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Database: PDB
Entry: 4KUD
LinkDB: 4KUD
Original site: 4KUD 
HEADER    STRUCTURAL PROTEIN/TRANSCRIPTION/DNA    22-MAY-13   4KUD              
TITLE     CRYSTAL STRUCTURE OF N-TERMINAL ACETYLATED SIR3 BAH DOMAIN D205N      
TITLE    2 MUTANT IN COMPLEX WITH YEAST NUCLEOSOME CORE PARTICLE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3;                                                
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H4;                                                
COMPND   7 CHAIN: B, F;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: HISTONE H2A.2;                                             
COMPND  12 CHAIN: C, G;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: HISTONE H2B.1;                                             
COMPND  16 CHAIN: D, H;                                                         
COMPND  17 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;                                
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: NUCLOESOME DNA;                                            
COMPND  21 CHAIN: I, J;                                                         
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: REGULATORY PROTEIN SIR3;                                   
COMPND  25 CHAIN: K, L;                                                         
COMPND  26 FRAGMENT: BAH DOMAIN, UNP RESIDUES 2-219;                            
COMPND  27 SYNONYM: SILENT INFORMATION REGULATOR 3;                             
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: HHT1, YBR010W, YBR0201, HHT2, SIN2, YNL031C, N2749;            
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: YEAST;                                              
SOURCE  14 ORGANISM_TAXID: 559292;                                              
SOURCE  15 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  16 GENE: HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752;                  
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  23 ORGANISM_COMMON: YEAST;                                              
SOURCE  24 ORGANISM_TAXID: 559292;                                              
SOURCE  25 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  26 GENE: HTA2, H2A2, YBL003C, YBL0103;                                  
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  33 ORGANISM_COMMON: YEAST;                                              
SOURCE  34 ORGANISM_TAXID: 559292;                                              
SOURCE  35 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  36 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;                        
SOURCE  37 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  39 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  40 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  41 MOL_ID: 5;                                                           
SOURCE  42 SYNTHETIC: YES;                                                      
SOURCE  43 MOL_ID: 6;                                                           
SOURCE  44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  45 ORGANISM_COMMON: YEAST;                                              
SOURCE  46 ORGANISM_TAXID: 559292;                                              
SOURCE  47 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  48 GENE: SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10;                     
SOURCE  49 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  50 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  51 EXPRESSION_SYSTEM_CELL: SF21;                                        
SOURCE  52 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEPROTEIN-DNA COMPLEX, NUCLEOSOME, BAH DOMAIN, SILENCING, NUCLEUS, 
KEYWDS   2 STRUCTURAL PROTEIN-TRANSCRIPTION-DNA COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.YANG,Q.FANG,M.WANG,R.REN,H.WANG,M.HE,Y.SUN,N.YANG,R.M.XU            
REVDAT   2   04-SEP-13 4KUD    1       JRNL                                     
REVDAT   1   07-AUG-13 4KUD    0                                                
JRNL        AUTH   D.YANG,Q.FANG,M.WANG,R.REN,H.WANG,M.HE,Y.SUN,N.YANG,R.M.XU   
JRNL        TITL   N ALPHA-ACETYLATED SIR3 STABILIZES THE CONFORMATION OF A     
JRNL        TITL 2 NUCLEOSOME-BINDING LOOP IN THE BAH DOMAIN                    
JRNL        REF    NAT.STRUCT.MOL.BIOL.                       2013              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   23934152                                                     
JRNL        DOI    10.1038/NSMB.2637                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53825                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2757                            
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 45.3900 -  8.6746    0.98     2527   141  0.1574 0.1649        
REMARK   3     2  8.6746 -  6.8931    0.99     2568   136  0.1560 0.2043        
REMARK   3     3  6.8931 -  6.0240    1.00     2548   133  0.2167 0.2456        
REMARK   3     4  6.0240 -  5.4742    1.00     2604   133  0.2103 0.2612        
REMARK   3     5  5.4742 -  5.0824    1.00     2565   135  0.1849 0.2409        
REMARK   3     6  5.0824 -  4.7831    1.00     2576   128  0.1730 0.2104        
REMARK   3     7  4.7831 -  4.5438    1.00     2517   142  0.1662 0.2000        
REMARK   3     8  4.5438 -  4.3462    1.00     2581   120  0.1756 0.1945        
