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Database: PDB
Entry: 4WNN
LinkDB: 4WNN
Original site: 4WNN 
HEADER    DNA BINDING PROTEIN                     13-OCT-14   4WNN              
TITLE     SPT16-H2A-H2B FACT HISTONE COMPLEX                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H2A.1;                                             
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H2B.1;                                             
COMPND   7 CHAIN: B, D, F, H;                                                   
COMPND   8 FRAGMENT: UNP RESIDUES 31-131;                                       
COMPND   9 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: SPT16;                                                     
COMPND  13 CHAIN: T;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: HTA1, H2A1, SPT11, YDR225W, YD9934.10;                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 559292;                                              
SOURCE  13 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  14 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;                        
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  20 ORGANISM_TAXID: 4932;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FACT, SPT16, HISTONE, POB3, H2A, H2B, DNA BINDING PROTEIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.KEMBLE,C.P.HILL,F.G.WHITBY,T.FORMOSA,L.L.MCCULLOUGH               
REVDAT   4   04-DEC-19 4WNN    1       REMARK                                   
REVDAT   3   27-SEP-17 4WNN    1       JRNL   REMARK                            
REVDAT   2   28-OCT-15 4WNN    1       JRNL                                     
REVDAT   1   21-OCT-15 4WNN    0                                                
JRNL        AUTH   D.J.KEMBLE,L.L.MCCULLOUGH,F.G.WHITBY,T.FORMOSA,C.P.HILL      
JRNL        TITL   FACT DISRUPTS NUCLEOSOME STRUCTURE BY BINDING H2A-H2B WITH   
JRNL        TITL 2 CONSERVED PEPTIDE MOTIFS.                                    
JRNL        REF    MOL.CELL                      V.  60   294 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26455391                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.09.008                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 77580                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3900                            
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 21.2243 -  5.4133    0.88     2349   137  0.1657 0.2019        
REMARK   3     2  5.4133 -  4.3085    0.98     2637   145  0.1413 0.1803        
REMARK   3     3  4.3085 -  3.7673    0.98     2650   125  0.1530 0.1940        
REMARK   3     4  3.7673 -  3.4245    0.99     2623   132  0.1606 0.1999        
REMARK   3     5  3.4245 -  3.1799    1.00     2688   137  0.1892 0.2958        
REMARK   3     6  3.1799 -  2.9929    1.00     2679   143  0.1975 0.2448        
REMARK   3     7  2.9929 -  2.8434    1.00     2654   167  0.1886 0.2297        
REMARK   3     8  2.8434 -  2.7199    1.00     2661   125  0.1830 0.2163        
REMARK   3     9  2.7199 -  2.6154    1.00     2638   138  0.1808 0.2197        
REMARK   3    10  2.6154 -  2.5253    1.00     2678   153  0.1797 0.2066        
REMARK   3    11  2.5253 -  2.4464    1.00     2682   141  0.1784 0.2233        
REMARK   3    12  2.4464 -  2.3766    1.00     2654   162  0.1867 0.2448        
REMARK   3    13  2.3766 -  2.3141    1.00     2702   123  0.1884 0.2536        
REMARK   3    14  2.3141 -  2.2577    1.00     2630   152  0.1911 0.2413        
REMARK   3    15  2.2577 -  2.2065    1.00     2685   126  0.1987 0.2326        
REMARK   3    16  2.2065 -  2.1595    1.00     2689   140  0.1796 0.2299        
REMARK   3    17  2.1595 -  2.1164    1.00     2655   139  0.1863 0.2414        
REMARK   3    18  2.1164 -  2.0765    1.00     2683   125  0.1864 0.2186        
REMARK   3    19  2.0765 -  2.0394    1.00     2719   138  0.1964 0.2038        
REMARK   3    20  2.0394 -  2.0049    1.00     2673   120  0.1995 0.2484        
REMARK   3    21  2.0049 -  1.9726    1.00     2656   151  0.2150 0.3007        
REMARK   3    22  1.9726 -  1.9422    1.00     2661   159  0.2516 0.3259        
REMARK   3    23  1.9422 -  1.9137    1.00     2701   144  0.2534 0.3117        
REMARK   3    24  1.9137 -  1.8868    1.00     2623   126  0.3001 0.3523        
REMARK   3    25  1.8868 -  1.8613    0.98     2607   155  0.3282 0.3991        
REMARK   3    26  1.8613 -  1.8371    0.97     2642   124  0.2748 0.2995        
REMARK   3    27  1.8371 -  1.8142    0.95     2497   141  0.2719 0.2841        
REMARK   3    28  1.8142 -  1.8000    0.84     2264   132  0.2832 0.3409        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.02                          
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      :  0.007           5853                                  
REMARK   3   ANGLE     :  0.952           7871                                  
REMARK   3   CHIRALITY :  0.039            906                                  
REMARK   3   PLANARITY :  0.005            997                                  
REMARK   3   DIHEDRAL  : 13.663           2256                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6745  -6.7327 -32.1876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2261 T22:   0.2678                                     
REMARK   3      T33:   0.2556 T12:   0.0215                                     
REMARK   3      T13:  -0.0037 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5860 L22:   0.6357                                     
REMARK   3      L33:   0.7295 L12:   0.1995                                     
REMARK   3      L13:   0.0803 L23:   0.2432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0486 S12:   0.1093 S13:  -0.0999                       
