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Database: PDB
Entry: 5D39
LinkDB: 5D39
Original site: 5D39 
HEADER    TRANSCRIPTION/DNA                       06-AUG-15   5D39              
TITLE     TRANSCRIPTION FACTOR-DNA COMPLEX                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 6;        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 123-658;                                      
COMPND   5 SYNONYM: IL-4 STAT;                                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(P*TP*CP*TP*GP*TP*CP*TP*TP*CP*CP*AP*GP*GP*AP*AP*AP*TP*CP*CP*AP*T)-  
COMPND  10 3');                                                                 
COMPND  11 CHAIN: N, F;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-                                                   
COMPND  15 D(P*AP*TP*GP*GP*AP*TP*TP*TP*CP*CP*TP*GP*GP*AP*AP*GP*AP*CP*AP*GP*A)-  
COMPND  16 3');                                                                 
COMPND  17 CHAIN: M, E;                                                         
COMPND  18 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: STAT6;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG7;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 SYNTHETIC: YES;                                                      
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_TAXID: 9606                                                 
KEYWDS    REGULATION, DNA BINDING, INNATE IMMUNE, TRANSCRIPTION-DNA COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LI,F.NIU,S.OUYANG,Z.LIU                                             
REVDAT   5   30-AUG-17 5D39    1       JRNL   REMARK                            
REVDAT   4   30-NOV-16 5D39    1       JRNL                                     
REVDAT   3   16-NOV-16 5D39    1       JRNL                                     
REVDAT   2   02-NOV-16 5D39    1       JRNL                                     
REVDAT   1   10-AUG-16 5D39    0                                                
JRNL        AUTH   J.LI,J.P.RODRIGUEZ,F.NIU,M.PU,J.WANG,L.W.HUNG,Q.SHAO,Y.ZHU,  
JRNL        AUTH 2 W.DING,Y.LIU,Y.DA,Z.YAO,J.YANG,Y.ZHAO,G.H.WEI,G.CHENG,       
JRNL        AUTH 3 Z.J.LIU,S.OUYANG                                             
JRNL        TITL   STRUCTURAL BASIS FOR DNA RECOGNITION BY STAT6                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113 13015 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   27803324                                                     
JRNL        DOI    10.1073/PNAS.1611228113                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 57110                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.760                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3118                            
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 44.1247 -  8.6664    0.92     5347   141  0.1576 0.2067        
REMARK   3     2  8.6664 -  6.8873    0.94     5457   149  0.1782 0.1792        
REMARK   3     3  6.8873 -  6.0191    0.95     5554   151  0.2239 0.2577        
REMARK   3     4  6.0191 -  5.4699    0.95     5518   140  0.2103 0.2340        
REMARK   3     5  5.4699 -  5.0784    0.95     5474   153  0.2153 0.2274        
REMARK   3     6  5.0784 -  4.7794    0.95     5582   153  0.1916 0.2380        
REMARK   3     7  4.7794 -  4.5403    0.96     5461   149  0.1808 0.1773        
REMARK   3     8  4.5403 -  4.3428    0.96     5570   147  0.1930 0.2307        
REMARK   3     9  4.3428 -  4.1758    0.95     5526   163  0.2045 0.2028        
REMARK   3    10  4.1758 -  4.0318    0.95     5474   140  0.2072 0.2528        
REMARK   3    11  4.0318 -  3.9058    0.94     5520   158  0.2306 0.2776        
REMARK   3    12  3.9058 -  3.7942    0.95     5415   138  0.2392 0.2930        
REMARK   3    13  3.7942 -  3.6944    0.95     5631   158  0.2400 0.2585        
REMARK   3    14  3.6944 -  3.6043    0.94     5402   155  0.2637 0.2811        
REMARK   3    15  3.6043 -  3.5224    0.94     5498   148  0.2641 0.3138        
REMARK   3    16  3.5224 -  3.4475    0.94     5427   128  0.2758 0.2798        
REMARK   3    17  3.4475 -  3.3785    0.94     5499   160  0.2846 0.3030        
REMARK   3    18  3.3785 -  3.3148    0.94     5493   149  0.3040 0.2955        
REMARK   3    19  3.3148 -  3.2556    0.94     5358   145  0.3094 0.3250        
REMARK   3    20  3.2556 -  3.2004    0.94     5592   146  0.3347 0.3702        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.770           
