GenomeNet

Database: PDB
Entry: 3G61
LinkDB: 3G61
Original site: 3G61 
HEADER    MEMBRANE PROTEIN                        05-FEB-09   3G61              
TITLE     STRUCTURE OF P-GLYCOPROTEIN REVEALS A MOLECULAR BASIS FOR POLY-       
TITLE    2 SPECIFIC DRUG BINDING                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MULTIDRUG RESISTANCE PROTEIN 1A;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MCG1178;                                                    
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ABCB1A, MCG_1178                                               
KEYWDS    P-GLYCOPROTEIN, PGP, MULTIDRUG RESISTANCE, MEMBRANE PROTEIN, CYCLE    
KEYWDS   2 PEPTIDES, ATP-BINDING, NUCLEOTIDE-BINDING                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.ALLER,J.YU,A.WARD,Y.WENG,S.CHITTABOINA,R.ZHUO,P.M.HARRELL,        
AUTHOR   2 Y.T.TRINH,Q.ZHANG,I.L.URBATSCH,G.CHANG                               
REVDAT   5   21-FEB-24 3G61    1       REMARK                                   
REVDAT   4   21-OCT-20 3G61    1       REMARK SEQADV HETSYN                     
REVDAT   3   13-NOV-13 3G61    1       HETATM HETNAM HETSYN HET                 
REVDAT   3 2                   1       FORMUL VERSN  REMARK                     
REVDAT   2   21-APR-09 3G61    1       JRNL                                     
REVDAT   1   24-MAR-09 3G61    0                                                
JRNL        AUTH   S.G.ALLER,J.YU,A.WARD,Y.WENG,S.CHITTABOINA,R.ZHUO,           
JRNL        AUTH 2 P.M.HARRELL,Y.T.TRINH,Q.ZHANG,I.L.URBATSCH,G.CHANG           
JRNL        TITL   STRUCTURE OF P-GLYCOPROTEIN REVEALS A MOLECULAR BASIS FOR    
JRNL        TITL 2 POLY-SPECIFIC DRUG BINDING.                                  
JRNL        REF    SCIENCE                       V. 323  1718 2009              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   19325113                                                     
JRNL        DOI    10.1126/SCIENCE.1168750                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 120841.900                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 26489                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.308                           
REMARK   3   FREE R VALUE                     : 0.356                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2642                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.62                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3624                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4600                       
REMARK   3   BIN FREE R VALUE                    : 0.4980                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 376                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18342                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 103.5                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 182.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -16.49000                                            
REMARK   3    B22 (A**2) : 50.71000                                             
REMARK   3    B33 (A**2) : -34.21000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.91                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.05                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 1.15                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.910                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 13.950; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 21.610; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 15.020; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 21.740; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.15                                                 
REMARK   3   BSOL        : 27.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : QZ59SSS.PAR                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3G61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051467.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97854                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26489                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.3                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-23% PEG400, 0.05M TRIS, 0.04%         
REMARK 280  SODIUM CHOLATE, PH 7.8, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 278K                                                    
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       48.87100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      187.90500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.48900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      187.90500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.87100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.48900            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     PHE A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     LYS A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A   627                                                      
REMARK 465     GLY A   628                                                      
REMARK 465     ASN A   629                                                      
REMARK 465     GLU A   630                                                      
REMARK 465     ILE A   631                                                      
REMARK 465     GLU A   632                                                      
REMARK 465     LEU A   633                                                      
REMARK 465     GLY A   634                                                      
REMARK 465     ASN A   635                                                      
REMARK 465     GLU A   636                                                      
REMARK 465     ALA A   637                                                      
REMARK 465     CYS A   638                                                      
REMARK 465     LYS A   639                                                      
REMARK 465     SER A   640                                                      
REMARK 465     LYS A   641                                                      
REMARK 465     ASP A   642                                                      
REMARK 465     GLU A   643                                                      
REMARK 465     ILE A   644                                                      