REMARK   3      S21:  -0.0332 S22:  -0.0360 S23:  -0.1065                       
REMARK   3      S31:   0.0889 S32:  -0.0423 S33:   0.0001                       
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 4WNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204148.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.127090                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77661                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1ID3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF ~ 60 X 60 MM FORMED WITHIN   
REMARK 280  10 DAYS IN 0.1M SPG (SUCCINIC ACID:SODIUM DIHYDROGEN PHOSPHATE:     
REMARK 280  GLYCINE ) PH 7, 25 % PEG 1500 (A4 OF THE PACT SUITE COMMERCIAL      
REMARK 280  SCREEN (QIAGEN)., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       54.83350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.65814            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       62.49000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       54.83350            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       31.65814            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.49000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       54.83350            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       31.65814            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.49000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.31627            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      124.98000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       63.31627            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      124.98000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       63.31627            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      124.98000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, T                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     THR A   102                                                      
REMARK 465     ILE A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     VAL A   108                                                      
REMARK 465     LEU A   109                                                      
REMARK 465     PRO A   110                                                      
REMARK 465     ASN A   111                                                      
REMARK 465     ILE A   112                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     GLN A   114                                                      
REMARK 465     ASN A   115                                                      
REMARK 465     LEU A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     LYS A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     SER A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     ALA A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     LYS A   126                                                      
REMARK 465     ALA A   127                                                      
REMARK 465     SER A   128                                                      
REMARK 465     GLN A   129                                                      
REMARK 465     GLU A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     SER B   127                                                      
REMARK 465     THR B   128                                                      
REMARK 465     GLN B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 465     MET C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     ALA C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     GLN C    16                                                      
REMARK 465     ASN C   100                                                      
REMARK 465     VAL C   101                                                      
REMARK 465     THR C   102                                                      
REMARK 465     ILE C   103                                                      
REMARK 465     ALA C   104                                                      
REMARK 465     GLN C   105                                                      
REMARK 465     GLY C   106                                                      
REMARK 465     GLY C   107                                                      
REMARK 465     VAL C   108                                                      
REMARK 465     LEU C   109                                                      
REMARK 465     PRO C   110                                                      
REMARK 465     ASN C   111                                                      
REMARK 465     ILE C   112                                                      
REMARK 465     HIS C   113                                                      
REMARK 465     GLN C   114                                                      
REMARK 465     ASN C   115                                                      
REMARK 465     LEU C   116                                                      
REMARK 465     LEU C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     LYS C   119                                                      
REMARK 465     LYS C   120                                                      
REMARK 465     SER C   121                                                      
REMARK 465     ALA C   122                                                      
REMARK 465     LYS C   123                                                      
REMARK 465     ALA C   124                                                      
REMARK 465     THR C   125                                                      
REMARK 465     LYS C   126                                                      
