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Database: PDB
Entry: 6PY8
LinkDB: 6PY8
Original site: 6PY8 
HEADER    DNA BINDING PROTEIN/DNA                 29-JUL-19   6PY8              
TITLE     CRYSTAL STRUCTURE OF THE RBPJ-NOTCH1-NRARP TERNARY COMPLEX BOUND TO   
TITLE    2 DNA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NOTCH-REGULATED ANKYRIN REPEAT-CONTAINING PROTEIN;         
COMPND   3 CHAIN: B, G;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DNA;                                                       
COMPND   7 CHAIN: A, X;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: DNA;                                                       
COMPND  11 CHAIN: D, Y;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS;        
COMPND  15 CHAIN: C, E;                                                         
COMPND  16 SYNONYM: CBF-1,J KAPPA-RECOMBINATION SIGNAL-BINDING PROTEIN,RBP-J    
COMPND  17 KAPPA,RBP-JK,RENAL CARCINOMA ANTIGEN NY-REN-30;                      
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND  21 CHAIN: F, K;                                                         
COMPND  22 SYNONYM: HN1,TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;           
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NRARP;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 GENE: RBPJ, IGKJRB, IGKJRB1, RBPJK, RBPSUH;                          
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 MOL_ID: 5;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 GENE: NOTCH1, TAN1;                                                  
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NOTCH1, NRARP, RBPJ, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.JARRETT,T.C.M.SEEGAR,S.C.BLACKLOW                                 
REVDAT   4   26-FEB-20 6PY8    1       JRNL                                     
REVDAT   3   18-DEC-19 6PY8    1       REMARK                                   
REVDAT   2   04-SEP-19 6PY8    1       COMPND REMARK DBREF  SEQRES              
REVDAT   2 2                   1       HELIX  SHEET  CRYST1 ATOM                
REVDAT   1   14-AUG-19 6PY8    0                                                
JRNL        AUTH   S.M.JARRETT,T.C.M.SEEGAR,M.ANDREWS,G.ADELMANT,J.A.MARTO,     
JRNL        AUTH 2 J.C.ASTER,S.C.BLACKLOW                                       
JRNL        TITL   EXTENSION OF THE NOTCH INTRACELLULAR DOMAIN ANKYRIN REPEAT   
JRNL        TITL 2 STACK BY NRARP PROMOTES FEEDBACK INHIBITION OF NOTCH         
JRNL        TITL 3 SIGNALING.                                                   
JRNL        REF    SCI.SIGNAL.                   V.  12       2019              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   31690634                                                     
JRNL        DOI    10.1126/SCISIGNAL.AAY2369                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472: ???)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26212                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.270                           
REMARK   3   R VALUE            (WORKING SET) : 0.267                           
REMARK   3   FREE R VALUE                     : 0.315                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.620                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 49.0125 -  9.0309    0.98     1855   154  0.2163 0.2357        
REMARK   3     2  9.0309 -  7.1754    1.00     1789   146  0.2259 0.2633        
REMARK   3     3  7.1754 -  6.2704    1.00     1765   147  0.2839 0.3499        
REMARK   3     4  6.2704 -  5.6981    1.00     1719   141  0.2807 0.3440        
REMARK   3     5  5.6981 -  5.2902    1.00     1746   144  0.2795 0.3701        
REMARK   3     6  5.2902 -  4.9786    1.00     1734   144  0.2671 0.3239        
REMARK   3     7  4.9786 -  4.7295    1.00     1718   141  0.2591 0.3318        
REMARK   3     8  4.7295 -  4.5237    1.00     1720   143  0.2692 0.2877        
REMARK   3     9  4.5237 -  4.3497    0.99     1710   140  0.2898 0.3569        
REMARK   3    10  4.3497 -  4.1997    1.00     1684   140  0.2874 0.3663        
REMARK   3    11  4.1997 -  4.0684    1.00     1737   143  0.3025 0.3308        
REMARK   3    12  4.0684 -  3.9522    1.00     1688   140  0.3191 0.3827        
REMARK   3    13  3.9522 -  3.8482    1.00     1698   139  0.3457 0.3792        
REMARK   3    14  3.8482 -  3.7543    0.96     1651   136  0.3642 0.4135        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          13699                                  
REMARK   3   ANGLE     :  0.573          18813                                  
REMARK   3   CHIRALITY :  0.040           2089                                  
REMARK   3   PLANARITY :  0.004           2246                                  
REMARK   3   DIHEDRAL  : 12.389           8045                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6PY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26271                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.754                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.460                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2F8X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 6.8, 200 MM SODIUM        
REMARK 280  FLUORIDE, 18% PEG 3350, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.94000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      150.71000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.82500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      150.71000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.94000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.82500            
REMARK 290   SMTRY3   4  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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, D, E, F                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, X, Y, C, K                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     CYS B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     LYS B   108                                                      
REMARK 465     TYR B   109                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     ALA B   111                                                      
REMARK 465     SER B   112                                                      
REMARK 465     GLY B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     GLN G     3                                                      
REMARK 465     ALA G     4                                                      
REMARK 465     GLU G     5                                                      
REMARK 465     LEU G     6                                                      
REMARK 465     SER G     7                                                      
REMARK 465     THR G     8                                                      
REMARK 465     CYS G     9                                                      
REMARK 465     SER G    10                                                      
REMARK 465     ALA G    11                                                      
REMARK 465     PRO G    12                                                      
REMARK 465     GLN G    13                                                      
REMARK 465     THR G    14                                                      
REMARK 465     GLN G    15                                                      
REMARK 465     ARG G    16                                                      
REMARK 465     ILE G    17                                                      
REMARK 465     MET G    37                                                      
