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Database: PDB
Entry: 4A0L
LinkDB: 4A0L
Original site: 4A0L 
HEADER    LIGASE/DNA-BINDING PROTEIN/DNA          09-SEP-11   4A0L              
TITLE     STRUCTURE OF DDB1-DDB2-CUL4B-RBX1 BOUND TO A 12 BP ABASIC SITE        
TITLE    2 CONTAINING DNA-DUPLEX                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: DDB P127 SUBUNIT, DNA DAMAGE-BINDING PROTEIN A, DDBA,       
COMPND   5 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, HBV X-ASSOCIATED PROTEIN 1,   
COMPND   6 XAP-1, UV-DAMAGED DNA-BINDING FACTOR, UV-DAMAGED DNA-BINDING PROTEIN 
COMPND   7 1, UV-DDB 1, XPE-BINDING FACTOR, XPE-BF, XERODERMA PIGMENTOSUM GROUP 
COMPND   8 E-COMPLEMENTING PROTEIN, XPCE;                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: DNA DAMAGE-BINDING PROTEIN 2;                              
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: RESIDUES 60-423;                                           
COMPND  14 SYNONYM: DAMAGE-SPECIFIC DNA-BINDING PROTEIN 2;                      
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 OTHER_DETAILS: VARIANT WITH GLN AT POSITION 180 AND ARG AT POSITION  
COMPND  17 214 SIMILAR TO PDB ENTRY 3EI2;                                       
COMPND  18 MOL_ID: 3;                                                           
COMPND  19 MOLECULE: CULLIN-4B;                                                 
COMPND  20 CHAIN: E, H;                                                         
COMPND  21 FRAGMENT: RESIDUES 193-913;                                          
COMPND  22 SYNONYM: CULLIN HOMOLOG 4B, CUL-4B;                                  
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 4;                                                           
COMPND  25 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  26 CHAIN: F, I;                                                         
COMPND  27 FRAGMENT: RESIDUES 12-108;                                           
COMPND  28 SYNONYM: RING FINGER PROTEIN 75, RING-BOX PROTEIN 1, RBX1;           
COMPND  29 ENGINEERED: YES;                                                     
COMPND  30 MOL_ID: 5;                                                           
COMPND  31 MOLECULE: 12 BP THF CONTAINING DNA DUPLEX;                           
COMPND  32 CHAIN: R, T;                                                         
COMPND  33 ENGINEERED: YES;                                                     
COMPND  34 MOL_ID: 6;                                                           
COMPND  35 MOLECULE: 12 BP DNA DUPLEX;                                          
COMPND  36 CHAIN: S, U;                                                         
COMPND  37 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: DANIO RERIO;                                    
SOURCE  13 ORGANISM_COMMON: ZEBRAFISH;                                          
SOURCE  14 ORGANISM_TAXID: 7955;                                                
SOURCE  15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  26 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  28 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  33 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  34 ORGANISM_TAXID: 10090;                                               
SOURCE  35 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  36 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  38 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  39 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  40 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;                         
SOURCE  41 MOL_ID: 5;                                                           
SOURCE  42 SYNTHETIC: YES;                                                      
SOURCE  43 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  44 ORGANISM_TAXID: 32630;                                               
SOURCE  45 MOL_ID: 6;                                                           
SOURCE  46 SYNTHETIC: YES;                                                      
SOURCE  47 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  48 ORGANISM_TAXID: 32630                                                
KEYWDS    LIGASE-DNA-BINDING PROTEIN-DNA COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.FISCHER,A.SCRIMA,H.GUT,N.H.THOMA                                  
REVDAT   4   03-APR-19 4A0L    1       REMARK                                   
REVDAT   3   27-MAR-19 4A0L    1       SOURCE LINK                              
REVDAT   2   07-NOV-12 4A0L    1       DBREF                                    
REVDAT   1   14-DEC-11 4A0L    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.    7.40 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) : 7.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13523                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.318                           
REMARK   3   R VALUE            (WORKING SET) : 0.318                           
REMARK   3   FREE R VALUE                     : 0.320                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1352                            
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 29.8623 - 15.2754    0.99     1255   140  0.3705 0.3597        
REMARK   3     2 15.2754 - 12.4073    0.99     1234   137  0.2662 0.3022        
REMARK   3     3 12.4073 - 10.9265    0.99     1205   134  0.2557 0.2379        
REMARK   3     4 10.9265 -  9.9683    0.99     1219   136  0.2706 0.3009        
REMARK   3     5  9.9683 -  9.2768    0.99     1206   134  0.3106 0.2798        
REMARK   3     6  9.2768 -  8.7444    0.99     1205   134  0.3482 0.3367        
REMARK   3     7  8.7444 -  8.3164    0.99     1241   137  0.3615 0.3354        
REMARK   3     8  8.3164 -  7.9615    0.99     1198   132  0.3661 0.4203        
REMARK   3     9  7.9615 -  7.6603    0.99     1206   134  0.3938 0.3798        
REMARK   3    10  7.6603 -  7.4001    0.99     1202   134  0.3847 0.3925        
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              : 143.7                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 344.0                          
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      :  0.008          36315                                  
REMARK   3   ANGLE     :  1.233          49309                                  
REMARK   3   CHIRALITY :  0.083           5617                                  
REMARK   3   PLANARITY :  0.006           6162                                  
REMARK   3   DIHEDRAL  : 18.545          13521                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0148  -1.7414  27.6910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6432 T22:   2.3331                                     
REMARK   3      T33:   1.6466 T12:   0.0956                                     
REMARK   3      T13:   0.6729 T23:  -0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1609 L22:   4.0697                                     
REMARK   3      L33:   3.0624 L12:   2.7587                                     
REMARK   3      L13:   2.2158 L23:   0.8725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4051 S12:   0.1255 S13:  -0.3400                       
REMARK   3      S21:   0.6988 S22:   0.1412 S23:   0.0398                       
REMARK   3      S31:  -0.1921 S32:  -0.4892 S33:  -0.4197                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B OR CHAIN R OR CHAIN S                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2836   2.0881  78.0278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.5984 T22:   3.7371                                     
REMARK   3      T33:   3.1938 T12:  -0.8239                                     
REMARK   3      T13:  -0.7651 T23:   0.4963                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8964 L22:   0.6248                                     
REMARK   3      L33:   4.6669 L12:   1.0343                                     
REMARK   3      L13:  -0.4768 L23:   0.0095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8249 S12:  -1.3288 S13:  -0.7139                       
REMARK   3      S21:  -0.1346 S22:  -0.6149 S23:   0.9720                       
REMARK   3      S31:  -0.3922 S32:   0.0608 S33:   1.1021                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -40.7837  58.3090  22.5275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7110 T22:   2.5306                                     
REMARK   3      T33:   1.3205 T12:  -0.0695                                     
REMARK   3      T13:   0.8212 T23:   0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1667 L22:   3.6670                                     
REMARK   3      L33:   1.8266 L12:   1.0470                                     
REMARK   3      L13:   1.7369 L23:   0.9735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:   0.4382 S13:  -0.5733                       
REMARK   3      S21:   0.1055 S22:   0.0722 S23:   0.5298                       
REMARK   3      S31:  -0.1616 S32:  -0.3858 S33:  -0.0735                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D OR CHAIN T OR CHAIN U                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3555  62.8684  69.1982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3320 T22:   2.2801                                     
REMARK   3      T33:   1.9873 T12:  -0.5710                                     
REMARK   3      T13:   0.0855 T23:   0.4647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0569 L22:   5.7683                                     
REMARK   3      L33:   3.5564 L12:  -1.3109                                     
REMARK   3      L13:   1.4749 L23:   2.7493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1303 S12:  -1.1532 S13:  -0.6923                       
REMARK   3      S21:   0.7035 S22:   0.3116 S23:   0.5368                       
REMARK   3      S31:   1.9510 S32:  -1.1286 S33:  -1.2954                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E OR CHAIN F                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1137 -53.0881  75.5630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.7293 T22:   3.7199                                     
REMARK   3      T33:   2.1247 T12:   0.4348                                     
REMARK   3      T13:   0.2504 T23:  -0.4777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0915 L22:   1.4119                                     
REMARK   3      L33:  -0.0962 L12:   0.8887                                     
REMARK   3      L13:  -0.1422 L23:  -0.2719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8920 S12:  -1.5618 S13:   0.2388                       
REMARK   3      S21:   2.2109 S22:   0.5971 S23:  -0.4475                       
REMARK   3      S31:  -1.3757 S32:  -0.7753 S33:  -0.2562                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN H OR CHAIN I                                     
REMARK   3    ORIGIN FOR THE GROUP (A): -71.9759  31.4826  77.2020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.4176 T22:   3.2456                                     
REMARK   3      T33:   2.9480 T12:  -0.4538                                     
REMARK   3      T13:  -0.4172 T23:  -0.1055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8139 L22:   1.0881                                     
REMARK   3      L33:   0.1116 L12:   0.4156                                     
REMARK   3      L13:  -0.3379 L23:  -0.8166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1779 S12:  -0.9941 S13:   0.2729                       
REMARK   3      S21:   1.1918 S22:  -0.1075 S23:  -0.0393                       
REMARK   3      S31:  -0.4284 S32:  -0.2648 S33:  -0.1488                       
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 AND CUL4B RESIDUES 208-209 HAVE    
REMARK   3  BEEN REMOVED DUE TO UNCERTAINTY OF CONFORMATIONS.                   
REMARK   3  STEREOCHEMISTRY IS BASED ON THE SEARCH MODELS 3EI2 AND 4A0C.        