REMARK   3     9  4.3462 -  4.1790    1.00     2573   126  0.1807 0.2465        
REMARK   3    10  4.1790 -  4.0349    1.00     2578   135  0.2011 0.2520        
REMARK   3    11  4.0349 -  3.9088    1.00     2540   134  0.2024 0.2695        
REMARK   3    12  3.9088 -  3.7971    1.00     2599   130  0.2127 0.2413        
REMARK   3    13  3.7971 -  3.6972    1.00     2531   158  0.2160 0.2749        
REMARK   3    14  3.6972 -  3.6070    0.99     2493   144  0.2162 0.2570        
REMARK   3    15  3.6070 -  3.5250    0.99     2571   141  0.2383 0.2761        
REMARK   3    16  3.5250 -  3.4501    0.99     2568   135  0.2494 0.3072        
REMARK   3    17  3.4501 -  3.3811    0.99     2515   154  0.2653 0.2957        
REMARK   3    18  3.3811 -  3.3173    0.99     2558   153  0.2698 0.3370        
REMARK   3    19  3.3173 -  3.2581    0.99     2518   134  0.2932 0.2993        
REMARK   3    20  3.2581 -  3.2028    0.99     2538   145  0.3060 0.3238        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.28                                          
REMARK   3   B_SOL              : 38.97                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 81.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 94.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.15500                                              
REMARK   3    B22 (A**2) : 7.15500                                              
REMARK   3    B33 (A**2) : -14.31000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.006          16557                                  
REMARK   3   ANGLE     :  0.980          23610                                  
REMARK   3   CHIRALITY :  0.055           2653                                  
REMARK   3   PLANARITY :  0.003           1988                                  
REMARK   3   DIHEDRAL  : 24.572           6704                                  
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 4KUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079805.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
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          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54233                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1ID3, 2FVU                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 400, 0.1M KCL, 0.01M CACL2,      
REMARK 280  0.05M SODIUM CITRATE(PH4.8), VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.30667            
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      332.61333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      249.46000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      415.76667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.15333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     LYS A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     ARG A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     MET B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA 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     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     THR C   124                                                      
REMARK 465     ALA 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     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     PRO D    13                                                      
REMARK 465     ALA D    14                                                      
REMARK 465     GLU D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     LYS D    17                                                      
REMARK 465     PRO D    18                                                      
REMARK 465     ALA D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     LYS D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     SER D    24                                                      
REMARK 465     THR D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     THR D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     LYS D    30                                                      
REMARK 465     LYS D    31                                                      
REMARK 465     ARG D    32                                                      
REMARK 465     SER D    33                                                      
REMARK 465     LYS D    34                                                      
REMARK 465     ALA D    35                                                      
REMARK 465     ARG D    36                                                      
REMARK 465     ALA D   130                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     THR E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     GLY E    13                                                      
REMARK 465     LYS E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     PRO E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     LEU E    20                                                      
REMARK 465     ALA E    21                                                      
REMARK 465     SER E    22                                                      
REMARK 465     LYS E    23                                                      
REMARK 465     ALA E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     ARG E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     PRO E    30                                                      
