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Database: PDB
Entry: 4A0K
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Original site: 4A0K 
HEADER    LIGASE/DNA-BINDING PROTEIN/DNA          09-SEP-11   4A0K              
TITLE     STRUCTURE OF DDB1-DDB2-CUL4A-RBX1 BOUND TO A 12 BP ABASIC SITE        
TITLE    2 CONTAINING DNA-DUPLEX                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-4A;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 38-759;                                           
COMPND   5 SYNONYM: CULLIN HOMOLOG 4A, CUL-4A;                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: RESIDUES 12-108;                                           
COMPND  11 SYNONYM: RING FINGER PROTEIN 75, RING-BOX PROTEIN 1, RBX1;           
COMPND  12 EC: 6.3.2.-;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: DDB P127 SUBUNIT, DNA DAMAGE-BINDING PROTEIN A, DDBA,       
COMPND  18 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, HBV X-ASSOCIATED PROTEIN 1,   
COMPND  19 XAP-1, UV-DAMAGED DNA-BINDING FACTOR, UV-DAMAGED DNA-BINDING PROTEIN 
COMPND  20 1, UV-DDB 1, XPE-BINDING FACTOR, XPE-BF, XERODERMA PIGMENTOSUM GROUP 
COMPND  21 E-COMPLEMENTING PROTEIN, XPCE;                                       
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 4;                                                           
COMPND  24 MOLECULE: DNA DAMAGE-BINDING PROTEIN 2;                              
COMPND  25 CHAIN: D;                                                            
COMPND  26 FRAGMENT: RESIDUES 60-423;                                           
COMPND  27 SYNONYM: DAMAGE-SPECIFIC DNA-BINDING PROTEIN 2;                      
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 OTHER_DETAILS: VARIANT WITH GLN AT POSITION 180 AND ARG AT POSITION  
COMPND  30 214 (SIMILAR TO PDB ENTRY 3EI2);                                     
COMPND  31 MOL_ID: 5;                                                           
COMPND  32 MOLECULE: 12 BP THF CONTAINING DNA;                                  
COMPND  33 CHAIN: E;                                                            
COMPND  34 ENGINEERED: YES;                                                     
COMPND  35 MOL_ID: 6;                                                           
COMPND  36 MOLECULE: 12 BP DNA;                                                 
COMPND  37 CHAIN: F;                                                            
COMPND  38 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   5 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  25 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: DANIO RERIO;                                    
SOURCE  30 ORGANISM_COMMON: ZEBRAFISH;                                          
SOURCE  31 ORGANISM_TAXID: 7955;                                                
SOURCE  32 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  34 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  37 MOL_ID: 5;                                                           
SOURCE  38 SYNTHETIC: YES;                                                      
SOURCE  39 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  40 ORGANISM_TAXID: 32630;                                               
SOURCE  41 MOL_ID: 6;                                                           
SOURCE  42 SYNTHETIC: YES;                                                      
SOURCE  43 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  44 ORGANISM_TAXID: 32630                                                
KEYWDS    LIGASE-DNA-BINDING PROTEIN-DNA COMPLEX, DNA-BINDING PROTEIN-DNA       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.FISCHER,A.SCRIMA,H.GUT,N.H.THOMA                                  
REVDAT   2   03-APR-19 4A0K    1       SOURCE LINK                              
REVDAT   1   14-DEC-11 4A0K    0                                                
JRNL        AUTH   E.S.FISCHER,A.SCRIMA,K.BOHM,S.MATSUMOTO,G.M.LINGARAJU,       
JRNL        AUTH 2 M.FATY,T.YASUDA,S.CAVADINI,M.WAKASUGI,F.HANAOKA,S.IWAI,      
JRNL        AUTH 3 H.GUT,K.SUGASAWA,N.H.THOMA                                   
JRNL        TITL   THE MOLECULAR BASIS OF CRL4(DDB2/CSA) UBIQUITIN LIGASE       
JRNL        TITL 2 ARCHITECTURE, TARGETING, AND ACTIVATION.                     
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 147  1024 2011              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   22118460                                                     
JRNL        DOI    10.1016/J.CELL.2011.10.035                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 5.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.050                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11036                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.269                           
REMARK   3   R VALUE            (WORKING SET) : 0.269                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 552                             
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 19.9768 -  9.1793    0.99     2668   140  0.2250 0.2239        
REMARK   3     2  9.1793 -  7.4073    0.99     2611   138  0.2871 0.3020        
REMARK   3     3  7.4073 -  6.5080    1.00     2599   137  0.3334 0.2887        
REMARK   3     4  6.5080 -  5.9300    1.00     2606   137  0.3465 0.3778        
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              : 0.31                                          
REMARK   3   B_SOL              : 236.7                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.910            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 299.0                          
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      :  0.009          18289                                  
REMARK   3   ANGLE     :  1.403          24837                                  
REMARK   3   CHIRALITY :  0.090           2810                                  
REMARK   3   PLANARITY :  0.007           3105                                  
REMARK   3   DIHEDRAL  : 18.193           6809                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A OR CHAIN B                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3407 -27.5625  88.1813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1879 T22:   3.4784                                     
REMARK   3      T33:   3.8378 T12:  -0.3417                                     
REMARK   3      T13:   0.0634 T23:  -0.2172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6306 L22:   1.0331                                     
REMARK   3      L33:   4.2149 L12:  -0.5980                                     
REMARK   3      L13:   1.0235 L23:  -1.2087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0371 S12:   0.1693 S13:  -0.4993                       
REMARK   3      S21:   0.0313 S22:   0.0860 S23:   0.1894                       
REMARK   3      S31:   0.3820 S32:  -0.1062 S33:   0.0133                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 394:706)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4022  21.2380  23.1633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.6317 T22:   4.5330                                     
REMARK   3      T33:   3.4783 T12:   0.0388                                     
REMARK   3      T13:   0.1428 T23:  -0.2808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1420 L22:   2.2302                                     
REMARK   3      L33:   2.9225 L12:   1.5832                                     
REMARK   3      L13:  -0.5243 L23:  -1.1908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1206 S12:  -0.2889 S13:   0.5376                       
REMARK   3      S21:   0.6165 S22:   0.0860 S23:   0.0294                       
REMARK   3      S31:  -1.5956 S32:   0.5233 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN D OR CHAIN E OR CHAIN F                          
REMARK   3    ORIGIN FOR THE GROUP (A): -60.8693  11.4057  95.7163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.6971 T22:   3.7015                                     
REMARK   3      T33:   3.6823 T12:  -0.1934                                     
REMARK   3      T13:  -0.0989 T23:  -0.2304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2939 L22:   1.5235                                     
REMARK   3      L33:   2.7289 L12:   0.3049                                     
REMARK   3      L13:  -0.3957 L23:   1.0302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5643 S12:  -1.3764 S13:  -0.3812                       
REMARK   3      S21:   1.0204 S22:   0.0946 S23:  -0.1617                       
REMARK   3      S31:   0.0295 S32:   0.5836 S33:  -0.0006                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 14:354)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -57.0682  30.7061  53.1332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.9880 T22:   3.5877                                     
REMARK   3      T33:   4.0109 T12:  -0.0368                                     
