SOURCE  36 HIS2A:CG33829, CG33829, HIS2A:CG33832, CG33832, HIS2A:CG33835,       
SOURCE  37 CG33835, HIS2A:CG33838, CG33838, HIS2A:CG33841, CG33841,             
SOURCE  38 HIS2A:CG33844, CG33844, HIS2A:CG33847, CG33847, HIS2A:CG33850,       
SOURCE  39 CG33850, HIS2A:CG33862, CG33862, HIS2A:CG33865, CG33865;             
SOURCE  40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  41 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  42 MOL_ID: 4;                                                           
SOURCE  43 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  44 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  45 ORGANISM_TAXID: 7227;                                                
SOURCE  46 GENE: HIS2B, HIS2B:CG17949, CG17949, HIS2B:CG33868, CG33868,         
SOURCE  47 HIS2B:CG33870, CG33870, HIS2B:CG33872, CG33872, HIS2B:CG33874,       
SOURCE  48 CG33874, HIS2B:CG33876, CG33876, HIS2B:CG33878, CG33878,             
SOURCE  49 HIS2B:CG33880, CG33880, HIS2B:CG33882, CG33882, HIS2B:CG33884,       
SOURCE  50 CG33884, HIS2B:CG33886, CG33886, HIS2B:CG33888, CG33888,             
SOURCE  51 HIS2B:CG33890, CG33890, HIS2B:CG33892, CG33892, HIS2B:CG33894,       
SOURCE  52 CG33894, HIS2B:CG33896, CG33896, HIS2B:CG33898, CG33898,             
SOURCE  53 HIS2B:CG33900, CG33900, HIS2B:CG33902, CG33902, HIS2B:CG33904,       
SOURCE  54 CG33904, HIS2B:CG33906, CG33906, HIS2B:CG33908, CG33908,             
SOURCE  55 HIS2B:CG33910, CG33910;                                              
SOURCE  56 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  57 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  58 MOL_ID: 5;                                                           
SOURCE  59 SYNTHETIC: YES;                                                      
SOURCE  60 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  61 ORGANISM_TAXID: 32630;                                               
SOURCE  62 OTHER_DETAILS: 167 BP WIDOM 601 DNA;                                 
SOURCE  63 MOL_ID: 6;                                                           
SOURCE  64 SYNTHETIC: YES;                                                      
SOURCE  65 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  66 ORGANISM_TAXID: 32630;                                               
SOURCE  67 OTHER_DETAILS: 167 BP WIDOM 601 DNA;                                 
SOURCE  68 MOL_ID: 7;                                                           
SOURCE  69 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  70 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  71 ORGANISM_TAXID: 9031;                                                
SOURCE  72 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  73 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOSOME CORE PARTICLE, HISTONE FOLD, CHROMOSOME, CHROMATIN,        
KEYWDS   2 GLOBULAR DOMAIN, HISTONE H5, GH5, 167 BP NUCLEOSOME, CHROMATOSOME,   
KEYWDS   3 NUCLEOSOME PACKING, 30 NM CHROMATIN FIBER, LINKER HISTONE H5, LINKER 
KEYWDS   4 DNA, NUCLEOSOME BINDING PROTEIN, PROTEIN DNA COMPLEXES, DNA BINDING, 
KEYWDS   5 CHROMATIN HIGHER ORDER STRUCTURE, CHROMATIN FOLDING, CHROMATIN       
KEYWDS   6 BINDING PROTEIN-DNA COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.JIANG,B.R.ZHOU                                                    
REVDAT   1   31-OCT-18 5WCU    0                                                
JRNL        AUTH   B.R.ZHOU,J.JIANG,R.GHIRLANDO,D.NOROUZI,K.N.SATHISH YADAV,    
JRNL        AUTH 2 H.FENG,R.WANG,P.ZHANG,V.ZHURKIN,Y.BAI                        
JRNL        TITL   REVISIT OF RECONSTITUTED 30-NM NUCLEOSOME ARRAYS REVEALS AN  
JRNL        TITL 2 ENSEMBLE OF DYNAMIC STRUCTURES.                              