REMARK 465     ASP A   645                                                      
REMARK 465     ASN A   646                                                      
REMARK 465     LEU A   647                                                      
REMARK 465     ASP A   648                                                      
REMARK 465     MET A   649                                                      
REMARK 465     SER A   650                                                      
REMARK 465     SER A   651                                                      
REMARK 465     LYS A   652                                                      
REMARK 465     ASP A   653                                                      
REMARK 465     SER A   654                                                      
REMARK 465     GLY A   655                                                      
REMARK 465     SER A   656                                                      
REMARK 465     SER A   657                                                      
REMARK 465     LEU A   658                                                      
REMARK 465     ILE A   659                                                      
REMARK 465     ARG A   660                                                      
REMARK 465     ARG A   661                                                      
REMARK 465     ARG A   662                                                      
REMARK 465     SER A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     ARG A   665                                                      
REMARK 465     LYS A   666                                                      
REMARK 465     SER A   667                                                      
REMARK 465     ILE A   668                                                      
REMARK 465     CYS A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     PRO A   671                                                      
REMARK 465     HIS A   672                                                      
REMARK 465     ASP A   673                                                      
REMARK 465     GLN A   674                                                      
REMARK 465     ASP A   675                                                      
REMARK 465     ARG A   676                                                      
REMARK 465     LYS A   677                                                      
REMARK 465     LEU A   678                                                      
REMARK 465     SER A   679                                                      
REMARK 465     THR A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     GLU A   682                                                      
REMARK 465     ALA A   683                                                      
REMARK 465     GLY A  1272                                                      
REMARK 465     ALA A  1273                                                      
REMARK 465     LYS A  1274                                                      
REMARK 465     ARG A  1275                                                      
REMARK 465     SER A  1276                                                      
REMARK 465     TYR A  1277                                                      
REMARK 465     VAL A  1278                                                      
REMARK 465     HIS A  1279                                                      
REMARK 465     HIS A  1280                                                      
REMARK 465     HIS A  1281                                                      
REMARK 465     HIS A  1282                                                      
REMARK 465     HIS A  1283                                                      
REMARK 465     HIS A  1284                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     ASN B    14                                                      
REMARK 465     PHE B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     MET B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     SER B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     ALA B   627                                                      
REMARK 465     GLY B   628                                                      
REMARK 465     ASN B   629                                                      
REMARK 465     GLU B   630                                                      
REMARK 465     ILE B   631                                                      
REMARK 465     GLU B   632                                                      
REMARK 465     LEU B   633                                                      
REMARK 465     GLY B   634                                                      
REMARK 465     ASN B   635                                                      
REMARK 465     GLU B   636                                                      
REMARK 465     ALA B   637                                                      
REMARK 465     CYS B   638                                                      
REMARK 465     LYS B   639                                                      
REMARK 465     SER B   640                                                      
REMARK 465     LYS B   641                                                      
REMARK 465     ASP B   642                                                      
REMARK 465     GLU B   643                                                      
REMARK 465     ILE B   644                                                      
REMARK 465     ASP B   645                                                      
REMARK 465     ASN B   646                                                      
REMARK 465     LEU B   647                                                      
REMARK 465     ASP B   648                                                      
REMARK 465     MET B   649                                                      
REMARK 465     SER B   650                                                      
REMARK 465     SER B   651                                                      
REMARK 465     LYS B   652                                                      
REMARK 465     ASP B   653                                                      
REMARK 465     SER B   654                                                      