REMARK   3      T13:  -0.1714 T23:  -0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4472 L22:   2.7570                                     
REMARK   3      L33:   2.4310 L12:  -2.5183                                     
REMARK   3      L13:  -0.3039 L23:   0.3470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5602 S12:   0.8819 S13:   0.4902                       
REMARK   3      S21:  -0.5866 S22:   0.0477 S23:   0.1515                       
REMARK   3      S31:  -0.7780 S32:  -0.9763 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:13 OR RESSEQ 355:393 OR RESSEQ   
REMARK   3               707:1043)                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7486   0.9137  58.1470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.6458 T22:   3.5411                                     
REMARK   3      T33:   3.9367 T12:   0.0606                                     
REMARK   3      T13:   0.2045 T23:  -0.4741                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5433 L22:   4.8935                                     
REMARK   3      L33:   3.7347 L12:   1.6867                                     
REMARK   3      L13:  -0.7926 L23:   0.0841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2349 S12:  -0.2978 S13:  -0.8729                       
REMARK   3      S21:  -0.5714 S22:   0.1730 S23:  -0.4015                       
REMARK   3      S31:   0.7937 S32:   0.8889 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1044:1140)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -22.4402  31.8814  61.8636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.5501 T22:   3.7396                                     
REMARK   3      T33:   4.3267 T12:  -0.9168                                     
REMARK   3      T13:   0.2044 T23:  -0.3133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0437 L22:   0.3311                                     
REMARK   3      L33:   1.0509 L12:  -0.0774                                     
REMARK   3      L13:   0.9009 L23:   0.2261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0638 S12:  -1.0174 S13:   0.7716                       
REMARK   3      S21:  -0.0451 S22:  -0.6177 S23:  -0.2682                       
REMARK   3      S31:  -0.7477 S32:   0.8647 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE MOLECULAR REPLACEMENT SOLUTION HAS    
REMARK   3  BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE       
REMARK   3  COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED            
REMARK   3  RESOLUTION. RBX1 RESIDUES 40-108 HAVE BEEN REMOVED DUE TO           
REMARK   3  UNCERTAINTY OF CONFORMATIONS. STEREOCHEMISTRY IS BASED ON THE       
REMARK   3  SEARCH MODELS 3EI2 AND 2HYE.                                        
REMARK   4                                                                      
REMARK   4 4A0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049592.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11289                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.410                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MOLREP                                         
REMARK 200 STARTING MODEL: PDB ENTRIES 2HYE AND 3EI2                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 8.3, 33% PEG 200       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      105.32500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.01000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      105.32500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.01000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 124530 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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    18                                                      
REMARK 465     HIS A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     ASN A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     TYR A    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     MET B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     VAL B    -1                                                      
REMARK 465     ASP B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     TYR B     5                                                      
REMARK 465     PHE B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     ASN B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     ASP B    40                                                      
REMARK 465     ASN B    41                                                      
REMARK 465     CYS B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     ILE B    44                                                      
REMARK 465     CYS B    45                                                      
REMARK 465     ARG B    46                                                      
REMARK 465     ASN B    47                                                      
REMARK 465     HIS B    48                                                      
REMARK 465     ILE B    49                                                      
REMARK 465     MET B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     LEU B    52                                                      
REMARK 465     CYS B    53                                                      
REMARK 465     ILE B    54                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     CYS B    56                                                      
REMARK 465     GLN B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     ASN B    59                                                      
REMARK 465     GLN B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     ALA B    63                                                      
REMARK 465     THR B    64                                                      
REMARK 465     SER B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     CYS B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     TRP B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     VAL B    74                                                      
REMARK 465     CYS B    75                                                      
REMARK 465     ASN B    76                                                      
REMARK 465     HIS B    77                                                      
REMARK 465     ALA B    78                                                      
REMARK 465     PHE B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     PHE B    81                                                      
REMARK 465     HIS B    82                                                      
REMARK 465     CYS B    83                                                      
REMARK 465     ILE B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     TRP B    87                                                      
REMARK 465     LEU B    88                                                      
REMARK 465     LYS B    89                                                      
REMARK 465     THR B    90                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     GLN B    92                                                      
REMARK 465     VAL B    93                                                      
REMARK 465     CYS B    94                                                      
REMARK 465     PRO B    95                                                      
REMARK 465     LEU B    96                                                      
REMARK 465     ASP B    97                                                      
REMARK 465     ASN B    98                                                      
REMARK 465     ARG B    99                                                      
REMARK 465     GLU B   100                                                      
REMARK 465     TRP B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     PHE B   103                                                      
REMARK 465     GLN B   104                                                      
REMARK 465     LYS B   105                                                      
REMARK 465     TYR B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     HIS B   108                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     VAL C   -11                                                      
REMARK 465     ASP C   -10                                                      
REMARK 465     GLU C    -9                                                      
REMARK 465     ASN C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     TYR C    -6                                                      
REMARK 465     PHE C    -5                                                      
REMARK 465     GLN C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ARG C     0                                                      
REMARK 465     MET C   291                                                      
REMARK 465     ASP C   292                                                      