REMARK   4                                                                      
REMARK   4 4A0L 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_1290049591.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0015                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13547                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 7.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 7.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3EI2, 4A0C                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH 6.2, 3.1% PEG 6000, 4%      
REMARK 280  ETHYLENEGLYCOL                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       77.92000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 123470 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, R, S                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 121070 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, I, T, U                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     MET A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     SER A   772                                                      
REMARK 465     SER A   773                                                      
REMARK 465     SER A   774                                                      
REMARK 465     THR A   775                                                      
REMARK 465     ALA A   776                                                      
REMARK 465     PRO A   777                                                      
REMARK 465     HIS A   778                                                      
REMARK 465     GLU A   779                                                      
REMARK 465     THR A   780                                                      
REMARK 465     SER A   781                                                      
REMARK 465     PHE A   782                                                      
REMARK 465     GLY A   783                                                      
REMARK 465     ASN A  1016                                                      
REMARK 465     LEU A  1017                                                      
REMARK 465     GLY A  1018                                                      
REMARK 465     GLU A  1019                                                      
REMARK 465     THR A  1020                                                      
REMARK 465     SER A  1021                                                      
REMARK 465     THR A  1022                                                      
REMARK 465     LEU A  1112                                                      
REMARK 465     GLN A  1113                                                      
REMARK 465     TYR A  1114                                                      
REMARK 465     ASP A  1115                                                      
REMARK 465     ASP A  1116                                                      
REMARK 465     GLY A  1117                                                      
REMARK 465     SER A  1118                                                      
REMARK 465     GLY A  1119                                                      
REMARK 465     MET A  1120                                                      
REMARK 465     LYS A  1121                                                      
REMARK 465     ARG A  1122                                                      
REMARK 465     GLU A  1123                                                      
REMARK 465     MET B    76                                                      
REMARK 465     HIS B    77                                                      
REMARK 465     HIS B    78                                                      
REMARK 465     HIS B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     HIS B    81                                                      
REMARK 465     HIS B    82                                                      
REMARK 465     ARG B    83                                                      
REMARK 465     ARG B    84                                                      
REMARK 465     LEU B    85                                                      
REMARK 465     VAL B    86                                                      
REMARK 465     PRO B    87                                                      
REMARK 465     ARG B    88                                                      
REMARK 465     GLY B    89                                                      
REMARK 465     SER B    90                                                      
REMARK 465     GLY B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     ARG B    93                                                      
REMARK 465     THR B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     GLN B    97                                                      
REMARK 465     LYS B    98                                                      
REMARK 465     LYS B    99                                                      
REMARK 465     VAL B   100                                                      
REMARK 465     ASP B   456                                                      
REMARK 465     THR B   457                                                      
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 465     GLY E   189                                                      
REMARK 465     GLY E   190                                                      
REMARK 465     GLY E   191                                                      
REMARK 465     ARG E   192                                                      
REMARK 465     GLY E   193                                                      
REMARK 465     SER E   194                                                      
REMARK 465     ALA E   195                                                      
REMARK 465     LYS E   208                                                      
REMARK 465     LEU E   209                                                      
REMARK 465     PRO E   209A                                                     
REMARK 465     GLY E   574                                                      
REMARK 465     ASN E   575                                                      
REMARK 465     LYS E   576                                                      
REMARK 465     VAL E   671                                                      
REMARK 465     PRO E   672                                                      
REMARK 465     GLY E   673                                                      
REMARK 465     ASN E   674                                                      
REMARK 465     MET F    11                                                      
REMARK 465     GLY F    12                                                      
REMARK 465     THR F    13                                                      
REMARK 465     ASN F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     GLY F    16                                                      
REMARK 465     ALA F    17                                                      
REMARK 465     GLY F    18                                                      
REMARK 465     ASP F    40                                                      
REMARK 465     ASN F    41                                                      
REMARK 465     CYS F    42                                                      
REMARK 465     ALA F    43                                                      
REMARK 465     ILE F    44                                                      
REMARK 465     CYS F    45                                                      
REMARK 465     ARG F    46                                                      
REMARK 465     ASN F    47                                                      
REMARK 465     HIS F    48                                                      
REMARK 465     ILE F    49                                                      
REMARK 465     MET F    50                                                      
REMARK 465     ASP F    51                                                      
REMARK 465     LEU F    52                                                      
REMARK 465     CYS F    53                                                      
REMARK 465     ILE F    54                                                      
REMARK 465     GLU F    55                                                      
REMARK 465     CYS F    56                                                      
REMARK 465     GLN F    57                                                      
REMARK 465     ALA F    58                                                      
REMARK 465     ASN F    59                                                      
REMARK 465     GLN F    60                                                      
REMARK 465     ALA F    61                                                      
REMARK 465     SER F    62                                                      
REMARK 465     ALA F    63                                                      
REMARK 465     THR F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     GLU F    66                                                      
REMARK 465     GLU F    67                                                      
REMARK 465     CYS F    68                                                      
REMARK 465     THR F    69                                                      
REMARK 465     VAL F    70                                                      
REMARK 465     ALA F    71                                                      
REMARK 465     TRP F    72                                                      
REMARK 465     GLY F    73                                                      
REMARK 465     VAL F    74                                                      
REMARK 465     CYS F    75                                                      
REMARK 465     ASN F    76                                                      
REMARK 465     HIS F    77                                                      
REMARK 465     ALA F    78                                                      
REMARK 465     PHE F    79                                                      
REMARK 465     HIS F    80                                                      
REMARK 465     PHE F    81                                                      
REMARK 465     HIS F    82                                                      
REMARK 465     CYS F    83                                                      
REMARK 465     ILE F    84                                                      
REMARK 465     SER F    85                                                      
REMARK 465     ARG F    86                                                      
REMARK 465     TRP F    87                                                      
REMARK 465     LEU F    88                                                      
REMARK 465     LYS F    89                                                      
REMARK 465     THR F    90                                                      
REMARK 465     ARG F    91                                                      
REMARK 465     GLN F    92                                                      
REMARK 465     VAL F    93                                                      
REMARK 465     CYS F    94                                                      
REMARK 465     PRO F    95                                                      
REMARK 465     LEU F    96                                                      
REMARK 465     ASP F    97                                                      
REMARK 465     ASN F    98                                                      
REMARK 465     ARG F    99                                                      
REMARK 465     GLU F   100                                                      
REMARK 465     TRP F   101                                                      
REMARK 465     GLU F   102                                                      
REMARK 465     PHE F   103                                                      
REMARK 465     GLN F   104                                                      
REMARK 465     LYS F   105                                                      
REMARK 465     TYR F   106                                                      
REMARK 465     GLY F   107                                                      
REMARK 465     HIS F   108                                                      
REMARK 465     GLY H   189                                                      
REMARK 465     GLY H   190                                                      
REMARK 465     GLY H   191                                                      
REMARK 465     ARG H   192                                                      
REMARK 465     GLY H   193                                                      
REMARK 465     SER H   194                                                      
REMARK 465     ALA H   195                                                      