REMARK 465     GLY B   655                                                      
REMARK 465     SER B   656                                                      
REMARK 465     SER B   657                                                      
REMARK 465     LEU B   658                                                      
REMARK 465     ILE B   659                                                      
REMARK 465     ARG B   660                                                      
REMARK 465     ARG B   661                                                      
REMARK 465     ARG B   662                                                      
REMARK 465     SER B   663                                                      
REMARK 465     THR B   664                                                      
REMARK 465     ARG B   665                                                      
REMARK 465     LYS B   666                                                      
REMARK 465     SER B   667                                                      
REMARK 465     ILE B   668                                                      
REMARK 465     CYS B   669                                                      
REMARK 465     GLY B   670                                                      
REMARK 465     PRO B   671                                                      
REMARK 465     HIS B   672                                                      
REMARK 465     ASP B   673                                                      
REMARK 465     GLN B   674                                                      
REMARK 465     ASP B   675                                                      
REMARK 465     ARG B   676                                                      
REMARK 465     LYS B   677                                                      
REMARK 465     LEU B   678                                                      
REMARK 465     SER B   679                                                      
REMARK 465     THR B   680                                                      
REMARK 465     LYS B   681                                                      
REMARK 465     GLU B   682                                                      
REMARK 465     ALA B   683                                                      
REMARK 465     GLY B  1272                                                      
REMARK 465     ALA B  1273                                                      
REMARK 465     LYS B  1274                                                      
REMARK 465     ARG B  1275                                                      
REMARK 465     SER B  1276                                                      
REMARK 465     TYR B  1277                                                      
REMARK 465     VAL B  1278                                                      
REMARK 465     HIS B  1279                                                      
REMARK 465     HIS B  1280                                                      
REMARK 465     HIS B  1281                                                      
REMARK 465     HIS B  1282                                                      
REMARK 465     HIS B  1283                                                      
REMARK 465     HIS B  1284                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU B   155     N    GLY B   157              2.03            
REMARK 500   O    GLU A   155     N    GLY A   157              2.05            
REMARK 500   O    GLU B   552     N    THR B   554              2.11            
REMARK 500   O    ARG A   589     N    ALA A   591              2.17            
REMARK 500   O    GLU B   321     N    SER B   323              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  65   C   -  N   -  CA  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    GLY A 165   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    LYS A 267   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    PRO A 346   C   -  N   -  CA  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    PHE A 374   N   -  CA  -  C   ANGL. DEV. =  22.5 DEGREES          
REMARK 500    ASP A 450   N   -  CA  -  C   ANGL. DEV. = -21.7 DEGREES          
REMARK 500    GLY A 575   N   -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    PRO A 923   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    TYR A1017   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    LYS A1098   N   -  CA  -  C   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    ASP A1159   N   -  CA  -  C   ANGL. DEV. = -20.0 DEGREES          
REMARK 500    PRO B  65   C   -  N   -  CA  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    PRO B  65   C   -  N   -  CD  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    GLY B 165   N   -  CA  -  C   ANGL. DEV. = -17.3 DEGREES          
REMARK 500    PRO B 346   C   -  N   -  CA  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    SER B 370   N   -  CA  -  C   ANGL. DEV. =  27.3 DEGREES          
REMARK 500    LYS B1098   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ASP B1159   N   -  CA  -  C   ANGL. DEV. = -22.7 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    SER A  34      -64.16    -16.22                                   
REMARK 500    VAL A  35      -80.33    -41.82                                   
REMARK 500    THR A  37      -70.60    -61.64                                   
REMARK 500    PHE A  39      -71.18    -49.45                                   
REMARK 500    ALA A  42      117.30     79.99                                   
REMARK 500    TRP A  44      -92.36    -66.09                                   
REMARK 500    VAL A  52      -77.94    -28.89                                   
REMARK 500    ASP A  73      -54.08    -20.65                                   
REMARK 500    SER A  88      -22.03     51.23                                   
REMARK 500    ASN A  90     -135.57   -173.23                                   
REMARK 500    LEU A 103      -74.27    -61.49                                   
REMARK 500    PHE A 131      -85.80    -49.63                                   
REMARK 500    TRP A 132      -70.72    -15.12                                   
REMARK 500    CYS A 133     -102.12    -62.83                                   
REMARK 500    LEU A 134      -68.97     -8.57                                   
REMARK 500    ALA A 135      -89.26    -45.29                                   