REMARK 465     THR G    38                                                      
REMARK 465     ASN G    39                                                      
REMARK 465     CYS G    40                                                      
REMARK 465     GLU G    41                                                      
REMARK 465     PHE G    42                                                      
REMARK 465     ASN G    43                                                      
REMARK 465     TYR G   109                                                      
REMARK 465     ALA G   110                                                      
REMARK 465     ALA G   111                                                      
REMARK 465     SER G   112                                                      
REMARK 465     GLY G   113                                                      
REMARK 465     ARG G   114                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     CYS C   440                                                      
REMARK 465     SER C   441                                                      
REMARK 465     ALA C   442                                                      
REMARK 465     ALA C   443                                                      
REMARK 465     GLY C   444                                                      
REMARK 465     ALA C   445                                                      
REMARK 465     ILE C   446                                                      
REMARK 465     LEU C   447                                                      
REMARK 465     ARG C   448                                                      
REMARK 465     ALA C   449                                                      
REMARK 465     ASN C   450                                                      
REMARK 465     SER C   451                                                      
REMARK 465     SER C   452                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     GLU E    10                                                      
REMARK 465     ALA E   442                                                      
REMARK 465     ALA E   443                                                      
REMARK 465     GLY E   444                                                      
REMARK 465     ALA E   445                                                      
REMARK 465     ILE E   446                                                      
REMARK 465     LEU E   447                                                      
REMARK 465     ARG E   448                                                      
REMARK 465     ALA E   449                                                      
REMARK 465     ASN E   450                                                      
REMARK 465     SER E   451                                                      
REMARK 465     SER E   452                                                      
REMARK 465     ALA F  1779                                                      
REMARK 465     SER F  1780                                                      
REMARK 465     LYS F  1781                                                      
REMARK 465     LYS F  1782                                                      
REMARK 465     LYS F  1783                                                      
REMARK 465     ARG F  1784                                                      
REMARK 465     ARG F  1785                                                      
REMARK 465     GLU F  1786                                                      
REMARK 465     PRO F  1787                                                      
REMARK 465     LEU F  1788                                                      
REMARK 465     GLY F  1789                                                      
REMARK 465     GLU F  1790                                                      
REMARK 465     ASP F  1791                                                      
REMARK 465     SER F  1792                                                      
REMARK 465     VAL F  1793                                                      
REMARK 465     GLY F  1794                                                      
REMARK 465     LEU F  1795                                                      
REMARK 465     LYS F  1796                                                      
REMARK 465     PRO F  1797                                                      
REMARK 465     LEU F  1798                                                      
REMARK 465     LYS F  1799                                                      
REMARK 465     ASN F  1800                                                      
REMARK 465     ALA F  1801                                                      
REMARK 465     SER F  1802                                                      
REMARK 465     ASP F  1803                                                      
REMARK 465     GLY F  1804                                                      
REMARK 465     ALA F  1805                                                      
REMARK 465     LEU F  1806                                                      
REMARK 465     MET F  1807                                                      
REMARK 465     ASP F  1808                                                      
REMARK 465     ASP F  1809                                                      
REMARK 465     ASN F  1810                                                      
REMARK 465     GLN F  1811                                                      
REMARK 465     ASN F  1812                                                      
REMARK 465     GLU F  1813                                                      
REMARK 465     TRP F  1814                                                      
REMARK 465     GLY F  1815                                                      
REMARK 465     ASP F  1816                                                      
REMARK 465     GLU F  1817                                                      
REMARK 465     ASP F  1818                                                      
REMARK 465     LEU F  1819                                                      
REMARK 465     GLU F  1820                                                      
REMARK 465     THR F  1821                                                      
REMARK 465     LYS F  1822                                                      
REMARK 465     LYS F  1823                                                      
REMARK 465     PHE F  1824                                                      
REMARK 465     ARG F  1825                                                      
REMARK 465     PHE F  1826                                                      
REMARK 465     GLU F  1827                                                      
REMARK 465     GLU F  1828                                                      
REMARK 465     PRO F  1829                                                      
REMARK 465     VAL F  1830                                                      
REMARK 465     VAL F  1831                                                      
REMARK 465     LEU F  1832                                                      
REMARK 465     PRO F  1833                                                      
REMARK 465     ASP F  1834                                                      
REMARK 465     LEU F  1835                                                      
REMARK 465     ASP F  1836                                                      