REMARK 465     GLY C   293                                                      
REMARK 465     THR C   294                                                      
REMARK 465     SER C   772                                                      
REMARK 465     SER C   773                                                      
REMARK 465     SER C   774                                                      
REMARK 465     THR C   775                                                      
REMARK 465     ALA C   776                                                      
REMARK 465     PRO C   777                                                      
REMARK 465     HIS C   778                                                      
REMARK 465     GLU C   779                                                      
REMARK 465     THR C   780                                                      
REMARK 465     SER C   781                                                      
REMARK 465     PHE C   782                                                      
REMARK 465     GLY C   783                                                      
REMARK 465     ASN C  1016                                                      
REMARK 465     LEU C  1017                                                      
REMARK 465     GLY C  1018                                                      
REMARK 465     GLU C  1019                                                      
REMARK 465     THR C  1020                                                      
REMARK 465     SER C  1021                                                      
REMARK 465     THR C  1022                                                      
REMARK 465     LEU C  1112                                                      
REMARK 465     GLN C  1113                                                      
REMARK 465     TYR C  1114                                                      
REMARK 465     ASP C  1115                                                      
REMARK 465     ASP C  1116                                                      
REMARK 465     GLY C  1117                                                      
REMARK 465     SER C  1118                                                      
REMARK 465     GLY C  1119                                                      
REMARK 465     MET C  1120                                                      
REMARK 465     LYS C  1121                                                      
REMARK 465     ARG C  1122                                                      
REMARK 465     GLU C  1123                                                      
REMARK 465     MET D    76                                                      
REMARK 465     HIS D    77                                                      
REMARK 465     HIS D    78                                                      
REMARK 465     HIS D    79                                                      
REMARK 465     HIS D    80                                                      
REMARK 465     HIS D    81                                                      
REMARK 465     HIS D    82                                                      
REMARK 465     ARG D    83                                                      
REMARK 465     ARG D    84                                                      
REMARK 465     LEU D    85                                                      
REMARK 465     VAL D    86                                                      
REMARK 465     PRO D    87                                                      
REMARK 465     ARG D    88                                                      
REMARK 465     GLY D    89                                                      
REMARK 465     SER D    90                                                      
REMARK 465     GLY D    91                                                      
REMARK 465     GLY D    92                                                      
REMARK 465     ARG D    93                                                      
REMARK 465     THR D    94                                                      
REMARK 465     GLY D    95                                                      
REMARK 465     GLY D    96                                                      
REMARK 465     GLN D    97                                                      
REMARK 465     LYS D    98                                                      
REMARK 465     LYS D    99                                                      
REMARK 465     VAL D   100                                                      
REMARK 465     ASP D   456                                                      
REMARK 465     THR D   457                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  54    CG   CD1  CD2                                       
REMARK 470     ARG A  71    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 151    OG                                                  
REMARK 470     PHE A 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 193    CG1  CG2  CD1                                       
REMARK 470     ILE A 200    CG1  CG2  CD1                                       
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 209    CG1  CG2                                            
REMARK 470     LEU A 224    CG   CD1  CD2                                       
REMARK 470     VAL A 226    CG1  CG2                                            
REMARK 470     ARG A 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 313    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 367    CG   OD1  OD2                                       
REMARK 470     LYS A 371    CG   CD   CE   NZ                                   
REMARK 470     ASN A 421    CG   OD1  ND2                                       
REMARK 470     GLU A 423    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 507    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 510    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 513    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 586    CG   CD   CE   NZ                                   
REMARK 470     LYS A 635    CG   CD   CE   NZ                                   
REMARK 470     VAL A 682    CG1  CG2                                            
REMARK 470     ASN A 713    CG   OD1  ND2                                       
REMARK 470     LEU A 714    CG   CD1  CD2                                       
REMARK 470     LYS A 749    CG   CD   CE   NZ                                   
REMARK 470     GLU C 117    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 147    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 392    CG   OD1  ND2                                       
REMARK 470     ARG C 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 670    CG   OD1  ND2                                       
REMARK 470     LYS C 709    CG   CD   CE   NZ                                   
REMARK 470     LEU C 710    CG   CD1  CD2                                       
REMARK 470     GLU C 842    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 909    CG1  CG2  CD1                                       
REMARK 470     ARG C 928    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET C1014    CG   SD   CE                                        
REMARK 470     TYR D 108    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE D 118    CG1  CG2  CD1                                       
REMARK 470     LEU D 122    CG   CD1  CD2                                       
REMARK 470     GLU D 128    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 132    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 168    CG   CD   CE   NZ                                   
REMARK 470     ASP D 237    CG   OD1  OD2                                       
REMARK 470     ASN D 315    CG   OD1  ND2                                       
REMARK 470     ARG D 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG C   103     NZ   LYS C   769     1565     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR C  13   C     ALA C  14   N       0.152                       
REMARK 500    THR C 354   C     ASN C 355   N      -0.271                       
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    PHE A  48   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    HIS A 181   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ILE A 182   N   -  CA  -  C   ANGL. DEV. =  25.2 DEGREES          
REMARK 500    HIS A 298   CB  -  CA  -  C   ANGL. DEV. = -21.5 DEGREES          
REMARK 500    PRO C 412   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    SER C 624   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    PRO C 656   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO C 688   CA  -  N   -  CD  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    PRO C 688   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ASP C 689   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500     DC E  11   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG F   2   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG F   2   O4' -  C1' -  N9  ANGL. DEV. =   4.1 DEGREES          