JRNL        REF    J. MOL. BIOL.                 V. 430  3093 2018              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   29959925                                                     
JRNL        DOI    10.1016/J.JMB.2018.06.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.62                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.930                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15266                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.140                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1548                            
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 45.4439 - 12.2422    0.87     1238   140  0.1363 0.1725        
REMARK   3     2 12.2422 -  9.7485    0.88     1241   136  0.1373 0.1392        
REMARK   3     3  9.7485 -  8.5255    0.88     1268   141  0.1596 0.2009        
REMARK   3     4  8.5255 -  7.7502    0.88     1247   138  0.1722 0.2220        
REMARK   3     5  7.7502 -  7.1970    0.88     1252   137  0.2024 0.2800        
REMARK   3     6  7.1970 -  6.7741    0.88     1263   143  0.2240 0.2862        
REMARK   3     7  6.7741 -  6.4359    0.88     1237   135  0.2239 0.3535        
REMARK   3     8  6.4359 -  6.1564    0.89     1278   142  0.2683 0.3730        
REMARK   3     9  6.1564 -  5.9199    0.89     1260   136  0.2854 0.4027        
REMARK   3    10  5.9199 -  5.7161    0.87     1229   137  0.3003 0.3789        
REMARK   3    11  5.7161 -  5.5376    0.87     1220   136  0.3327 0.3545        
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) : 29.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 176.6                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.005          28441                                  
REMARK   3   ANGLE     :  0.751          41235                                  
REMARK   3   CHIRALITY :  0.041           4678                                  
REMARK   3   PLANARITY :  0.004           2928                                  
REMARK   3   DIHEDRAL  : 24.504          14822                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5WCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228670.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 4.0                                
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                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15268                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.70600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.700                              
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: 4QLC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NH4NO3, 10% MPD (V/V), PH 4.0,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: UNDECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: UNDECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 62380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 82510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -404.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 61970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 83250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -384.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O, P, Q, R, S, T,         
REMARK 350                    AND CHAINS: V                                     
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     VAL B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     ALA E   135                                                      
REMARK 465     LYS G    15                                                      
REMARK 465     ARG H    28                                                      
REMARK 465      DG I   165                                                      
REMARK 465      DA I   166                                                      
REMARK 465      DT I   167                                                      
REMARK 465     VAL L    21                                                      
REMARK 465     LEU L    22                                                      
REMARK 465     ALA O   135                                                      
REMARK 465     LYS Q    15                                                      
REMARK 465     ARG R    28                                                      
REMARK 465      DG S   165                                                      
REMARK 465      DA S   166                                                      
REMARK 465      DT S   167                                                      
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     PRO A  38    CG   CD                                             
REMARK 470     HIS A  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A  61    CG   CD1  CD2                                       
REMARK 470     THR C  76    OG1  CG2                                            
REMARK 470     LEU G  63    CG   CD1  CD2                                       
REMARK 470     GLU H  73    CG   CD   OE1  OE2                                  
REMARK 470     THR P  80    OG1  CG2                                            
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   OH   TYR N    37     OP1   DG T   132              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC I 150   O3'    DC I 150   C3'    -0.041                       
REMARK 500     DC I 153   O3'    DC I 153   C3'    -0.047                       