REMARK 500    ILE A 140      -75.52    -42.63                                   
REMARK 500    HIS A 141      -48.06    -28.54                                   
REMARK 500    ARG A 144      -81.80    -55.02                                   
REMARK 500    PHE A 148      -71.21    -43.61                                   
REMARK 500    MET A 152      -16.97    -46.19                                   
REMARK 500    GLU A 155      174.97     45.09                                   
REMARK 500    ILE A 156      -47.97      1.68                                   
REMARK 500    ASP A 160      -79.90    -32.54                                   
REMARK 500    VAL A 161     -146.20   -105.70                                   
REMARK 500    HIS A 162      173.17     72.00                                   
REMARK 500    VAL A 164      -12.91     45.34                                   
REMARK 500    PHE A 190      -78.06    -30.20                                   
REMARK 500    PHE A 196      -71.86    -61.71                                   
REMARK 500    PHE A 200      -76.61    -76.67                                   
REMARK 500    ILE A 201      -82.57    -26.87                                   
REMARK 500    PHE A 204      -75.48   -158.88                                   
REMARK 500    TRP A 208       -6.62     50.30                                   
REMARK 500    LYS A 209      -14.46    173.76                                   
REMARK 500    ILE A 214      -74.10    -60.66                                   
REMARK 500    LEU A 215      -53.50    -29.06                                   
REMARK 500    ALA A 216      -82.90    -57.38                                   
REMARK 500    SER A 218      -79.37    -61.44                                   
REMARK 500    PRO A 219      -35.90    -39.64                                   
REMARK 500    ILE A 227      -72.16    -55.01                                   
REMARK 500    GLU A 251      -62.55   -105.68                                   
REMARK 500    GLU A 252      175.61     61.52                                   
REMARK 500    ALA A 255     -157.69    -81.49                                   
REMARK 500    ALA A 256       18.49     51.29                                   
REMARK 500    ARG A 258      -73.47    -49.26                                   
REMARK 500    PHE A 263      -32.11   -132.82                                   
REMARK 500    GLN A 266      -70.81    -54.01                                   
REMARK 500    LYS A 267      -12.09     50.31                                   
REMARK 500    LYS A 268      -60.73    -98.73                                   
REMARK 500    GLU A 269      -73.65    -37.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     553 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 916         0.07    SIDE CHAIN                              
REMARK 500    TYR B 916         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     2J8 A 6002                                                       
REMARK 610     2J8 B 6004                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 A 6001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 A 6002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 B 6003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 B 6004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G5U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G60   RELATED DB: PDB                                   
DBREF  3G61 A    1  1276  UNP    Q5I1Y5   Q5I1Y5_MOUSE     1   1276             
DBREF  3G61 B    1  1276  UNP    Q5I1Y5   Q5I1Y5_MOUSE     1   1276             
SEQADV 3G61 TYR A 1277  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 VAL A 1278  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1279  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1280  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1281  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1282  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1283  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS A 1284  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 TYR B 1277  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 VAL B 1278  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1279  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1280  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1281  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1282  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1283  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQADV 3G61 HIS B 1284  UNP  Q5I1Y5              EXPRESSION TAG                 
SEQRES   1 A 1284  MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS          
SEQRES   2 A 1284  ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS          
SEQRES   3 A 1284  LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE          
SEQRES   4 A 1284  ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL          
SEQRES   5 A 1284  GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO          
SEQRES   6 A 1284  LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE          
SEQRES   7 A 1284  ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET          
SEQRES   8 A 1284  SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU          
SEQRES   9 A 1284  GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE          
SEQRES  10 A 1284  GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER          
SEQRES  11 A 1284  PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE          
SEQRES  12 A 1284  ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE          
SEQRES  13 A 1284  GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR          
SEQRES  14 A 1284  ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE          
SEQRES  15 A 1284  GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR          
SEQRES  16 A 1284  PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP          
SEQRES  17 A 1284  LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU          
SEQRES  18 A 1284  GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER          
SEQRES  19 A 1284  PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY          
SEQRES  20 A 1284  ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL          
SEQRES  21 A 1284  ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR          
SEQRES  22 A 1284  ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS          