REMARK 465     ALA C   127                                                      
REMARK 465     SER C   128                                                      
REMARK 465     GLN C   129                                                      
REMARK 465     GLU C   130                                                      
REMARK 465     LEU C   131                                                      
REMARK 465     MET D    29                                                      
REMARK 465     SER D   127                                                      
REMARK 465     THR D   128                                                      
REMARK 465     GLN D   129                                                      
REMARK 465     ALA D   130                                                      
REMARK 465     MET E     0                                                      
REMARK 465     SER E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLY E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     ALA E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     ALA E    11                                                      
REMARK 465     ALA E    12                                                      
REMARK 465     LYS E    13                                                      
REMARK 465     ALA E    14                                                      
REMARK 465     SER E    15                                                      
REMARK 465     GLN E    16                                                      
REMARK 465     ASN E   100                                                      
REMARK 465     VAL E   101                                                      
REMARK 465     THR E   102                                                      
REMARK 465     ILE E   103                                                      
REMARK 465     ALA E   104                                                      
REMARK 465     GLN E   105                                                      
REMARK 465     GLY E   106                                                      
REMARK 465     GLY E   107                                                      
REMARK 465     VAL E   108                                                      
REMARK 465     LEU E   109                                                      
REMARK 465     PRO E   110                                                      
REMARK 465     ASN E   111                                                      
REMARK 465     ILE E   112                                                      
REMARK 465     HIS E   113                                                      
REMARK 465     GLN E   114                                                      
REMARK 465     ASN E   115                                                      
REMARK 465     LEU E   116                                                      
REMARK 465     LEU E   117                                                      
REMARK 465     PRO E   118                                                      
REMARK 465     LYS E   119                                                      
REMARK 465     LYS E   120                                                      
REMARK 465     SER E   121                                                      
REMARK 465     ALA E   122                                                      
REMARK 465     LYS E   123                                                      
REMARK 465     ALA E   124                                                      
REMARK 465     THR E   125                                                      
REMARK 465     LYS E   126                                                      
REMARK 465     ALA E   127                                                      
REMARK 465     SER E   128                                                      
REMARK 465     GLN E   129                                                      
REMARK 465     GLU E   130                                                      
REMARK 465     LEU E   131                                                      
REMARK 465     SER F   127                                                      
REMARK 465     THR F   128                                                      
REMARK 465     GLN F   129                                                      
REMARK 465     ALA F   130                                                      
REMARK 465     MET G     0                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     GLY G     5                                                      
REMARK 465     GLY G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     ALA G     8                                                      
REMARK 465     GLY G     9                                                      
REMARK 465     SER G    10                                                      
REMARK 465     ALA G    11                                                      
REMARK 465     ALA G    12                                                      
REMARK 465     LYS G    13                                                      
REMARK 465     ALA G    14                                                      
REMARK 465     SER G    15                                                      
REMARK 465     GLN G    16                                                      
REMARK 465     GLY G    99                                                      
REMARK 465     ASN G   100                                                      
REMARK 465     VAL G   101                                                      
REMARK 465     THR G   102                                                      