REMARK 500     DA J  22   O3'    DA J  22   C3'    -0.040                       
REMARK 500     DA J  24   O3'    DA J  24   C3'    -0.041                       
REMARK 500     DC J  75   O3'    DC J  75   C3'    -0.039                       
REMARK 500     DG J  86   O3'    DG J  86   C3'    -0.042                       
REMARK 500     DG J  88   O3'    DG J  88   C3'    -0.037                       
REMARK 500     DA J 131   O3'    DA J 131   C3'    -0.042                       
REMARK 500     DC J 152   O3'    DC J 152   C3'    -0.038                       
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     DC I   3   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DC I   9   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC I  34   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DC I  63   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC I  64   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DC I  89   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DT I 122   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT I 127   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DG I 136   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG I 155   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT I 163   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC J   3   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC J  10   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG J  15   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DT J  27   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DA J  71   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG J 122   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA J 127   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC J 136   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG J 141   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC J 144   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DT J 150   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC J 163   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DC J 164   O4' -  C1' -  N1  ANGL. DEV. =   2.1 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    PRO C 109       99.32    -68.86                                   
REMARK 500    THR E  45      -51.02   -126.74                                   
REMARK 500    PRO G 109       99.61    -68.87                                   
REMARK 500    ASP H  48       51.23    -95.61                                   
REMARK 500    ILE H  51      119.46   -170.97                                   
REMARK 500    SER H 120      -90.17    -62.33                                   
REMARK 500    PRO M 109       99.50    -68.75                                   
REMARK 500    TYR N  34       68.85   -117.67                                   
REMARK 500    PRO Q 109       99.43    -68.79                                   
REMARK 500    PRO U  26     -163.17    -69.17                                   
REMARK 500    ARG U  74      -72.74    -80.81                                   
REMARK 500    LEU U  75        7.56    -65.17                                   
REMARK 500    LYS U  85       88.12     63.34                                   
REMARK 500    HIS V  25      154.58    178.70                                   
REMARK 500    PRO V  26     -169.97    -70.17                                   
REMARK 500    ASN V  63        2.93    -68.06                                   
REMARK 500    ARG V  74      -60.12    -99.73                                   
REMARK 500    LYS V  85      113.41     77.43                                   
REMARK 500    ALA V  89       41.71    -91.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5WCU A   38   135  UNP    P02299   H3_DROME        39    136             
DBREF  5WCU B   21   102  UNP    P84040   H4_DROME        22    103             
DBREF  5WCU C   15   118  UNP    P84051   H2A_DROME       15    118             
DBREF  5WCU D   28   121  UNP    P02283   H2B_DROME       29    122             
DBREF  5WCU E   38   135  UNP    P02299   H3_DROME        39    136             
DBREF  5WCU F   21   102  UNP    P84040   H4_DROME        22    103             
DBREF  5WCU G   15   118  UNP    P84051   H2A_DROME       15    118             
DBREF  5WCU H   28   121  UNP    P02283   H2B_DROME       29    122             
DBREF  5WCU I    1   167  PDB    5WCU     5WCU             1    167             
DBREF  5WCU J    1   167  PDB    5WCU     5WCU             1    167             
DBREF  5WCU K   38   135  UNP    P02299   H3_DROME        39    136             
DBREF  5WCU L   21   102  UNP    P84040   H4_DROME        22    103             
DBREF  5WCU M   15   118  UNP    P84051   H2A_DROME       15    118             
DBREF  5WCU N   28   121  UNP    P02283   H2B_DROME       29    122             
DBREF  5WCU O   38   135  UNP    P02299   H3_DROME        39    136             
DBREF  5WCU P   21   102  UNP    P84040   H4_DROME        22    103             
DBREF  5WCU Q   15   118  UNP    P84051   H2A_DROME       15    118             
DBREF  5WCU R   28   121  UNP    P02283   H2B_DROME       29    122             
DBREF  5WCU S    1   167  PDB    5WCU     5WCU             1    167             
DBREF  5WCU T    1   167  PDB    5WCU     5WCU             1    167             
DBREF  5WCU U   22    97  UNP    P02259   H5_CHICK        23     98             
DBREF  5WCU V   22    97  UNP    P02259   H5_CHICK        23     98             