SEQRES  23 A 1284  LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE          
SEQRES  24 A 1284  LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR          
SEQRES  25 A 1284  GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY          
SEQRES  26 A 1284  GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA          
SEQRES  27 A 1284  PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE          
SEQRES  28 A 1284  ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE          
SEQRES  29 A 1284  ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER          
SEQRES  30 A 1284  GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE          
SEQRES  31 A 1284  LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL          
SEQRES  32 A 1284  GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY          
SEQRES  33 A 1284  GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS          
SEQRES  34 A 1284  SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO          
SEQRES  35 A 1284  LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG          
SEQRES  36 A 1284  THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL          
SEQRES  37 A 1284  VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA          
SEQRES  38 A 1284  GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP          
SEQRES  39 A 1284  GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP          
SEQRES  40 A 1284  PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL          
SEQRES  41 A 1284  GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN          
SEQRES  42 A 1284  ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS          
SEQRES  43 A 1284  ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP THR          
SEQRES  44 A 1284  GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA          
SEQRES  45 A 1284  ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU          
SEQRES  46 A 1284  SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP          
SEQRES  47 A 1284  GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU          
SEQRES  48 A 1284  MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR          
SEQRES  49 A 1284  GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA          
SEQRES  50 A 1284  CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP MET SER          
SEQRES  51 A 1284  SER LYS ASP SER GLY SER SER LEU ILE ARG ARG ARG SER          
SEQRES  52 A 1284  THR ARG LYS SER ILE CYS GLY PRO HIS ASP GLN ASP ARG          
SEQRES  53 A 1284  LYS LEU SER THR LYS GLU ALA LEU ASP GLU ASP VAL PRO          
SEQRES  54 A 1284  PRO ALA SER PHE TRP ARG ILE LEU LYS LEU ASN SER THR          
SEQRES  55 A 1284  GLU TRP PRO TYR PHE VAL VAL GLY ILE PHE CYS ALA ILE          
SEQRES  56 A 1284  ILE ASN GLY GLY LEU GLN PRO ALA PHE SER VAL ILE PHE          
SEQRES  57 A 1284  SER LYS VAL VAL GLY VAL PHE THR ASN GLY GLY PRO PRO          
SEQRES  58 A 1284  GLU THR GLN ARG GLN ASN SER ASN LEU PHE SER LEU LEU          
SEQRES  59 A 1284  PHE LEU ILE LEU GLY ILE ILE SER PHE ILE THR PHE PHE          
SEQRES  60 A 1284  LEU GLN GLY PHE THR PHE GLY LYS ALA GLY GLU ILE LEU          
SEQRES  61 A 1284  THR LYS ARG LEU ARG TYR MET VAL PHE LYS SER MET LEU          
SEQRES  62 A 1284  ARG GLN ASP VAL SER TRP PHE ASP ASP PRO LYS ASN THR          
SEQRES  63 A 1284  THR GLY ALA LEU THR THR ARG LEU ALA ASN ASP ALA ALA          
SEQRES  64 A 1284  GLN VAL LYS GLY ALA THR GLY SER ARG LEU ALA VAL ILE          
SEQRES  65 A 1284  PHE GLN ASN ILE ALA ASN LEU GLY THR GLY ILE ILE ILE          
SEQRES  66 A 1284  SER LEU ILE TYR GLY TRP GLN LEU THR LEU LEU LEU LEU          
SEQRES  67 A 1284  ALA ILE VAL PRO ILE ILE ALA ILE ALA GLY VAL VAL GLU          
SEQRES  68 A 1284  MET LYS MET LEU SER GLY GLN ALA LEU LYS ASP LYS LYS          
SEQRES  69 A 1284  GLU LEU GLU GLY SER GLY LYS ILE ALA THR GLU ALA ILE          
SEQRES  70 A 1284  GLU ASN PHE ARG THR VAL VAL SER LEU THR ARG GLU GLN          
SEQRES  71 A 1284  LYS PHE GLU THR MET TYR ALA GLN SER LEU GLN ILE PRO          
SEQRES  72 A 1284  TYR ARG ASN ALA MET LYS LYS ALA HIS VAL PHE GLY ILE          
SEQRES  73 A 1284  THR PHE SER PHE THR GLN ALA MET MET TYR PHE SER TYR          
SEQRES  74 A 1284  ALA ALA CYS PHE ARG PHE GLY ALA TYR LEU VAL THR GLN          
SEQRES  75 A 1284  GLN LEU MET THR PHE GLU ASN VAL LEU LEU VAL PHE SER          
SEQRES  76 A 1284  ALA ILE VAL PHE GLY ALA MET ALA VAL GLY GLN VAL SER          
SEQRES  77 A 1284  SER PHE ALA PRO ASP TYR ALA LYS ALA THR VAL SER ALA          
SEQRES  78 A 1284  SER HIS ILE ILE ARG ILE ILE GLU LYS THR PRO GLU ILE          
SEQRES  79 A 1284  ASP SER TYR SER THR GLN GLY LEU LYS PRO ASN MET LEU          
SEQRES  80 A 1284  GLU GLY ASN VAL GLN PHE SER GLY VAL VAL PHE ASN TYR          
SEQRES  81 A 1284  PRO THR ARG PRO SER ILE PRO VAL LEU GLN GLY LEU SER          
SEQRES  82 A 1284  LEU GLU VAL LYS LYS GLY GLN THR LEU ALA LEU VAL GLY          
SEQRES  83 A 1284  SER SER GLY CYS GLY LYS SER THR VAL VAL GLN LEU LEU          
SEQRES  84 A 1284  GLU ARG PHE TYR ASP PRO MET ALA GLY SER VAL PHE LEU          
SEQRES  85 A 1284  ASP GLY LYS GLU ILE LYS GLN LEU ASN VAL GLN TRP LEU          
SEQRES  86 A 1284  ARG ALA GLN LEU GLY ILE VAL SER GLN GLU PRO ILE LEU          
SEQRES  87 A 1284  PHE ASP CYS SER ILE ALA GLU ASN ILE ALA TYR GLY ASP          
SEQRES  88 A 1284  ASN SER ARG VAL VAL SER TYR GLU GLU ILE VAL ARG ALA          
SEQRES  89 A 1284  ALA LYS GLU ALA ASN ILE HIS GLN PHE ILE ASP SER LEU          
SEQRES  90 A 1284  PRO ASP LYS TYR ASN THR ARG VAL GLY ASP LYS GLY THR          
SEQRES  91 A 1284  GLN LEU SER GLY GLY GLN LYS GLN ARG ILE ALA ILE ALA          
SEQRES  92 A 1284  ARG ALA LEU VAL ARG GLN PRO HIS ILE LEU LEU LEU ASP          
SEQRES  93 A 1284  GLU ALA THR SER ALA LEU ASP THR GLU SER GLU LYS VAL          
SEQRES  94 A 1284  VAL GLN GLU ALA LEU ASP LYS ALA ARG GLU GLY ARG THR          
SEQRES  95 A 1284  CYS ILE VAL ILE ALA HIS ARG LEU SER THR ILE GLN ASN          
SEQRES  96 A 1284  ALA ASP LEU ILE VAL VAL ILE GLN ASN GLY LYS VAL LYS          
SEQRES  97 A 1284  GLU HIS GLY THR HIS GLN GLN LEU LEU ALA GLN LYS GLY          
SEQRES  98 A 1284  ILE TYR PHE SER MET VAL SER VAL GLN ALA GLY ALA LYS          
SEQRES  99 A 1284  ARG SER TYR VAL HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B 1284  MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS          