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      :  0.006          17677                                  
REMARK   3   ANGLE     :  1.321          24207                                  
REMARK   3   CHIRALITY :  0.054           2726                                  
REMARK   3   PLANARITY :  0.007           2814                                  
REMARK   3   DIHEDRAL  : 21.352           6821                                  
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 5D39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212554.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57110                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.69500                            
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: 4Y5U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE (PH 5.6), 0.1 M NACL,      
REMARK 280  20% ISOPROPYL ALCOHOL AND 8% PEG4000, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 289K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, N, M, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, N, M                            
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 55700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     TRP A   123                                                      
REMARK 465     LYS A   124                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     VAL A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     LEU A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     ILE A   166                                                      
REMARK 465     GLU A   167                                                      
REMARK 465     THR A   168                                                      
REMARK 465     PRO A   169                                                      
REMARK 465     ALA A   170                                                      
REMARK 465     ASN A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     THR A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     ALA A   304                                                      
REMARK 465     SER A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     GLN A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     PRO A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     ALA A   334                                                      
REMARK 465     ARG A   652                                                      
REMARK 465     ASP A   653                                                      
REMARK 465     GLN A   654                                                      
REMARK 465     PRO A   655                                                      
REMARK 465     LEU A   656                                                      
REMARK 465     PRO A   657                                                      
REMARK 465     THR A   658                                                      
REMARK 465     SER B   120                                                      
REMARK 465     ASN B   121                                                      
REMARK 465     ALA B   122                                                      
REMARK 465     TRP B   123                                                      
REMARK 465     LYS B   124                                                      
REMARK 465     GLN B   152                                                      
REMARK 465     LYS B   153                                                      
REMARK 465     GLY B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     GLY B   158                                                      
REMARK 465     GLN B   159                                                      
REMARK 465     VAL B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     LEU B   162                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     ILE B   166                                                      
REMARK 465     GLU B   167                                                      
REMARK 465     THR B   168                                                      
REMARK 465     PRO B   169                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     ASN B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     THR B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     ALA B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     LEU B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     ALA B   304                                                      
REMARK 465     SER B   325                                                      