REMARK 500     DC F   3   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT F   5   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DA F  10   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG F  11   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC F  12   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  52       41.73    -77.46                                   
REMARK 500    PRO A  55     -143.06    -70.54                                   
REMARK 500    ASP A  56      114.36    162.49                                   
REMARK 500    ASN A  57      -26.82   -156.78                                   
REMARK 500    TYR A  58       46.91    -59.29                                   
REMARK 500    THR A  59      -78.54   -143.24                                   
REMARK 500    ARG A  71      -18.69    -44.16                                   
REMARK 500    SER A  75       50.55     26.31                                   
REMARK 500    SER A  76       47.95     10.17                                   
REMARK 500    ASN A  82       87.05     48.69                                   
REMARK 500    LEU A  83     -105.32     -4.58                                   
REMARK 500    GLU A  84      -86.73      8.83                                   
REMARK 500    GLU A  91      -32.00    -36.67                                   
REMARK 500    HIS A  96      133.44    -20.53                                   
REMARK 500    LYS A  97      -33.59     97.53                                   
REMARK 500    GLU A 111      -36.95    -39.61                                   
REMARK 500    LEU A 119      -64.18    -10.75                                   
REMARK 500    ARG A 122       35.08    -78.60                                   
REMARK 500    GLU A 123     -143.79    -96.23                                   
REMARK 500    SER A 125       70.06   -119.82                                   
REMARK 500    ASP A 127       98.68    167.69                                   
REMARK 500    SER A 128        7.60    -69.29                                   
REMARK 500    VAL A 129      -77.05    -98.49                                   
REMARK 500    PHE A 131      -39.01    -37.40                                   
REMARK 500    CYS A 143      -70.32    -67.02                                   
REMARK 500    THR A 159      -74.37   -137.52                                   
REMARK 500    GLN A 163       53.42    -94.62                                   
REMARK 500    ASN A 164      106.91   -173.37                                   
REMARK 500    HIS A 181      -75.89    -71.30                                   
REMARK 500    ASP A 185       42.84     24.87                                   
REMARK 500    GLN A 189      -76.65    -54.52                                   
REMARK 500    LYS A 191      -18.64   -179.93                                   
REMARK 500    GLU A 201      -32.35    -36.77                                   
REMARK 500    ARG A 204       22.76    -62.69                                   
REMARK 500    SER A 205       26.37   -160.62                                   
REMARK 500    GLU A 207       96.79     30.34                                   
REMARK 500    ALA A 208     -111.71    -50.87                                   
REMARK 500    VAL A 209        3.91    140.57                                   
REMARK 500    ASP A 210       93.22     64.92                                   
REMARK 500    ASP A 223      -27.20    -38.72                                   
REMARK 500    TYR A 227      -73.70    -66.44                                   
REMARK 500    LYS A 228       49.70    -65.93                                   
REMARK 500    ASP A 229      -32.59   -174.16                                   
REMARK 500    PHE A 231      -36.35   -145.08                                   
REMARK 500    LEU A 233      -74.15    -45.54                                   
REMARK 500    ASN A 240       21.49    -61.97                                   
REMARK 500    CYS A 241      -59.97   -128.63                                   
REMARK 500    GLN A 248      -70.23    -49.80                                   
REMARK 500    GLU A 255     -167.04    -68.36                                   
REMARK 500    THR A 276     -112.87    -68.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     215 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2B5M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF DDB1                                            
REMARK 900 RELATED ID: 2B5L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF DDB1 IN COMPLEX WITH SIMIAN VIRUS 5 VPROTEIN    
REMARK 900 RELATED ID: 4A11   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HSDDB1-HSCSA COMPLEX                                
REMARK 900 RELATED ID: 2HYE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DDB1-CUL4A-RBX1-SV5V COMPLEX                
REMARK 900 RELATED ID: 2B5N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DDB1 BPB DOMAIN                             
REMARK 900 RELATED ID: 4A0L   RELATED DB: PDB                                   
REMARK 900 N.A. (WILL BE GIVEN UPON ACCEPTANCE OF THE PUBLICATION AND FINAL     
REMARK 900 PUBLICATION TITLE)                                                   
REMARK 900 RELATED ID: 4A0A   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 16 BP CPD- DUPLEX (PYRIMIDINE  
REMARK 900 AT D-1 POSITION) AT 3.6 A RESOLUTION (CPD 3)                         
REMARK 900 RELATED ID: 4A0B   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 16 BP CPD- DUPLEX (PYRIMIDINE  
REMARK 900 AT D-1 POSITION) AT 3.8 A RESOLUTION (CPD 4)                         
REMARK 900 RELATED ID: 4A08   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 13 BP CPD- DUPLEX (PURINE AT   
REMARK 900 D-1 POSITION) AT 3.0 A RESOLUTION (CPD 1)                            
REMARK 900 RELATED ID: 4A09   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 15 BP CPD- DUPLEX (PURINE AT   
REMARK 900 D-1 POSITION) AT 3.1 A RESOLUTION (CPD 2)                            
REMARK 900 RELATED ID: 4A0C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX                            
DBREF  4A0K A   38   759  UNP    Q13619   CUL4A_HUMAN     38    759             
DBREF  4A0K B   12   108  UNP    P62878   RBX1_MOUSE      12    108             
DBREF  4A0K C    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  4A0K D   94   457  UNP    Q2YDS1   DDB2_DANRE      60    423             
DBREF  4A0K E    1    12  PDB    4A0K     4A0K             1     12             
DBREF  4A0K F    1    12  PDB    4A0K     4A0K             1     12             
SEQADV 4A0K MET A   18  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   19  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   20  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   21  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   22  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   23  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K HIS A   24  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K VAL A   25  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K ASP A   26  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLU A   27  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLU A   28  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K ASN A   29  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K LEU A   30  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K TYR A   31  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K PHE A   32  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLN A   33  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLY A   34  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLY A   35  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K GLY A   36  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K ARG A   37  UNP  Q13619              EXPRESSION TAG                 
SEQADV 4A0K MET B   -8  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -7  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -6  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -5  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -4  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -3  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K HIS B   -2  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K VAL B   -1  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K ASP B    0  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLU B    1  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLU B    2  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K ASN B    3  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K LEU B    4  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K TYR B    5  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K PHE B    6  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLN B    7  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLY B    8  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLY B    9  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K GLY B   10  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K ARG B   11  UNP  P62877              EXPRESSION TAG                 