SEQRES   1 A   98  PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU          
SEQRES   2 A   98  ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG          
SEQRES   3 A   98  LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN          
SEQRES   4 A   98  ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL          
SEQRES   5 A   98  MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY          
SEQRES   6 A   98  LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS          
SEQRES   7 A   98  ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG          
SEQRES   8 A   98  ARG ILE ARG GLY GLU ARG ALA                                  
SEQRES   1 B   82  VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA          
SEQRES   2 B   82  ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE          
SEQRES   3 B   82  SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS          
SEQRES   4 B   82  VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR          
SEQRES   5 B   82  THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP          
SEQRES   6 B   82  VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR          
SEQRES   7 B   82  GLY PHE GLY GLY                                              
SEQRES   1 C  104  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   2 C  104  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   3 C  104  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   4 C  104  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   5 C  104  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   6 C  104  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   7 C  104  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   8 C  104  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES   1 D   94  ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS          
SEQRES   2 D   94  VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER          
SEQRES   3 D   94  LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE          
SEQRES   4 D   94  PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS          
SEQRES   5 D   94  TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN          
SEQRES   6 D   94  THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS          
SEQRES   7 D   94  HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR          
SEQRES   8 D   94  THR SER SER                                                  
SEQRES   1 E   98  PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU          
SEQRES   2 E   98  ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG          
SEQRES   3 E   98  LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN          
SEQRES   4 E   98  ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL          
SEQRES   5 E   98  MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY          
SEQRES   6 E   98  LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS          
SEQRES   7 E   98  ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG          
SEQRES   8 E   98  ARG ILE ARG GLY GLU ARG ALA                                  
SEQRES   1 F   82  VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA          
SEQRES   2 F   82  ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE          
SEQRES   3 F   82  SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS          
SEQRES   4 F   82  VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR          
SEQRES   5 F   82  THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP          
SEQRES   6 F   82  VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR          
SEQRES   7 F   82  GLY PHE GLY GLY                                              
SEQRES   1 G  104  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   2 G  104  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   3 G  104  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   4 G  104  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   5 G  104  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   6 G  104  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   7 G  104  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   8 G  104  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES   1 H   94  ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS          
SEQRES   2 H   94  VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER          
SEQRES   3 H   94  LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE          
SEQRES   4 H   94  PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS          
SEQRES   5 H   94  TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN          
SEQRES   6 H   94  THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS          
SEQRES   7 H   94  HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR          
SEQRES   8 H   94  THR SER SER                                                  
SEQRES   1 I  167   DA  DT  DC  DG  DG  DC  DC  DG  DC  DC  DA  DT  DC          
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  DG  DA          
SEQRES  13 I  167   DT  DG  DC  DA  DT  DG  DT  DA  DG  DA  DT                  
SEQRES   1 J  167   DA  DT  DC  DT  DA  DC  DA  DT  DG  DC  DA  DT  DC          
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  DG  DA          
SEQRES  13 J  167   DT  DG  DG  DC  DG  DG  DC  DC  DG  DA  DT                  