REMARK 465     VAL B   326                                                      
REMARK 465     PRO B   327                                                      
REMARK 465     GLN B   328                                                      
REMARK 465     GLY B   329                                                      
REMARK 465     PRO B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     ALA B   332                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     ALA B   334                                                      
REMARK 465     ARG B   373                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     ARG B   652                                                      
REMARK 465     ASP B   653                                                      
REMARK 465     GLN B   654                                                      
REMARK 465     PRO B   655                                                      
REMARK 465     LEU B   656                                                      
REMARK 465     PRO B   657                                                      
REMARK 465     THR B   658                                                      
REMARK 465     SER C   120                                                      
REMARK 465     ASN C   121                                                      
REMARK 465     ALA C   122                                                      
REMARK 465     TRP C   123                                                      
REMARK 465     LYS C   124                                                      
REMARK 465     GLN C   152                                                      
REMARK 465     LYS C   153                                                      
REMARK 465     GLY C   154                                                      
REMARK 465     ALA C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     ALA C   157                                                      
REMARK 465     GLY C   158                                                      
REMARK 465     GLN C   159                                                      
REMARK 465     VAL C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     LEU C   162                                                      
REMARK 465     HIS C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     LEU C   165                                                      
REMARK 465     ILE C   166                                                      
REMARK 465     GLU C   167                                                      
REMARK 465     THR C   168                                                      
REMARK 465     PRO C   169                                                      
REMARK 465     ALA C   170                                                      
REMARK 465     ASN C   171                                                      
REMARK 465     GLY C   172                                                      
REMARK 465     THR C   173                                                      
REMARK 465     GLY C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     SER C   176                                                      
REMARK 465     LEU C   302                                                      
REMARK 465     GLY C   303                                                      
REMARK 465     ALA C   304                                                      
REMARK 465     SER C   325                                                      
REMARK 465     VAL C   326                                                      
REMARK 465     PRO C   327                                                      
REMARK 465     GLN C   328                                                      
REMARK 465     GLY C   329                                                      
REMARK 465     PRO C   330                                                      
REMARK 465     GLY C   331                                                      
REMARK 465     ALA C   332                                                      
REMARK 465     GLY C   333                                                      
REMARK 465     ALA C   334                                                      
REMARK 465     ARG C   373                                                      
REMARK 465     LYS C   374                                                      
REMARK 465     GLY C   375                                                      