REMARK 465     ASP F  1837                                                      
REMARK 465     GLN F  1838                                                      
REMARK 465     THR F  1839                                                      
REMARK 465     ASP F  1840                                                      
REMARK 465     HIS F  1841                                                      
REMARK 465     ARG F  1842                                                      
REMARK 465     GLN F  1843                                                      
REMARK 465     TRP F  1844                                                      
REMARK 465     THR F  1845                                                      
REMARK 465     GLN F  1846                                                      
REMARK 465     GLN F  1847                                                      
REMARK 465     HIS F  1848                                                      
REMARK 465     LEU F  1849                                                      
REMARK 465     ASP F  1850                                                      
REMARK 465     ALA F  1851                                                      
REMARK 465     ALA F  1852                                                      
REMARK 465     ASP F  1853                                                      
REMARK 465     LEU F  1854                                                      
REMARK 465     ARG F  1855                                                      
REMARK 465     MET F  1856                                                      
REMARK 465     SER F  1857                                                      
REMARK 465     ALA F  1858                                                      
REMARK 465     MET F  1859                                                      
REMARK 465     ALA F  1860                                                      
REMARK 465     PRO F  1861                                                      
REMARK 465     THR F  1862                                                      
REMARK 465     PRO F  1863                                                      
REMARK 465     PRO F  1864                                                      
REMARK 465     GLN F  1865                                                      
REMARK 465     GLY F  1866                                                      
REMARK 465     GLU F  1867                                                      
REMARK 465     VAL F  1868                                                      
REMARK 465     ASP F  1869                                                      
REMARK 465     ALA F  1870                                                      
REMARK 465     ASP F  1871                                                      
REMARK 465     CYS F  1872                                                      
REMARK 465     MET F  1873                                                      
REMARK 465     ASP F  1874                                                      
REMARK 465     GLY F  1893                                                      
REMARK 465     GLY F  1894                                                      
REMARK 465     GLY F  1895                                                      
REMARK 465     LEU F  1896                                                      
REMARK 465     GLU F  1897                                                      
REMARK 465     THR F  1898                                                      
REMARK 465     GLY F  1899                                                      
REMARK 465     ASN F  1900                                                      
REMARK 465     SER F  1901                                                      
REMARK 465     GLU F  1902                                                      
REMARK 465     GLU F  1903                                                      
REMARK 465     ARG F  2121                                                      
REMARK 465     SER F  2122                                                      
REMARK 465     PRO F  2123                                                      
REMARK 465     GLN F  2124                                                      
REMARK 465     LEU F  2125                                                      
REMARK 465     HIS F  2126                                                      
REMARK 465     GLY F  2127                                                      
REMARK 465     ALA F  2128                                                      
REMARK 465     ALA K  1779                                                      
REMARK 465     SER K  1780                                                      
REMARK 465     LYS K  1781                                                      
REMARK 465     LYS K  1782                                                      
REMARK 465     LYS K  1783                                                      
REMARK 465     ARG K  1784                                                      
REMARK 465     ARG K  1785                                                      
REMARK 465     GLU K  1786                                                      
REMARK 465     PRO K  1787                                                      
REMARK 465     LEU K  1788                                                      
REMARK 465     GLY K  1789                                                      
REMARK 465     GLU K  1790                                                      
REMARK 465     ASP K  1791                                                      
REMARK 465     SER K  1792                                                      
REMARK 465     VAL K  1793                                                      
REMARK 465     GLY K  1794                                                      
REMARK 465     LEU K  1795                                                      
REMARK 465     LYS K  1796                                                      
REMARK 465     PRO K  1797                                                      
REMARK 465     LEU K  1798                                                      
REMARK 465     LYS K  1799                                                      
REMARK 465     ASN K  1800                                                      
REMARK 465     ALA K  1801                                                      
REMARK 465     SER K  1802                                                      
REMARK 465     ASP K  1803                                                      
REMARK 465     GLY K  1804                                                      
REMARK 465     ALA K  1805                                                      
REMARK 465     LEU K  1806                                                      
REMARK 465     MET K  1807                                                      
REMARK 465     ASP K  1808                                                      
REMARK 465     ASP K  1809                                                      
REMARK 465     ASN K  1810                                                      
REMARK 465     GLN K  1811                                                      
REMARK 465     ASN K  1812                                                      
REMARK 465     GLU K  1813                                                      
REMARK 465     TRP K  1814                                                      
REMARK 465     GLY K  1815                                                      
REMARK 465     ASP K  1816                                                      
REMARK 465     GLU K  1817                                                      