SEQADV 4A0K MET C  -18  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -17  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -16  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -15  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -14  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -13  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K HIS C  -12  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K VAL C  -11  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K ASP C  -10  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K GLU C   -9  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K ASN C   -8  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K LEU C   -7  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K TYR C   -6  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K PHE C   -5  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K GLN C   -4  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K GLY C   -3  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K GLY C   -2  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K GLY C   -1  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K ARG C    0  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0K MET D   76  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   77  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   78  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   79  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   80  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   81  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K HIS D   82  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K ARG D   83  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K ARG D   84  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K LEU D   85  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K VAL D   86  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K PRO D   87  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K ARG D   88  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K GLY D   89  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K SER D   90  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K GLY D   91  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K GLY D   92  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K ARG D   93  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0K GLN D  180  UNP  Q2YDS1    LEU   146 VARIANT                        
SEQADV 4A0K ARG D  214  UNP  Q2YDS1    TRP   180 VARIANT                        
SEQRES   1 A  742  MET HIS HIS HIS HIS HIS HIS VAL ASP GLU GLU ASN LEU          
SEQRES   2 A  742  TYR PHE GLN GLY GLY GLY ARG GLY GLY SER LYS LYS LEU          
SEQRES   3 A  742  VAL ILE LYS ASN PHE ARG ASP ARG PRO ARG LEU PRO ASP          
SEQRES   4 A  742  ASN TYR THR GLN ASP THR TRP ARG LYS LEU HIS GLU ALA          
SEQRES   5 A  742  VAL ARG ALA VAL GLN SER SER THR SER ILE ARG TYR ASN          
SEQRES   6 A  742  LEU GLU GLU LEU TYR GLN ALA VAL GLU ASN LEU CYS SER          
SEQRES   7 A  742  HIS LYS VAL SER PRO MET LEU TYR LYS GLN LEU ARG GLN          
SEQRES   8 A  742  ALA CYS GLU ASP HIS VAL GLN ALA GLN ILE LEU PRO PHE          
SEQRES   9 A  742  ARG GLU ASP SER LEU ASP SER VAL LEU PHE LEU LYS LYS          
SEQRES  10 A  742  ILE ASN THR CYS TRP GLN ASP HIS CYS ARG GLN MET ILE          
SEQRES  11 A  742  MET ILE ARG SER ILE PHE LEU PHE LEU ASP ARG THR TYR          
SEQRES  12 A  742  VAL LEU GLN ASN SER THR LEU PRO SER ILE TRP ASP MET          
SEQRES  13 A  742  GLY LEU GLU LEU PHE ARG THR HIS ILE ILE SER ASP LYS          
SEQRES  14 A  742  MET VAL GLN SER LYS THR ILE ASP GLY ILE LEU LEU LEU          
SEQRES  15 A  742  ILE GLU ARG GLU ARG SER GLY GLU ALA VAL ASP ARG SER          
SEQRES  16 A  742  LEU LEU ARG SER LEU LEU GLY MET LEU SER ASP LEU GLN          
SEQRES  17 A  742  VAL TYR LYS ASP SER PHE GLU LEU LYS PHE LEU GLU GLU          
SEQRES  18 A  742  THR ASN CYS LEU TYR ALA ALA GLU GLY GLN ARG LEU MET          
SEQRES  19 A  742  GLN GLU ARG GLU VAL PRO GLU TYR LEU ASN HIS VAL SER          
SEQRES  20 A  742  LYS ARG LEU GLU GLU GLU GLY ASP ARG VAL ILE THR TYR          
SEQRES  21 A  742  LEU ASP HIS SER THR GLN LYS PRO LEU ILE ALA CYS VAL          
SEQRES  22 A  742  GLU LYS GLN LEU LEU GLY GLU HIS LEU THR ALA ILE LEU          
SEQRES  23 A  742  GLN LYS GLY LEU ASP HIS LEU LEU ASP GLU ASN ARG VAL          
SEQRES  24 A  742  PRO ASP LEU ALA GLN MET TYR GLN LEU PHE SER ARG VAL          
SEQRES  25 A  742  ARG GLY GLY GLN GLN ALA LEU LEU GLN HIS TRP SER GLU          
SEQRES  26 A  742  TYR ILE LYS THR PHE GLY THR ALA ILE VAL ILE ASN PRO          
SEQRES  27 A  742  GLU LYS ASP LYS ASP MET VAL GLN ASP LEU LEU ASP PHE          
SEQRES  28 A  742  LYS ASP LYS VAL ASP HIS VAL ILE GLU VAL CYS PHE GLN          
SEQRES  29 A  742  LYS ASN GLU ARG PHE VAL ASN LEU MET LYS GLU SER PHE          
SEQRES  30 A  742  GLU THR PHE ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU          
SEQRES  31 A  742  LEU ILE ALA LYS HIS VAL ASP SER LYS LEU ARG ALA GLY          
SEQRES  32 A  742  ASN LYS GLU ALA THR ASP GLU GLU LEU GLU ARG THR LEU          
SEQRES  33 A  742  ASP LYS ILE MET ILE LEU PHE ARG PHE ILE HIS GLY LYS          
SEQRES  34 A  742  ASP VAL PHE GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS          
SEQRES  35 A  742  ARG LEU LEU VAL GLY LYS SER ALA SER VAL ASP ALA GLU          
SEQRES  36 A  742  LYS SER MET LEU SER LYS LEU LYS HIS GLU CYS GLY ALA          
SEQRES  37 A  742  ALA PHE THR SER LYS LEU GLU GLY MET PHE LYS ASP MET          
SEQRES  38 A  742  GLU LEU SER LYS ASP ILE MET VAL HIS PHE LYS GLN HIS          
SEQRES  39 A  742  MET GLN ASN GLN SER ASP SER GLY PRO ILE ASP LEU THR          
SEQRES  40 A  742  VAL ASN ILE LEU THR MET GLY TYR TRP PRO THR TYR THR          
SEQRES  41 A  742  PRO MET GLU VAL HIS LEU THR PRO GLU MET ILE LYS LEU          
SEQRES  42 A  742  GLN GLU VAL PHE LYS ALA PHE TYR LEU GLY LYS HIS SER          
SEQRES  43 A  742  GLY ARG LYS LEU GLN TRP GLN THR THR LEU GLY HIS ALA          
SEQRES  44 A  742  VAL LEU LYS ALA GLU PHE LYS GLU GLY LYS LYS GLU PHE          
SEQRES  45 A  742  GLN VAL SER LEU PHE GLN THR LEU VAL LEU LEU MET PHE          
SEQRES  46 A  742  ASN GLU GLY ASP GLY PHE SER PHE GLU GLU ILE LYS MET          
SEQRES  47 A  742  ALA THR GLY ILE GLU ASP SER GLU LEU ARG ARG THR LEU          
SEQRES  48 A  742  GLN SER LEU ALA CYS GLY LYS ALA ARG VAL LEU ILE LYS          
SEQRES  49 A  742  SER PRO LYS GLY LYS GLU VAL GLU ASP GLY ASP LYS PHE          
SEQRES  50 A  742  ILE PHE ASN GLY GLU PHE LYS HIS LYS LEU PHE ARG ILE          
SEQRES  51 A  742  LYS ILE ASN GLN ILE GLN MET LYS GLU THR VAL GLU GLU          
SEQRES  52 A  742  GLN VAL SER THR THR GLU ARG VAL PHE GLN ASP ARG GLN          
SEQRES  53 A  742  TYR GLN ILE ASP ALA ALA ILE VAL ARG ILE MET LYS MET          
SEQRES  54 A  742  ARG LYS THR LEU GLY HIS ASN LEU LEU VAL SER GLU LEU          
SEQRES  55 A  742  TYR ASN GLN LEU LYS PHE PRO VAL LYS PRO GLY ASP LEU          
SEQRES  56 A  742  LYS LYS ARG ILE GLU SER LEU ILE ASP ARG ASP TYR MET          
SEQRES  57 A  742  GLU ARG ASP LYS ASP ASN PRO ASN GLN TYR HIS TYR VAL          
SEQRES  58 A  742  ALA                                                          
SEQRES   1 B  117  MET HIS HIS HIS HIS HIS HIS VAL ASP GLU GLU ASN LEU          
SEQRES   2 B  117  TYR PHE GLN GLY GLY GLY ARG GLY THR ASN SER GLY ALA          
SEQRES   3 B  117  GLY LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN ALA VAL          
SEQRES   4 B  117  ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN CYS ALA          
SEQRES   5 B  117  ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE GLU CYS          
SEQRES   6 B  117  GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU CYS THR          
SEQRES   7 B  117  VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS PHE HIS          
SEQRES   8 B  117  CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL CYS PRO          
SEQRES   9 B  117  LEU ASP ASN ARG GLU TRP GLU PHE GLN LYS TYR GLY HIS          
SEQRES   1 C 1159  MET HIS HIS HIS HIS HIS HIS VAL ASP GLU ASN LEU TYR          
SEQRES   2 C 1159  PHE GLN GLY GLY GLY ARG MET SER TYR ASN TYR VAL VAL          
SEQRES   3 C 1159  THR ALA GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR          
SEQRES   4 C 1159  GLY HIS PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE          
SEQRES   5 C 1159  ALA LYS ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA          
SEQRES   6 C 1159  GLU GLY LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY          
SEQRES   7 C 1159  LYS ILE ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU          