REMARK 465     GLN C   580                                                      
REMARK 465     ASP C   581                                                      
REMARK 465     ARG C   652                                                      
REMARK 465     ASP C   653                                                      
REMARK 465     GLN C   654                                                      
REMARK 465     PRO C   655                                                      
REMARK 465     LEU C   656                                                      
REMARK 465     PRO C   657                                                      
REMARK 465     THR C   658                                                      
REMARK 465     SER D   120                                                      
REMARK 465     ASN D   121                                                      
REMARK 465     ALA D   122                                                      
REMARK 465     TRP D   123                                                      
REMARK 465     LYS D   124                                                      
REMARK 465     LYS D   153                                                      
REMARK 465     GLY D   154                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     GLU D   156                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     GLY D   158                                                      
REMARK 465     GLN D   159                                                      
REMARK 465     VAL D   160                                                      
REMARK 465     SER D   161                                                      
REMARK 465     LEU D   162                                                      
REMARK 465     HIS D   163                                                      
REMARK 465     SER D   164                                                      
REMARK 465     LEU D   165                                                      
REMARK 465     ILE D   166                                                      
REMARK 465     GLU D   167                                                      
REMARK 465     THR D   168                                                      
REMARK 465     PRO D   169                                                      
REMARK 465     ALA D   170                                                      
REMARK 465     ASN D   171                                                      
REMARK 465     GLY D   172                                                      
REMARK 465     THR D   173                                                      
REMARK 465     GLY D   174                                                      
REMARK 465     PRO D   175                                                      
REMARK 465     SER D   176                                                      
REMARK 465     LEU D   302                                                      
REMARK 465     GLY D   303                                                      
REMARK 465     ALA D   304                                                      
REMARK 465     SER D   325                                                      
REMARK 465     VAL D   326                                                      
REMARK 465     PRO D   327                                                      
REMARK 465     GLN D   328                                                      
REMARK 465     GLY D   329                                                      
REMARK 465     PRO D   330                                                      
REMARK 465     GLY D   331                                                      
REMARK 465     ALA D   332                                                      
REMARK 465     GLY D   333                                                      
REMARK 465     ALA D   334                                                      
REMARK 465     ARG D   373                                                      
REMARK 465     LYS D   374                                                      
REMARK 465     GLY D   375                                                      
REMARK 465     ARG D   652                                                      
REMARK 465     ASP D   653                                                      
REMARK 465     GLN D   654                                                      
REMARK 465     PRO D   655                                                      
REMARK 465     LEU D   656                                                      