REMARK 465     ILE G   103                                                      
REMARK 465     ALA G   104                                                      
REMARK 465     GLN G   105                                                      
REMARK 465     GLY G   106                                                      
REMARK 465     GLY G   107                                                      
REMARK 465     VAL G   108                                                      
REMARK 465     LEU G   109                                                      
REMARK 465     PRO G   110                                                      
REMARK 465     ASN G   111                                                      
REMARK 465     ILE G   112                                                      
REMARK 465     HIS G   113                                                      
REMARK 465     GLN G   114                                                      
REMARK 465     ASN G   115                                                      
REMARK 465     LEU G   116                                                      
REMARK 465     LEU G   117                                                      
REMARK 465     PRO G   118                                                      
REMARK 465     LYS G   119                                                      
REMARK 465     LYS G   120                                                      
REMARK 465     SER G   121                                                      
REMARK 465     ALA G   122                                                      
REMARK 465     LYS G   123                                                      
REMARK 465     ALA G   124                                                      
REMARK 465     THR G   125                                                      
REMARK 465     LYS G   126                                                      
REMARK 465     ALA G   127                                                      
REMARK 465     SER G   128                                                      
REMARK 465     GLN G   129                                                      
REMARK 465     GLU G   130                                                      
REMARK 465     LEU G   131                                                      
REMARK 465     SER H   127                                                      
REMARK 465     THR H   128                                                      
REMARK 465     GLN H   129                                                      
REMARK 465     ALA H   130                                                      
REMARK 465     GLY T   953                                                      
REMARK 465     ILE T   954                                                      
REMARK 465     LYS T   955                                                      
REMARK 465     LYS T   956                                                      
REMARK 465     THR T   957                                                      
REMARK 465     ASP T   958                                                      
REMARK 465     ASP T   959                                                      
REMARK 465     GLU T   960                                                      
REMARK 465     ALA T   961                                                      
REMARK 465     SER T   962                                                      
REMARK 465     ASP T   963                                                      
REMARK 465     GLU T   964                                                      
REMARK 465     SER T   965                                                      
REMARK 465     GLU T   966                                                      
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 B    45     O    HOH B   201              2.13            
REMARK 500   OD1  ASP B    71     O    HOH B   231              2.14            
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    LYS G  75       83.91     56.14                                   
REMARK 500    ARG H  32       78.11    -67.65                                   
REMARK 500    ALA H  35      -70.73   -138.42                                   
REMARK 500    ARG H  36     -140.76     52.00                                   
REMARK 500    LYS H  37       78.38   -169.96                                   
REMARK 500    GLU H  38      107.56    -17.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 337        DISTANCE =  6.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 201                 
DBREF  4WNN A    0   131  UNP    P04911   H2A1_YEAST       1    132             
DBREF  4WNN B   30   130  UNP    P02293   H2B1_YEAST      31    131             
DBREF  4WNN C    0   131  UNP    P04911   H2A1_YEAST       1    132             
DBREF  4WNN D   30   130  UNP    P02293   H2B1_YEAST      31    131             
DBREF  4WNN E    0   131  UNP    P04911   H2A1_YEAST       1    132             
DBREF  4WNN F   30   130  UNP    P02293   H2B1_YEAST      31    131             
DBREF  4WNN G    0   131  UNP    P04911   H2A1_YEAST       1    132             
DBREF  4WNN H   30   130  UNP    P02293   H2B1_YEAST      31    131             
DBREF  4WNN T  953   972  PDB    4WNN     4WNN           953    972             
SEQADV 4WNN MET B   29  UNP  P02293              INITIATING METHIONINE          
SEQADV 4WNN MET D   29  UNP  P02293              INITIATING METHIONINE          
SEQADV 4WNN MET F   29  UNP  P02293              INITIATING METHIONINE          
SEQADV 4WNN MET H   29  UNP  P02293              INITIATING METHIONINE          
SEQRES   1 A  132  MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA          
SEQRES   2 A  132  LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR          