REMARK 465     LYS H   208                                                      
REMARK 465     LEU H   209                                                      
REMARK 465     PRO H   209A                                                     
REMARK 465     GLY H   574                                                      
REMARK 465     ASN H   575                                                      
REMARK 465     LYS H   576                                                      
REMARK 465     VAL H   671                                                      
REMARK 465     PRO H   672                                                      
REMARK 465     GLY H   673                                                      
REMARK 465     ASN H   674                                                      
REMARK 465     MET I    11                                                      
REMARK 465     GLY I    12                                                      
REMARK 465     THR I    13                                                      
REMARK 465     ASN I    14                                                      
REMARK 465     SER I    15                                                      
REMARK 465     GLY I    16                                                      
REMARK 465     ALA I    17                                                      
REMARK 465     GLY I    18                                                      
REMARK 465     ASP I    40                                                      
REMARK 465     ASN I    41                                                      
REMARK 465     CYS I    42                                                      
REMARK 465     ALA I    43                                                      
REMARK 465     ILE I    44                                                      
REMARK 465     CYS I    45                                                      
REMARK 465     ARG I    46                                                      
REMARK 465     ASN I    47                                                      
REMARK 465     HIS I    48                                                      
REMARK 465     ILE I    49                                                      
REMARK 465     MET I    50                                                      
REMARK 465     ASP I    51                                                      
REMARK 465     LEU I    52                                                      
REMARK 465     CYS I    53                                                      
REMARK 465     ILE I    54                                                      
REMARK 465     GLU I    55                                                      
REMARK 465     CYS I    56                                                      
REMARK 465     GLN I    57                                                      
REMARK 465     ALA I    58                                                      
REMARK 465     ASN I    59                                                      
REMARK 465     GLN I    60                                                      
REMARK 465     ALA I    61                                                      
REMARK 465     SER I    62                                                      
REMARK 465     ALA I    63                                                      
REMARK 465     THR I    64                                                      
REMARK 465     SER I    65                                                      
REMARK 465     GLU I    66                                                      
REMARK 465     GLU I    67                                                      
REMARK 465     CYS I    68                                                      
REMARK 465     THR I    69                                                      
REMARK 465     VAL I    70                                                      
REMARK 465     ALA I    71                                                      
REMARK 465     TRP I    72                                                      
REMARK 465     GLY I    73                                                      
REMARK 465     VAL I    74                                                      
REMARK 465     CYS I    75                                                      
REMARK 465     ASN I    76                                                      
REMARK 465     HIS I    77                                                      
REMARK 465     ALA I    78                                                      
REMARK 465     PHE I    79                                                      
REMARK 465     HIS I    80                                                      
REMARK 465     PHE I    81                                                      
REMARK 465     HIS I    82                                                      
REMARK 465     CYS I    83                                                      
REMARK 465     ILE I    84                                                      
REMARK 465     SER I    85                                                      
REMARK 465     ARG I    86                                                      
REMARK 465     TRP I    87                                                      
REMARK 465     LEU I    88                                                      
REMARK 465     LYS I    89                                                      
REMARK 465     THR I    90                                                      
REMARK 465     ARG I    91                                                      
REMARK 465     GLN I    92                                                      
REMARK 465     VAL I    93                                                      
REMARK 465     CYS I    94                                                      
REMARK 465     PRO I    95                                                      
REMARK 465     LEU I    96                                                      
REMARK 465     ASP I    97                                                      
REMARK 465     ASN I    98                                                      
REMARK 465     ARG I    99                                                      
REMARK 465     GLU I   100                                                      
REMARK 465     TRP I   101                                                      
REMARK 465     GLU I   102                                                      
REMARK 465     PHE I   103                                                      
REMARK 465     GLN I   104                                                      
REMARK 465     LYS I   105                                                      
REMARK 465     TYR I   106                                                      
REMARK 465     GLY I   107                                                      
REMARK 465     HIS I   108                                                      
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     ARG A 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     PHE A 323    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 388    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 389    CG1  CG2  CD1                                       
REMARK 470     ILE A 390    CG1  CG2  CD1                                       
REMARK 470     ARG A 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 392    CG   OD1  ND2                                       
REMARK 470     LYS A 408    CG   CD   CE   NZ                                   
REMARK 470     TRP A 561    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 561    CZ3  CH2                                            
REMARK 470     ARG A 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 663    CG   OD1  ND2                                       
REMARK 470     ASN A 670    CG   OD1  ND2                                       
REMARK 470     ASN A 672    CG   OD1  ND2                                       
REMARK 470     GLU A 706    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 708    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 722    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 769    CB   CG   CD   CE   NZ                              
REMARK 470     VAL A 836    CG1  CG2                                            
REMARK 470     PRO A 843    CG   CD                                             
REMARK 470     TYR A 871    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 910    CG   SD   CE                                        
REMARK 470     ARG A 989    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 991    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET A1014    CG   SD   CE                                        
REMARK 470     GLN A1025    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1063    CG   CD   CE   NZ                                   
REMARK 470     ARG A1080    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A1102    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A1134    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1138    CD   NE   CZ   NH1  NH2                             
REMARK 470     THR B 103    OG1  CG2                                            
REMARK 470     SER B 104    OG                                                  
REMARK 470     LEU B 106    CG   CD1  CD2                                       
REMARK 470     HIS B 107    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS B 119    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 158    OG1  CG2                                            
REMARK 470     ARG B 289    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 112    CG1  CG2  CD1                                       
REMARK 470     ARG C 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 208    CG   CD   CE   NZ                                   
REMARK 470     GLU C 368    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 408    CG   CD   CE   NZ                                   
REMARK 470     TRP C 561    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 561    CZ3  CH2                                            
REMARK 470     PHE C 668    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 769    CB   CG   CD   CE   NZ                              
REMARK 470     GLN C 859    CG   CD   OE1  NE2                                  
REMARK 470     TYR C 871    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE C 949    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 989    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 991    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET C1014    CG   SD   CE                                        
REMARK 470     GLN C1025    CG   CD   OE1  NE2                                  
REMARK 470     LEU C1051    CG   CD1  CD2                                       
REMARK 470     MET C1054    CG   SD   CE                                        
REMARK 470     LYS C1063    CG   CD   CE   NZ                                   
REMARK 470     LYS C1067    CG   CD   CE   NZ                                   
REMARK 470     ARG C1080    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C1102    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN C1106    CG   CD   OE1  NE2                                  
REMARK 470     GLU C1107    CG   CD   OE1  OE2                                  
REMARK 470     ARG C1138    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS E 204    CG   CD   CE   NZ                                   
REMARK 470     LYS E 206    CG   CD   CE   NZ                                   
REMARK 470     GLU E 238    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 290    CG   OD1  OD2                                       
REMARK 470     TRP E 293    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP E 293    CZ3  CH2                                            
REMARK 470     ARG E 298    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL E 342    CG1  CG2                                            
REMARK 470     LEU E 353    CG   CD1  CD2                                       
REMARK 470     GLU E 357    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 363    CG1  CG2  CD1                                       
REMARK 470     ARG E 365    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E 367    CG   CD1  CD2                                       
REMARK 470     GLU E 386    CG   CD   OE1  OE2                                  
REMARK 470     TYR E 413    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR E 431    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU E 445    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 446    CG   CD   CE   NZ                                   
REMARK 470     ASN E 553    CG   OD1  ND2                                       
REMARK 470     MET E 591    CG   SD   CE                                        
REMARK 470     PHE E 594    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU E 636    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 800    CG   CD   CE   NZ                                   
REMARK 470     LEU E 818    CG   CD1  CD2                                       
REMARK 470     TRP F  33    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP F  33    CZ3  CH2                                            