REMARK 465     SER E    31                                                      
REMARK 465     THR E    32                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     VAL E    35                                                      
REMARK 465     ARG E   134                                                      
REMARK 465     SER E   135                                                      
REMARK 465     MET F     0                                                      
REMARK 465     SER F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     LYS F    12                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ALA 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     LYS G   120                                                      
REMARK 465     SER G   121                                                      
REMARK 465     ALA G   122                                                      
REMARK 465     LYS G   123                                                      
REMARK 465     THR G   124                                                      
REMARK 465     ALA 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     MET H     0                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     LYS H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     GLU H     5                                                      
REMARK 465     LYS H     6                                                      
REMARK 465     LYS H     7                                                      
REMARK 465     PRO H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     SER H    10                                                      
REMARK 465     LYS H    11                                                      
REMARK 465     ALA H    12                                                      
REMARK 465     PRO H    13                                                      
REMARK 465     ALA H    14                                                      
REMARK 465     GLU H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     LYS H    17                                                      
REMARK 465     PRO H    18                                                      
REMARK 465     ALA H    19                                                      
REMARK 465     ALA H    20                                                      
REMARK 465     LYS H    21                                                      
REMARK 465     LYS H    22                                                      
REMARK 465     THR H    23                                                      
REMARK 465     SER H    24                                                      
REMARK 465     THR H    25                                                      
REMARK 465     SER H    26                                                      
REMARK 465     THR H    27                                                      
REMARK 465     ASP H    28                                                      
REMARK 465     GLY H    29                                                      
REMARK 465     LYS H    30                                                      
REMARK 465     LYS H    31                                                      
REMARK 465     ARG H    32                                                      
REMARK 465     SER H    33                                                      
REMARK 465     LYS H    34                                                      
REMARK 465     ALA H    35                                                      
REMARK 465     ALA H   130                                                      
REMARK 465     VAL K   215                                                      
REMARK 465     SER K   216                                                      
REMARK 465     GLY K   217                                                      
REMARK 465     GLN K   218                                                      
REMARK 465     LYS K   219                                                      
REMARK 465     HIS K   220                                                      
REMARK 465     HIS K   221                                                      
REMARK 465     HIS K   222                                                      
REMARK 465     HIS K   223                                                      
REMARK 465     HIS K   224                                                      
REMARK 465     HIS K   225                                                      
REMARK 465     VAL L   215                                                      
REMARK 465     SER L   216                                                      
REMARK 465     GLY L   217                                                      
REMARK 465     GLN L   218                                                      
REMARK 465     LYS L   219                                                      
REMARK 465     HIS L   220                                                      
REMARK 465     HIS L   221                                                      
REMARK 465     HIS L   222                                                      
REMARK 465     HIS L   223                                                      
REMARK 465     HIS L   224                                                      