REMARK 465     ASP K  1818                                                      
REMARK 465     LEU K  1819                                                      
REMARK 465     GLU K  1820                                                      
REMARK 465     THR K  1821                                                      
REMARK 465     LYS K  1822                                                      
REMARK 465     LYS K  1823                                                      
REMARK 465     PHE K  1824                                                      
REMARK 465     ARG K  1825                                                      
REMARK 465     PHE K  1826                                                      
REMARK 465     GLU K  1827                                                      
REMARK 465     GLU K  1828                                                      
REMARK 465     PRO K  1829                                                      
REMARK 465     VAL K  1830                                                      
REMARK 465     VAL K  1831                                                      
REMARK 465     LEU K  1832                                                      
REMARK 465     PRO K  1833                                                      
REMARK 465     ASP K  1834                                                      
REMARK 465     LEU K  1835                                                      
REMARK 465     ASP K  1836                                                      
REMARK 465     ASP K  1837                                                      
REMARK 465     GLN K  1838                                                      
REMARK 465     THR K  1839                                                      
REMARK 465     ASP K  1840                                                      
REMARK 465     HIS K  1841                                                      
REMARK 465     ARG K  1842                                                      
REMARK 465     GLN K  1843                                                      
REMARK 465     TRP K  1844                                                      
REMARK 465     THR K  1845                                                      
REMARK 465     GLN K  1846                                                      
REMARK 465     GLN K  1847                                                      
REMARK 465     HIS K  1848                                                      
REMARK 465     LEU K  1849                                                      
REMARK 465     ASP K  1850                                                      
REMARK 465     ALA K  1851                                                      
REMARK 465     ALA K  1852                                                      
REMARK 465     ASP K  1853                                                      
REMARK 465     LEU K  1854                                                      
REMARK 465     ARG K  1855                                                      
REMARK 465     MET K  1856                                                      
REMARK 465     SER K  1857                                                      
REMARK 465     ALA K  1858                                                      
REMARK 465     MET K  1859                                                      
REMARK 465     ALA K  1860                                                      
REMARK 465     PRO K  1861                                                      
REMARK 465     THR K  1862                                                      
REMARK 465     PRO K  1863                                                      
REMARK 465     PRO K  1864                                                      
REMARK 465     GLN K  1865                                                      
REMARK 465     GLY K  1866                                                      
REMARK 465     GLU K  1867                                                      
REMARK 465     VAL K  1868                                                      
REMARK 465     ASP K  1869                                                      
REMARK 465     ALA K  1870                                                      
REMARK 465     ASP K  1871                                                      
REMARK 465     CYS K  1872                                                      
REMARK 465     MET K  1873                                                      
REMARK 465     ASP K  1874                                                      
REMARK 465     GLY K  1894                                                      
REMARK 465     GLY K  1895                                                      
REMARK 465     LEU K  1896                                                      
REMARK 465     GLU K  1897                                                      
REMARK 465     THR K  1898                                                      
REMARK 465     GLY K  1899                                                      
REMARK 465     ASN K  1900                                                      
REMARK 465     ARG K  2121                                                      
REMARK 465     SER K  2122                                                      
REMARK 465     PRO K  2123                                                      
REMARK 465     GLN K  2124                                                      
REMARK 465     LEU K  2125                                                      
REMARK 465     HIS K  2126                                                      
REMARK 465     GLY K  2127                                                      
REMARK 465     ALA K  2128                                                      
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     GLN B  13    CG   CD   OE1  NE2                                  
REMARK 470     THR B  14    OG1  CG2                                            
REMARK 470     GLN B  15    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  17    CG1  CG2  CD1                                       
REMARK 470     PHE B  18    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B  19    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  20    CG   CD   OE1  OE2                                  
REMARK 470     VAL B  22    CG1  CG2                                            
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     ASN B  26    CG   OD1  ND2                                       
REMARK 470     THR B  27    OG1  CG2                                            
REMARK 470     GLN B  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  30    CG   CD1  CD2                                       
REMARK 470     GLN B  31    CG   CD   OE1  NE2                                  
REMARK 470     SER B  32    OG                                                  
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     LEU B  34    CG   CD1  CD2                                       
REMARK 470     GLN B  35    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  36    CG   OD1  ND2                                       
REMARK 470     MET B  37    CG   SD   CE                                        
REMARK 470     THR B  38    OG1  CG2                                            
REMARK 470     ASN B  39    CG   OD1  ND2                                       
REMARK 470     CYS B  40    SG                                                  
REMARK 470     GLU B  41    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  42    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B  43    CG   OD1  ND2                                       