REMARK 465     PRO D   657                                                      
REMARK 465     THR D   658                                                      
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   OD1  ASP B   637     NH2  ARG B   639              1.13            
REMARK 500   O    GLU D   372     OE1  GLU D   377              1.34            
REMARK 500   OD1  ASP B   637     NH1  ARG B   639              1.69            
REMARK 500   O    ALA A   245     CD2  LEU A   249              1.69            
REMARK 500   O    GLY A   246     CG   LEU A   249              1.71            
REMARK 500   OE2  GLU B   587     NZ   LYS D   636              1.85            
REMARK 500   CG   ASP B   637     NH2  ARG B   639              1.92            
REMARK 500   O    GLN C   585     O    HOH C   701              1.95            
REMARK 500   O    LYS B   319     O    HOH B   701              1.96            
REMARK 500   O    ASP B   429     OG   SER B   433              2.00            
REMARK 500   CD   ARG D   437     O    VAL D   441              2.01            
REMARK 500   O    ASP B   637     O    PTR B   641              2.02            
REMARK 500   OE2  GLU C   381     NZ   LYS C   504              2.03            
REMARK 500   CA   ARG C   437     O    HOH C   735              2.04            
REMARK 500   O    LEU A   310     O    VAL A   345              2.04            
REMARK 500   OE2  GLU D   381     NZ   LYS D   504              2.06            
REMARK 500   C    GLU D   372     OE1  GLU D   377              2.06            
REMARK 500   NE   ARG D   437     O    VAL D   441              2.07            
REMARK 500   OG   SER D   378     OE2  GLU D   381              2.09            
REMARK 500   O    LEU B   183     OG1  THR B   187              2.12            
REMARK 500   O    ASP A   429     OG   SER A   433              2.14            
REMARK 500   CB   LEU C   359     O    HOH C   706              2.14            
REMARK 500   O    LEU C   612     O    HOH C   702              2.14            
REMARK 500   CD2  LEU D   179     CD2  LEU D   182              2.15            
REMARK 500   CA   GLY A   397     O    HOH A   741              2.15            
REMARK 500   OE2  GLU B   381     NZ   LYS B   504              2.16            
REMARK 500   NH2  ARG D   437     CA   PHE D   440              2.17            
REMARK 500   CG   GLN A   125     O    HOH A   750              2.17            
REMARK 500   O    LEU C   609     O    HOH C   702              2.17            
REMARK 500   O4    DT N    21     N6    DA M     1              2.18            
REMARK 500   OG   SER D   433     NH1  ARG D   437              2.18            
REMARK 500   O    GLY C   638     O    HOH C   703              2.18            
REMARK 500   O    MET B   181     NE2  GLN B   184              2.18            
REMARK 500   CB   GLU C   177     O    HOH C   734              2.18            
REMARK 500   NZ   LYS C   621     O    HOH C   702              2.19            
REMARK 500   OE1  GLU C   381     NZ   LYS C   504              2.19            
REMARK 500   O    LEU B   359     NZ   LYS B   361              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DT N   1   C1'    DT N   1   N1      0.088                       
REMARK 500     DT N   1   C2     DT N   1   O2     -0.052                       
REMARK 500     DG N   4   O3'    DG N   4   C3'    -0.039                       
REMARK 500     DA M   5   O3'    DA M   5   C3'    -0.037                       
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    LEU B 508   CA  -  CB  -  CG  ANGL. DEV. =  20.8 DEGREES          
REMARK 500    LEU C 151   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    LEU C 182   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500     DT N   1   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DC N   2   O4' -  C1' -  N1  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DT N   3   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DC N  10   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA N  14   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC N  18   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DA N  20   C1' -  O4' -  C4' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DA N  20   O4' -  C1' -  N9  ANGL. DEV. =   7.9 DEGREES          
REMARK 500     DA M   1   O4' -  C1' -  N9  ANGL. DEV. =   5.6 DEGREES          