REMARK 465     HIS L   225                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER C    46     OP2   DA J   257              2.04            
REMARK 500   NH1  ARG G    33     OP1   DA J   176              2.17            
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. =   2.3 DEGREES          
REMARK 500     DC I  10   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT I  21   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT I  23   O4' -  C4' -  C3' ANGL. DEV. =  -3.1 DEGREES          
REMARK 500     DT I  23   O4' -  C1' -  N1  ANGL. DEV. =   5.5 DEGREES          
REMARK 500     DC I  25   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC I  26   O4' -  C1' -  N1  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DA I  27   C3' -  C2' -  C1' ANGL. DEV. =  -6.2 DEGREES          
REMARK 500     DA I  27   O4' -  C1' -  N9  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DA I  28   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DA I  29   C3' -  C2' -  C1' ANGL. DEV. =  -7.7 DEGREES          
REMARK 500     DA I  29   O4' -  C1' -  N9  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DG I  33   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT I  48   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC I  53   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA I  55   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DG I  59   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DG I  59   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT I  64   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DG I  68   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG I  68   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT I  75   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DC I  76   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC I  77   C3' -  C2' -  C1' ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     DC I  79   C3' -  C2' -  C1' ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DC I  89   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG I  94   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DA I  95   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DT I  96   C3' -  C2' -  C1' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DT I  96   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DG I 100   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DG I 100   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA I 102   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DA I 110   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DA I 115   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DA I 115   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC I 116   O4' -  C1' -  N1  ANGL. DEV. =   5.1 DEGREES          
REMARK 500     DT I 123   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG I 125   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DA I 127   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DT I 128   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT I 130   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DG I 135   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG I 137   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT J 154   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DC J 158   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC J 162   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC J 162   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DA J 163   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG J 164   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     102 ANGLE DEVIATIONS.                             
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    ARG B  95       77.70   -117.96                                   
REMARK 500    ASP C  73       -9.41    -55.31                                   
REMARK 500    LEU C  98       55.99   -110.04                                   
REMARK 500    ASN C 111       99.84   -163.39                                   
REMARK 500    HIS D  52       89.88   -154.68                                   
REMARK 500    PRO E  43      109.85    -51.59                                   
REMARK 500    ARG G  37       78.84   -107.75                                   
REMARK 500    LEU G  98       49.67   -107.00                                   
REMARK 500    HIS H  52       85.21   -152.85                                   
REMARK 500    SER H 127        4.00    -68.82                                   
REMARK 500    GLN K  19       39.08   -150.07                                   
REMARK 500    ASN K  26       83.55     56.08                                   
REMARK 500    ASP K 160       91.48    -62.21                                   
REMARK 500    ARG K 169      -29.92   -141.58                                   
REMARK 500    GLU K 182      -74.35   -110.64                                   
REMARK 500    LYS K 183       78.80   -104.13                                   
REMARK 500    ASP L  17     -165.10    -73.96                                   
REMARK 500    GLN L  19       40.17    -95.83                                   
REMARK 500    THR L  65     -146.51   -131.65                                   
REMARK 500    ARG L 106       62.35   -165.17                                   
REMARK 500    PRO L 115     -165.63    -72.50                                   
REMARK 500    ARG L 169      -36.02   -147.81                                   