REMARK 470     LYS H 204    CG   CD   CE   NZ                                   
REMARK 470     LYS H 206    CG   CD   CE   NZ                                   
REMARK 470     ILE H 233    CG1  CG2  CD1                                       
REMARK 470     GLU H 238    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 276    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 345    CG   CD   CE   NZ                                   
REMARK 470     GLU H 357    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 365    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 378    CG   CD1  CD2                                       
REMARK 470     GLU H 423    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 427    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 428    CG   CD1  CD2                                       
REMARK 470     TYR H 431    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU H 432    CG   CD1  CD2                                       
REMARK 470     VAL H 483    CG1  CG2                                            
REMARK 470     LYS H 525    CG   CD   CE   NZ                                   
REMARK 470     LEU H 818    CG   CD1  CD2                                       
REMARK 470     VAL I  38    CG1  CG2                                            
REMARK 470     VAL I  39    CG1  CG2                                            
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    PRO A 412   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    SER A 624   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    PRO A 656   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO A 688   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ASP A 689   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    PRO A 716   C   -  N   -  CD  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    PRO C 412   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    SER C 624   N   -  CA  -  C   ANGL. DEV. =  18.9 DEGREES          
REMARK 500    PRO C 656   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO C 688   CA  -  N   -  CD  ANGL. DEV. =  -8.4 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    PRO E 556   C   -  N   -  CD  ANGL. DEV. = -17.4 DEGREES          
REMARK 500     DC R  13   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG S   4   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DG S   4   O4' -  C1' -  N9  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DC S   5   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DT S   7   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DA S  12   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG S  13   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC S  14   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DC T  13   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG U   4   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG U   4   O4' -  C1' -  N9  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DC U   5   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DT U   7   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DA U  12   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG U  13   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC U  14   O4' -  C1' -  N1  ANGL. DEV. =   2.9 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    LYS A  35       76.33   -116.08                                   
REMARK 500    ASN A  36      -91.14     61.33                                   
REMARK 500    GLU A  47       55.36     34.03                                   
REMARK 500    LEU A 145       63.09   -101.14                                   
REMARK 500    HIS A 163       78.06   -119.98                                   
REMARK 500    ASN A 241       86.20   -160.18                                   
REMARK 500    LEU A 317      -72.51   -111.30                                   
REMARK 500    ASP A 318      149.82   -177.40                                   
REMARK 500    LEU A 367      -93.40    -64.82                                   
REMARK 500    ARG A 369     -138.11   -108.79                                   
REMARK 500    GLN A 372      -93.31    -75.78                                   
REMARK 500    PHE A 382     -144.36     54.23                                   
REMARK 500    ILE A 389     -118.46   -150.62                                   
REMARK 500    ILE A 390      169.24    139.05                                   
REMARK 500    ARG A 391      117.57   -179.51                                   
REMARK 500    ASN A 392       69.37    -61.20                                   
REMARK 500    ASP A 403       61.95   -107.67                                   
REMARK 500    LEU A 413     -164.59   -102.73                                   
REMARK 500    ARG A 414       84.86   -157.64                                   
REMARK 500    ASN A 418      -82.86    -63.74                                   
REMARK 500    ASP A 423        4.24   -155.17                                   
REMARK 500    VAL A 430     -108.93    -43.35                                   
REMARK 500    GLN A 432      175.08    173.94                                   
REMARK 500    THR A 446     -146.61    -87.29                                   
REMARK 500    MET A 449      -78.02    -38.26                                   
REMARK 500    ASP A 453       -4.10   -144.00                                   
REMARK 500    CYS A 460      142.20    174.52                                   
REMARK 500    GLN A 481      -96.72    -76.68                                   
REMARK 500    SER A 488      140.56    171.19                                   
REMARK 500    TRP A 490     -179.13    -66.29                                   
REMARK 500    PRO A 493      -42.96    -28.11                                   
REMARK 500    CYS A 503      167.26    168.02                                   
REMARK 500    SER A 505      -59.18    -28.70                                   
REMARK 500    ASP A 542      118.21   -162.34                                   
REMARK 500    LEU A 546     -163.49   -129.97                                   
REMARK 500    SER A 549      159.97    -37.79                                   
REMARK 500    ASN A 550       77.73   -110.47                                   
REMARK 500    TRP A 561      -67.21   -105.52                                   
REMARK 500    THR A 562      -87.37    -64.18                                   
REMARK 500    ASP A 563      -24.34    -34.59                                   
REMARK 500    ALA A 566       89.65   -163.74                                   
REMARK 500    LEU A 571      -72.31    -55.57                                   
REMARK 500    LEU A 582     -105.68   -145.75                                   
REMARK 500    GLU A 585      -10.16   -141.36                                   
REMARK 500    ARG A 589      -14.38   -142.36                                   
REMARK 500    LEU A 592      125.32    177.58                                   
REMARK 500    PHE A 596      -71.37    -98.76                                   
REMARK 500    SER A 598       -3.13    158.99                                   
REMARK 500    ALA A 605      114.94   -161.39                                   
REMARK 500    LEU A 606     -178.68    -66.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     318 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: 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: 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                            
REMARK 900 RELATED ID: 4A0K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI4   RELATED DB: PDB                                   
DBREF  4A0L C    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  4A0L A    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  4A0L B   94   457  UNP    Q2YDS1   DDB2_DANRE      60    423             
DBREF  4A0L D   94   457  UNP    Q2YDS1   DDB2_DANRE      60    423             
DBREF  4A0L E  193   913  UNP    Q13620   CUL4B_HUMAN    192    913             
DBREF  4A0L H  193   913  UNP    Q13620   CUL4B_HUMAN    192    913             
DBREF  4A0L F   12   108  UNP    P62878   RBX1_MOUSE      12    108             
DBREF  4A0L I   12   108  UNP    P62878   RBX1_MOUSE      12    108             
DBREF  4A0L R    3    14  PDB    4A0L     4A0L             3     14             
DBREF  4A0L S    3    14  PDB    4A0L     4A0L             3     14             
DBREF  4A0L T    3    14  PDB    4A0L     4A0L             3     14             
DBREF  4A0L U    3    14  PDB    4A0L     4A0L             3     14             
SEQADV 4A0L GLY A   -3  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L GLY A   -2  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L GLY A   -1  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L ARG A    0  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L MET B   76  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   77  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   78  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   79  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   80  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   81  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS B   82  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG B   83  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG B   84  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L LEU B   85  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L VAL B   86  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L PRO B   87  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG B   88  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY B   89  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L SER B   90  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY B   91  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY B   92  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG B   93  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLN B  180  UNP  Q2YDS1    LEU   146 VARIANT                        
SEQADV 4A0L ARG B  214  UNP  Q2YDS1    TRP   180 VARIANT                        
SEQADV 4A0L GLY C   -3  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L GLY C   -2  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L GLY C   -1  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L ARG C    0  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4A0L MET D   76  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   77  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   78  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   79  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   80  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   81  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L HIS D   82  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG D   83  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG D   84  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L LEU D   85  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L VAL D   86  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L PRO D   87  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG D   88  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY D   89  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L SER D   90  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY D   91  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLY D   92  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L ARG D   93  UNP  Q2YDS1              EXPRESSION TAG                 
SEQADV 4A0L GLN D  180  UNP  Q2YDS1    LEU   146 VARIANT                        
SEQADV 4A0L ARG D  214  UNP  Q2YDS1    TRP   180 VARIANT                        
SEQADV 4A0L GLY E  189  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L GLY E  190  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L GLY E  191  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L ARG E  192  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L MET F   11  UNP  P62878              EXPRESSION TAG                 
SEQADV 4A0L GLY H  189  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L GLY H  190  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L GLY H  191  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L ARG H  192  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A0L MET I   11  UNP  P62878              EXPRESSION TAG                 
SEQRES   1 A 1144  GLY GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA          
SEQRES   2 A 1144  GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS          
SEQRES   3 A 1144  PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS          
SEQRES   4 A 1144  ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY          
SEQRES   5 A 1144  LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE          
SEQRES   6 A 1144  ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS          
SEQRES   7 A 1144  ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS          
SEQRES   8 A 1144  ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE          
SEQRES   9 A 1144  ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY          
SEQRES  10 A 1144  ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO          