REMARK 500     DT M   2   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DG M   3   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA M   5   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT M   7   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DG M  12   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA M  15   O4' -  C1' -  N9  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DA M  21   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DT E   6   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DA E  15   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT F   1   O4' -  C1' -  N1  ANGL. DEV. =   2.3 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    THR A 376        4.22     82.81                                   
REMARK 500    GLU A 377       97.58    -49.04                                   
REMARK 500    PRO A 396       93.84    -53.44                                   
REMARK 500    MET A 435     -131.50     55.06                                   
REMARK 500    HIS A 494       37.86    -93.39                                   
REMARK 500    GLN A 580     -130.06     64.30                                   
REMARK 500    LYS A 618       35.19   -149.84                                   
REMARK 500    GLU B 149       17.98    -69.49                                   
REMARK 500    GLU B 248       55.71    -93.27                                   
REMARK 500    LEU B 310       77.46     78.49                                   
REMARK 500    SER B 336       50.34     33.76                                   
REMARK 500    THR B 393       46.84     70.74                                   
REMARK 500    HIS B 494       35.69    -94.62                                   
REMARK 500    ILE B 542      147.91   -176.53                                   
REMARK 500    GLN B 580      -57.85     73.07                                   
REMARK 500    LYS B 618      -55.33     72.62                                   
REMARK 500    LYS B 619      124.10    -35.94                                   
REMARK 500    MET B 634     -134.92     53.68                                   
REMARK 500    ASP B 637     -178.73    148.10                                   
REMARK 500    THR C 337       55.31     39.23                                   
REMARK 500    HIS C 494       34.37    -94.78                                   
REMARK 500    LEU C 508     -131.09     56.04                                   
REMARK 500    ALA D 180      -16.69     93.01                                   
REMARK 500    ASN D 213        8.49     85.03                                   
REMARK 500    PRO D 216      141.92    -33.83                                   
REMARK 500    THR D 337       28.20     49.79                                   
REMARK 500    VAL D 379      -56.44     71.97                                   
REMARK 500    LYS D 398      -54.60   -127.17                                   
REMARK 500    GLN D 580     -130.62     64.40                                   
REMARK 500    LYS D 618        2.56     58.49                                   
REMARK 500    MET D 634     -177.62     78.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  219     SER A  220                 -149.49                    
REMARK 500 ALA B  245     GLY B  246                  146.29                    
REMARK 500 ALA D  180     MET D  181                  144.46                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5D39 A  123   658  UNP    P42226   STAT6_HUMAN    123    658             
DBREF  5D39 B  123   658  UNP    P42226   STAT6_HUMAN    123    658             
DBREF  5D39 C  123   658  UNP    P42226   STAT6_HUMAN    123    658             
DBREF  5D39 D  123   658  UNP    P42226   STAT6_HUMAN    123    658             
DBREF  5D39 N    1    21  PDB    5D39     5D39             1     21             
DBREF  5D39 M    1    21  PDB    5D39     5D39             1     21             
DBREF  5D39 E    1    21  PDB    5D39     5D39             1     21             
DBREF  5D39 F    1    21  PDB    5D39     5D39             1     21             
SEQADV 5D39 SER A  120  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ASN A  121  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ALA A  122  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 SER B  120  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ASN B  121  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ALA B  122  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 SER C  120  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ASN C  121  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ALA C  122  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 SER D  120  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ASN D  121  UNP  P42226              EXPRESSION TAG                 