REMARK 500    GLU L 182      -82.63   -119.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KUI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KUL   RELATED DB: PDB                                   
DBREF  4KUD A    0   135  UNP    P61830   H3_YEAST         1    136             
DBREF  4KUD B    0   102  UNP    P02309   H4_YEAST         1    103             
DBREF  4KUD C    0   131  UNP    P04912   H2A2_YEAST       1    132             
DBREF  4KUD D    0   130  UNP    P02293   H2B1_YEAST       1    131             
DBREF  4KUD E    0   135  UNP    P61830   H3_YEAST         1    136             
DBREF  4KUD F    0   102  UNP    P02309   H4_YEAST         1    103             
DBREF  4KUD G    0   131  UNP    P04912   H2A2_YEAST       1    132             
DBREF  4KUD H    0   130  UNP    P02293   H2B1_YEAST       1    131             
DBREF  4KUD I    1   146  PDB    4KUD     4KUD             1    146             
DBREF  4KUD J  147   292  PDB    4KUD     4KUD           147    292             
DBREF  4KUD K    2   219  UNP    P06701   SIR3_YEAST       2    219             
DBREF  4KUD L    2   219  UNP    P06701   SIR3_YEAST       2    219             
SEQADV 4KUD ALA C    1  UNP  P04912    SER     2 ENGINEERED MUTATION            
SEQADV 4KUD ALA G    1  UNP  P04912    SER     2 ENGINEERED MUTATION            
SEQADV 4KUD ASN K  205  UNP  P06701    ASP   205 ENGINEERED MUTATION            
SEQADV 4KUD HIS K  220  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS K  221  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS K  222  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS K  223  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS K  224  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS K  225  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD ASN L  205  UNP  P06701    ASP   205 ENGINEERED MUTATION            
SEQADV 4KUD HIS L  220  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS L  221  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS L  222  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS L  223  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS L  224  UNP  P06701              EXPRESSION TAG                 
SEQADV 4KUD HIS L  225  UNP  P06701              EXPRESSION TAG                 
SEQRES   1 A  136  MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY          
SEQRES   2 A  136  GLY LYS ALA PRO ARG LYS GLN LEU ALA SER LYS ALA ALA          
SEQRES   3 A  136  ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO          
SEQRES   4 A  136  HIS ARG TYR LYS PRO GLY THR VAL ALA LEU ARG GLU ILE          
SEQRES   5 A  136  ARG ARG PHE GLN LYS SER THR GLU LEU LEU ILE ARG LYS          
SEQRES   6 A  136  LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP          
SEQRES   7 A  136  PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA ILE GLY          
SEQRES   8 A  136  ALA LEU GLN GLU SER VAL GLU ALA TYR LEU VAL SER LEU          
SEQRES   9 A  136  PHE GLU ASP THR ASN LEU ALA ALA ILE HIS ALA LYS ARG          
SEQRES  10 A  136  VAL THR ILE GLN LYS LYS ASP ILE LYS LEU ALA ARG ARG          
SEQRES  11 A  136  LEU ARG GLY GLU ARG SER                                      
SEQRES   1 B  103  MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS          
SEQRES   2 B  103  GLY GLY ALA LYS ARG HIS ARG LYS ILE LEU ARG ASP ASN          
SEQRES   3 B  103  ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA          
SEQRES   4 B  103  ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR          
SEQRES   5 B  103  GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU GLU SER          
SEQRES   6 B  103  VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS ALA LYS          
SEQRES   7 B  103  ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR ALA LEU          
SEQRES   8 B  103  LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY              
SEQRES   1 C  132  MET ALA 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 THR ALA LYS ALA SER GLN          
SEQRES  11 C  132  GLU LEU                                                      
SEQRES   1 D  131  MET SER ALA LYS ALA GLU LYS LYS PRO ALA SER LYS ALA          
SEQRES   2 D  131  PRO ALA GLU LYS LYS PRO ALA ALA LYS LYS THR SER THR          
SEQRES   3 D  131  SER THR ASP GLY LYS LYS ARG SER LYS ALA ARG LYS GLU          
SEQRES   4 D  131  THR TYR SER SER TYR ILE TYR LYS VAL LEU LYS GLN THR          
SEQRES   5 D  131  HIS PRO ASP THR GLY ILE SER GLN LYS SER MET SER ILE          
SEQRES   6 D  131  LEU ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA          
SEQRES   7 D  131  THR GLU ALA SER LYS LEU ALA ALA TYR ASN LYS LYS SER          
SEQRES   8 D  131  THR ILE SER ALA ARG GLU ILE GLN THR ALA VAL ARG LEU          
SEQRES   9 D  131  ILE LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU          
SEQRES  10 D  131  GLY THR ARG ALA VAL THR LYS TYR SER SER SER THR GLN          
SEQRES  11 D  131  ALA                                                          
SEQRES   1 E  136  MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY          
SEQRES   2 E  136  GLY LYS ALA PRO ARG LYS GLN LEU ALA SER LYS ALA ALA          
SEQRES   3 E  136  ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO          
SEQRES   4 E  136  HIS ARG TYR LYS PRO GLY THR VAL ALA LEU ARG GLU ILE          
SEQRES   5 E  136  ARG ARG PHE GLN LYS SER THR GLU LEU LEU ILE ARG LYS          
SEQRES   6 E  136  LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP          