REMARK 470     PHE G  18    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN G  19    CG   CD   OE1  NE2                                  
REMARK 470     GLU G  20    CG   CD   OE1  OE2                                  
REMARK 470     VAL G  22    CG1  CG2                                            
REMARK 470     ARG G  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  24    CG   CD   CE   NZ                                   
REMARK 470     ASN G  26    CG   OD1  ND2                                       
REMARK 470     THR G  27    CB   OG1  CG2                                       
REMARK 470     GLN G  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU G  29    CG   CD   OE1  OE2                                  
REMARK 470     LEU G  30    CG   CD1  CD2                                       
REMARK 470     GLN G  31    CG   CD   OE1  NE2                                  
REMARK 470     SER G  32    OG                                                  
REMARK 470     LEU G  33    CG   CD1  CD2                                       
REMARK 470     LEU G  34    CG   CD1  CD2                                       
REMARK 470     GLN G  35    CG   CD   OE1  NE2                                  
REMARK 470     ASN G  36    CG   OD1  ND2                                       
REMARK 470     VAL F1910    CG1  CG2                                            
REMARK 470     ILE F1911    CG1  CG2  CD1                                       
REMARK 470     SER F1912    OG                                                  
REMARK 470     ASP F1913    CG   OD1  OD2                                       
REMARK 470     PHE F1914    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE F1915    CG1  CG2  CD1                                       
REMARK 470     VAL K1910    CG1  CG2                                            
REMARK 470     ILE K1911    CG1  CG2  CD1                                       
REMARK 470     SER K1912    OG                                                  
REMARK 470     ASP K1913    CG   OD1  OD2                                       
REMARK 470     PHE K1914    CG   CD1  CD2  CE1  CE2  CZ                         
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    THR B  38     -152.10     59.58                                   
REMARK 500    VAL B  44     -137.62     40.44                                   
REMARK 500    ASN B  45      108.86    -53.51                                   
REMARK 500    ARG G  23     -122.07     58.86                                   
REMARK 500    LEU G  30     -158.67   -100.15                                   
REMARK 500    LYS C  50       58.80   -154.33                                   
REMARK 500    ASN C 135       31.98    -86.26                                   
REMARK 500    SER C 136       -0.03     66.52                                   
REMARK 500    LYS C 156     -177.68    -68.74                                   
REMARK 500    ASP C 164        1.08     81.06                                   
REMARK 500    ALA C 198       49.55   -108.06                                   
REMARK 500    ASP C 214       69.11   -102.31                                   
REMARK 500    GLN C 256       46.52     38.55                                   
REMARK 500    SER C 267     -166.62    -79.81                                   
REMARK 500    ARG C 281     -136.31     60.31                                   
REMARK 500    MET C 282       81.93     55.81                                   
REMARK 500    GLU C 289      -13.77     71.65                                   
REMARK 500    VAL C 337       36.09    -96.07                                   
REMARK 500    ASN C 367       44.19    -80.29                                   
REMARK 500    LYS E  50       58.18   -155.84                                   
REMARK 500    GLN E  96       35.28    -99.03                                   
REMARK 500    GLU E  97      133.96     61.51                                   
REMARK 500    ASN E 135       31.69    -85.48                                   
REMARK 500    SER E 136       -0.23     66.19                                   
REMARK 500    ASP E 164        8.61   -154.45                                   
REMARK 500    ALA E 198       47.95   -106.79                                   
REMARK 500    GLU E 215     -156.77   -145.35                                   
REMARK 500    GLU E 219      -10.87     70.08                                   
REMARK 500    GLN E 256       43.03     37.98                                   
REMARK 500    SER E 267     -167.75    -78.90                                   
REMARK 500    GLU E 280     -105.99     52.45                                   
REMARK 500    MET E 282      101.29    -45.26                                   
REMARK 500    GLN E 288      -88.97     51.33                                   
REMARK 500    CYS E 299       57.41   -146.74                                   
REMARK 500    VAL E 337       36.85    -96.04                                   
REMARK 500    ASN E 367       42.91    -80.48                                   
REMARK 500    PRO E 436     -100.83    -78.02                                   
REMARK 500    ARG F1760      -35.02   -132.76                                   
REMARK 500    ASN F1876       77.86     53.76                                   
REMARK 500    ASP F1881     -107.63     58.99                                   
REMARK 500    GLN F1917     -155.78     57.62                                   
REMARK 500    ARG F1927      -65.69    -91.96                                   
REMARK 500    ASP F1990       30.35    -98.54                                   
REMARK 500    ASN F2051       31.06    -95.89                                   
REMARK 500    MET F2106       66.14     60.69                                   
REMARK 500    GLU F2116      -51.19   -129.75                                   
REMARK 500    ARG K1760      -34.77   -131.31                                   
REMARK 500    GLU K1905       33.00    -85.15                                   
REMARK 500    GLN K1917     -155.53   -109.25                                   
REMARK 500    ARG K1927      -66.26    -91.78                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6PY8 B    1   114  UNP    Q7Z6K4   NRARP_HUMAN      1    114             
DBREF  6PY8 G    1   114  UNP    Q7Z6K4   NRARP_HUMAN      1    114             
DBREF  6PY8 A    1    16  PDB    6PY8     6PY8             1     16             
DBREF  6PY8 X    1    16  PDB    6PY8     6PY8             1     16             
DBREF  6PY8 D  101   116  PDB    6PY8     6PY8           101    116             
DBREF  6PY8 Y  101   116  PDB    6PY8     6PY8           101    116             
DBREF  6PY8 C    9   452  UNP    Q06330   SUH_HUMAN       23    466             
DBREF  6PY8 E    9   452  UNP    Q06330   SUH_HUMAN       23    466             
DBREF  6PY8 F 1759  2128  UNP    P46531   NOTC1_HUMAN   1759   2127             
DBREF  6PY8 K 1759  2128  UNP    P46531   NOTC1_HUMAN   1759   2127             
SEQRES   1 B  114  MET SER GLN ALA GLU LEU SER THR CYS SER ALA PRO GLN          
SEQRES   2 B  114  THR GLN ARG ILE PHE GLN GLU ALA VAL ARG LYS GLY ASN          
SEQRES   3 B  114  THR GLN GLU LEU GLN SER LEU LEU GLN ASN MET THR ASN          
SEQRES   4 B  114  CYS GLU PHE ASN VAL ASN SER PHE GLY PRO GLU GLY GLN          
SEQRES   5 B  114  THR ALA LEU HIS GLN SER VAL ILE ASP GLY ASN LEU GLU          
SEQRES   6 B  114  LEU VAL LYS LEU LEU VAL LYS PHE GLY ALA ASP ILE ARG          
SEQRES   7 B  114  LEU ALA ASN ARG ASP GLY TRP SER ALA LEU HIS ILE ALA          