SEQRES   1 K   98  PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU          
SEQRES   2 K   98  ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG          
SEQRES   3 K   98  LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN          
SEQRES   4 K   98  ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL          
SEQRES   5 K   98  MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY          
SEQRES   6 K   98  LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS          
SEQRES   7 K   98  ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG          
SEQRES   8 K   98  ARG ILE ARG GLY GLU ARG ALA                                  
SEQRES   1 L   82  VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA          
SEQRES   2 L   82  ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE          
SEQRES   3 L   82  SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS          
SEQRES   4 L   82  VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR          
SEQRES   5 L   82  THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP          
SEQRES   6 L   82  VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR          
SEQRES   7 L   82  GLY PHE GLY GLY                                              
SEQRES   1 M  104  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   2 M  104  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   3 M  104  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   4 M  104  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   5 M  104  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   6 M  104  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   7 M  104  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   8 M  104  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES   1 N   94  ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS          
SEQRES   2 N   94  VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER          
SEQRES   3 N   94  LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE          
SEQRES   4 N   94  PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS          
SEQRES   5 N   94  TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN          
SEQRES   6 N   94  THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS          
SEQRES   7 N   94  HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR          
SEQRES   8 N   94  THR SER SER                                                  
SEQRES   1 O   98  PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU          
SEQRES   2 O   98  ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG          
SEQRES   3 O   98  LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN          
SEQRES   4 O   98  ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL          
SEQRES   5 O   98  MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY          
SEQRES   6 O   98  LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS          
SEQRES   7 O   98  ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG          
SEQRES   8 O   98  ARG ILE ARG GLY GLU ARG ALA                                  
SEQRES   1 P   82  VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA          
SEQRES   2 P   82  ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE          
SEQRES   3 P   82  SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS          
SEQRES   4 P   82  VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR          
SEQRES   5 P   82  THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP          
SEQRES   6 P   82  VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR          
SEQRES   7 P   82  GLY PHE GLY GLY                                              
SEQRES   1 Q  104  LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL          
SEQRES   2 Q  104  GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA          
SEQRES   3 Q  104  GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA          
SEQRES   4 Q  104  VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA          
SEQRES   5 Q  104  GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE          
SEQRES   6 Q  104  PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU          
SEQRES   7 Q  104  LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY          
SEQRES   8 Q  104  GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS          
SEQRES   1 R   94  ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS          
SEQRES   2 R   94  VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER          
SEQRES   3 R   94  LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE          
SEQRES   4 R   94  PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS          
SEQRES   5 R   94  TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN          
SEQRES   6 R   94  THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS          
SEQRES   7 R   94  HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR          
SEQRES   8 R   94  THR SER SER                                                  
SEQRES   1 S  167   DA  DT  DC  DG  DG  DC  DC  DG  DC  DC  DA  DT  DC          
SEQRES   2 S  167   DG  DA  DG  DA  DA  DT  DC  DC  DC  DG  DG  DT  DG          
SEQRES   3 S  167   DC  DC  DG  DA  DG  DG  DC  DC  DG  DC  DT  DC  DA          
SEQRES   4 S  167   DA  DT  DT  DG  DG  DT  DC  DG  DT  DA  DG  DA  DC          
SEQRES   5 S  167   DA  DG  DC  DT  DC  DT  DA  DG  DC  DA  DC  DC  DG          