SEQRES   2 B 1284  ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS          
SEQRES   3 B 1284  LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE          
SEQRES   4 B 1284  ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL          
SEQRES   5 B 1284  GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO          
SEQRES   6 B 1284  LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE          
SEQRES   7 B 1284  ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET          
SEQRES   8 B 1284  SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU          
SEQRES   9 B 1284  GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE          
SEQRES  10 B 1284  GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER          
SEQRES  11 B 1284  PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE          
SEQRES  12 B 1284  ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE          
SEQRES  13 B 1284  GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR          
SEQRES  14 B 1284  ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE          
SEQRES  15 B 1284  GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR          
SEQRES  16 B 1284  PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP          
SEQRES  17 B 1284  LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU          
SEQRES  18 B 1284  GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER          
SEQRES  19 B 1284  PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY          
SEQRES  20 B 1284  ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL          
SEQRES  21 B 1284  ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR          
SEQRES  22 B 1284  ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS          
SEQRES  23 B 1284  LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE          
SEQRES  24 B 1284  LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR          
SEQRES  25 B 1284  GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY          
SEQRES  26 B 1284  GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA          
SEQRES  27 B 1284  PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE          
SEQRES  28 B 1284  ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE          
SEQRES  29 B 1284  ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER          
SEQRES  30 B 1284  GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE          
SEQRES  31 B 1284  LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL          
SEQRES  32 B 1284  GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY          
SEQRES  33 B 1284  GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS          
SEQRES  34 B 1284  SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO          
SEQRES  35 B 1284  LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG          
SEQRES  36 B 1284  THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL          
SEQRES  37 B 1284  VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA          
SEQRES  38 B 1284  GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP          
SEQRES  39 B 1284  GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP          
SEQRES  40 B 1284  PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL          
SEQRES  41 B 1284  GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN          
SEQRES  42 B 1284  ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS          
SEQRES  43 B 1284  ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP THR          
SEQRES  44 B 1284  GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA          
SEQRES  45 B 1284  ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU          
SEQRES  46 B 1284  SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP          
SEQRES  47 B 1284  GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU          
SEQRES  48 B 1284  MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR          
SEQRES  49 B 1284  GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA          
SEQRES  50 B 1284  CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP MET SER          
SEQRES  51 B 1284  SER LYS ASP SER GLY SER SER LEU ILE ARG ARG ARG SER          
SEQRES  52 B 1284  THR ARG LYS SER ILE CYS GLY PRO HIS ASP GLN ASP ARG          
SEQRES  53 B 1284  LYS LEU SER THR LYS GLU ALA LEU ASP GLU ASP VAL PRO          
SEQRES  54 B 1284  PRO ALA SER PHE TRP ARG ILE LEU LYS LEU ASN SER THR          
SEQRES  55 B 1284  GLU TRP PRO TYR PHE VAL VAL GLY ILE PHE CYS ALA ILE          
SEQRES  56 B 1284  ILE ASN GLY GLY LEU GLN PRO ALA PHE SER VAL ILE PHE          
SEQRES  57 B 1284  SER LYS VAL VAL GLY VAL PHE THR ASN GLY GLY PRO PRO          
SEQRES  58 B 1284  GLU THR GLN ARG GLN ASN SER ASN LEU PHE SER LEU LEU          
SEQRES  59 B 1284  PHE LEU ILE LEU GLY ILE ILE SER PHE ILE THR PHE PHE          
SEQRES  60 B 1284  LEU GLN GLY PHE THR PHE GLY LYS ALA GLY GLU ILE LEU          
SEQRES  61 B 1284  THR LYS ARG LEU ARG TYR MET VAL PHE LYS SER MET LEU          
SEQRES  62 B 1284  ARG GLN ASP VAL SER TRP PHE ASP ASP PRO LYS ASN THR          
SEQRES  63 B 1284  THR GLY ALA LEU THR THR ARG LEU ALA ASN ASP ALA ALA          
SEQRES  64 B 1284  GLN VAL LYS GLY ALA THR GLY SER ARG LEU ALA VAL ILE          
SEQRES  65 B 1284  PHE GLN ASN ILE ALA ASN LEU GLY THR GLY ILE ILE ILE          
SEQRES  66 B 1284  SER LEU ILE TYR GLY TRP GLN LEU THR LEU LEU LEU LEU          
SEQRES  67 B 1284  ALA ILE VAL PRO ILE ILE ALA ILE ALA GLY VAL VAL GLU          
SEQRES  68 B 1284  MET LYS MET LEU SER GLY GLN ALA LEU LYS ASP LYS LYS          
SEQRES  69 B 1284  GLU LEU GLU GLY SER GLY LYS ILE ALA THR GLU ALA ILE          
SEQRES  70 B 1284  GLU ASN PHE ARG THR VAL VAL SER LEU THR ARG GLU GLN          
SEQRES  71 B 1284  LYS PHE GLU THR MET TYR ALA GLN SER LEU GLN ILE PRO          
SEQRES  72 B 1284  TYR ARG ASN ALA MET LYS LYS ALA HIS VAL PHE GLY ILE          
SEQRES  73 B 1284  THR PHE SER PHE THR GLN ALA MET MET TYR PHE SER TYR          
SEQRES  74 B 1284  ALA ALA CYS PHE ARG PHE GLY ALA TYR LEU VAL THR GLN          
SEQRES  75 B 1284  GLN LEU MET THR PHE GLU ASN VAL LEU LEU VAL PHE SER          
SEQRES  76 B 1284  ALA ILE VAL PHE GLY ALA MET ALA VAL GLY GLN VAL SER          
SEQRES  77 B 1284  SER PHE ALA PRO ASP TYR ALA LYS ALA THR VAL SER ALA          
SEQRES  78 B 1284  SER HIS ILE ILE ARG ILE ILE GLU LYS THR PRO GLU ILE          
SEQRES  79 B 1284  ASP SER TYR SER THR GLN GLY LEU LYS PRO ASN MET LEU          