SEQRES   8 B  114  ALA PHE GLY GLY HIS GLN ASP ILE VAL LEU TYR LEU ILE          
SEQRES   9 B  114  THR LYS ALA LYS TYR ALA ALA SER GLY ARG                      
SEQRES   1 G  114  MET SER GLN ALA GLU LEU SER THR CYS SER ALA PRO GLN          
SEQRES   2 G  114  THR GLN ARG ILE PHE GLN GLU ALA VAL ARG LYS GLY ASN          
SEQRES   3 G  114  THR GLN GLU LEU GLN SER LEU LEU GLN ASN MET THR ASN          
SEQRES   4 G  114  CYS GLU PHE ASN VAL ASN SER PHE GLY PRO GLU GLY GLN          
SEQRES   5 G  114  THR ALA LEU HIS GLN SER VAL ILE ASP GLY ASN LEU GLU          
SEQRES   6 G  114  LEU VAL LYS LEU LEU VAL LYS PHE GLY ALA ASP ILE ARG          
SEQRES   7 G  114  LEU ALA ASN ARG ASP GLY TRP SER ALA LEU HIS ILE ALA          
SEQRES   8 G  114  ALA PHE GLY GLY HIS GLN ASP ILE VAL LEU TYR LEU ILE          
SEQRES   9 G  114  THR LYS ALA LYS TYR ALA ALA SER GLY ARG                      
SEQRES   1 A   16   DT  DT  DG  DA  DC  DT  DG  DT  DG  DG  DG  DA  DA          
SEQRES   2 A   16   DA  DG  DA                                                  
SEQRES   1 X   16   DT  DT  DG  DA  DC  DT  DG  DT  DG  DG  DG  DA  DA          
SEQRES   2 X   16   DA  DG  DA                                                  
SEQRES   1 D   16   DA  DA  DT  DC  DT  DT  DT  DC  DC  DC  DA  DC  DA          
SEQRES   2 D   16   DG  DT  DC                                                  
SEQRES   1 Y   16   DA  DA  DT  DC  DT  DT  DT  DC  DC  DC  DA  DC  DA          
SEQRES   2 Y   16   DG  DT  DC                                                  
SEQRES   1 C  444  GLY GLU ARG PRO PRO PRO LYS ARG LEU THR ARG GLU ALA          
SEQRES   2 C  444  MET ARG ASN TYR LEU LYS GLU ARG GLY ASP GLN THR VAL          
SEQRES   3 C  444  LEU ILE LEU HIS ALA LYS VAL ALA GLN LYS SER TYR GLY          
SEQRES   4 C  444  ASN GLU LYS ARG PHE PHE CYS PRO PRO PRO CYS VAL TYR          
SEQRES   5 C  444  LEU MET GLY SER GLY TRP LYS LYS LYS LYS GLU GLN MET          
SEQRES   6 C  444  GLU ARG ASP GLY CYS SER GLU GLN GLU SER GLN PRO CYS          
SEQRES   7 C  444  ALA PHE ILE GLY ILE GLY ASN SER ASP GLN GLU MET GLN          
SEQRES   8 C  444  GLN LEU ASN LEU GLU GLY LYS ASN TYR CYS THR ALA LYS          
SEQRES   9 C  444  THR LEU TYR ILE SER ASP SER ASP LYS ARG LYS HIS PHE          
SEQRES  10 C  444  MET LEU SER VAL LYS MET PHE TYR GLY ASN SER ASP ASP          
SEQRES  11 C  444  ILE GLY VAL PHE LEU SER LYS ARG ILE LYS VAL ILE SER          
SEQRES  12 C  444  LYS PRO SER LYS LYS LYS GLN SER LEU LYS ASN ALA ASP          
SEQRES  13 C  444  LEU CYS ILE ALA SER GLY THR LYS VAL ALA LEU PHE ASN          
SEQRES  14 C  444  ARG LEU ARG SER GLN THR VAL SER THR ARG TYR LEU HIS          
SEQRES  15 C  444  VAL GLU GLY GLY ASN PHE HIS ALA SER SER GLN GLN TRP          
SEQRES  16 C  444  GLY ALA PHE PHE ILE HIS LEU LEU ASP ASP ASP GLU SER          
SEQRES  17 C  444  GLU GLY GLU GLU PHE THR VAL ARG ASP GLY TYR ILE HIS          
SEQRES  18 C  444  TYR GLY GLN THR VAL LYS LEU VAL CYS SER VAL THR GLY          
SEQRES  19 C  444  MET ALA LEU PRO ARG LEU ILE ILE ARG LYS VAL ASP LYS          
SEQRES  20 C  444  GLN THR ALA LEU LEU ASP ALA ASP ASP PRO VAL SER GLN          
SEQRES  21 C  444  LEU HIS LYS CYS ALA PHE TYR LEU LYS ASP THR GLU ARG          
SEQRES  22 C  444  MET TYR LEU CYS LEU SER GLN GLU ARG ILE ILE GLN PHE          
SEQRES  23 C  444  GLN ALA THR PRO CYS PRO LYS GLU PRO ASN LYS GLU MET          
SEQRES  24 C  444  ILE ASN ASP GLY ALA SER TRP THR ILE ILE SER THR ASP          
SEQRES  25 C  444  LYS ALA GLU TYR THR PHE TYR GLU GLY MET GLY PRO VAL          
SEQRES  26 C  444  LEU ALA PRO VAL THR PRO VAL PRO VAL VAL GLU SER LEU          
SEQRES  27 C  444  GLN LEU ASN GLY GLY GLY ASP VAL ALA MET LEU GLU LEU          
SEQRES  28 C  444  THR GLY GLN ASN PHE THR PRO ASN LEU ARG VAL TRP PHE          
SEQRES  29 C  444  GLY ASP VAL GLU ALA GLU THR MET TYR ARG CYS GLY GLU          
SEQRES  30 C  444  SER MET LEU CYS VAL VAL PRO ASP ILE SER ALA PHE ARG          
SEQRES  31 C  444  GLU GLY TRP ARG TRP VAL ARG GLN PRO VAL GLN VAL PRO          
SEQRES  32 C  444  VAL THR LEU VAL ARG ASN ASP GLY ILE ILE TYR SER THR          
SEQRES  33 C  444  SER LEU THR PHE THR TYR THR PRO GLU PRO GLY PRO ARG          
SEQRES  34 C  444  PRO HIS CYS SER ALA ALA GLY ALA ILE LEU ARG ALA ASN          
SEQRES  35 C  444  SER SER                                                      
SEQRES   1 E  444  GLY GLU ARG PRO PRO PRO LYS ARG LEU THR ARG GLU ALA          
SEQRES   2 E  444  MET ARG ASN TYR LEU LYS GLU ARG GLY ASP GLN THR VAL          
SEQRES   3 E  444  LEU ILE LEU HIS ALA LYS VAL ALA GLN LYS SER TYR GLY          
SEQRES   4 E  444  ASN GLU LYS ARG PHE PHE CYS PRO PRO PRO CYS VAL TYR          
SEQRES   5 E  444  LEU MET GLY SER GLY TRP LYS LYS LYS LYS GLU GLN MET          
SEQRES   6 E  444  GLU ARG ASP GLY CYS SER GLU GLN GLU SER GLN PRO CYS          
SEQRES   7 E  444  ALA PHE ILE GLY ILE GLY ASN SER ASP GLN GLU MET GLN          
SEQRES   8 E  444  GLN LEU ASN LEU GLU GLY LYS ASN TYR CYS THR ALA LYS          
SEQRES   9 E  444  THR LEU TYR ILE SER ASP SER ASP LYS ARG LYS HIS PHE          
SEQRES  10 E  444  MET LEU SER VAL LYS MET PHE TYR GLY ASN SER ASP ASP          
SEQRES  11 E  444  ILE GLY VAL PHE LEU SER LYS ARG ILE LYS VAL ILE SER          
SEQRES  12 E  444  LYS PRO SER LYS LYS LYS GLN SER LEU LYS ASN ALA ASP          
SEQRES  13 E  444  LEU CYS ILE ALA SER GLY THR LYS VAL ALA LEU PHE ASN          
SEQRES  14 E  444  ARG LEU ARG SER GLN THR VAL SER THR ARG TYR LEU HIS          
SEQRES  15 E  444  VAL GLU GLY GLY ASN PHE HIS ALA SER SER GLN GLN TRP          
SEQRES  16 E  444  GLY ALA PHE PHE ILE HIS LEU LEU ASP ASP ASP GLU SER          
SEQRES  17 E  444  GLU GLY GLU GLU PHE THR VAL ARG ASP GLY TYR ILE HIS          
SEQRES  18 E  444  TYR GLY GLN THR VAL LYS LEU VAL CYS SER VAL THR GLY          
SEQRES  19 E  444  MET ALA LEU PRO ARG LEU ILE ILE ARG LYS VAL ASP LYS          
SEQRES  20 E  444  GLN THR ALA LEU LEU ASP ALA ASP ASP PRO VAL SER GLN          
SEQRES  21 E  444  LEU HIS LYS CYS ALA PHE TYR LEU LYS ASP THR GLU ARG          
SEQRES  22 E  444  MET TYR LEU CYS LEU SER GLN GLU ARG ILE ILE GLN PHE          
SEQRES  23 E  444  GLN ALA THR PRO CYS PRO LYS GLU PRO ASN LYS GLU MET          
SEQRES  24 E  444  ILE ASN ASP GLY ALA SER TRP THR ILE ILE SER THR ASP          
SEQRES  25 E  444  LYS ALA GLU TYR THR PHE TYR GLU GLY MET GLY PRO VAL          
SEQRES  26 E  444  LEU ALA PRO VAL THR PRO VAL PRO VAL VAL GLU SER LEU          
SEQRES  27 E  444  GLN LEU ASN GLY GLY GLY ASP VAL ALA MET LEU GLU LEU          
SEQRES  28 E  444  THR GLY GLN ASN PHE THR PRO ASN LEU ARG VAL TRP PHE          
SEQRES  29 E  444  GLY ASP VAL GLU ALA GLU THR MET TYR ARG CYS GLY GLU          
SEQRES  30 E  444  SER MET LEU CYS VAL VAL PRO ASP ILE SER ALA PHE ARG          
SEQRES  31 E  444  GLU GLY TRP ARG TRP VAL ARG GLN PRO VAL GLN VAL PRO          
SEQRES  32 E  444  VAL THR LEU VAL ARG ASN ASP GLY ILE ILE TYR SER THR          
SEQRES  33 E  444  SER LEU THR PHE THR TYR THR PRO GLU PRO GLY PRO ARG          
SEQRES  34 E  444  PRO HIS CYS SER ALA ALA GLY ALA ILE LEU ARG ALA ASN          
SEQRES  35 E  444  SER SER                                                      
SEQRES   1 F  369  LYS ARG ARG ARG GLN HIS GLY GLN LEU TRP PHE PRO GLU          
SEQRES   2 F  369  GLY PHE LYS VAL SER GLU ALA SER LYS LYS LYS ARG ARG          
SEQRES   3 F  369  GLU PRO LEU GLY GLU ASP SER VAL GLY LEU LYS PRO LEU          
SEQRES   4 F  369  LYS ASN ALA SER ASP GLY ALA LEU MET ASP ASP ASN GLN          
SEQRES   5 F  369  ASN GLU TRP GLY ASP GLU ASP LEU GLU THR LYS LYS PHE          
SEQRES   6 F  369  ARG PHE GLU GLU PRO VAL VAL LEU PRO ASP LEU ASP ASP          