SEQRES   6 S  167   DC  DT  DT  DA  DA  DA  DC  DG  DC  DA  DC  DG  DT          
SEQRES   7 S  167   DA  DC  DG  DC  DG  DC  DT  DG  DT  DC  DC  DC  DC          
SEQRES   8 S  167   DC  DG  DC  DG  DT  DT  DT  DT  DA  DA  DC  DC  DG          
SEQRES   9 S  167   DC  DC  DA  DA  DG  DG  DG  DG  DA  DT  DT  DA  DC          
SEQRES  10 S  167   DT  DC  DC  DC  DT  DA  DG  DT  DC  DT  DC  DC  DA          
SEQRES  11 S  167   DG  DG  DC  DA  DC  DG  DT  DG  DT  DC  DA  DG  DA          
SEQRES  12 S  167   DT  DA  DT  DA  DT  DA  DC  DA  DT  DC  DC  DG  DA          
SEQRES  13 S  167   DT  DG  DC  DA  DT  DG  DT  DA  DG  DA  DT                  
SEQRES   1 T  167   DA  DT  DC  DT  DA  DC  DA  DT  DG  DC  DA  DT  DC          
SEQRES   2 T  167   DG  DG  DA  DT  DG  DT  DA  DT  DA  DT  DA  DT  DC          
SEQRES   3 T  167   DT  DG  DA  DC  DA  DC  DG  DT  DG  DC  DC  DT  DG          
SEQRES   4 T  167   DG  DA  DG  DA  DC  DT  DA  DG  DG  DG  DA  DG  DT          
SEQRES   5 T  167   DA  DA  DT  DC  DC  DC  DC  DT  DT  DG  DG  DC  DG          
SEQRES   6 T  167   DG  DT  DT  DA  DA  DA  DA  DC  DG  DC  DG  DG  DG          
SEQRES   7 T  167   DG  DG  DA  DC  DA  DG  DC  DG  DC  DG  DT  DA  DC          
SEQRES   8 T  167   DG  DT  DG  DC  DG  DT  DT  DT  DA  DA  DG  DC  DG          
SEQRES   9 T  167   DG  DT  DG  DC  DT  DA  DG  DA  DG  DC  DT  DG  DT          
SEQRES  10 T  167   DC  DT  DA  DC  DG  DA  DC  DC  DA  DA  DT  DT  DG          
SEQRES  11 T  167   DA  DG  DC  DG  DG  DC  DC  DT  DC  DG  DG  DC  DA          
SEQRES  12 T  167   DC  DC  DG  DG  DG  DA  DT  DT  DC  DT  DC  DG  DA          
SEQRES  13 T  167   DT  DG  DG  DC  DG  DG  DC  DC  DG  DA  DT                  
SEQRES   1 U   76  SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA          
SEQRES   2 U   76  ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG          
SEQRES   3 U   76  GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL          
SEQRES   4 U   76  GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG          
SEQRES   5 U   76  ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY          
SEQRES   6 U   76  VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS                  
SEQRES   1 V   76  SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA          
SEQRES   2 V   76  ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG          
SEQRES   3 V   76  GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL          
SEQRES   4 V   76  GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG          
SEQRES   5 V   76  ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY          
SEQRES   6 V   76  VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS                  
HELIX    1 AA1 GLY A   44  SER A   57  1                                  14    
HELIX    2 AA2 ARG A   63  LYS A   79  1                                  17    
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   42  1                                  13    
HELIX    7 AA7 LEU B   49  ALA B   76  1                                  28    
HELIX    8 AA8 THR B   82  GLY B   94  1                                  13    
HELIX    9 AA9 SER C   16  GLY C   22  1                                   7    
HELIX   10 AB1 PRO C   26  GLY C   37  1                                  12    
HELIX   11 AB2 GLY C   46  ASN C   73  1                                  28    
HELIX   12 AB3 ILE C   79  ASP C   90  1                                  12    
HELIX   13 AB4 ASP C   90  LEU C   97  1                                   8    
HELIX   14 AB5 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 PRO D  100  SER D  121  1                                  22    
HELIX   18 AB9 THR E   45  SER E   57  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   42  1                                  13    
HELIX   24 AC6 LEU F   49  ALA F   76  1                                  28    
HELIX   25 AC7 THR F   82  GLY F   94  1                                  13    
HELIX   26 AC8 ARG G   17  GLY G   22  1                                   6    
HELIX   27 AC9 PRO G   26  GLY G   37  1                                  12    
HELIX   28 AD1 GLY G   46  ASN G   73  1                                  28    
HELIX   29 AD2 ILE G   79  ASP G   90  1                                  12    
HELIX   30 AD3 ASP G   90  LEU G   97  1                                   8    
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 PRO H  100  SER H  121  1                                  22    
HELIX   35 AD8 GLY K   44  SER K   57  1                                  14    
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   42  1                                  13    
HELIX   41 AE5 LEU L   49  ALA L   76  1                                  28    
HELIX   42 AE6 THR L   82  GLY L   94  1                                  13    
HELIX   43 AE7 SER M   16  GLY M   22  1                                   7    
HELIX   44 AE8 PRO M   26  GLY M   37  1                                  12    
HELIX   45 AE9 GLY M   46  ASN M   73  1                                  28    
HELIX   46 AF1 ILE M   79  ASP M   90  1                                  12    
HELIX   47 AF2 ASP M   90  LEU M   97  1                                   8    
HELIX   48 AF3 GLN M  112  LEU M  116  5                                   5    
HELIX   49 AF4 ALA N   35  HIS N   46  1                                  12    
HELIX   50 AF5 SER N   52  ASN N   81  1                                  30    