SEQRES   8 C 1159  SER LYS ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN          
SEQRES   9 C 1159  ALA CYS ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE          
SEQRES  10 C 1159  ASP ILE ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG          
SEQRES  11 C 1159  ILE GLY ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE          
SEQRES  12 C 1159  ASP PRO GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP          
SEQRES  13 C 1159  GLY LEU PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS          
SEQRES  14 C 1159  GLU LEU LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS          
SEQRES  15 C 1159  VAL ILE ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO          
SEQRES  16 C 1159  THR ILE CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS          
SEQRES  17 C 1159  VAL LYS THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE          
SEQRES  18 C 1159  ASN LYS GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU          
SEQRES  19 C 1159  ALA SER MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY          
SEQRES  20 C 1159  ALA ILE ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN          
SEQRES  21 C 1159  GLY ASP LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS          
SEQRES  22 C 1159  GLN SER THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN          
SEQRES  23 C 1159  GLY SER ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU          
SEQRES  24 C 1159  PHE MET LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY          
SEQRES  25 C 1159  THR VAL THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY          
SEQRES  26 C 1159  GLU THR SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN          
SEQRES  27 C 1159  GLY VAL VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN          
SEQRES  28 C 1159  LEU VAL LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER          
SEQRES  29 C 1159  TYR VAL VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO          
SEQRES  30 C 1159  ILE VAL ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY          
SEQRES  31 C 1159  GLN GLY GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU          
SEQRES  32 C 1159  GLY SER LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS          
SEQRES  33 C 1159  GLU HIS ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU          
SEQRES  34 C 1159  TRP PRO LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP          
SEQRES  35 C 1159  THR LEU VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU          
SEQRES  36 C 1159  MET LEU ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET          
SEQRES  37 C 1159  GLY PHE VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN          
SEQRES  38 C 1159  VAL ALA HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER          
SEQRES  39 C 1159  VAL ARG LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER          
SEQRES  40 C 1159  GLU TRP LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA          
SEQRES  41 C 1159  SER CYS ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG          
SEQRES  42 C 1159  ALA LEU TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG          
SEQRES  43 C 1159  GLN ILE SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS          
SEQRES  44 C 1159  LEU ASP ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER          
SEQRES  45 C 1159  PRO LEU CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA          
SEQRES  46 C 1159  ARG ILE LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS          
SEQRES  47 C 1159  GLU MET LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU          
SEQRES  48 C 1159  MET THR THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA          
SEQRES  49 C 1159  LEU GLY ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE          
SEQRES  50 C 1159  GLU THR GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU          
SEQRES  51 C 1159  GLY THR GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU          
SEQRES  52 C 1159  SER THR THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR          
SEQRES  53 C 1159  VAL ILE TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN          
SEQRES  54 C 1159  VAL ASN LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN          
SEQRES  55 C 1159  SER ASP GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN          
SEQRES  56 C 1159  SER THR LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS          
SEQRES  57 C 1159  LEU HIS ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG          
SEQRES  58 C 1159  LYS ILE CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL          
SEQRES  59 C 1159  LEU SER SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY          
SEQRES  60 C 1159  THR THR ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU          
SEQRES  61 C 1159  SER SER SER VAL SER SER SER LYS LEU PHE SER SER SER          
SEQRES  62 C 1159  THR ALA PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU          
SEQRES  63 C 1159  VAL HIS ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU          
SEQRES  64 C 1159  VAL LEU HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA          
SEQRES  65 C 1159  LEU SER LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN          
SEQRES  66 C 1159  THR TYR PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU          
SEQRES  67 C 1159  GLU ALA GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN          
SEQRES  68 C 1159  TYR SER ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU          
SEQRES  69 C 1159  VAL LYS GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY          
SEQRES  70 C 1159  LYS LEU LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR          
SEQRES  71 C 1159  GLU TRP THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN          
SEQRES  72 C 1159  HIS TYR ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS          
SEQRES  73 C 1159  GLY ASP PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL          
SEQRES  74 C 1159  LEU LEU LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU          
SEQRES  75 C 1159  GLU ILE ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA          
SEQRES  76 C 1159  VAL GLU ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU          
SEQRES  77 C 1159  ASN ALA PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA          
SEQRES  78 C 1159  ALA THR THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL          
SEQRES  79 C 1159  GLY LEU PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS          
SEQRES  80 C 1159  HIS GLY SER LEU VAL MET GLN ASN LEU GLY GLU THR SER          
SEQRES  81 C 1159  THR PRO THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN          
SEQRES  82 C 1159  GLY MET ILE GLY LEU VAL THR SER LEU SER GLU SER TRP          
SEQRES  83 C 1159  TYR ASN LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS          
SEQRES  84 C 1159  VAL ILE LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP          
SEQRES  85 C 1159  ARG SER PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR          
SEQRES  86 C 1159  GLY PHE ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP          
SEQRES  87 C 1159  ILE SER ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU          
SEQRES  88 C 1159  GLN TYR ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR          
SEQRES  89 C 1159  ALA ASP ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG          
SEQRES  90 C 1159  ILE HIS                                                      
SEQRES   1 D  382  MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG          
SEQRES   2 D  382  GLY SER GLY GLY ARG THR GLY GLY GLN LYS LYS VAL GLY          
SEQRES   3 D  382  GLN THR SER ILE LEU HIS TYR ILE TYR LYS SER SER LEU          
SEQRES   4 D  382  GLY GLN SER ILE HIS ALA GLN LEU ARG GLN CYS LEU GLN          
SEQRES   5 D  382  GLU PRO PHE ILE ARG SER LEU LYS SER TYR LYS LEU HIS          
SEQRES   6 D  382  ARG THR ALA SER PRO PHE ASP ARG ARG VAL THR SER LEU          
SEQRES   7 D  382  GLU TRP HIS PRO THR HIS PRO THR THR VAL ALA VAL GLY          
SEQRES   8 D  382  SER LYS GLY GLY ASP ILE ILE LEU TRP ASP TYR ASP VAL          
SEQRES   9 D  382  GLN ASN LYS THR SER PHE ILE GLN GLY MET GLY PRO GLY          
SEQRES  10 D  382  ASP ALA ILE THR GLY MET LYS PHE ASN GLN PHE ASN THR          
SEQRES  11 D  382  ASN GLN LEU PHE VAL SER SER ILE ARG GLY ALA THR THR          
SEQRES  12 D  382  LEU ARG ASP PHE SER GLY SER VAL ILE GLN VAL PHE ALA          
SEQRES  13 D  382  LYS THR ASP SER TRP ASP TYR TRP TYR CYS CYS VAL ASP          
SEQRES  14 D  382  VAL SER VAL SER ARG GLN MET LEU ALA THR GLY ASP SER          
SEQRES  15 D  382  THR GLY ARG LEU LEU LEU LEU GLY LEU ASP GLY HIS GLU          
SEQRES  16 D  382  ILE PHE LYS GLU LYS LEU HIS LYS ALA LYS VAL THR HIS          
SEQRES  17 D  382  ALA GLU PHE ASN PRO ARG CYS ASP TRP LEU MET ALA THR          
SEQRES  18 D  382  SER SER VAL ASP ALA THR VAL LYS LEU TRP ASP LEU ARG          