SEQRES   7 F  369  GLN THR ASP HIS ARG GLN TRP THR GLN GLN HIS LEU ASP          
SEQRES   8 F  369  ALA ALA ASP LEU ARG MET SER ALA MET ALA PRO THR PRO          
SEQRES   9 F  369  PRO GLN GLY GLU VAL ASP ALA ASP CYS MET ASP VAL ASN          
SEQRES  10 F  369  VAL ARG GLY PRO ASP GLY PHE THR PRO LEU MET ILE ALA          
SEQRES  11 F  369  SER CYS SER GLY GLY GLY LEU GLU THR GLY ASN SER GLU          
SEQRES  12 F  369  GLU GLU GLU ASP ALA PRO ALA VAL ILE SER ASP PHE ILE          
SEQRES  13 F  369  TYR GLN GLY ALA SER LEU HIS ASN GLN THR ASP ARG THR          
SEQRES  14 F  369  GLY GLU THR ALA LEU HIS LEU ALA ALA ARG TYR SER ARG          
SEQRES  15 F  369  SER ASP ALA ALA LYS ARG LEU LEU GLU ALA SER ALA ASP          
SEQRES  16 F  369  ALA ASN ILE GLN ASP ASN MET GLY ARG THR PRO LEU HIS          
SEQRES  17 F  369  ALA ALA VAL SER ALA ASP ALA GLN GLY VAL PHE GLN ILE          
SEQRES  18 F  369  LEU ILE ARG ASN ARG ALA THR ASP LEU ASP ALA ARG MET          
SEQRES  19 F  369  HIS ASP GLY THR THR PRO LEU ILE LEU ALA ALA ARG LEU          
SEQRES  20 F  369  ALA VAL GLU GLY MET LEU GLU ASP LEU ILE ASN SER HIS          
SEQRES  21 F  369  ALA ASP VAL ASN ALA VAL ASP ASP LEU GLY LYS SER ALA          
SEQRES  22 F  369  LEU HIS TRP ALA ALA ALA VAL ASN ASN VAL ASP ALA ALA          
SEQRES  23 F  369  VAL VAL LEU LEU LYS ASN GLY ALA ASN LYS ASP MET GLN          
SEQRES  24 F  369  ASN ASN ARG GLU GLU THR PRO LEU PHE LEU ALA ALA ARG          
SEQRES  25 F  369  GLU GLY SER TYR GLU THR ALA LYS VAL LEU LEU ASP HIS          
SEQRES  26 F  369  PHE ALA ASN ARG ASP ILE THR ASP HIS MET ASP ARG LEU          
SEQRES  27 F  369  PRO ARG ASP ILE ALA GLN GLU ARG MET HIS HIS ASP ILE          
SEQRES  28 F  369  VAL ARG LEU LEU ASP GLU TYR ASN LEU VAL ARG SER PRO          
SEQRES  29 F  369  GLN LEU HIS GLY ALA                                          
SEQRES   1 K  369  LYS ARG ARG ARG GLN HIS GLY GLN LEU TRP PHE PRO GLU          
SEQRES   2 K  369  GLY PHE LYS VAL SER GLU ALA SER LYS LYS LYS ARG ARG          
SEQRES   3 K  369  GLU PRO LEU GLY GLU ASP SER VAL GLY LEU LYS PRO LEU          
SEQRES   4 K  369  LYS ASN ALA SER ASP GLY ALA LEU MET ASP ASP ASN GLN          
SEQRES   5 K  369  ASN GLU TRP GLY ASP GLU ASP LEU GLU THR LYS LYS PHE          
SEQRES   6 K  369  ARG PHE GLU GLU PRO VAL VAL LEU PRO ASP LEU ASP ASP          
SEQRES   7 K  369  GLN THR ASP HIS ARG GLN TRP THR GLN GLN HIS LEU ASP          
SEQRES   8 K  369  ALA ALA ASP LEU ARG MET SER ALA MET ALA PRO THR PRO          
SEQRES   9 K  369  PRO GLN GLY GLU VAL ASP ALA ASP CYS MET ASP VAL ASN          
SEQRES  10 K  369  VAL ARG GLY PRO ASP GLY PHE THR PRO LEU MET ILE ALA          
SEQRES  11 K  369  SER CYS SER GLY GLY GLY LEU GLU THR GLY ASN SER GLU          
SEQRES  12 K  369  GLU GLU GLU ASP ALA PRO ALA VAL ILE SER ASP PHE ILE          
SEQRES  13 K  369  TYR GLN GLY ALA SER LEU HIS ASN GLN THR ASP ARG THR          
SEQRES  14 K  369  GLY GLU THR ALA LEU HIS LEU ALA ALA ARG TYR SER ARG          
SEQRES  15 K  369  SER ASP ALA ALA LYS ARG LEU LEU GLU ALA SER ALA ASP          
SEQRES  16 K  369  ALA ASN ILE GLN ASP ASN MET GLY ARG THR PRO LEU HIS          
SEQRES  17 K  369  ALA ALA VAL SER ALA ASP ALA GLN GLY VAL PHE GLN ILE          
SEQRES  18 K  369  LEU ILE ARG ASN ARG ALA THR ASP LEU ASP ALA ARG MET          
SEQRES  19 K  369  HIS ASP GLY THR THR PRO LEU ILE LEU ALA ALA ARG LEU          
SEQRES  20 K  369  ALA VAL GLU GLY MET LEU GLU ASP LEU ILE ASN SER HIS          
SEQRES  21 K  369  ALA ASP VAL ASN ALA VAL ASP ASP LEU GLY LYS SER ALA          
SEQRES  22 K  369  LEU HIS TRP ALA ALA ALA VAL ASN ASN VAL ASP ALA ALA          
SEQRES  23 K  369  VAL VAL LEU LEU LYS ASN GLY ALA ASN LYS ASP MET GLN          
SEQRES  24 K  369  ASN ASN ARG GLU GLU THR PRO LEU PHE LEU ALA ALA ARG          
SEQRES  25 K  369  GLU GLY SER TYR GLU THR ALA LYS VAL LEU LEU ASP HIS          
SEQRES  26 K  369  PHE ALA ASN ARG ASP ILE THR ASP HIS MET ASP ARG LEU          
SEQRES  27 K  369  PRO ARG ASP ILE ALA GLN GLU ARG MET HIS HIS ASP ILE          
SEQRES  28 K  369  VAL ARG LEU LEU ASP GLU TYR ASN LEU VAL ARG SER PRO          
SEQRES  29 K  369  GLN LEU HIS GLY ALA                                          
HELIX    1 AA1 GLN B   15  ARG B   23  1                                   9    
HELIX    2 AA2 LYS B   24  ASN B   26  5                                   3    
HELIX    3 AA3 THR B   27  MET B   37  1                                  11    
HELIX    4 AA4 THR B   53  GLY B   62  1                                  10    
HELIX    5 AA5 ASN B   63  PHE B   73  1                                  11    
HELIX    6 AA6 SER B   86  GLY B   95  1                                  10    
HELIX    7 AA7 HIS B   96  LYS B  106  1                                  11    
HELIX    8 AA8 GLN G   31  ASN G   36  1                                   6    
HELIX    9 AA9 THR G   53  GLY G   62  1                                  10    
HELIX   10 AB1 ASN G   63  PHE G   73  1                                  11    
HELIX   11 AB2 SER G   86  GLY G   95  1                                  10    
HELIX   12 AB3 HIS G   96  LYS G  108  1                                  13    
HELIX   13 AB4 THR C   18  ARG C   29  1                                  12    
HELIX   14 AB5 SER C   64  ARG C   75  1                                  12    
HELIX   15 AB6 GLY C  351  VAL C  354  5                                   4    
HELIX   16 AB7 ASP C  393  PHE C  397  5                                   5    
HELIX   17 AB8 THR E   18  ARG E   29  1                                  12    
HELIX   18 AB9 SER E   64  ARG E   75  1                                  12    
HELIX   19 AC1 GLY E  351  VAL E  354  5                                   4    
HELIX   20 AC2 ASP E  393  PHE E  397  5                                   5    
HELIX   21 AC3 PHE F 1773  GLU F 1777  5                                   5    
HELIX   22 AC4 THR F 1884  SER F 1892  1                                   9    
HELIX   23 AC5 ASP F 1906  TYR F 1916  1                                  11    
HELIX   24 AC6 THR F 1931  TYR F 1939  1                                   9    
HELIX   25 AC7 ARG F 1941  ALA F 1951  1                                  11    
HELIX   26 AC8 THR F 1964  ALA F 1972  1                                   9    
HELIX   27 AC9 ALA F 1974  ARG F 1983  1                                  10    
HELIX   28 AD1 THR F 1998  LEU F 2006  1                                   9    
HELIX   29 AD2 LEU F 2012  SER F 2018  1                                   7    
HELIX   30 AD3 SER F 2031  VAL F 2039  1                                   9    
HELIX   31 AD4 ASN F 2041  ASN F 2051  1                                  11    
HELIX   32 AD5 THR F 2064  GLU F 2072  1                                   9    
HELIX   33 AD6 SER F 2074  HIS F 2084  1                                  11    
HELIX   34 AD7 LEU F 2097  ARG F 2105  1                                   9    
HELIX   35 AD8 HIS F 2107  TYR F 2117  1                                  11    
HELIX   36 AD9 PHE K 1773  GLU K 1777  5                                   5    
HELIX   37 AE1 THR K 1884  GLY K 1893  1                                  10    
HELIX   38 AE2 ASP K 1906  GLN K 1917  1                                  12    
HELIX   39 AE3 THR K 1931  TYR K 1939  1                                   9    
HELIX   40 AE4 ARG K 1941  ALA K 1951  1                                  11    
HELIX   41 AE5 THR K 1964  ALA K 1972  1                                   9    
HELIX   42 AE6 ALA K 1974  ARG K 1983  1                                  10    
HELIX   43 AE7 THR K 1998  LEU K 2006  1                                   9    
HELIX   44 AE8 LEU K 2012  SER K 2018  1                                   7    