SEQRES  11 A 1144  GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU          
SEQRES  12 A 1144  PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU          
SEQRES  13 A 1144  LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE          
SEQRES  14 A 1144  ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE          
SEQRES  15 A 1144  CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS          
SEQRES  16 A 1144  THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS          
SEQRES  17 A 1144  GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER          
SEQRES  18 A 1144  MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE          
SEQRES  19 A 1144  ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP          
SEQRES  20 A 1144  LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER          
SEQRES  21 A 1144  THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER          
SEQRES  22 A 1144  ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET          
SEQRES  23 A 1144  LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL          
SEQRES  24 A 1144  THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR          
SEQRES  25 A 1144  SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL          
SEQRES  26 A 1144  VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL          
SEQRES  27 A 1144  LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL          
SEQRES  28 A 1144  VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL          
SEQRES  29 A 1144  ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY          
SEQRES  30 A 1144  GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER          
SEQRES  31 A 1144  LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU HIS          
SEQRES  32 A 1144  ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP PRO          
SEQRES  33 A 1144  LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR LEU          
SEQRES  34 A 1144  VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET LEU          
SEQRES  35 A 1144  ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY PHE          
SEQRES  36 A 1144  VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL ALA          
SEQRES  37 A 1144  HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL ARG          
SEQRES  38 A 1144  LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU TRP          
SEQRES  39 A 1144  LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER CYS          
SEQRES  40 A 1144  ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA LEU          
SEQRES  41 A 1144  TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN ILE          
SEQRES  42 A 1144  SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU ASP          
SEQRES  43 A 1144  ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO LEU          
SEQRES  44 A 1144  CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG ILE          
SEQRES  45 A 1144  LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU MET          
SEQRES  46 A 1144  LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET THR          
SEQRES  47 A 1144  THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU GLY          
SEQRES  48 A 1144  ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU THR          
SEQRES  49 A 1144  GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY THR          
SEQRES  50 A 1144  GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER THR          
SEQRES  51 A 1144  THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL ILE          
SEQRES  52 A 1144  TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL ASN          
SEQRES  53 A 1144  LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER ASP          
SEQRES  54 A 1144  GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER THR          
SEQRES  55 A 1144  LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU HIS          
SEQRES  56 A 1144  ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS ILE          
SEQRES  57 A 1144  CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU SER          
SEQRES  58 A 1144  SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR THR          
SEQRES  59 A 1144  ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER SER          
SEQRES  60 A 1144  SER VAL SER SER SER LYS LEU PHE SER SER SER THR ALA          
SEQRES  61 A 1144  PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL HIS          
SEQRES  62 A 1144  ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL LEU          
SEQRES  63 A 1144  HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU SER          
SEQRES  64 A 1144  LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR TYR          
SEQRES  65 A 1144  PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU ALA          
SEQRES  66 A 1144  GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR SER          
SEQRES  67 A 1144  ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL LYS          
SEQRES  68 A 1144  GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS LEU          
SEQRES  69 A 1144  LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU TRP          
SEQRES  70 A 1144  THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS TYR          
SEQRES  71 A 1144  ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY ASP          
SEQRES  72 A 1144  PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU LEU          
SEQRES  73 A 1144  LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU ILE          
SEQRES  74 A 1144  ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL GLU          
SEQRES  75 A 1144  ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN ALA          
SEQRES  76 A 1144  PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA THR          
SEQRES  77 A 1144  THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY LEU          
SEQRES  78 A 1144  PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS GLY          
SEQRES  79 A 1144  SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR PRO          
SEQRES  80 A 1144  THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY MET          
SEQRES  81 A 1144  ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR ASN          
SEQRES  82 A 1144  LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL ILE          
SEQRES  83 A 1144  LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG SER          
SEQRES  84 A 1144  PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY PHE          
SEQRES  85 A 1144  ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE SER          
SEQRES  86 A 1144  ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN TYR          
SEQRES  87 A 1144  ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA ASP          
SEQRES  88 A 1144  ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG ILE HIS          
SEQRES   1 B  382  MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG          
SEQRES   2 B  382  GLY SER GLY GLY ARG THR GLY GLY GLN LYS LYS VAL GLY          
SEQRES   3 B  382  GLN THR SER ILE LEU HIS TYR ILE TYR LYS SER SER LEU          
SEQRES   4 B  382  GLY GLN SER ILE HIS ALA GLN LEU ARG GLN CYS LEU GLN          
SEQRES   5 B  382  GLU PRO PHE ILE ARG SER LEU LYS SER TYR LYS LEU HIS          
SEQRES   6 B  382  ARG THR ALA SER PRO PHE ASP ARG ARG VAL THR SER LEU          
SEQRES   7 B  382  GLU TRP HIS PRO THR HIS PRO THR THR VAL ALA VAL GLY          
SEQRES   8 B  382  SER LYS GLY GLY ASP ILE ILE LEU TRP ASP TYR ASP VAL          
SEQRES   9 B  382  GLN ASN LYS THR SER PHE ILE GLN GLY MET GLY PRO GLY          
SEQRES  10 B  382  ASP ALA ILE THR GLY MET LYS PHE ASN GLN PHE ASN THR          
SEQRES  11 B  382  ASN GLN LEU PHE VAL SER SER ILE ARG GLY ALA THR THR          
SEQRES  12 B  382  LEU ARG ASP PHE SER GLY SER VAL ILE GLN VAL PHE ALA          
SEQRES  13 B  382  LYS THR ASP SER TRP ASP TYR TRP TYR CYS CYS VAL ASP          
SEQRES  14 B  382  VAL SER VAL SER ARG GLN MET LEU ALA THR GLY ASP SER          
SEQRES  15 B  382  THR GLY ARG LEU LEU LEU LEU GLY LEU ASP GLY HIS GLU          
SEQRES  16 B  382  ILE PHE LYS GLU LYS LEU HIS LYS ALA LYS VAL THR HIS          
SEQRES  17 B  382  ALA GLU PHE ASN PRO ARG CYS ASP TRP LEU MET ALA THR          
SEQRES  18 B  382  SER SER VAL ASP ALA THR VAL LYS LEU TRP ASP LEU ARG          
SEQRES  19 B  382  ASN ILE LYS ASP LYS ASN SER TYR ILE ALA GLU MET PRO          
SEQRES  20 B  382  HIS GLU LYS PRO VAL ASN ALA ALA TYR PHE ASN PRO THR          
SEQRES  21 B  382  ASP SER THR LYS LEU LEU THR THR ASP GLN ARG ASN GLU          
SEQRES  22 B  382  ILE ARG VAL TYR SER SER TYR ASP TRP SER LYS PRO ASP          
SEQRES  23 B  382  GLN ILE ILE ILE HIS PRO HIS ARG GLN PHE GLN HIS LEU          
SEQRES  24 B  382  THR PRO ILE LYS ALA THR TRP HIS PRO MET TYR ASP LEU          
SEQRES  25 B  382  ILE VAL ALA GLY ARG TYR PRO ASP ASP GLN LEU LEU LEU          
SEQRES  26 B  382  ASN ASP LYS ARG THR ILE ASP ILE TYR ASP ALA ASN SER          
SEQRES  27 B  382  GLY GLY LEU VAL HIS GLN LEU ARG ASP PRO ASN ALA ALA          
SEQRES  28 B  382  GLY ILE ILE SER LEU ASN LYS PHE SER PRO THR GLY ASP          
SEQRES  29 B  382  VAL LEU ALA SER GLY MET GLY PHE ASN ILE LEU ILE TRP          
SEQRES  30 B  382  ASN ARG GLU ASP THR                                          
SEQRES   1 C 1144  GLY GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA          
SEQRES   2 C 1144  GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS          
SEQRES   3 C 1144  PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS          
SEQRES   4 C 1144  ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY          
SEQRES   5 C 1144  LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE          
SEQRES   6 C 1144  ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS          
SEQRES   7 C 1144  ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS          
SEQRES   8 C 1144  ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE          
SEQRES   9 C 1144  ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY          
SEQRES  10 C 1144  ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO          
SEQRES  11 C 1144  GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU          
SEQRES  12 C 1144  PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU          
SEQRES  13 C 1144  LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE          
SEQRES  14 C 1144  ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE          
SEQRES  15 C 1144  CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS          
SEQRES  16 C 1144  THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS          
SEQRES  17 C 1144  GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER          
SEQRES  18 C 1144  MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE          
SEQRES  19 C 1144  ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP          
SEQRES  20 C 1144  LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER          
SEQRES  21 C 1144  THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER          
SEQRES  22 C 1144  ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET          
SEQRES  23 C 1144  LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL          
SEQRES  24 C 1144  THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR          
SEQRES  25 C 1144  SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL          
SEQRES  26 C 1144  VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL          
SEQRES  27 C 1144  LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL          
SEQRES  28 C 1144  VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL          
SEQRES  29 C 1144  ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY          
SEQRES  30 C 1144  GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER          
SEQRES  31 C 1144  LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU HIS          
SEQRES  32 C 1144  ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP PRO          
SEQRES  33 C 1144  LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR LEU          
SEQRES  34 C 1144  VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET LEU          
SEQRES  35 C 1144  ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY PHE          
SEQRES  36 C 1144  VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL ALA          
SEQRES  37 C 1144  HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL ARG          
SEQRES  38 C 1144  LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU TRP          
SEQRES  39 C 1144  LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER CYS          
SEQRES  40 C 1144  ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA LEU          
SEQRES  41 C 1144  TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN ILE          
SEQRES  42 C 1144  SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU ASP          
SEQRES  43 C 1144  ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO LEU          
SEQRES  44 C 1144  CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG ILE          
SEQRES  45 C 1144  LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU MET          
SEQRES  46 C 1144  LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET THR          
SEQRES  47 C 1144  THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU GLY          
SEQRES  48 C 1144  ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU THR          