SEQRES  80 B 1284  GLU GLY ASN VAL GLN PHE SER GLY VAL VAL PHE ASN TYR          
SEQRES  81 B 1284  PRO THR ARG PRO SER ILE PRO VAL LEU GLN GLY LEU SER          
SEQRES  82 B 1284  LEU GLU VAL LYS LYS GLY GLN THR LEU ALA LEU VAL GLY          
SEQRES  83 B 1284  SER SER GLY CYS GLY LYS SER THR VAL VAL GLN LEU LEU          
SEQRES  84 B 1284  GLU ARG PHE TYR ASP PRO MET ALA GLY SER VAL PHE LEU          
SEQRES  85 B 1284  ASP GLY LYS GLU ILE LYS GLN LEU ASN VAL GLN TRP LEU          
SEQRES  86 B 1284  ARG ALA GLN LEU GLY ILE VAL SER GLN GLU PRO ILE LEU          
SEQRES  87 B 1284  PHE ASP CYS SER ILE ALA GLU ASN ILE ALA TYR GLY ASP          
SEQRES  88 B 1284  ASN SER ARG VAL VAL SER TYR GLU GLU ILE VAL ARG ALA          
SEQRES  89 B 1284  ALA LYS GLU ALA ASN ILE HIS GLN PHE ILE ASP SER LEU          
SEQRES  90 B 1284  PRO ASP LYS TYR ASN THR ARG VAL GLY ASP LYS GLY THR          
SEQRES  91 B 1284  GLN LEU SER GLY GLY GLN LYS GLN ARG ILE ALA ILE ALA          
SEQRES  92 B 1284  ARG ALA LEU VAL ARG GLN PRO HIS ILE LEU LEU LEU ASP          
SEQRES  93 B 1284  GLU ALA THR SER ALA LEU ASP THR GLU SER GLU LYS VAL          
SEQRES  94 B 1284  VAL GLN GLU ALA LEU ASP LYS ALA ARG GLU GLY ARG THR          
SEQRES  95 B 1284  CYS ILE VAL ILE ALA HIS ARG LEU SER THR ILE GLN ASN          
SEQRES  96 B 1284  ALA ASP LEU ILE VAL VAL ILE GLN ASN GLY LYS VAL LYS          
SEQRES  97 B 1284  GLU HIS GLY THR HIS GLN GLN LEU LEU ALA GLN LYS GLY          
SEQRES  98 B 1284  ILE TYR PHE SER MET VAL SER VAL GLN ALA GLY ALA LYS          
SEQRES  99 B 1284  ARG SER TYR VAL HIS HIS HIS HIS HIS HIS                      
HET    2J8  A6001      36                                                       
HET    2J8  A6002      17                                                       
HET    2J8  B6003      36                                                       
HET    2J8  B6004      17                                                       
HETNAM     2J8 (4S,11S,18S)-4,11,18-TRI(PROPAN-2-YL)-6,13,20-                   
HETNAM   2 2J8  TRISELENA-3,10,17,22,23,24-                                     
HETNAM   3 2J8  HEXAAZATETRACYCLO[17.2.1.1~5,8~.1~12,15~]TETRACOSA-             
HETNAM   4 2J8  1(21),5(24),7,12(23),14,19(22)-HEXAENE-2,9,16-TRIONE            
HETSYN     2J8 CYCLIC-TRIS-(S)-VALINESELENAZOLE; QZ59-SSS                       
FORMUL   3  2J8    4(C24 H30 N6 O3 SE3)                                         
HELIX    1   1 VAL A   35  ARG A   40  1                                   6    
HELIX    2   2 GLY A   43  SER A   88  1                                  46    
HELIX    3   3 SER A   92  MET A  152  1                                  61    
HELIX    4   4 ASN A  153  GLU A  155  5                                   3    
HELIX    5   5 ILE A  156  VAL A  161  1                                   6    
HELIX    6   6 GLY A  165  ARG A  206  1                                  42    
HELIX    7   7 LYS A  209  VAL A  249  1                                  41    
HELIX    8   8 ALA A  256  ALA A  262  1                                   7    
HELIX    9   9 LYS A  268  ILE A  318  1                                  51    
HELIX   10  10 VAL A  327  ASN A  367  1                                  41    
HELIX   11  11 GLY A  428  MET A  436  1                                   9    
HELIX   12  12 ASN A  458  ILE A  465  1                                   8    
HELIX   13  13 THR A  479  ARG A  488  1                                  10    
HELIX   14  14 THR A  492  ALA A  503  1                                  12    
HELIX   15  15 ALA A  505  LEU A  512  1                                   8    
HELIX   16  16 HIS A  514  THR A  518  5                                   5    
HELIX   17  17 SER A  528  ASN A  544  1                                  17    
HELIX   18  18 ASP A  558  ARG A  573  1                                  16    
HELIX   19  19 ARG A  584  ASN A  590  1                                   7    
HELIX   20  20 ASN A  607  ARG A  613  1                                   7    
HELIX   21  21 GLY A  616  THR A  626  1                                  11    
HELIX   22  22 TRP A  694  TRP A  704  1                                  11    
HELIX   23  23 PHE A  707  ASN A  737  1                                  31    
HELIX   24  24 GLU A  742  ARG A  794  1                                  53    
HELIX   25  25 VAL A  797  ASP A  802  1                                   6    
HELIX   26  26 THR A  806  TYR A  849  1                                  44    
HELIX   27  27 GLN A  852  ASN A  899  1                                  48    
HELIX   28  28 ARG A  908  TYR A  958  1                                  51    
HELIX   29  29 ASN A  969  SER A  989  1                                  21    
HELIX   30  30 TYR A  994  LYS A 1010  1                                  17    
HELIX   31  31 THR A 1042  ILE A 1046  5                                   5    
HELIX   32  32 GLY A 1071  ARG A 1081  1                                  11    
HELIX   33  33 ASN A 1101  ARG A 1106  1                                   6    
HELIX   34  34 SER A 1122  ALA A 1128  1                                   7    
HELIX   35  35 SER A 1137  ALA A 1148  1                                  12    
HELIX   36  36 ILE A 1150  SER A 1156  1                                   7    
HELIX   37  37 SER A 1173  GLN A 1189  1                                  17    
HELIX   38  38 ASP A 1203  ALA A 1217  1                                  15    
HELIX   39  39 THR A 1252  GLN A 1259  1                                   8    
HELIX   40  40 GLY A 1261  ALA A 1271  1                                  11    
HELIX   41  41 VAL B   35  ARG B   40  1                                   6    
HELIX   42  42 GLY B   43  SER B   88  1                                  46    
HELIX   43  43 SER B   92  MET B  152  1                                  61    
HELIX   44  44 ASN B  153  GLU B  155  5                                   3    
HELIX   45  45 ILE B  156  VAL B  161  1                                   6    
HELIX   46  46 GLY B  165  ARG B  206  1                                  42    
HELIX   47  47 LYS B  209  VAL B  249  1                                  41    
HELIX   48  48 ALA B  256  ALA B  262  1                                   7    
HELIX   49  49 LYS B  268  ILE B  318  1                                  51    
HELIX   50  50 VAL B  327  ASN B  367  1                                  41    
HELIX   51  51 GLY B  428  GLN B  437  1                                  10    