SEQRES   7 E  136  PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA ILE GLY          
SEQRES   8 E  136  ALA LEU GLN GLU SER VAL GLU ALA TYR LEU VAL SER LEU          
SEQRES   9 E  136  PHE GLU ASP THR ASN LEU ALA ALA ILE HIS ALA LYS ARG          
SEQRES  10 E  136  VAL THR ILE GLN LYS LYS ASP ILE LYS LEU ALA ARG ARG          
SEQRES  11 E  136  LEU ARG GLY GLU ARG SER                                      
SEQRES   1 F  103  MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS          
SEQRES   2 F  103  GLY GLY ALA LYS ARG HIS ARG LYS ILE LEU ARG ASP ASN          
SEQRES   3 F  103  ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA          
SEQRES   4 F  103  ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR          
SEQRES   5 F  103  GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU GLU SER          
SEQRES   6 F  103  VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS ALA LYS          
SEQRES   7 F  103  ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR ALA LEU          
SEQRES   8 F  103  LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY              
SEQRES   1 G  132  MET ALA 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 THR ALA LYS ALA SER GLN          
SEQRES  11 G  132  GLU LEU                                                      
SEQRES   1 H  131  MET SER ALA LYS ALA GLU LYS LYS PRO ALA SER LYS ALA          
SEQRES   2 H  131  PRO ALA GLU LYS LYS PRO ALA ALA LYS LYS THR SER THR          
SEQRES   3 H  131  SER THR ASP GLY LYS LYS ARG SER LYS ALA ARG LYS GLU          
SEQRES   4 H  131  THR TYR SER SER TYR ILE TYR LYS VAL LEU LYS GLN THR          
SEQRES   5 H  131  HIS PRO ASP THR GLY ILE SER GLN LYS SER MET SER ILE          
SEQRES   6 H  131  LEU ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA          
SEQRES   7 H  131  THR GLU ALA SER LYS LEU ALA ALA TYR ASN LYS LYS SER          
SEQRES   8 H  131  THR ILE SER ALA ARG GLU ILE GLN THR ALA VAL ARG LEU          
SEQRES   9 H  131  ILE LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU          
SEQRES  10 H  131  GLY THR ARG ALA VAL THR LYS TYR SER SER SER THR GLN          
SEQRES  11 H  131  ALA                                                          
SEQRES   1 I  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 I  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 I  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 I  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 I  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 I  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 I  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 I  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 I  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 I  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 I  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 I  146   DG  DA  DT                                                  
SEQRES   1 J  146   DA  DT  DC  DA  DA  DT  DA  DT  DC  DC  DA  DC  DC          
SEQRES   2 J  146   DT  DG  DC  DA  DG  DA  DT  DT  DC  DT  DA  DC  DC          
SEQRES   3 J  146   DA  DA  DA  DA  DG  DT  DG  DT  DA  DT  DT  DT  DG          
SEQRES   4 J  146   DG  DA  DA  DA  DC  DT  DG  DC  DT  DC  DC  DA  DT          
SEQRES   5 J  146   DC  DA  DA  DA  DA  DG  DG  DC  DA  DT  DG  DT  DT          
SEQRES   6 J  146   DC  DA  DG  DC  DG  DG  DA  DA  DT  DT  DC  DC  DG          
SEQRES   7 J  146   DC  DT  DG  DA  DA  DC  DA  DT  DG  DC  DC  DT  DT          
SEQRES   8 J  146   DT  DT  DG  DA  DT  DG  DG  DA  DG  DC  DA  DG  DT          
SEQRES   9 J  146   DT  DT  DC  DC  DA  DA  DA  DT  DA  DC  DA  DC  DT          
SEQRES  10 J  146   DT  DT  DT  DG  DG  DT  DA  DG  DA  DA  DT  DC  DT          
SEQRES  11 J  146   DG  DC  DA  DG  DG  DT  DG  DG  DA  DT  DA  DT  DT          
SEQRES  12 J  146   DG  DA  DT                                                  
SEQRES   1 K  224  AYA LYS THR LEU LYS ASP LEU ASP GLY TRP GLN VAL ILE          
SEQRES   2 K  224  ILE THR ASP ASP GLN GLY ARG VAL ILE ASP ASP ASN ASN          
SEQRES   3 K  224  ARG ARG ARG SER ARG LYS ARG GLY GLY GLU ASN VAL PHE          
SEQRES   4 K  224  LEU LYS ARG ILE SER ASP GLY LEU SER PHE GLY LYS GLY          
SEQRES   5 K  224  GLU SER VAL ILE PHE ASN ASP ASN VAL THR GLU THR TYR          
SEQRES   6 K  224  SER VAL TYR LEU ILE HIS GLU ILE ARG LEU ASN THR LEU          
SEQRES   7 K  224  ASN ASN VAL VAL GLU ILE TRP VAL PHE SER TYR LEU ARG          
SEQRES   8 K  224  TRP PHE GLU LEU LYS PRO LYS LEU TYR TYR GLU GLN PHE          
SEQRES   9 K  224  ARG PRO ASP LEU ILE LYS GLU ASP HIS PRO LEU GLU PHE          
SEQRES  10 K  224  TYR LYS ASP LYS PHE PHE ASN GLU VAL ASN LYS SER GLU          
SEQRES  11 K  224  LEU TYR LEU THR ALA GLU LEU SER GLU ILE TRP LEU LYS          
SEQRES  12 K  224  ASP PHE ILE ALA VAL GLY GLN ILE LEU PRO GLU SER GLN          
SEQRES  13 K  224  TRP ASN ASP SER SER ILE ASP LYS ILE GLU ASP ARG ASP          
SEQRES  14 K  224  PHE LEU VAL ARG TYR ALA CYS GLU PRO THR ALA GLU LYS          
SEQRES  15 K  224  PHE VAL PRO ILE ASP ILE PHE GLN ILE ILE ARG ARG VAL          
SEQRES  16 K  224  LYS GLU MET GLU PRO LYS GLN SER ASN GLU TYR LEU LYS          
SEQRES  17 K  224  ARG VAL SER VAL PRO VAL SER GLY GLN LYS HIS HIS HIS          
SEQRES  18 K  224  HIS HIS HIS                                                  
SEQRES   1 L  224  AYA LYS THR LEU LYS ASP LEU ASP GLY TRP GLN VAL ILE          