SEQRES  49 C 1144  GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY THR          
SEQRES  50 C 1144  GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER THR          
SEQRES  51 C 1144  THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL ILE          
SEQRES  52 C 1144  TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL ASN          
SEQRES  53 C 1144  LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER ASP          
SEQRES  54 C 1144  GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER THR          
SEQRES  55 C 1144  LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU HIS          
SEQRES  56 C 1144  ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS ILE          
SEQRES  57 C 1144  CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU SER          
SEQRES  58 C 1144  SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR THR          
SEQRES  59 C 1144  ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER SER          
SEQRES  60 C 1144  SER VAL SER SER SER LYS LEU PHE SER SER SER THR ALA          
SEQRES  61 C 1144  PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL HIS          
SEQRES  62 C 1144  ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL LEU          
SEQRES  63 C 1144  HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU SER          
SEQRES  64 C 1144  LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR TYR          
SEQRES  65 C 1144  PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU ALA          
SEQRES  66 C 1144  GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR SER          
SEQRES  67 C 1144  ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL LYS          
SEQRES  68 C 1144  GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS LEU          
SEQRES  69 C 1144  LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU TRP          
SEQRES  70 C 1144  THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS TYR          
SEQRES  71 C 1144  ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY ASP          
SEQRES  72 C 1144  PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU LEU          
SEQRES  73 C 1144  LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU ILE          
SEQRES  74 C 1144  ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL GLU          
SEQRES  75 C 1144  ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN ALA          
SEQRES  76 C 1144  PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA THR          
SEQRES  77 C 1144  THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY LEU          
SEQRES  78 C 1144  PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS GLY          
SEQRES  79 C 1144  SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR PRO          
SEQRES  80 C 1144  THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY MET          
SEQRES  81 C 1144  ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR ASN          
SEQRES  82 C 1144  LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL ILE          
SEQRES  83 C 1144  LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG SER          
SEQRES  84 C 1144  PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY PHE          
SEQRES  85 C 1144  ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE SER          
SEQRES  86 C 1144  ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN TYR          
SEQRES  87 C 1144  ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA ASP          
SEQRES  88 C 1144  ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG 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  726  GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL ILE LYS          
SEQRES   2 E  726  ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN TYR THR          
SEQRES   3 E  726  ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA          
SEQRES   4 E  726  ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU GLU GLU          
SEQRES   5 E  726  LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR LYS ILE          
SEQRES   6 E  726  SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU          
SEQRES   7 E  726  ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP          
SEQRES   8 E  726  SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE ASP ARG          
SEQRES   9 E  726  CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET ILE ARG          
SEQRES  10 E  726  SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL LEU GLN          
SEQRES  11 E  726  ASN SER MET LEU PRO SER ILE TRP ASP MET GLY LEU GLU          
SEQRES  12 E  726  LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS VAL GLN          
SEQRES  13 E  726  ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG          
SEQRES  14 E  726  GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU LEU ARG          
SEQRES  15 E  726  SER LEU LEU SER MET LEU SER ASP LEU GLN ILE TYR GLN          
SEQRES  16 E  726  ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR ASN ARG          
SEQRES  17 E  726  LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN GLU ARG          
SEQRES  18 E  726  GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU          
SEQRES  19 E  726  GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU ASP GLN          
SEQRES  20 E  726  THR THR GLN LYS SER LEU ILE ALA THR VAL GLU LYS GLN          
SEQRES  21 E  726  LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN LYS GLY          
SEQRES  22 E  726  LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU          
SEQRES  23 E  726  SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG GLY GLY          
SEQRES  24 E  726  VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS          
SEQRES  25 E  726  ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU LYS ASP          
SEQRES  26 E  726  LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS ASP LYS          
SEQRES  27 E  726  VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU          
SEQRES  28 E  726  LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU THR PHE          
SEQRES  29 E  726  ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU ILE ALA          
SEQRES  30 E  726  LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN LYS GLU          
SEQRES  31 E  726  ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP LYS ILE          
SEQRES  32 E  726  MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP VAL PHE          
SEQRES  33 E  726  GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG LEU LEU          
SEQRES  34 E  726  VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS SER MET          
SEQRES  35 E  726  LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA PHE THR          
SEQRES  36 E  726  SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU LEU SER          
SEQRES  37 E  726  LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET GLN ASN          
SEQRES  38 E  726  GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL ASN ILE          
SEQRES  39 E  726  LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO MET GLU          
SEQRES  40 E  726  VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN GLU ILE          
SEQRES  41 E  726  PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY ARG LYS          
SEQRES  42 E  726  LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL LEU LYS          
SEQRES  43 E  726  ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN VAL SER          
SEQRES  44 E  726  LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN GLU GLY          
SEQRES  45 E  726  GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA THR GLY          
SEQRES  46 E  726  ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN SER LEU          
SEQRES  47 E  726  ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN PRO LYS          
SEQRES  48 E  726  GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE CYS ASN          
SEQRES  49 E  726  ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS ILE ASN          
SEQRES  50 E  726  GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN ALA SER          
SEQRES  51 E  726  THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR GLN ILE          
SEQRES  52 E  726  ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG LYS THR          
SEQRES  53 E  726  LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR ASN GLN          
SEQRES  54 E  726  LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS LYS ARG          
SEQRES  55 E  726  ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU ARG ASP          
SEQRES  56 E  726  LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA                  
SEQRES   1 F   98  MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU          
SEQRES   2 F   98  VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP          
SEQRES   3 F   98  ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE          
SEQRES   4 F   98  MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER          
SEQRES   5 F   98  ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS          
SEQRES   6 F   98  ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU          
SEQRES   7 F   98  LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP          
SEQRES   8 F   98  GLU PHE GLN LYS TYR GLY HIS                                  
SEQRES   1 H  726  GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL ILE LYS          
SEQRES   2 H  726  ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN TYR THR          
SEQRES   3 H  726  ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA          
SEQRES   4 H  726  ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU GLU GLU          
SEQRES   5 H  726  LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR LYS ILE          
SEQRES   6 H  726  SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU          
SEQRES   7 H  726  ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP          
SEQRES   8 H  726  SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE ASP ARG          
SEQRES   9 H  726  CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET ILE ARG          
SEQRES  10 H  726  SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL LEU GLN          
SEQRES  11 H  726  ASN SER MET LEU PRO SER ILE TRP ASP MET GLY LEU GLU          
SEQRES  12 H  726  LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS VAL GLN          
SEQRES  13 H  726  ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG          
SEQRES  14 H  726  GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU LEU ARG          
SEQRES  15 H  726  SER LEU LEU SER MET LEU SER ASP LEU GLN ILE TYR GLN          
SEQRES  16 H  726  ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR ASN ARG          
SEQRES  17 H  726  LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN GLU ARG          
SEQRES  18 H  726  GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU          
SEQRES  19 H  726  GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU ASP GLN          
SEQRES  20 H  726  THR THR GLN LYS SER LEU ILE ALA THR VAL GLU LYS GLN          
SEQRES  21 H  726  LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN LYS GLY          
SEQRES  22 H  726  LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU          
SEQRES  23 H  726  SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG GLY GLY          
SEQRES  24 H  726  VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS          
SEQRES  25 H  726  ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU LYS ASP          
SEQRES  26 H  726  LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS ASP LYS          
SEQRES  27 H  726  VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU          
SEQRES  28 H  726  LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU THR PHE          
SEQRES  29 H  726  ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU ILE ALA          
SEQRES  30 H  726  LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN LYS GLU          
SEQRES  31 H  726  ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP LYS ILE          
SEQRES  32 H  726  MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP VAL PHE          
SEQRES  33 H  726  GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG LEU LEU          
SEQRES  34 H  726  VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS SER MET          
SEQRES  35 H  726  LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA PHE THR          
SEQRES  36 H  726  SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU LEU SER          
SEQRES  37 H  726  LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET GLN ASN          
SEQRES  38 H  726  GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL ASN ILE          
SEQRES  39 H  726  LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO MET GLU          
SEQRES  40 H  726  VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN GLU ILE          
SEQRES  41 H  726  PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY ARG LYS          
SEQRES  42 H  726  LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL LEU LYS          
SEQRES  43 H  726  ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN VAL SER          
SEQRES  44 H  726  LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN GLU GLY          
SEQRES  45 H  726  GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA THR GLY          