HELIX   51 AF6 THR N   87  LEU N   99  1                                  13    
HELIX   52 AF7 PRO N  100  SER N  121  1                                  22    
HELIX   53 AF8 GLY O   44  SER O   57  1                                  14    
HELIX   54 AF9 ARG O   63  LYS O   79  1                                  17    
HELIX   55 AG1 GLN O   85  ALA O  114  1                                  30    
HELIX   56 AG2 MET O  120  GLY O  132  1                                  13    
HELIX   57 AG3 ASN P   25  ILE P   29  5                                   5    
HELIX   58 AG4 THR P   30  GLY P   42  1                                  13    
HELIX   59 AG5 LEU P   49  ALA P   76  1                                  28    
HELIX   60 AG6 THR P   82  GLY P   94  1                                  13    
HELIX   61 AG7 ARG Q   17  GLY Q   22  1                                   6    
HELIX   62 AG8 PRO Q   26  GLY Q   37  1                                  12    
HELIX   63 AG9 GLY Q   46  ASN Q   73  1                                  28    
HELIX   64 AH1 ILE Q   79  ASP Q   90  1                                  12    
HELIX   65 AH2 ASP Q   90  LEU Q   97  1                                   8    
HELIX   66 AH3 TYR R   34  HIS R   46  1                                  13    
HELIX   67 AH4 SER R   52  ASN R   81  1                                  30    
HELIX   68 AH5 THR R   87  LEU R   99  1                                  13    
HELIX   69 AH6 PRO R  100  SER R  121  1                                  22    
HELIX   70 AH7 THR U   27  GLU U   39  1                                  13    
HELIX   71 AH8 SER U   46  TYR U   58  1                                  13    
HELIX   72 AH9 ASN U   63  ALA U   78  1                                  16    
HELIX   73 AI1 THR V   27  GLU V   39  1                                  13    
HELIX   74 AI2 ARG V   47  TYR V   58  1                                  12    
HELIX   75 AI3 ASN V   63  LEU V   75  1                                  13    
HELIX   76 AI4 VAL V   87  SER V   90  5                                   4    
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 100  ILE G 102  1  O  THR G 101   N  THR B  96           
SHEET    1 AA4 2 ARG C  42  VAL C  43  0                                        
SHEET    2 AA4 2 THR D  85  ILE D  86  1  O  ILE D  86   N  ARG C  42           
SHEET    1 AA5 2 VAL C 100  ILE C 102  0                                        
SHEET    2 AA5 2 THR F  96  TYR F  98  1  O  THR F  96   N  THR C 101           
SHEET    1 AA6 2 ARG E  83  PHE E  84  0                                        
SHEET    2 AA6 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1 AA7 2 THR E 118  ILE E 119  0                                        
SHEET    2 AA7 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1 AA8 2 ARG G  42  VAL G  43  0                                        
SHEET    2 AA8 2 THR H  85  ILE H  86  1  O  ILE H  86   N  ARG G  42           
SHEET    1 AA9 2 ARG G  77  ILE G  78  0                                        
SHEET    2 AA9 2 GLY H  50  ILE H  51  1  O  GLY H  50   N  ILE G  78           
SHEET    1 AB1 2 ARG K  83  PHE K  84  0                                        
SHEET    2 AB1 2 THR L  80  VAL L  81  1  O  VAL L  81   N  ARG K  83           
SHEET    1 AB2 2 THR K 118  ILE K 119  0                                        
SHEET    2 AB2 2 ARG L  45  ILE L  46  1  O  ARG L  45   N  ILE K 119           
SHEET    1 AB3 2 THR L  96  TYR L  98  0                                        
SHEET    2 AB3 2 VAL Q 100  ILE Q 102  1  O  THR Q 101   N  THR L  96           
SHEET    1 AB4 2 ARG M  77  ILE M  78  0                                        
SHEET    2 AB4 2 GLY N  50  ILE N  51  1  O  GLY N  50   N  ILE M  78           
SHEET    1 AB5 2 VAL M 100  THR M 101  0                                        
SHEET    2 AB5 2 THR P  96  LEU P  97  1  O  THR P  96   N  THR M 101           
SHEET    1 AB6 2 ARG O  83  PHE O  84  0                                        
SHEET    2 AB6 2 THR P  80  VAL P  81  1  O  VAL P  81   N  ARG O  83           
SHEET    1 AB7 2 THR O 118  ILE O 119  0                                        
SHEET    2 AB7 2 ARG P  45  ILE P  46  1  O  ARG P  45   N  ILE O 119           
SHEET    1 AB8 2 ARG Q  42  VAL Q  43  0                                        
SHEET    2 AB8 2 THR R  85  ILE R  86  1  O  ILE R  86   N  ARG Q  42           
SHEET    1 AB9 2 ARG Q  77  ILE Q  78  0                                        
SHEET    2 AB9 2 GLY R  50  ILE R  51  1  O  GLY R  50   N  ILE Q  78           
SHEET    1 AC1 2 LEU U  81  GLN U  83  0                                        
SHEET    2 AC1 2 PHE U  93  LEU U  95 -1  O  ARG U  94   N  LYS U  82           
SHEET    1 AC2 3 SER V  45  SER V  46  0                                        
SHEET    2 AC2 3 SER V  92  LEU V  95 -1  O  PHE V  93   N  SER V  45           
SHEET    3 AC2 3 LEU V  81  GLN V  83 -1  N  LYS V  82   O  ARG V  94           
CRYST1   65.926  108.543  180.770 100.79  90.08  89.94 P 1           4          
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      0.015169 -0.000016  0.000019        0.00000                         
SCALE2      0.000000  0.009213  0.001756        0.00000                         
SCALE3      0.000000  0.000000  0.005631        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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