SEQRES   2 L  224  ILE THR ASP ASP GLN GLY ARG VAL ILE ASP ASP ASN ASN          
SEQRES   3 L  224  ARG ARG ARG SER ARG LYS ARG GLY GLY GLU ASN VAL PHE          
SEQRES   4 L  224  LEU LYS ARG ILE SER ASP GLY LEU SER PHE GLY LYS GLY          
SEQRES   5 L  224  GLU SER VAL ILE PHE ASN ASP ASN VAL THR GLU THR TYR          
SEQRES   6 L  224  SER VAL TYR LEU ILE HIS GLU ILE ARG LEU ASN THR LEU          
SEQRES   7 L  224  ASN ASN VAL VAL GLU ILE TRP VAL PHE SER TYR LEU ARG          
SEQRES   8 L  224  TRP PHE GLU LEU LYS PRO LYS LEU TYR TYR GLU GLN PHE          
SEQRES   9 L  224  ARG PRO ASP LEU ILE LYS GLU ASP HIS PRO LEU GLU PHE          
SEQRES  10 L  224  TYR LYS ASP LYS PHE PHE ASN GLU VAL ASN LYS SER GLU          
SEQRES  11 L  224  LEU TYR LEU THR ALA GLU LEU SER GLU ILE TRP LEU LYS          
SEQRES  12 L  224  ASP PHE ILE ALA VAL GLY GLN ILE LEU PRO GLU SER GLN          
SEQRES  13 L  224  TRP ASN ASP SER SER ILE ASP LYS ILE GLU ASP ARG ASP          
SEQRES  14 L  224  PHE LEU VAL ARG TYR ALA CYS GLU PRO THR ALA GLU LYS          
SEQRES  15 L  224  PHE VAL PRO ILE ASP ILE PHE GLN ILE ILE ARG ARG VAL          
SEQRES  16 L  224  LYS GLU MET GLU PRO LYS GLN SER ASN GLU TYR LEU LYS          
SEQRES  17 L  224  ARG VAL SER VAL PRO VAL SER GLY GLN LYS HIS HIS HIS          
SEQRES  18 L  224  HIS HIS HIS                                                  
MODRES 4KUD AYA K    2  ALA  N-ACETYLALANINE                                    
MODRES 4KUD AYA L    2  ALA  N-ACETYLALANINE                                    
HET    AYA  K   2       8                                                       
HET    AYA  L   2       8                                                       
HETNAM     AYA N-ACETYLALANINE                                                  
FORMUL  11  AYA    2(C5 H9 N O3)                                                
FORMUL  13  HOH   *66(H2 O)                                                     
HELIX    1   1 GLY A   44  SER A   57  1                                  14    
HELIX    2   2 ARG A   63  GLN A   76  1                                  14    
HELIX    3   3 GLN A   85  ALA A  114  1                                  30    
HELIX    4   4 GLN A  120  ARG A  131  1                                  12    
HELIX    5   5 ASP B   24  ILE B   29  5                                   6    
HELIX    6   6 THR B   30  GLY B   42  1                                  13    
HELIX    7   7 LEU B   49  ALA B   76  1                                  28    
HELIX    8   8 THR B   82  GLN B   93  1                                  12    
HELIX    9   9 SER C   17  ALA C   22  1                                   6    
HELIX   10  10 PRO C   27  GLY C   38  1                                  12    
HELIX   11  11 GLY C   47  ASP C   73  1                                  27    
HELIX   12  12 ILE C   80  ASP C   91  1                                  12    
HELIX   13  13 ASP C   91  LEU C   98  1                                   8    
HELIX   14  14 TYR D   40  HIS D   52  1                                  13    
HELIX   15  15 SER D   58  ASN D   87  1                                  30    
HELIX   16  16 SER D   93  LEU D  105  1                                  13    
HELIX   17  17 PRO D  106  THR D  128  1                                  23    
HELIX   18  18 GLY E   44  SER E   57  1                                  14    
HELIX   19  19 ARG E   63  GLN E   76  1                                  14    
HELIX   20  20 GLN E   85  ALA E  114  1                                  30    
HELIX   21  21 GLN E  120  ARG E  131  1                                  12    
HELIX   22  22 ASP F   24  ILE F   29  5                                   6    
HELIX   23  23 THR F   30  GLY F   42  1                                  13    
HELIX   24  24 LEU F   49  ALA F   76  1                                  28    
HELIX   25  25 THR F   82  GLN F   93  1                                  12    
HELIX   26  26 SER G   17  ALA G   22  1                                   6    
HELIX   27  27 PRO G   27  ARG G   37  1                                  11    
HELIX   28  28 GLY G   47  ASP G   73  1                                  27    
HELIX   29  29 ILE G   80  ASP G   91  1                                  12    
HELIX   30  30 ASP G   91  LEU G   98  1                                   8    
HELIX   31  31 TYR H   40  HIS H   52  1                                  13    
HELIX   32  32 SER H   58  ASN H   87  1                                  30    
HELIX   33  33 SER H   93  LEU H  105  1                                  13    
HELIX   34  34 PRO H  106  SER H  127  1                                  22    
HELIX   35  35 THR K    4  ASP K    9  5                                   6    
HELIX   36  36 ARG K   92  LEU K   96  5                                   5    
HELIX   37  37 LYS K   97  ARG K  106  1                                  10    
HELIX   38  38 ARG K  106  GLU K  112  1                                   7    
HELIX   39  39 PRO K  115  VAL K  127  1                                  13    
HELIX   40  40 TRP K  142  LYS K  144  5                                   3    
HELIX   41  41 PRO K  154  ASP K  160  1                                   7    
HELIX   42  42 ASP K  188  MET K  199  1                                  12    
HELIX   43  43 GLU K  200  SER K  212  1                                  13    
HELIX   44  44 LEU L    5  ASP L    9  5                                   5    