HELIX   52  52 ASN B  458  ILE B  465  1                                   8    
HELIX   53  53 THR B  479  ARG B  488  1                                  10    
HELIX   54  54 THR B  492  ALA B  503  1                                  12    
HELIX   55  55 ALA B  505  LEU B  512  1                                   8    
HELIX   56  56 HIS B  514  THR B  518  5                                   5    
HELIX   57  57 SER B  528  ASN B  544  1                                  17    
HELIX   58  58 ASP B  558  ARG B  573  1                                  16    
HELIX   59  59 ARG B  584  ASN B  590  1                                   7    
HELIX   60  60 ASN B  607  ARG B  613  1                                   7    
HELIX   61  61 GLY B  616  THR B  626  1                                  11    
HELIX   62  62 TRP B  694  TRP B  704  1                                  11    
HELIX   63  63 PHE B  707  ASN B  737  1                                  31    
HELIX   64  64 GLU B  742  ARG B  794  1                                  53    
HELIX   65  65 VAL B  797  ASP B  802  1                                   6    
HELIX   66  66 THR B  806  TYR B  849  1                                  44    
HELIX   67  67 GLN B  852  ASN B  899  1                                  48    
HELIX   68  68 ARG B  908  TYR B  958  1                                  51    
HELIX   69  69 ASN B  969  SER B  989  1                                  21    
HELIX   70  70 TYR B  994  GLU B 1009  1                                  16    
HELIX   71  71 THR B 1042  ILE B 1046  5                                   5    
HELIX   72  72 GLY B 1071  ARG B 1081  1                                  11    
HELIX   73  73 ASN B 1101  ARG B 1106  1                                   6    
HELIX   74  74 SER B 1122  ALA B 1128  1                                   7    
HELIX   75  75 SER B 1137  ALA B 1148  1                                  12    
HELIX   76  76 ILE B 1150  SER B 1156  1                                   7    
HELIX   77  77 SER B 1173  GLN B 1189  1                                  17    
HELIX   78  78 ASP B 1203  ALA B 1217  1                                  15    
HELIX   79  79 THR B 1252  GLN B 1259  1                                   8    
HELIX   80  80 GLY B 1261  ALA B 1271  1                                  11    
SHEET    1   A 4 LEU A 409  VAL A 413  0                                        
SHEET    2   A 4 LEU A 388  HIS A 394 -1  N  PHE A 390   O  LEU A 411           
SHEET    3   A 4 ASP A 444  ILE A 449 -1  O  SER A 448   N  GLU A 389           
SHEET    4   A 4 GLN A 452  ASP A 453 -1  O  GLN A 452   N  ILE A 449           
SHEET    1   B 6 ILE A 466  VAL A 469  0                                        
SHEET    2   B 6 ILE A 547  ASP A 551  1  O  ILE A 547   N  GLY A 467           
SHEET    3   B 6 THR A 577  ILE A 581  1  O  ILE A 581   N  LEU A 550           
SHEET    4   B 6 THR A 418  VAL A 422  1  N  VAL A 419   O  THR A 578           
SHEET    5   B 6 VAL A 593  GLY A 596  1  O  ALA A 595   N  VAL A 422           
SHEET    6   B 6 GLN A 605  GLY A 606 -1  O  GLY A 606   N  ILE A 594           
SHEET    1   C 3 LEU A1054  VAL A1056  0                                        
SHEET    2   C 3 VAL A1031  VAL A1037 -1  N  PHE A1033   O  LEU A1054           
SHEET    3   C 3 ALA A1087  PHE A1091 -1  O  SER A1089   N  SER A1034           
SHEET    1   D 6 ILE A1111  VAL A1112  0                                        
SHEET    2   D 6 ILE A1192  ASP A1196  1  O  LEU A1194   N  VAL A1112           
SHEET    3   D 6 THR A1222  ILE A1226  1  O  ILE A1224   N  LEU A1195           
SHEET    4   D 6 THR A1061  VAL A1065  1  N  LEU A1062   O  CYS A1223           
SHEET    5   D 6 LEU A1238  GLN A1243  1  O  ILE A1242   N  VAL A1065           
SHEET    6   D 6 LYS A1246  GLY A1251 -1  O  LYS A1246   N  GLN A1243           
SHEET    1   E 4 LEU B 409  VAL B 413  0                                        
SHEET    2   E 4 LEU B 388  HIS B 394 -1  N  PHE B 390   O  LEU B 411           
SHEET    3   E 4 ASP B 444  ILE B 449 -1  O  SER B 448   N  GLU B 389           
SHEET    4   E 4 GLN B 452  ASP B 453 -1  O  GLN B 452   N  ILE B 449           
SHEET    1   F 6 ILE B 466  VAL B 469  0                                        
SHEET    2   F 6 ILE B 547  ASP B 551  1  O  ILE B 547   N  GLY B 467           
SHEET    3   F 6 THR B 577  ILE B 581  1  O  ILE B 581   N  LEU B 550           
SHEET    4   F 6 THR B 418  VAL B 422  1  N  VAL B 419   O  THR B 578           
SHEET    5   F 6 VAL B 593  GLY B 596  1  O  ALA B 595   N  VAL B 422           
SHEET    6   F 6 GLN B 605  GLY B 606 -1  O  GLY B 606   N  ILE B 594           
SHEET    1   G 3 GLU B1055  VAL B1056  0                                        
SHEET    2   G 3 VAL B1031  VAL B1037 -1  N  VAL B1031   O  VAL B1056           
SHEET    3   G 3 ALA B1087  PHE B1091 -1  O  SER B1089   N  SER B1034           
SHEET    1   H 6 ILE B1111  VAL B1112  0                                        
SHEET    2   H 6 ILE B1192  ASP B1196  1  O  LEU B1194   N  VAL B1112           
SHEET    3   H 6 THR B1222  ILE B1226  1  O  ILE B1224   N  LEU B1195           
SHEET    4   H 6 THR B1061  VAL B1065  1  N  LEU B1062   O  CYS B1223           
SHEET    5   H 6 LEU B1238  GLN B1243  1  O  ILE B1242   N  VAL B1065           
SHEET    6   H 6 LYS B1246  GLY B1251 -1  O  LYS B1246   N  GLN B1243           
SITE     1 AC1  5 LEU A 300  TYR A 303  PHE A 339  VAL A 978                    
SITE     2 AC1  5 GLY A 985                                                     
SITE     1 AC2  7 PHE A 332  PHE A 728  TYR A 949  LEU A 971                    
SITE     2 AC2  7 PHE A 974  ILE A 977  VAL A 978                               
SITE     1 AC3  9 TYR B 303  PHE B 339  GLN B 721  PHE B 724                    
SITE     2 AC3  9 VAL B 978  MET B 982  GLY B 985  GLN B 986                    
SITE     3 AC3  9 SER B 989                                                     
SITE     1 AC4  5 PHE B 332  ILE B 336  TYR B 949  PHE B 974                    
SITE     2 AC4  5 VAL B 978                                                     
CRYST1   97.742  114.978  375.810  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      0.010231  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008697  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002661        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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