SEQRES  19 D  382  ASN ILE LYS ASP LYS ASN SER TYR ILE ALA GLU MET PRO          
SEQRES  20 D  382  HIS GLU LYS PRO VAL ASN ALA ALA TYR PHE ASN PRO THR          
SEQRES  21 D  382  ASP SER THR LYS LEU LEU THR THR ASP GLN ARG ASN GLU          
SEQRES  22 D  382  ILE ARG VAL TYR SER SER TYR ASP TRP SER LYS PRO ASP          
SEQRES  23 D  382  GLN ILE ILE ILE HIS PRO HIS ARG GLN PHE GLN HIS LEU          
SEQRES  24 D  382  THR PRO ILE LYS ALA THR TRP HIS PRO MET TYR ASP LEU          
SEQRES  25 D  382  ILE VAL ALA GLY ARG TYR PRO ASP ASP GLN LEU LEU LEU          
SEQRES  26 D  382  ASN ASP LYS ARG THR ILE ASP ILE TYR ASP ALA ASN SER          
SEQRES  27 D  382  GLY GLY LEU VAL HIS GLN LEU ARG ASP PRO ASN ALA ALA          
SEQRES  28 D  382  GLY ILE ILE SER LEU ASN LYS PHE SER PRO THR GLY ASP          
SEQRES  29 D  382  VAL LEU ALA SER GLY MET GLY PHE ASN ILE LEU ILE TRP          
SEQRES  30 D  382  ASN ARG GLU ASP THR                                          
SEQRES   1 E   12   DG  DC  DT  DA  DC  DT 3DR  DA  DC  DG  DC  DA              
SEQRES   1 F   12   DT  DG  DC  DG  DT  DA  DA  DG  DT  DA  DG  DC              
HET    3DR  E   7      11                                                       
HETNAM     3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE                           
HETSYN     3DR ABASIC DIDEOXYRIBOSE                                             
FORMUL   5  3DR    C5 H11 O6 P                                                  
HELIX    1   1 ASP A   61  ALA A   72  1                                  12    
HELIX    2   2 ASN A   82  CYS A   94  1                                  13    
HELIX    3   3 VAL A   98  ARG A  122  1                                  25    
HELIX    4   4 VAL A  129  PHE A  153  1                                  25    
HELIX    5   5 PHE A  153  ARG A  158  1                                   6    
HELIX    6   6 SER A  169  HIS A  181  1                                  13    
HELIX    7   7 VAL A  188  LYS A  191  5                                   4    
HELIX    8   8 THR A  192  ARG A  202  1                                  11    
HELIX    9   9 ASP A  210  LEU A  224  1                                  15    
HELIX   10  10 PHE A  231  ARG A  254  1                                  24    
HELIX   11  11 GLU A  255  GLU A  270  1                                  16    
HELIX   12  12 GLU A  270  ILE A  275  1                                   6    
HELIX   13  13 THR A  282  LEU A  295  1                                  14    
HELIX   14  14 LEU A  299  LYS A  305  1                                   7    
HELIX   15  15 GLY A  306  ASP A  312  1                                   7    
HELIX   16  16 ARG A  315  VAL A  329  1                                  15    
HELIX   17  17 GLY A  331  ILE A  353  1                                  23    
HELIX   18  18 ASN A  354  ASP A  358  5                                   5    
HELIX   19  19 ASP A  360  VAL A  378  1                                  19    
HELIX   20  20 ASN A  383  ASN A  399  1                                  17    
HELIX   21  21 ASN A  403  ARG A  418  1                                  16    
HELIX   22  22 GLY A  420  ALA A  424  5                                   5    
HELIX   23  23 GLU A  428  ARG A  441  1                                  14    
HELIX   24  24 GLY A  445  VAL A  463  1                                  19    
HELIX   25  25 SER A  468  HIS A  481  1                                  14    
HELIX   26  26 THR A  488  ASN A  514  1                                  27    
HELIX   27  27 THR A  544  GLY A  560  1                                  17    
HELIX   28  28 GLN A  570  LEU A  573  5                                   4    
HELIX   29  29 LEU A  593  PHE A  602  1                                  10    
HELIX   30  30 PHE A  610  THR A  617  1                                   8    
HELIX   31  31 GLU A  620  SER A  630  1                                  11    
HELIX   32  32 ASN A  670  LYS A  675  5                                   6    
HELIX   33  33 THR A  677  GLN A  690  1                                  14    
HELIX   34  34 ASP A  691  ARG A  707  1                                  17    
HELIX   35  35 HIS A  712  LEU A  723  1                                  12    
HELIX   36  36 LYS A  728  ARG A  742  1                                  15    
HELIX   37  37 PRO C  250  GLN C  255  1                                   6    
HELIX   38  38 ALA C  381  GLU C  384  5                                   4    
HELIX   39  39 GLU C  728  SER C  730  5                                   3    
HELIX   40  40 THR C  985  GLN C  990  1                                   6    
HELIX   41  41 SER C 1044  ILE C 1062  1                                  19    
HELIX   42  42 GLU C 1069  ARG C 1074  1                                   6    
HELIX   43  43 GLY C 1091  SER C 1096  1                                   6    
HELIX   44  44 PHE C 1097  ILE C 1100  5                                   4    
HELIX   45  45 SER C 1101  ALA C 1110  1                                  10    
HELIX   46  46 THR C 1125  ARG C 1138  1                                  14    
HELIX   47  47 SER D  104  LEU D  114  1                                  11    
HELIX   48  48 ILE D  118  GLN D  124  1                                   7    
HELIX   49  49 GLN D  127  LYS D  135  1                                   9    
SHEET    1  AA 2 ASP A 522  THR A 529  0                                        
SHEET    2  AA 2 PHE B  22  TRP B  35  1  O  LYS B  25   N  ASP A 522           
SHEET    1  AB 2 ARG A 565  LYS A 566  0                                        
SHEET    2  AB 2 PHE B  22  TRP B  35  1  O  ALA B  34   N  LYS A 566           
SHEET    1  AC 5 ILE A 667  LYS A 668  0                                        
SHEET    2  AC 5 GLU A 588  SER A 592  1  O  GLU A 588   N  ILE A 667           
SHEET    3  AC 5 HIS A 575  ALA A 580 -1  O  ALA A 576   N  VAL A 591           
SHEET    4  AC 5 PHE B  22  TRP B  35 -1  O  GLU B  23   N  LYS A 579           
SHEET    5  AC 5 ARG A 565  LYS A 566  1  O  LYS A 566   N  ALA B  34           
SHEET    1  AD 5 ILE A 667  LYS A 668  0                                        
SHEET    2  AD 5 GLU A 588  SER A 592  1  O  GLU A 588   N  ILE A 667           
SHEET    3  AD 5 HIS A 575  ALA A 580 -1  O  ALA A 576   N  VAL A 591           
SHEET    4  AD 5 PHE B  22  TRP B  35 -1  O  GLU B  23   N  LYS A 579           
SHEET    5  AD 5 ASP A 522  THR A 529  1  O  ASP A 522   N  TRP B  27           
SHEET    1  AE 3 PHE A 608  SER A 609  0                                        
SHEET    2  AE 3 LYS A 653  PHE A 656 -1  O  PHE A 654   N  PHE A 608           
SHEET    3  AE 3 LEU A 639  LYS A 641 -1  O  ILE A 640   N  ILE A 655           
SHEET    1  CA 5 VAL C1004  HIS C1009  0                                        
SHEET    2  CA 5 GLN C1025  THR C1032 -1  O  LEU C1029   N  CYS C1008           
SHEET    3  CA 5 ILE C1037  SER C1042 -1  O  GLY C1038   N  PHE C1030           
SHEET    4  CA 5 ASN C   4  GLN C  10 -1  O  TYR C   5   N  THR C1041           
SHEET    5  CA 5 PHE C1088  ASP C1090  1  O  ILE C1089   N  VAL C   6           
SHEET    1  CB 4 GLY C  17  GLY C  21  0                                        
SHEET    2  CB 4 ASN C  30  LYS C  35 -1  O  ASN C  30   N  GLY C  21           
SHEET    3  CB 4 ARG C  38  THR C  45 -1  O  ARG C  38   N  LYS C  35           
SHEET    4  CB 4 GLY C  48  GLY C  56 -1  O  GLY C  48   N  THR C  45           
SHEET    1  CC 4 ILE C  61  PHE C  67  0                                        
SHEET    2  CC 4 LEU C  76  THR C  81 -1  O  LEU C  76   N  PHE C  67           
SHEET    3  CC 4 ASN C  85  SER C  94 -1  O  ASN C  85   N  THR C  81           
SHEET    4  CC 4 SER C  97  ASN C 107 -1  O  SER C  97   N  SER C  94           
SHEET    1  CD 4 ILE C 121  ILE C 124  0                                        
SHEET    2  CD 4 MET C 130  ARG C 134 -1  O  GLY C 132   N  ILE C 123           
SHEET    3  CD 4 LEU C 139  PRO C 144 -1  O  LYS C 141   N  LEU C 133           
SHEET    4  CD 4 PHE C 155  ARG C 158 -1  O  PHE C 155   N  VAL C 142           
SHEET    1  CE 4 HIS C 163  PHE C 169  0                                        
SHEET    2  CE 4 THR C 177  ASP C 184 -1  O  CYS C 179   N  LYS C 168           
SHEET    3  CE 4 GLY C 187  SER C 196 -1  O  GLY C 187   N  ASP C 184           
SHEET    4  CE 4 GLU C 201  LYS C 204  1  O  GLU C 201   N  SER C 196           
SHEET    1  CF 4 HIS C 163  PHE C 169  0                                        
SHEET    2  CF 4 THR C 177  ASP C 184 -1  O  CYS C 179   N  LYS C 168           
SHEET    3  CF 4 GLY C 187  SER C 196 -1  O  GLY C 187   N  ASP C 184           
SHEET    4  CF 4 GLU C 210  ASN C 211 -1  O  GLU C 210   N  VAL C 190           
SHEET    1  CG 2 GLU C 201  LYS C 204  0                                        
SHEET    2  CG 2 GLY C 187  SER C 196  1  O  GLU C 194   N  ASN C 203           
SHEET    1  CH 4 MET C 218  ALA C 221  0                                        