SEQRES   3 A  132  PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY          
SEQRES   4 A  132  ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR          
SEQRES   5 A  132  LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU          
SEQRES   6 A  132  GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR          
SEQRES   7 A  132  ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN          
SEQRES   8 A  132  ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE          
SEQRES   9 A  132  ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU          
SEQRES  10 A  132  LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN          
SEQRES  11 A  132  GLU LEU                                                      
SEQRES   1 B  102  MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER          
SEQRES   2 B  102  SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP          
SEQRES   3 B  102  THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER          
SEQRES   4 B  102  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA          
SEQRES   5 B  102  SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER          
SEQRES   6 B  102  ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO          
SEQRES   7 B  102  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG          
SEQRES   8 B  102  ALA VAL THR LYS TYR SER SER SER THR GLN ALA                  
SEQRES   1 C  132  MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA          
SEQRES   2 C  132  LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR          
SEQRES   3 C  132  PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY          
SEQRES   4 C  132  ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR          
SEQRES   5 C  132  LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU          
SEQRES   6 C  132  GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR          
SEQRES   7 C  132  ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN          
SEQRES   8 C  132  ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE          
SEQRES   9 C  132  ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU          
SEQRES  10 C  132  LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN          
SEQRES  11 C  132  GLU LEU                                                      
SEQRES   1 D  102  MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER          
SEQRES   2 D  102  SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP          
SEQRES   3 D  102  THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER          
SEQRES   4 D  102  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA          
SEQRES   5 D  102  SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER          
SEQRES   6 D  102  ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO          
SEQRES   7 D  102  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG          
SEQRES   8 D  102  ALA VAL THR LYS TYR SER SER SER THR GLN ALA                  
SEQRES   1 E  132  MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA          
SEQRES   2 E  132  LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR          
SEQRES   3 E  132  PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY          
SEQRES   4 E  132  ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR          
SEQRES   5 E  132  LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU          
SEQRES   6 E  132  GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR          
SEQRES   7 E  132  ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN          
SEQRES   8 E  132  ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE          
SEQRES   9 E  132  ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU          
SEQRES  10 E  132  LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN          
SEQRES  11 E  132  GLU LEU                                                      
SEQRES   1 F  102  MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER          
SEQRES   2 F  102  SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP          
SEQRES   3 F  102  THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER          
SEQRES   4 F  102  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA          
SEQRES   5 F  102  SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER          
SEQRES   6 F  102  ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO          
SEQRES   7 F  102  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG          
SEQRES   8 F  102  ALA VAL THR LYS TYR SER SER SER THR GLN ALA                  
SEQRES   1 G  132  MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA          
SEQRES   2 G  132  LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR          
SEQRES   3 G  132  PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY          
SEQRES   4 G  132  ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR          
SEQRES   5 G  132  LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU          
SEQRES   6 G  132  GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR          
SEQRES   7 G  132  ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN          
SEQRES   8 G  132  ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE          
SEQRES   9 G  132  ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU          
SEQRES  10 G  132  LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN          
SEQRES  11 G  132  GLU LEU                                                      
SEQRES   1 H  102  MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER          
SEQRES   2 H  102  SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP          