SEQADV 5D39 ALA D  122  UNP  P42226              EXPRESSION TAG                 
SEQRES   1 A  539  SER ASN ALA TRP LYS GLN GLU GLU LEU LYS PHE LYS THR          
SEQRES   2 A  539  GLY LEU ARG ARG LEU GLN HIS ARG VAL GLY GLU ILE HIS          
SEQRES   3 A  539  LEU LEU ARG GLU ALA LEU GLN LYS GLY ALA GLU ALA GLY          
SEQRES   4 A  539  GLN VAL SER LEU HIS SER LEU ILE GLU THR PRO ALA ASN          
SEQRES   5 A  539  GLY THR GLY PRO SER GLU ALA LEU ALA MET LEU LEU GLN          
SEQRES   6 A  539  GLU THR THR GLY GLU LEU GLU ALA ALA LYS ALA LEU VAL          
SEQRES   7 A  539  LEU LYS ARG ILE GLN ILE TRP LYS ARG GLN GLN GLN LEU          
SEQRES   8 A  539  ALA GLY ASN GLY ALA PRO PHE GLU GLU SER LEU ALA PRO          
SEQRES   9 A  539  LEU GLN GLU ARG CYS GLU SER LEU VAL ASP ILE TYR SER          
SEQRES  10 A  539  GLN LEU GLN GLN GLU VAL GLY ALA ALA GLY GLY GLU LEU          
SEQRES  11 A  539  GLU PRO LYS THR ARG ALA SER LEU THR GLY ARG LEU ASP          
SEQRES  12 A  539  GLU VAL LEU ARG THR LEU VAL THR SER CYS PHE LEU VAL          
SEQRES  13 A  539  GLU LYS GLN PRO PRO GLN VAL LEU LYS THR GLN THR LYS          
SEQRES  14 A  539  PHE GLN ALA GLY VAL ARG PHE LEU LEU GLY LEU ARG PHE          
SEQRES  15 A  539  LEU GLY ALA PRO ALA LYS PRO PRO LEU VAL ARG ALA ASP          
SEQRES  16 A  539  MET VAL THR GLU LYS GLN ALA ARG GLU LEU SER VAL PRO          
SEQRES  17 A  539  GLN GLY PRO GLY ALA GLY ALA GLU SER THR GLY GLU ILE          
SEQRES  18 A  539  ILE ASN ASN THR VAL PRO LEU GLU ASN SER ILE PRO GLY          
SEQRES  19 A  539  ASN CYS CYS SER ALA LEU PHE LYS ASN LEU LEU LEU LYS          
SEQRES  20 A  539  LYS ILE LYS ARG CYS GLU ARG LYS GLY THR GLU SER VAL          
SEQRES  21 A  539  THR GLU GLU LYS CYS ALA VAL LEU PHE SER ALA SER PHE          
SEQRES  22 A  539  THR LEU GLY PRO GLY LYS LEU PRO ILE GLN LEU GLN ALA          
SEQRES  23 A  539  LEU SER LEU PRO LEU VAL VAL ILE VAL HIS GLY ASN GLN          
SEQRES  24 A  539  ASP ASN ASN ALA LYS ALA THR ILE LEU TRP ASP ASN ALA          
SEQRES  25 A  539  PHE SER GLU MET ASP ARG VAL PRO PHE VAL VAL ALA GLU          
SEQRES  26 A  539  ARG VAL PRO TRP GLU LYS MET CYS GLU THR LEU ASN LEU          
SEQRES  27 A  539  LYS PHE MET ALA GLU VAL GLY THR ASN ARG GLY LEU LEU          
SEQRES  28 A  539  PRO GLU HIS PHE LEU PHE LEU ALA GLN LYS ILE PHE ASN          
SEQRES  29 A  539  ASP ASN SER LEU SER MET GLU ALA PHE GLN HIS ARG SER          
SEQRES  30 A  539  VAL SER TRP SER GLN PHE ASN LYS GLU ILE LEU LEU GLY          
SEQRES  31 A  539  ARG GLY PHE THR PHE TRP GLN TRP PHE ASP GLY VAL LEU          
SEQRES  32 A  539  ASP LEU THR LYS ARG CYS LEU ARG SER TYR TRP SER ASP          
SEQRES  33 A  539  ARG LEU ILE ILE GLY PHE ILE SER LYS GLN TYR VAL THR          
SEQRES  34 A  539  SER LEU LEU LEU ASN GLU PRO ASP GLY THR PHE LEU LEU          
SEQRES  35 A  539  ARG PHE SER ASP SER GLU ILE GLY GLY ILE THR ILE ALA          
SEQRES  36 A  539  HIS VAL ILE ARG GLY GLN ASP GLY SER PRO GLN ILE GLU          
SEQRES  37 A  539  ASN ILE GLN PRO PHE SER ALA LYS ASP LEU SER ILE ARG          
SEQRES  38 A  539  SER LEU GLY ASP ARG ILE ARG ASP LEU ALA GLN LEU LYS          
SEQRES  39 A  539  ASN LEU TYR PRO LYS LYS PRO LYS ASP GLU ALA PHE ARG          
SEQRES  40 A  539  SER HIS TYR LYS PRO GLU GLN MET GLY LYS ASP GLY ARG          
SEQRES  41 A  539  GLY PTR VAL PRO ALA THR ILE LYS MET THR VAL GLU ARG          
SEQRES  42 A  539  ASP GLN PRO LEU PRO THR                                      
SEQRES   1 B  539  SER ASN ALA TRP LYS GLN GLU GLU LEU LYS PHE LYS THR          
SEQRES   2 B  539  GLY LEU ARG ARG LEU GLN HIS ARG VAL GLY GLU ILE HIS          
SEQRES   3 B  539  LEU LEU ARG GLU ALA LEU GLN LYS GLY ALA GLU ALA GLY          
SEQRES   4 B  539  GLN VAL SER LEU HIS SER LEU ILE GLU THR PRO ALA ASN          
SEQRES   5 B  539  GLY THR GLY PRO SER GLU ALA LEU ALA MET LEU LEU GLN          
SEQRES   6 B  539  GLU THR THR GLY GLU LEU GLU ALA ALA LYS ALA LEU VAL          
SEQRES   7 B  539  LEU LYS ARG ILE GLN ILE TRP LYS ARG GLN GLN GLN LEU          
SEQRES   8 B  539  ALA GLY ASN GLY ALA PRO PHE GLU GLU SER LEU ALA PRO          
SEQRES   9 B  539  LEU GLN GLU ARG CYS GLU SER LEU VAL ASP ILE TYR SER          
SEQRES  10 B  539  GLN LEU GLN GLN GLU VAL GLY ALA ALA GLY GLY GLU LEU          
SEQRES  11 B  539  GLU PRO LYS THR ARG ALA SER LEU THR GLY ARG LEU ASP          