SHEET    2  CH 4 ALA C 229  ILE C 232 -1  O  ILE C 230   N  ILE C 220           
SHEET    3  CH 4 ILE C 237  ASN C 241 -1  O  THR C 238   N  ILE C 231           
SHEET    4  CH 4 LYS C 244  ILE C 248 -1  O  LYS C 244   N  ASN C 241           
SHEET    1  CI 4 ILE C 258  ARG C 263  0                                        
SHEET    2  CI 4 ARG C 270  ASP C 275 -1  O  LEU C 272   N  ASN C 262           
SHEET    3  CI 4 ARG C 279  GLU C 288 -1  O  ARG C 279   N  ASP C 275           
SHEET    4  CI 4 THR C 296  GLU C 307 -1  O  THR C 296   N  GLU C 288           
SHEET    1  CJ 4 CYS C 313  ASP C 318  0                                        
SHEET    2  CJ 4 VAL C 321  GLY C 325 -1  O  VAL C 321   N  LEU C 317           
SHEET    3  CJ 4 SER C 331  LEU C 336 -1  O  GLN C 332   N  VAL C 324           
SHEET    4  CJ 4 VAL C 347  PHE C 353 -1  O  VAL C 348   N  LYS C 335           
SHEET    1  CK 4 ILE C 359  VAL C 365  0                                        
SHEET    2  CK 4 GLN C 374  SER C 379 -1  O  GLN C 374   N  VAL C 365           
SHEET    3  CK 4 SER C 386  ARG C 391 -1  O  SER C 386   N  SER C 379           
SHEET    4  CK 4 ARG C 713  PRO C 716 -1  O  ARG C 713   N  ILE C 389           
SHEET    1  CL 4 ALA C 400  SER C 401  0                                        
SHEET    2  CL 4 LEU C 699  GLY C 702 -1  O  ILE C 701   N  ALA C 400           
SHEET    3  CL 4 SER C 690  ALA C 694 -1  O  LEU C 691   N  GLY C 702           
SHEET    4  CL 4 TYR C 678  LEU C 682 -1  O  TYR C 678   N  ALA C 694           
SHEET    1  CM 4 LEU C 410  LEU C 413  0                                        
SHEET    2  CM 4 THR C 424  LEU C 427 -1  O  THR C 424   N  LEU C 413           
SHEET    3  CM 4 VAL C 435  ASN C 439 -1  O  LEU C 436   N  LEU C 425           
SHEET    4  CM 4 GLU C 442  GLU C 445 -1  O  GLU C 442   N  ASN C 439           
SHEET    1  CN 4 THR C 457  VAL C 463  0                                        
SHEET    2  CN 4 GLN C 467  THR C 472 -1  O  GLN C 467   N  VAL C 463           
SHEET    3  CN 4 VAL C 476  SER C 480 -1  O  ARG C 477   N  GLN C 470           
SHEET    4  CN 4 LEU C 486  SER C 488 -1  N  VAL C 487   O  LEU C 478           
SHEET    1  CO 4 VAL C 500  ALA C 501  0                                        
SHEET    2  CO 4 GLN C 507  VAL C 512 -1  N  ALA C 511   O  VAL C 500           
SHEET    3  CO 4 ALA C 515  HIS C 522 -1  O  ALA C 515   N  VAL C 512           
SHEET    4  CO 4 GLU C 525  GLU C 533 -1  O  GLU C 525   N  HIS C 522           
SHEET    1  CP 4 VAL C 538  ASP C 542  0                                        
SHEET    2  CP 4 LEU C 555  LEU C 560 -1  O  ALA C 557   N  ASP C 542           
SHEET    3  CP 4 ILE C 568  LYS C 570 -1  O  LEU C 569   N  CYS C 556           
SHEET    4  CP 4 GLU C 575  HIS C 578 -1  O  GLU C 575   N  LYS C 570           
SHEET    1  CQ 2 PRO C 588  SER C 590  0                                        
SHEET    2  CQ 2 ALA C 605  LEU C 606 -1  O  ALA C 605   N  ARG C 589           
SHEET    1  CR 4 MET C 593  THR C 595  0                                        
SHEET    2  CR 4 HIS C 600  LEU C 603 -1  O  TYR C 601   N  THR C 594           
SHEET    3  CR 4 ALA C 610  PHE C 614 -1  O  PHE C 614   N  LEU C 602           
SHEET    4  CR 4 LYS C 627  THR C 630 -1  O  LYS C 627   N  TYR C 613           
SHEET    1  CS 2 PHE C 641  ARG C 642  0                                        
SHEET    2  CS 2 THR C 647  ASN C 648 -1  O  ASN C 648   N  PHE C 641           
SHEET    1  CT 2 TYR C 660  SER C 661  0                                        
SHEET    2  CT 2 LEU C 666  VAL C 667 -1  O  VAL C 667   N  TYR C 660           
SHEET    1  CU 2 SER C 720  GLN C 727  0                                        
SHEET    2  CU 2 CYS C 732  GLN C 743 -1  O  CYS C 732   N  GLN C 727           
SHEET    1  CV 2 THR C 749  ALA C 751  0                                        
SHEET    2  CV 2 CYS C 732  GLN C 743  1  O  VAL C 742   N  THR C 750           
SHEET    1  CW 5 SER C 762  VAL C 765  0                                        
SHEET    2  CW 5 VAL C 801  GLN C 806  1  O  LEU C 802   N  SER C 762           
SHEET    3  CW 5 GLU C 785  ASP C 795 -1  O  LEU C 791   N  HIS C 805           
SHEET    4  CW 5 CYS C 732  GLN C 743 -1  O  PHE C 733   N  ILE C 794           
SHEET    5  CW 5 THR C 749  ALA C 751  1  O  THR C 750   N  VAL C 742           
SHEET    1  CX 5 SER C 762  VAL C 765  0                                        
SHEET    2  CX 5 VAL C 801  GLN C 806  1  O  LEU C 802   N  SER C 762           
SHEET    3  CX 5 GLU C 785  ASP C 795 -1  O  LEU C 791   N  HIS C 805           
SHEET    4  CX 5 CYS C 732  GLN C 743 -1  O  PHE C 733   N  ILE C 794           
SHEET    5  CX 5 SER C 720  GLN C 727 -1  O  SER C 720   N  SER C 738           
SHEET    1  CY 4 GLU C 811  CYS C 819  0                                        
SHEET    2  CY 4 TYR C 828  MET C 835 -1  O  TYR C 828   N  CYS C 819           
SHEET    3  CY 4 GLY C 846  TYR C 853 -1  O  ARG C 847   N  THR C 833           
SHEET    4  CY 4 LEU C 858  VAL C 866 -1  O  GLN C 859   N  GLN C 852           
SHEET    1  CZ 4 VAL C 870  PHE C 876  0                                        
SHEET    2  CZ 4 LYS C 879  ILE C 884 -1  O  LYS C 879   N  PHE C 876           
SHEET    3  CZ 4 THR C 887  TRP C 893 -1  O  THR C 887   N  ILE C 884           
SHEET    4  CZ 4 LEU C 899  HIS C 905 -1  O  ARG C 900   N  GLU C 892           
SHEET    1  C0 4 ALA C 911  LYS C 917  0                                        
SHEET    2  C0 4 PHE C 920  ASP C 925 -1  O  PHE C 920   N  LYS C 917           
SHEET    3  C0 4 VAL C 930  LYS C 936 -1  O  LEU C 931   N  VAL C 923           
SHEET    4  C0 4 ASN C 941  ARG C 947 -1  O  ASN C 941   N  LYS C 936           
SHEET    1  C1 4 MET C 954  ILE C 959  0                                        
SHEET    2  C1 4 ASN C 964  GLU C 969 -1  O  LEU C 966   N  GLU C 958           
SHEET    3  C1 4 ASN C 973  LYS C 979 -1  O  ASN C 973   N  GLU C 969           
SHEET    4  C1 4 LEU C 992  HIS C 999 -1  O  GLN C 993   N  GLN C 978           
SHEET    1  C2 2 PHE C1076  HIS C1077  0                                        
SHEET    2  C2 2 THR C1082  GLU C1083 -1  O  GLU C1083   N  PHE C1076           
SHEET    1  DA 4 LYS D 138  ALA D 143  0                                        
SHEET    2  DA 4 ASN D 448  ASN D 453 -1  O  ILE D 449   N  ALA D 143           
SHEET    3  DA 4 LEU D 441  MET D 445 -1  O  LEU D 441   N  TRP D 452           
SHEET    4  DA 4 ILE D 429  PHE D 434 -1  N  SER D 430   O  GLY D 444           
SHEET    1  DB 4 VAL D 150  TRP D 155  0                                        
SHEET    2  DB 4 THR D 162  SER D 167 -1  O  ALA D 164   N  GLU D 154           
SHEET    3  DB 4 ILE D 172  ASP D 176 -1  O  ILE D 173   N  VAL D 165           
SHEET    4  DB 4 THR D 183  ILE D 186 -1  O  SER D 184   N  LEU D 174           
SHEET    1  DC 4 ILE D 195  PHE D 200  0                                        
SHEET    2  DC 4 GLN D 207  SER D 212 -1  O  PHE D 209   N  LYS D 199           
SHEET    3  DC 4 ALA D 216  ASP D 221 -1  O  ALA D 216   N  SER D 212           
SHEET    4  DC 4 VAL D 226  VAL D 229 -1  N  ILE D 227   O  LEU D 219           
SHEET    1  DD 4 TYR D 240  SER D 246  0                                        
SHEET    2  DD 4 MET D 251  ASP D 256 -1  O  MET D 251   N  SER D 246           
SHEET    3  DD 4 ARG D 260  GLY D 265 -1  O  ARG D 260   N  ASP D 256           
SHEET    4  DD 4 GLU D 270  LYS D 275 -1  N  ILE D 271   O  LEU D 263           
SHEET    1  DE 4 VAL D 281  ASN D 287  0                                        
SHEET    2  DE 4 CYS D 290  SER D 298 -1  N  CYS D 290   O  ASN D 287           
SHEET    3  DE 4 THR D 302  ASP D 307 -1  O  THR D 302   N  SER D 298           
SHEET    4  DE 4 ALA D 319  PRO D 322 -1  O  ALA D 319   N  LEU D 305           
SHEET    1  DF 4 VAL D 327  PHE D 332  0                                        
SHEET    2  DF 4 LYS D 339  ASP D 344 -1  O  LEU D 341   N  TYR D 331           
SHEET    3  DF 4 GLU D 348  SER D 353 -1  O  GLU D 348   N  ASP D 344           
SHEET    4  DF 4 GLN D 362  ILE D 365 -1  O  GLN D 362   N  VAL D 351           
SHEET    1  DG 4 THR D 380  TRP D 381  0                                        
SHEET    2  DG 4 LEU D 387  GLY D 391 -1  O  VAL D 389   N  THR D 380           
SHEET    3  DG 4 ILE D 406  ASP D 410 -1  O  ASP D 407   N  ALA D 390           
SHEET    4  DG 4 LEU D 416  LEU D 420 -1  N  VAL D 417   O  ILE D 408           
LINK         O3'  DT E   6                 P   3DR E   7     1555   1555  1.61  
LINK         O3' 3DR E   7                 P    DA E   8     1555   1555  1.61  
CISPEP   1 GLU C  224    PRO C  225          0        12.11                     
CISPEP   2 GLY C  357    PRO C  358          0        -5.23                     
CRYST1  210.650   78.020  276.620  90.00 108.50  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004747  0.000000  0.001588        0.00000                         
SCALE2      0.000000  0.012817  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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