SEQRES   3 H  102  THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER          
SEQRES   4 H  102  PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA          
SEQRES   5 H  102  SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER          
SEQRES   6 H  102  ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO          
SEQRES   7 H  102  GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG          
SEQRES   8 H  102  ALA VAL THR LYS TYR SER SER SER THR GLN ALA                  
SEQRES   1 T   20  GLY ILE LYS LYS THR ASP ASP GLU ALA SER ASP GLU SER          
SEQRES   2 T   20  GLU GLU GLU VAL SER GLU TYR                                  
HET    PO4  A 201       5                                                       
HET    PO4  E 201       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL  10  PO4    2(O4 P 3-)                                                   
FORMUL  12  HOH   *388(H2 O)                                                    
HELIX    1 AA1 SER A   17  GLY A   23  1                                   7    
HELIX    2 AA2 PRO A   27  GLY A   38  1                                  12    
HELIX    3 AA3 SER A   46  ASN A   74  1                                  29    
HELIX    4 AA4 ILE A   80  ASN A   90  1                                  11    
HELIX    5 AA5 ASP A   91  GLY A   99  1                                   9    
HELIX    6 AA6 TYR B   40  HIS B   52  1                                  13    
HELIX    7 AA7 SER B   58  ASN B   87  1                                  30    
HELIX    8 AA8 SER B   93  LEU B  105  1                                  13    
HELIX    9 AA9 PRO B  106  SER B  126  1                                  21    
HELIX   10 AB1 ARG C   18  GLY C   23  1                                   6    
HELIX   11 AB2 PRO C   27  GLY C   38  1                                  12    
HELIX   12 AB3 SER C   46  ASN C   74  1                                  29    
HELIX   13 AB4 ILE C   80  ASN C   90  1                                  11    
HELIX   14 AB5 ASP C   91  LEU C   98  1                                   8    
HELIX   15 AB6 TYR D   40  HIS D   52  1                                  13    
HELIX   16 AB7 SER D   58  ASN D   87  1                                  30    
HELIX   17 AB8 SER D   93  LEU D  105  1                                  13    
HELIX   18 AB9 PRO D  106  SER D  126  1                                  21    
HELIX   19 AC1 ARG E   18  ALA E   22  1                                   5    
HELIX   20 AC2 PRO E   27  GLY E   38  1                                  12    
HELIX   21 AC3 SER E   46  ASN E   74  1                                  29    
HELIX   22 AC4 ILE E   80  ASP E   91  1                                  12    
HELIX   23 AC5 ASP E   91  GLY E   99  1                                   9    
HELIX   24 AC6 TYR F   40  HIS F   52  1                                  13    
HELIX   25 AC7 SER F   58  ASN F   87  1                                  30    
HELIX   26 AC8 SER F   93  LEU F  105  1                                  13    
HELIX   27 AC9 PRO F  106  SER F  125  1                                  20    
HELIX   28 AD1 ARG G   18  GLY G   23  1                                   6    
HELIX   29 AD2 PRO G   27  ARG G   37  1                                  11    
HELIX   30 AD3 SER G   46  ARG G   72  1                                  27    
HELIX   31 AD4 ILE G   80  ASN G   90  1                                  11    
HELIX   32 AD5 ASP G   91  LEU G   98  1                                   8    
HELIX   33 AD6 TYR H   40  HIS H   52  1                                  13    
HELIX   34 AD7 SER H   58  ASN H   87  1                                  30    
HELIX   35 AD8 SER H   93  LEU H  105  1                                  13    
HELIX   36 AD9 PRO H  106  SER H  125  1                                  20    
SHEET    1 AA1 2 ARG A  43  ILE A  44  0                                        
SHEET    2 AA1 2 THR B  91  ILE B  92  1  O  ILE B  92   N  ARG A  43           
SHEET    1 AA2 2 ARG A  78  ILE A  79  0                                        
SHEET    2 AA2 2 GLY B  56  ILE B  57  1  O  GLY B  56   N  ILE A  79           
SHEET    1 AA3 2 ARG C  43  ILE C  44  0                                        
SHEET    2 AA3 2 THR D  91  ILE D  92  1  O  ILE D  92   N  ARG C  43           
SHEET    1 AA4 2 ARG C  78  ILE C  79  0                                        
SHEET    2 AA4 2 GLY D  56  ILE D  57  1  O  GLY D  56   N  ILE C  79           
SHEET    1 AA5 2 ARG E  43  ILE E  44  0                                        
SHEET    2 AA5 2 THR F  91  ILE F  92  1  O  ILE F  92   N  ARG E  43           
SHEET    1 AA6 2 ARG E  78  ILE E  79  0                                        
SHEET    2 AA6 2 GLY F  56  ILE F  57  1  O  GLY F  56   N  ILE E  79           
SHEET    1 AA7 2 ARG G  43  ILE G  44  0                                        
SHEET    2 AA7 2 THR H  91  ILE H  92  1  O  ILE H  92   N  ARG G  43           
SHEET    1 AA8 2 ARG G  78  ILE G  79  0                                        
SHEET    2 AA8 2 GLY H  56  ILE H  57  1  O  GLY H  56   N  ILE G  79           
CISPEP   1 SER H   33    LYS H   34          0        26.30                     
SITE     1 AC1  4 THR A  77  ARG A  78  GLY B  56  ASN C  95                    
SITE     1 AC2  4 THR E  77  ARG E  78  GLY F  56  ASN G  95                    
CRYST1  109.667  109.667  187.470  90.00  90.00 120.00 H 3          36          
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      0.009119  0.005265  0.000000        0.00000                         
SCALE2      0.000000  0.010529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005334        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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