HELIX   45  45 LYS L   97  ARG L  106  1                                  10    
HELIX   46  46 ARG L  106  GLU L  112  1                                   7    
HELIX   47  47 PRO L  115  VAL L  127  1                                  13    
HELIX   48  48 TRP L  142  LYS L  144  5                                   3    
HELIX   49  49 PRO L  154  ASP L  160  1                                   7    
HELIX   50  50 ASP L  188  MET L  199  1                                  12    
HELIX   51  51 GLU L  200  SER L  212  1                                  13    
SHEET    1   A 2 ARG A  83  PHE A  84  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A  83           
SHEET    1   B 2 THR A 118  ILE A 119  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1   C 2 THR B  96  TYR B  98  0                                        
SHEET    2   C 2 VAL G 101  ILE G 103  1  O  THR G 102   N  TYR B  98           
SHEET    1   D 2 ARG C  43  ILE C  44  0                                        
SHEET    2   D 2 THR D  91  ILE D  92  1  O  ILE D  92   N  ARG C  43           
SHEET    1   E 2 ARG C  78  ILE C  79  0                                        
SHEET    2   E 2 GLY D  56  ILE D  57  1  O  GLY D  56   N  ILE C  79           
SHEET    1   F 2 VAL C 101  ILE C 103  0                                        
SHEET    2   F 2 THR F  96  TYR F  98  1  O  THR F  96   N  THR C 102           
SHEET    1   G 2 ARG E  83  PHE E  84  0                                        
SHEET    2   G 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1   H 2 THR E 118  ILE E 119  0                                        
SHEET    2   H 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1   I 2 ARG G  43  ILE G  44  0                                        
SHEET    2   I 2 THR H  91  ILE H  92  1  O  ILE H  92   N  ARG G  43           
SHEET    1   J 2 ARG G  78  ILE G  79  0                                        
SHEET    2   J 2 GLY H  56  ILE H  57  1  O  GLY H  56   N  ILE G  79           
SHEET    1   K 4 VAL K  22  ILE K  23  0                                        
SHEET    2   K 4 TRP K  11  THR K  16 -1  N  ILE K  15   O  ILE K  23           
SHEET    3   K 4 ASN K  38  ARG K  43 -1  O  PHE K  40   N  ILE K  14           
SHEET    4   K 4 SER K  49  PHE K  50 -1  O  PHE K  50   N  LEU K  41           
SHEET    1   L 7 PHE K 146  VAL K 149  0                                        
SHEET    2   L 7 SER K  55  ASP K  60 -1  N  ILE K  57   O  ALA K 148           
SHEET    3   L 7 THR K  65  LEU K  76 -1  O  TYR K  69   N  VAL K  56           
SHEET    4   L 7 VAL K  83  LEU K  91 -1  O  GLU K  84   N  ARG K  75           
SHEET    5   L 7 GLU K 131  ILE K 141 -1  O  TYR K 133   N  LEU K  91           
SHEET    6   L 7 ASP K 170  ALA K 176  1  O  LEU K 172   N  LEU K 132           
SHEET    7   L 7 GLN K 151  ILE K 152  1  N  GLN K 151   O  PHE K 171           
SHEET    1   M 7 PHE K 146  VAL K 149  0                                        
SHEET    2   M 7 SER K  55  ASP K  60 -1  N  ILE K  57   O  ALA K 148           
SHEET    3   M 7 THR K  65  LEU K  76 -1  O  TYR K  69   N  VAL K  56           
SHEET    4   M 7 VAL K  83  LEU K  91 -1  O  GLU K  84   N  ARG K  75           
SHEET    5   M 7 GLU K 131  ILE K 141 -1  O  TYR K 133   N  LEU K  91           
SHEET    6   M 7 ASP K 170  ALA K 176  1  O  LEU K 172   N  LEU K 132           
SHEET    7   M 7 VAL K 185  PRO K 186 -1  O  VAL K 185   N  ALA K 176           
SHEET    1   N 4 VAL L  22  ILE L  23  0                                        
SHEET    2   N 4 TRP L  11  THR L  16 -1  N  ILE L  15   O  ILE L  23           
SHEET    3   N 4 ASN L  38  ARG L  43 -1  O  LYS L  42   N  GLN L  12           
SHEET    4   N 4 SER L  49  PHE L  50 -1  O  PHE L  50   N  LEU L  41           
SHEET    1   O 7 PHE L 146  VAL L 149  0                                        
SHEET    2   O 7 SER L  55  ASP L  60 -1  N  ILE L  57   O  ALA L 148           
SHEET    3   O 7 THR L  65  LEU L  76 -1  O  SER L  67   N  PHE L  58           
SHEET    4   O 7 VAL L  83  LEU L  91 -1  O  GLU L  84   N  ARG L  75           
SHEET    5   O 7 GLU L 131  ILE L 141 -1  O  TYR L 133   N  LEU L  91           
SHEET    6   O 7 ASP L 170  ALA L 176  1  O  LEU L 172   N  LEU L 132           
SHEET    7   O 7 GLN L 151  ILE L 152  1  N  GLN L 151   O  PHE L 171           
SHEET    1   P 7 PHE L 146  VAL L 149  0                                        
SHEET    2   P 7 SER L  55  ASP L  60 -1  N  ILE L  57   O  ALA L 148           
SHEET    3   P 7 THR L  65  LEU L  76 -1  O  SER L  67   N  PHE L  58           
SHEET    4   P 7 VAL L  83  LEU L  91 -1  O  GLU L  84   N  ARG L  75           
SHEET    5   P 7 GLU L 131  ILE L 141 -1  O  TYR L 133   N  LEU L  91           
SHEET    6   P 7 ASP L 170  ALA L 176  1  O  LEU L 172   N  LEU L 132           
SHEET    7   P 7 VAL L 185  PRO L 186 -1  O  VAL L 185   N  ALA L 176           
LINK         C   AYA K   2                 N   LYS K   3     1555   1555  1.33  
LINK         C   AYA L   2                 N   LYS L   3     1555   1555  1.33  
CRYST1  108.330  108.330  498.920  90.00  90.00 120.00 P 61         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009231  0.005330  0.000000        0.00000                         
SCALE2      0.000000  0.010659  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002004        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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