SEQRES  46 H  726  ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN SER LEU          
SEQRES  47 H  726  ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN PRO LYS          
SEQRES  48 H  726  GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE CYS ASN          
SEQRES  49 H  726  ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS ILE ASN          
SEQRES  50 H  726  GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN ALA SER          
SEQRES  51 H  726  THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR GLN ILE          
SEQRES  52 H  726  ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG LYS THR          
SEQRES  53 H  726  LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR ASN GLN          
SEQRES  54 H  726  LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS LYS ARG          
SEQRES  55 H  726  ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU ARG ASP          
SEQRES  56 H  726  LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA                  
SEQRES   1 I   98  MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU          
SEQRES   2 I   98  VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP          
SEQRES   3 I   98  ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE          
SEQRES   4 I   98  MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER          
SEQRES   5 I   98  ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS          
SEQRES   6 I   98  ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU          
SEQRES   7 I   98  LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP          
SEQRES   8 I   98  GLU PHE GLN LYS TYR GLY HIS                                  
SEQRES   1 R   12   DG  DC  DT  DA  DC  DT 3DR  DA  DC  DG  DC  DA              
SEQRES   1 S   12   DT  DG  DC  DG  DT  DA  DA  DG  DT  DA  DG  DC              
SEQRES   1 T   12   DG  DC  DT  DA  DC  DT 3DR  DA  DC  DG  DC  DA              
SEQRES   1 U   12   DT  DG  DC  DG  DT  DA  DA  DG  DT  DA  DG  DC              
HET    3DR  R   9      11                                                       
HET    3DR  T   9      11                                                       
HETNAM     3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE                           
HETSYN     3DR ABASIC DIDEOXYRIBOSE                                             
FORMUL   9  3DR    2(C5 H11 O6 P)                                               
HELIX    1   1 PRO A  250  GLN A  255  1                                   6    
HELIX    2   2 ALA A  381  GLY A  385  5                                   5    
HELIX    3   3 GLU A  728  SER A  730  5                                   3    
HELIX    4   4 THR A  985  GLN A  990  1                                   6    
HELIX    5   5 SER A 1044  ILE A 1062  1                                  19    
HELIX    6   6 GLU A 1069  ARG A 1074  1                                   6    
HELIX    7   7 GLY A 1091  SER A 1096  1                                   6    
HELIX    8   8 PHE A 1097  ILE A 1100  5                                   4    
HELIX    9   9 SER A 1101  ALA A 1110  1                                  10    
HELIX   10  10 THR A 1125  ARG A 1138  1                                  14    
HELIX   11  11 SER B  104  LEU B  114  1                                  11    
HELIX   12  12 ILE B  118  LYS B  135  1                                  18    
HELIX   13  13 PRO C  250  GLN C  255  1                                   6    
HELIX   14  14 ALA C  381  GLU C  384  5                                   4    
HELIX   15  15 GLU C  728  SER C  730  5                                   3    
HELIX   16  16 THR C  985  GLN C  990  1                                   6    
HELIX   17  17 SER C 1044  ILE C 1062  1                                  19    
HELIX   18  18 GLU C 1069  ARG C 1074  1                                   6    
HELIX   19  19 GLY C 1091  SER C 1096  1                                   6    
HELIX   20  20 PHE C 1097  ILE C 1100  5                                   4    
HELIX   21  21 SER C 1101  ALA C 1110  1                                  10    
HELIX   22  22 THR C 1125  ARG C 1138  1                                  14    
HELIX   23  23 SER D  104  LEU D  114  1                                  11    
HELIX   24  24 ILE D  118  LYS D  135  1                                  18    
HELIX   25  25 GLU E  215  LYS E  219  5                                   5    
HELIX   26  26 ALA E  223  GLN E  228  1                                   6    
HELIX   27  27 GLU E  239  GLU E  245  1                                   7    
HELIX   28  28 SER E  253  LYS E  269  1                                  17    
HELIX   29  29 GLN E  271  ARG E  276  1                                   6    
HELIX   30  30 ASP E  281  PHE E  307  1                                  27    
HELIX   31  31 PHE E  307  THR E  313  1                                   7    
HELIX   32  32 THR E  313  ASN E  318  1                                   6    
HELIX   33  33 SER E  323  ARG E  333  1                                  11    
HELIX   34  34 GLN E  340  ARG E  358  1                                  19    
HELIX   35  35 SER E  366  LEU E  378  1                                  13    
HELIX   36  36 ILE E  380  PHE E  385  1                                   6    
HELIX   37  37 PHE E  385  LEU E  404  1                                  20    
HELIX   38  38 GLU E  409  LEU E  428  1                                  20    
HELIX   39  39 ILE E  429  TYR E  431  5                                   3    
HELIX   40  40 GLN E  437  LEU E  449  1                                  13    
HELIX   41  41 HIS E  452  GLY E  460  1                                   9    
HELIX   42  42 GLY E  460  GLU E  467  1                                   8    
HELIX   43  43 ARG E  469  SER E  481  1                                  13    
HELIX   44  44 GLY E  485  VAL E  506  1                                  22    
HELIX   45  45 ASN E  508  ASP E  512  5                                   5    
HELIX   46  46 MET E  515  CYS E  533  1                                  19    
HELIX   47  47 ASN E  537  ASN E  553  1                                  17    
HELIX   48  48 ASN E  557  LYS E  570  1                                  14    
HELIX   49  49 LEU E  583  ARG E  595  1                                  13    
HELIX   50  50 GLY E  599  VAL E  617  1                                  19    
HELIX   51  51 ASP E  624  LYS E  632  1                                   9    
HELIX   52  52 ALA E  639  LYS E  644  1                                   6    
HELIX   53  53 GLU E  646  ASN E  670  1                                  25    
HELIX   54  54 GLU E  700  GLN E  705  1                                   6    
HELIX   55  55 GLN E  705  LEU E  713  1                                   9    
HELIX   56  56 LEU E  747  MET E  755  1                                   9    
HELIX   57  57 PHE E  756  GLU E  758  5                                   3    
HELIX   58  58 LEU E  764  GLY E  772  1                                   9    
HELIX   59  59 GLU E  774  LEU E  782  1                                   9    
HELIX   60  60 GLN E  825  LYS E  829  5                                   5    
HELIX   61  61 THR E  831  ARG E  861  1                                  31    
HELIX   62  62 LEU E  869  LEU E  877  1                                   9    
HELIX   63  63 LYS E  882  ASP E  895  1                                  14    
HELIX   64  64 GLU H  215  LYS H  219  5                                   5    
HELIX   65  65 ALA H  223  ASN H  229  1                                   7    
HELIX   66  66 GLU H  239  GLU H  245  1                                   7    
HELIX   67  67 SER H  253  LYS H  269  1                                  17    
HELIX   68  68 GLN H  271  ARG H  276  1                                   6    
HELIX   69  69 ASP H  281  PHE H  307  1                                  27    
HELIX   70  70 PHE H  307  THR H  313  1                                   7    
HELIX   71  71 THR H  313  ASN H  318  1                                   6    
HELIX   72  72 SER H  323  ILE H  336  1                                  14    
HELIX   73  73 GLN H  340  ARG H  358  1                                  19    
HELIX   74  74 ARG H  365  ASP H  377  1                                  13    
HELIX   75  75 ILE H  380  PHE H  385  1                                   6    
HELIX   76  76 PHE H  385  LEU H  404  1                                  20    
HELIX   77  77 GLU H  409  LEU H  428  1                                  20    
HELIX   78  78 THR H  436  LEU H  449  1                                  14    
HELIX   79  79 HIS H  452  GLY H  460  1                                   9    
HELIX   80  80 GLY H  460  ASN H  468  1                                   9    
HELIX   81  81 ARG H  469  SER H  481  1                                  13    
HELIX   82  82 GLY H  485  VAL H  506  1                                  22    
HELIX   83  83 ASN H  508  ASP H  512  5                                   5    
HELIX   84  84 MET H  515  CYS H  533  1                                  19    
HELIX   85  85 ASN H  537  ASN H  553  1                                  17    
HELIX   86  86 ASN H  557  LYS H  570  1                                  14    
HELIX   87  87 LEU H  583  ARG H  595  1                                  13    
HELIX   88  88 LYS H  600  VAL H  617  1                                  18    
HELIX   89  89 ASP H  624  LYS H  632  1                                   9    
HELIX   90  90 ALA H  639  LYS H  644  1                                   6    
HELIX   91  91 GLU H  646  ASN H  670  1                                  25    
HELIX   92  92 GLU H  700  GLN H  705  1                                   6    
HELIX   93  93 GLN H  705  LEU H  713  1                                   9    
HELIX   94  94 LEU H  747  MET H  755  1                                   9    
HELIX   95  95 PHE H  756  GLU H  758  5                                   3    
HELIX   96  96 LEU H  764  GLY H  772  1                                   9    
HELIX   97  97 GLU H  774  LEU H  782  1                                   9    
HELIX   98  98 GLN H  825  LYS H  829  5                                   5    
HELIX   99  99 THR H  831  ARG H  861  1                                  31    
HELIX  100 100 LEU H  869  LEU H  877  1                                   9    
HELIX  101 101 LYS H  882  ASP H  895  1                                  14    
SHEET    1  AA 5 VAL A1004  HIS A1009  0                                        
SHEET    2  AA 5 GLN A1025  THR A1032 -1  O  LEU A1029   N  CYS A1008           
SHEET    3  AA 5 ILE A1037  SER A1042 -1  O  GLY A1038   N  PHE A1030           
SHEET    4  AA 5 ASN A   4  GLN A  10 -1  O  TYR A   5   N  THR A1041           
SHEET    5  AA 5 PHE A1088  ASP A1090  1  O  ILE A1089   N  VAL A   6           
SHEET    1  AB 4 GLY A  17  GLY A  21  0                                        
SHEET    2  AB 4 ASN A  30  LYS A  35 -1  O  ASN A  30   N  GLY A  21           
SHEET    3  AB 4 ARG A  38  THR A  45 -1  O  ARG A  38   N  LYS A  35           
SHEET    4  AB 4 GLY A  48  GLY A  56 -1  O  GLY A  48   N  THR A  45           
SHEET    1  AC 4 ILE A  61  PHE A  67  0                                        
SHEET    2  AC 4 LEU A  76  THR A  81 -1  O  LEU A  76   N  PHE A  67           
SHEET    3  AC 4 ASN A  85  SER A  94 -1  O  ASN A  85   N  THR A  81           
SHEET    4  AC 4 SER A  97  ASN A 107 -1  O  SER A  97   N  SER A  94           
SHEET    1  AD 4 ILE A 121  ILE A 124  0                                        
SHEET    2  AD 4 MET A 130  ARG A 134 -1  O  GLY A 132   N  ILE A 123           
SHEET    3  AD 4 LEU A 139  PRO A 144 -1  O  LYS A 141   N  LEU A 133           
SHEET    4  AD 4 PHE A 155  ARG A 158 -1  O  PHE A 155   N  VAL A 142           
SHEET    1  AE 4 VAL A 164  PHE A 169  0                                        
SHEET    2  AE 4 THR A 177  ASP A 184 -1  O  CYS A 179   N  LYS A 168           
SHEET    3  AE 4 GLY A 187  SER A 196 -1  O  GLY A 187   N  ASP A 184           
SHEET    4  AE 4 GLU A 201  LYS A 204  1  O  GLU A 201   N  SER A 196           
SHEET    1  AF 4 VAL A 164  PHE A 169  0                                        
SHEET    2  AF 4 THR A 177  ASP A 184 -1  O  CYS A 179   N  LYS A 168           
SHEET    3  AF 4 GLY A 187  SER A 196 -1  O  GLY A 187   N  ASP A 184           
SHEET    4  AF 4 GLU A 210  VAL A 212 -1  O  GLU A 210   N  VAL A 190           
SHEET    1  AG 2 GLU A 201  LYS A 204  0                                        
SHEET    2  AG 2 GLY A 187  SER A 196  1  O  GLU A 194   N  ASN A 203           
SHEET    1  AH 4 MET A 218  ALA A 221  0                                        
SHEET    2  AH 4 ALA A 229  ILE A 232 -1  O  ILE A 230   N  ILE A 220           
SHEET    3  AH 4 ILE A 237  ASN A 241 -1  O  THR A 238   N  ILE A 231           
SHEET    4  AH 4 LYS A 244  ILE A 248 -1  O  LYS A 244   N  ASN A 241           
SHEET    1  AI 4 ILE A 258  ARG A 263  0                                        
SHEET    2  AI 4 ARG A 270  ASP A 275 -1  O  LEU A 272   N  ASN A 262           
SHEET    3  AI 4 ARG A 279  GLU A 288 -1  O  ARG A 279   N  ASP A 275           
SHEET    4  AI 4 THR A 296  GLU A 307 -1  O  THR A 296   N  GLU A 288           