HELIX   45 AE9 SER K 2031  VAL K 2039  1                                   9    
HELIX   46 AF1 ASN K 2041  ASN K 2051  1                                  11    
HELIX   47 AF2 THR K 2064  GLU K 2072  1                                   9    
HELIX   48 AF3 SER K 2074  HIS K 2084  1                                  11    
HELIX   49 AF4 LEU K 2097  ARG K 2105  1                                   9    
HELIX   50 AF5 HIS K 2107  TYR K 2117  1                                  11    
SHEET    1 AA1 9 VAL C 223  ARG C 224  0                                        
SHEET    2 AA1 9 PHE C 206  LEU C 211 -1  N  LEU C 210   O  ARG C 224           
SHEET    3 AA1 9 THR C 233  CYS C 238 -1  O  VAL C 237   N  PHE C 207           
SHEET    4 AA1 9 LEU C 248  LYS C 252 -1  O  LEU C 248   N  VAL C 234           
SHEET    5 AA1 9 HIS C 270  LEU C 276 -1  O  ALA C 273   N  ARG C 251           
SHEET    6 AA1 9 TRP C 314  TYR C 324 -1  O  ILE C 316   N  HIS C 270           
SHEET    7 AA1 9 VAL C  34  ALA C  39 -1  N  HIS C  38   O  ASP C 320           
SHEET    8 AA1 9 CYS C  58  TYR C  60 -1  O  CYS C  58   N  LEU C  37           
SHEET    9 AA1 9 TYR C 108  THR C 110 -1  O  CYS C 109   N  VAL C  59           
SHEET    1 AA2 4 ARG C 187  TYR C 188  0                                        
SHEET    2 AA2 4 LYS C 172  ASN C 177 -1  N  ASN C 177   O  ARG C 187           
SHEET    3 AA2 4 PHE C 206  LEU C 211 -1  O  PHE C 206   N  VAL C 173           
SHEET    4 AA2 4 VAL C 223  ARG C 224 -1  O  ARG C 224   N  LEU C 210           
SHEET    1 AA3 7 VAL C 223  ARG C 224  0                                        
SHEET    2 AA3 7 PHE C 206  LEU C 211 -1  N  LEU C 210   O  ARG C 224           
SHEET    3 AA3 7 LYS C 172  ASN C 177 -1  N  VAL C 173   O  PHE C 206           
SHEET    4 AA3 7 TRP C 314  TYR C 324 -1  O  THR C 319   N  LYS C 172           
SHEET    5 AA3 7 VAL C  34  ALA C  39 -1  N  HIS C  38   O  ASP C 320           
SHEET    6 AA3 7 CYS C  58  TYR C  60 -1  O  CYS C  58   N  LEU C  37           
SHEET    7 AA3 7 TYR C 108  THR C 110 -1  O  CYS C 109   N  VAL C  59           
SHEET    1 AA4 3 VAL C  41  GLN C  43  0                                        
SHEET    2 AA4 3 ILE C 147  ILE C 150  1  O  LYS C 148   N  ALA C  42           
SHEET    3 AA4 3 HIS C 124  PHE C 125 -1  N  PHE C 125   O  ILE C 147           
SHEET    1 AA5 4 GLN C  99  LEU C 101  0                                        
SHEET    2 AA5 4 PRO C  85  ILE C  91 -1  N  ILE C  89   O  GLN C  99           
SHEET    3 AA5 4 LEU C 127  TYR C 133 -1  O  SER C 128   N  GLY C  90           
SHEET    4 AA5 4 ASP C 138  LEU C 143 -1  O  PHE C 142   N  VAL C 129           
SHEET    1 AA6 2 HIS C 190  GLU C 192  0                                        
SHEET    2 AA6 2 ASN C 195  HIS C 197 -1  O  ASN C 195   N  GLU C 192           
SHEET    1 AA7 2 ALA C 258  LEU C 259  0                                        
SHEET    2 AA7 2 LYS C 305  GLU C 306 -1  O  GLU C 306   N  ALA C 258           
SHEET    1 AA8 2 TYR C 283  SER C 287  0                                        
SHEET    2 AA8 2 ARG C 290  PHE C 294 -1  O  PHE C 294   N  TYR C 283           
SHEET    1 AA9 4 TYR C 327  GLU C 328  0                                        
SHEET    2 AA9 4 ILE C 420  TYR C 422 -1  O  ILE C 421   N  TYR C 327           
SHEET    3 AA9 4 VAL C 408  ARG C 416 -1  N  LEU C 414   O  TYR C 422           
SHEET    4 AA9 4 LEU C 368  PHE C 372 -1  N  TRP C 371   O  THR C 413           
SHEET    1 AB1 4 TYR C 327  GLU C 328  0                                        
SHEET    2 AB1 4 ILE C 420  TYR C 422 -1  O  ILE C 421   N  TYR C 327           
SHEET    3 AB1 4 VAL C 408  ARG C 416 -1  N  LEU C 414   O  TYR C 422           
SHEET    4 AB1 4 THR C 427  TYR C 430 -1  O  TYR C 430   N  VAL C 408           
SHEET    1 AB2 4 VAL C 342  ASN C 349  0                                        
SHEET    2 AB2 4 MET C 356  GLN C 362 -1  O  GLU C 358   N  GLN C 347           
SHEET    3 AB2 4 SER C 386  VAL C 390 -1  O  MET C 387   N  LEU C 359           
SHEET    4 AB2 4 THR C 379  CYS C 383 -1  N  MET C 380   O  LEU C 388           
SHEET    1 AB3 7 TYR E 108  THR E 110  0                                        
SHEET    2 AB3 7 CYS E  58  TYR E  60 -1  N  VAL E  59   O  CYS E 109           
SHEET    3 AB3 7 VAL E  34  ALA E  39 -1  N  LEU E  37   O  CYS E  58           
SHEET    4 AB3 7 TRP E 314  TYR E 324 -1  O  ALA E 322   N  ILE E  36           
SHEET    5 AB3 7 THR E 171  PHE E 176 -1  N  LYS E 172   O  THR E 319           
SHEET    6 AB3 7 PHE E 206  LEU E 211 -1  O  PHE E 206   N  VAL E 173           
SHEET    7 AB3 7 VAL E 223  ARG E 224 -1  O  ARG E 224   N  LEU E 210           
SHEET    1 AB4 9 TYR E 108  THR E 110  0                                        
SHEET    2 AB4 9 CYS E  58  TYR E  60 -1  N  VAL E  59   O  CYS E 109           
SHEET    3 AB4 9 VAL E  34  ALA E  39 -1  N  LEU E  37   O  CYS E  58           
SHEET    4 AB4 9 TRP E 314  TYR E 324 -1  O  ALA E 322   N  ILE E  36           
SHEET    5 AB4 9 HIS E 270  TYR E 275 -1  N  CYS E 272   O  TRP E 314           
SHEET    6 AB4 9 LEU E 248  LYS E 252 -1  N  ARG E 251   O  ALA E 273           
SHEET    7 AB4 9 THR E 233  CYS E 238 -1  N  VAL E 234   O  LEU E 248           
SHEET    8 AB4 9 PHE E 206  LEU E 211 -1  N  LEU E 211   O  THR E 233           
SHEET    9 AB4 9 VAL E 223  ARG E 224 -1  O  ARG E 224   N  LEU E 210           
SHEET    1 AB5 5 VAL E  41  GLN E  43  0                                        
SHEET    2 AB5 5 ASP E 138  ILE E 150  1  O  LYS E 148   N  ALA E  42           
SHEET    3 AB5 5 HIS E 124  TYR E 133 -1  N  VAL E 129   O  PHE E 142           
SHEET    4 AB5 5 PRO E  85  ILE E  91 -1  N  GLY E  90   O  SER E 128           
SHEET    5 AB5 5 GLN E  99  LEU E 101 -1  O  LEU E 101   N  ALA E  87           
SHEET    1 AB6 2 HIS E 190  GLU E 192  0                                        
SHEET    2 AB6 2 ASN E 195  HIS E 197 -1  O  HIS E 197   N  HIS E 190           
SHEET    1 AB7 2 THR E 257  LEU E 259  0                                        
SHEET    2 AB7 2 LYS E 305  MET E 307 -1  O  GLU E 306   N  ALA E 258           
SHEET    1 AB8 2 TYR E 283  SER E 287  0                                        
SHEET    2 AB8 2 ARG E 290  PHE E 294 -1  O  ARG E 290   N  SER E 287           
SHEET    1 AB9 5 TYR E 327  GLU E 328  0                                        
SHEET    2 AB9 5 ILE E 420  TYR E 422 -1  O  ILE E 421   N  TYR E 327           
SHEET    3 AB9 5 VAL E 408  ARG E 416 -1  N  LEU E 414   O  TYR E 422           
SHEET    4 AB9 5 LEU E 368  PHE E 372 -1  N  ARG E 369   O  VAL E 415           
SHEET    5 AB9 5 VAL E 375  GLU E 376 -1  O  VAL E 375   N  PHE E 372           
SHEET    1 AC1 4 TYR E 327  GLU E 328  0                                        
SHEET    2 AC1 4 ILE E 420  TYR E 422 -1  O  ILE E 421   N  TYR E 327           
SHEET    3 AC1 4 VAL E 408  ARG E 416 -1  N  LEU E 414   O  TYR E 422           
SHEET    4 AC1 4 THR E 427  TYR E 430 -1  O  TYR E 430   N  VAL E 408           
SHEET    1 AC2 4 VAL E 342  ASN E 349  0                                        
SHEET    2 AC2 4 MET E 356  GLN E 362 -1  O  GLU E 358   N  GLN E 347           
SHEET    3 AC2 4 SER E 386  VAL E 390 -1  O  MET E 387   N  LEU E 359           
SHEET    4 AC2 4 THR E 379  CYS E 383 -1  N  MET E 380   O  LEU E 388           
CRYST1   79.880  103.650  301.420  90.00  90.00  90.00 P 21 21 21    8          
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      0.012519  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003318        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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