SHEET    1  AJ 4 CYS A 313  ASP A 318  0                                        
SHEET    2  AJ 4 VAL A 321  GLY A 325 -1  O  VAL A 321   N  LEU A 317           
SHEET    3  AJ 4 SER A 331  LEU A 336 -1  O  GLN A 332   N  VAL A 324           
SHEET    4  AJ 4 VAL A 347  PHE A 353 -1  O  VAL A 348   N  LYS A 335           
SHEET    1  AK 2 ILE A 359  VAL A 365  0                                        
SHEET    2  AK 2 GLN A 374  SER A 379 -1  O  GLN A 374   N  VAL A 365           
SHEET    1  AL 4 ALA A 400  SER A 401  0                                        
SHEET    2  AL 4 LEU A 699  GLY A 702 -1  O  ILE A 701   N  ALA A 400           
SHEET    3  AL 4 SER A 690  ALA A 694 -1  O  LEU A 691   N  GLY A 702           
SHEET    4  AL 4 TYR A 678  LEU A 682 -1  O  TYR A 678   N  ALA A 694           
SHEET    1  AM 4 LEU A 410  LEU A 413  0                                        
SHEET    2  AM 4 THR A 424  LEU A 427 -1  O  THR A 424   N  LEU A 413           
SHEET    3  AM 4 VAL A 435  ASN A 439 -1  O  LEU A 436   N  LEU A 425           
SHEET    4  AM 4 GLU A 442  GLU A 445 -1  O  GLU A 442   N  ASN A 439           
SHEET    1  AN 4 THR A 457  VAL A 463  0                                        
SHEET    2  AN 4 GLN A 467  THR A 472 -1  O  GLN A 467   N  VAL A 463           
SHEET    3  AN 4 VAL A 476  SER A 480 -1  O  ARG A 477   N  GLN A 470           
SHEET    4  AN 4 LEU A 486  SER A 488 -1  N  VAL A 487   O  LEU A 478           
SHEET    1  AO 4 VAL A 500  ALA A 501  0                                        
SHEET    2  AO 4 GLN A 507  VAL A 512 -1  N  ALA A 511   O  VAL A 500           
SHEET    3  AO 4 ALA A 515  HIS A 522 -1  O  ALA A 515   N  VAL A 512           
SHEET    4  AO 4 GLU A 525  GLU A 533 -1  O  GLU A 525   N  HIS A 522           
SHEET    1  AP 4 VAL A 538  ASP A 542  0                                        
SHEET    2  AP 4 LEU A 555  LEU A 560 -1  O  ALA A 557   N  ASP A 542           
SHEET    3  AP 4 ILE A 568  LYS A 570 -1  O  LEU A 569   N  CYS A 556           
SHEET    4  AP 4 GLU A 575  HIS A 578 -1  O  GLU A 575   N  LYS A 570           
SHEET    1  AQ 2 PRO A 588  SER A 590  0                                        
SHEET    2  AQ 2 ALA A 605  LEU A 606 -1  O  ALA A 605   N  ARG A 589           
SHEET    1  AR 4 MET A 593  THR A 595  0                                        
SHEET    2  AR 4 HIS A 600  LEU A 603 -1  O  TYR A 601   N  THR A 594           
SHEET    3  AR 4 ALA A 610  PHE A 614 -1  O  PHE A 614   N  LEU A 602           
SHEET    4  AR 4 LYS A 627  THR A 630 -1  O  LYS A 627   N  TYR A 613           
SHEET    1  AS 2 PHE A 641  ARG A 642  0                                        
SHEET    2  AS 2 THR A 647  ASN A 648 -1  O  ASN A 648   N  PHE A 641           
SHEET    1  AT 2 TYR A 660  SER A 661  0                                        
SHEET    2  AT 2 LEU A 666  VAL A 667 -1  O  VAL A 667   N  TYR A 660           
SHEET    1  AU 2 SER A 720  GLN A 727  0                                        
SHEET    2  AU 2 CYS A 732  GLN A 743 -1  O  CYS A 732   N  GLN A 727           
SHEET    1  AV 2 THR A 749  ALA A 751  0                                        
SHEET    2  AV 2 CYS A 732  GLN A 743  1  O  VAL A 742   N  THR A 750           
SHEET    1  AW 5 SER A 762  VAL A 765  0                                        
SHEET    2  AW 5 VAL A 801  GLN A 806  1  O  LEU A 802   N  SER A 762           
SHEET    3  AW 5 GLU A 785  ASP A 795 -1  O  LEU A 791   N  HIS A 805           
SHEET    4  AW 5 CYS A 732  GLN A 743 -1  O  PHE A 733   N  ILE A 794           
SHEET    5  AW 5 THR A 749  ALA A 751  1  O  THR A 750   N  VAL A 742           
SHEET    1  AX 5 SER A 762  VAL A 765  0                                        
SHEET    2  AX 5 VAL A 801  GLN A 806  1  O  LEU A 802   N  SER A 762           
SHEET    3  AX 5 GLU A 785  ASP A 795 -1  O  LEU A 791   N  HIS A 805           
SHEET    4  AX 5 CYS A 732  GLN A 743 -1  O  PHE A 733   N  ILE A 794           
SHEET    5  AX 5 SER A 720  GLN A 727 -1  O  SER A 720   N  SER A 738           
SHEET    1  AY 4 GLU A 811  CYS A 819  0                                        
SHEET    2  AY 4 TYR A 828  MET A 835 -1  O  TYR A 828   N  CYS A 819           
SHEET    3  AY 4 GLY A 846  TYR A 853 -1  O  ARG A 847   N  THR A 833           
SHEET    4  AY 4 LEU A 858  VAL A 866 -1  O  GLN A 859   N  GLN A 852           
SHEET    1  AZ 4 VAL A 870  PHE A 876  0                                        
SHEET    2  AZ 4 LYS A 879  ILE A 884 -1  O  LYS A 879   N  PHE A 876           
SHEET    3  AZ 4 THR A 887  TRP A 893 -1  O  THR A 887   N  ILE A 884           
SHEET    4  AZ 4 LEU A 899  HIS A 905 -1  O  ARG A 900   N  GLU A 892           
SHEET    1  A0 4 ALA A 911  LYS A 917  0                                        
SHEET    2  A0 4 PHE A 920  ASP A 925 -1  O  PHE A 920   N  LYS A 917           
SHEET    3  A0 4 VAL A 930  LYS A 936 -1  O  LEU A 931   N  VAL A 923           
SHEET    4  A0 4 ASN A 941  ARG A 947 -1  O  ASN A 941   N  LYS A 936           
SHEET    1  A1 4 MET A 954  ILE A 959  0                                        
SHEET    2  A1 4 ASN A 964  GLU A 969 -1  O  LEU A 966   N  GLU A 958           
SHEET    3  A1 4 ASN A 973  LYS A 979 -1  O  ASN A 973   N  GLU A 969           
SHEET    4  A1 4 LEU A 992  HIS A 999 -1  O  GLN A 993   N  GLN A 978           
SHEET    1  A2 2 PHE A1076  HIS A1077  0                                        
SHEET    2  A2 2 THR A1082  GLU A1083 -1  O  GLU A1083   N  PHE A1076           
SHEET    1  BA 4 LYS B 138  ALA B 143  0                                        
SHEET    2  BA 4 ASN B 448  ASN B 453 -1  O  ILE B 449   N  ALA B 143           
SHEET    3  BA 4 LEU B 441  MET B 445 -1  O  LEU B 441   N  TRP B 452           
SHEET    4  BA 4 ILE B 429  PHE B 434 -1  N  SER B 430   O  GLY B 444           
SHEET    1  BB 4 VAL B 150  TRP B 155  0                                        
SHEET    2  BB 4 THR B 162  SER B 167 -1  O  ALA B 164   N  GLU B 154           
SHEET    3  BB 4 ILE B 172  ASP B 176 -1  O  ILE B 173   N  VAL B 165           
SHEET    4  BB 4 THR B 183  ILE B 186 -1  O  SER B 184   N  LEU B 174           
SHEET    1  BC 4 ILE B 195  PHE B 200  0                                        
SHEET    2  BC 4 GLN B 207  SER B 212 -1  O  PHE B 209   N  LYS B 199           
SHEET    3  BC 4 ALA B 216  ASP B 221 -1  O  ALA B 216   N  SER B 212           
SHEET    4  BC 4 VAL B 226  VAL B 229 -1  N  ILE B 227   O  LEU B 219           
SHEET    1  BD 4 TYR B 240  SER B 246  0                                        
SHEET    2  BD 4 MET B 251  ASP B 256 -1  O  MET B 251   N  SER B 246           
SHEET    3  BD 4 ARG B 260  GLY B 265 -1  O  ARG B 260   N  ASP B 256           
SHEET    4  BD 4 GLU B 270  LYS B 275 -1  N  ILE B 271   O  LEU B 263           
SHEET    1  BE 4 VAL B 281  ASN B 287  0                                        
SHEET    2  BE 4 CYS B 290  SER B 298 -1  N  CYS B 290   O  ASN B 287           
SHEET    3  BE 4 THR B 302  ASP B 307 -1  O  THR B 302   N  SER B 298           
SHEET    4  BE 4 ALA B 319  PRO B 322 -1  O  ALA B 319   N  LEU B 305           
SHEET    1  BF 4 VAL B 327  PHE B 332  0                                        
SHEET    2  BF 4 LYS B 339  ASP B 344 -1  O  LEU B 341   N  TYR B 331           
SHEET    3  BF 4 GLU B 348  SER B 353 -1  O  GLU B 348   N  ASP B 344           
SHEET    4  BF 4 GLN B 362  ILE B 365 -1  O  GLN B 362   N  VAL B 351           
SHEET    1  BG 4 THR B 380  TRP B 381  0                                        
SHEET    2  BG 4 LEU B 387  GLY B 391 -1  O  VAL B 389   N  THR B 380           
SHEET    3  BG 4 ILE B 406  ASP B 410 -1  O  ASP B 407   N  ALA B 390           
SHEET    4  BG 4 LEU B 416  LEU B 420 -1  N  VAL B 417   O  ILE B 408           
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 VAL C 164  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 VAL C 164  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  VAL C 212 -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  GLY C 393 -1  O  SER C 386   N  SER C 379           
SHEET    4  CK 4 LYS C 709  PRO C 716 -1  O  LYS C 709   N  GLY C 393           
SHEET    1  CL 4 ILE C 396  SER C 401  0                                        
SHEET    2  CL 4 LEU C 699  ILE C 704 -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           
SHEET    1  EA 2 GLU E 676  LEU E 677  0                                        
SHEET    2  EA 2 LYS F  26  TRP F  33 -1  N  TRP F  27   O  GLU E 676           
SHEET    1  EB 2 ASN E 680  THR E 683  0                                        
SHEET    2  EB 2 LYS F  26  TRP F  33  1  O  ALA F  29   N  ASN E 680           
SHEET    1  EC 4 ILE E 821  LYS E 822  0                                        
SHEET    2  EC 4 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  EC 4 LEU E 721  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  EC 4 PHE F  22  VAL F  24  1  O  GLU F  23   N  LYS E 733           
SHEET    1  ED 5 ILE E 821  LYS E 822  0                                        
SHEET    2  ED 5 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  ED 5 LEU E 721  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  ED 5 LYS F  26  TRP F  33 -1  N  LYS F  26   O  VAL E 731           
SHEET    5  ED 5 ASN E 680  THR E 683  1  O  ASN E 680   N  ALA F  31           
SHEET    1  FA 2 PHE F  22  VAL F  24  0                                        
SHEET    2  FA 2 LEU E 721  ALA E 734  1  O  LYS E 733   N  GLU F  23           
SHEET    1  EE 5 ILE E 821  LYS E 822  0                                        
SHEET    2  EE 5 GLU E 742  SER E 746  1  O  GLU E 742   N  ILE E 821           
SHEET    3  EE 5 LEU E 721  ALA E 734 -1  O  CYS E 730   N  VAL E 745           
SHEET    4  EE 5 LYS F  26  TRP F  33 -1  N  LYS F  26   O  VAL E 731           
SHEET    5  EE 5 GLU E 676  LEU E 677 -1  O  GLU E 676   N  TRP F  27           
SHEET    1  EF 3 PHE E 762  SER E 763  0                                        
SHEET    2  EF 3 LYS E 807  CYS E 810 -1  O  PHE E 808   N  PHE E 762           
SHEET    3  EF 3 LEU E 793  LYS E 795 -1  O  ALA E 794   N  ILE E 809           
SHEET    1  EG 3 THR E 863  SER E 865  0                                        
SHEET    2  EG 3 GLN E 908  ASN E 910 -1  O  TYR E 909   N  LEU E 864           
SHEET    3  EG 3 GLU E 900  ARG E 901 -1  O  GLU E 900   N  ASN E 910           
SHEET    1  HA 2 GLU H 676  LEU H 677  0                                        
SHEET    2  HA 2 LYS I  26  TRP I  35 -1  N  TRP I  27   O  GLU H 676           
SHEET    1  HB 2 ASN H 680  THR H 683  0                                        
SHEET    2  HB 2 LYS I  26  TRP I  35  1  O  ALA I  29   N  ASN H 680           
SHEET    1  HC 4 ILE H 821  LYS H 822  0                                        
SHEET    2  HC 4 GLU H 742  SER H 746  1  O  GLU H 742   N  ILE H 821           
SHEET    3  HC 4 ARG H 719  ALA H 734 -1  O  CYS H 730   N  VAL H 745           
SHEET    4  HC 4 PHE I  22  VAL I  24  1  O  GLU I  23   N  LYS H 733           
SHEET    1  HD 5 ILE H 821  LYS H 822  0                                        
SHEET    2  HD 5 GLU H 742  SER H 746  1  O  GLU H 742   N  ILE H 821           
SHEET    3  HD 5 ARG H 719  ALA H 734 -1  O  CYS H 730   N  VAL H 745           
SHEET    4  HD 5 LYS I  26  TRP I  35 -1  N  LYS I  26   O  VAL H 731           
SHEET    5  HD 5 ASN H 680  THR H 683  1  O  ASN H 680   N  ALA I  31           
SHEET    1  IA 2 PHE I  22  VAL I  24  0                                        
SHEET    2  IA 2 ARG H 719  ALA H 734  1  O  LYS H 733   N  GLU I  23           
SHEET    1  HE 5 ILE H 821  LYS H 822  0                                        
SHEET    2  HE 5 GLU H 742  SER H 746  1  O  GLU H 742   N  ILE H 821           
SHEET    3  HE 5 ARG H 719  ALA H 734 -1  O  CYS H 730   N  VAL H 745           
SHEET    4  HE 5 LYS I  26  TRP I  35 -1  N  LYS I  26   O  VAL H 731           
SHEET    5  HE 5 GLU H 676  LEU H 677 -1  O  GLU H 676   N  TRP I  27           
SHEET    1  HF 3 PHE H 762  SER H 763  0                                        
SHEET    2  HF 3 LYS H 807  CYS H 810 -1  O  PHE H 808   N  PHE H 762           
SHEET    3  HF 3 LEU H 793  LYS H 795 -1  O  ALA H 794   N  ILE H 809           
SHEET    1  HG 3 THR H 863  SER H 865  0                                        
SHEET    2  HG 3 GLN H 908  ASN H 910 -1  O  TYR H 909   N  LEU H 864           
SHEET    3  HG 3 GLU H 900  ARG H 901 -1  O  GLU H 900   N  ASN H 910           
LINK         O3'  DT R   8                 P   3DR R   9     1555   1555  1.60  
LINK         O3' 3DR R   9                 P    DA R  10     1555   1555  1.61  
LINK         O3'  DT T   8                 P   3DR T   9     1555   1555  1.60  
LINK         O3' 3DR T   9                 P    DA T  10     1555   1555  1.61  
CISPEP   1 GLU A  224    PRO A  225          0        11.76                     
CISPEP   2 GLY A  357    PRO A  358          0        -5.20                     
CISPEP   3 GLU C  224    PRO C  225          0        11.89                     
CISPEP   4 GLY C  357    PRO C  358          0        -5.26                     
CRYST1  130.800  155.840  255.390  90.00  94.17  90.00 P 1 21 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      0.007645  0.000000  0.000557        0.00000                         
SCALE2      0.000000  0.006417  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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