SEQRES  12 B  539  GLU VAL LEU ARG THR LEU VAL THR SER CYS PHE LEU VAL          
SEQRES  13 B  539  GLU LYS GLN PRO PRO GLN VAL LEU LYS THR GLN THR LYS          
SEQRES  14 B  539  PHE GLN ALA GLY VAL ARG PHE LEU LEU GLY LEU ARG PHE          
SEQRES  15 B  539  LEU GLY ALA PRO ALA LYS PRO PRO LEU VAL ARG ALA ASP          
SEQRES  16 B  539  MET VAL THR GLU LYS GLN ALA ARG GLU LEU SER VAL PRO          
SEQRES  17 B  539  GLN GLY PRO GLY ALA GLY ALA GLU SER THR GLY GLU ILE          
SEQRES  18 B  539  ILE ASN ASN THR VAL PRO LEU GLU ASN SER ILE PRO GLY          
SEQRES  19 B  539  ASN CYS CYS SER ALA LEU PHE LYS ASN LEU LEU LEU LYS          
SEQRES  20 B  539  LYS ILE LYS ARG CYS GLU ARG LYS GLY THR GLU SER VAL          
SEQRES  21 B  539  THR GLU GLU LYS CYS ALA VAL LEU PHE SER ALA SER PHE          
SEQRES  22 B  539  THR LEU GLY PRO GLY LYS LEU PRO ILE GLN LEU GLN ALA          
SEQRES  23 B  539  LEU SER LEU PRO LEU VAL VAL ILE VAL HIS GLY ASN GLN          
SEQRES  24 B  539  ASP ASN ASN ALA LYS ALA THR ILE LEU TRP ASP ASN ALA          
SEQRES  25 B  539  PHE SER GLU MET ASP ARG VAL PRO PHE VAL VAL ALA GLU          
SEQRES  26 B  539  ARG VAL PRO TRP GLU LYS MET CYS GLU THR LEU ASN LEU          
SEQRES  27 B  539  LYS PHE MET ALA GLU VAL GLY THR ASN ARG GLY LEU LEU          
SEQRES  28 B  539  PRO GLU HIS PHE LEU PHE LEU ALA GLN LYS ILE PHE ASN          
SEQRES  29 B  539  ASP ASN SER LEU SER MET GLU ALA PHE GLN HIS ARG SER          
SEQRES  30 B  539  VAL SER TRP SER GLN PHE ASN LYS GLU ILE LEU LEU GLY          
SEQRES  31 B  539  ARG GLY PHE THR PHE TRP GLN TRP PHE ASP GLY VAL LEU          
SEQRES  32 B  539  ASP LEU THR LYS ARG CYS LEU ARG SER TYR TRP SER ASP          
SEQRES  33 B  539  ARG LEU ILE ILE GLY PHE ILE SER LYS GLN TYR VAL THR          
SEQRES  34 B  539  SER LEU LEU LEU ASN GLU PRO ASP GLY THR PHE LEU LEU          
SEQRES  35 B  539  ARG PHE SER ASP SER GLU ILE GLY GLY ILE THR ILE ALA          
SEQRES  36 B  539  HIS VAL ILE ARG GLY GLN ASP GLY SER PRO GLN ILE GLU          
SEQRES  37 B  539  ASN ILE GLN PRO PHE SER ALA LYS ASP LEU SER ILE ARG          
SEQRES  38 B  539  SER LEU GLY ASP ARG ILE ARG ASP LEU ALA GLN LEU LYS          
SEQRES  39 B  539  ASN LEU TYR PRO LYS LYS PRO LYS ASP GLU ALA PHE ARG          
SEQRES  40 B  539  SER HIS TYR LYS PRO GLU GLN MET GLY LYS ASP GLY ARG          
SEQRES  41 B  539  GLY PTR VAL PRO ALA THR ILE LYS MET THR VAL GLU ARG          
SEQRES  42 B  539  ASP GLN PRO LEU PRO THR                                      
SEQRES   1 C  539  SER ASN ALA TRP LYS GLN GLU GLU LEU LYS PHE LYS THR          
SEQRES   2 C  539  GLY LEU ARG ARG LEU GLN HIS ARG VAL GLY GLU ILE HIS          
SEQRES   3 C  539  LEU LEU ARG GLU ALA LEU GLN LYS GLY ALA GLU ALA GLY          
SEQRES   4 C  539  GLN VAL SER LEU HIS SER LEU ILE GLU THR PRO ALA ASN          
SEQRES   5 C  539  GLY THR GLY PRO SER GLU ALA LEU ALA MET LEU LEU GLN          
SEQRES   6 C  539  GLU THR THR GLY GLU LEU GLU ALA ALA LYS ALA LEU VAL          
SEQRES   7 C  539  LEU LYS ARG ILE GLN ILE TRP LYS ARG GLN GLN GLN LEU          
SEQRES   8 C  539  ALA GLY ASN GLY ALA PRO PHE GLU GLU SER LEU ALA PRO          
SEQRES   9 C  539  LEU GLN GLU ARG CYS GLU SER LEU VAL ASP ILE TYR SER          
SEQRES  10 C  539  GLN LEU GLN GLN GLU VAL GLY ALA ALA GLY GLY GLU LEU          
SEQRES  11 C  539  GLU PRO LYS THR ARG ALA SER LEU THR GLY ARG LEU ASP          
SEQRES  12 C  539  GLU VAL LEU ARG THR LEU VAL THR SER CYS PHE LEU VAL          
SEQRES  13 C  539  GLU LYS GLN PRO PRO GLN VAL LEU LYS THR GLN THR LYS          
SEQRES  14 C  539  PHE GLN ALA GLY VAL ARG PHE LEU LEU GLY LEU ARG PHE          
SEQRES  15 C  539  LEU GLY ALA PRO ALA LYS PRO PRO LEU VAL ARG ALA ASP          
SEQRES  16 C  539  MET VAL THR GLU LYS GLN ALA ARG GLU LEU SER VAL PRO          
SEQRES  17 C  539  GLN GLY PRO GLY ALA GLY ALA GLU SER THR GLY GLU ILE          
SEQRES  18 C  539  ILE ASN ASN THR VAL PRO LEU GLU ASN SER ILE PRO GLY          
SEQRES  19 C  539  ASN CYS CYS SER ALA LEU PHE LYS ASN LEU LEU LEU LYS          
SEQRES  20 C  539  LYS ILE LYS ARG CYS GLU ARG LYS GLY THR GLU SER VAL          
SEQRES  21 C  539  THR GLU GLU LYS CYS ALA VAL LEU PHE SER ALA SER PHE          
SEQRES  22 C  539  THR LEU GLY PRO GLY LYS LEU PRO ILE GLN LEU GLN ALA          
SEQRES  23 C  539  LEU SER LEU PRO LEU VAL VAL ILE VAL HIS GLY ASN GLN          
SEQRES  24 C  539  ASP ASN ASN ALA LYS ALA THR ILE LEU TRP ASP ASN ALA          
SEQRES  25 C  539  PHE SER GLU MET ASP ARG VAL PRO PHE VAL VAL ALA GLU          
SEQRES  26 C  539  ARG VAL PRO TRP GLU LYS MET CYS GLU THR LEU ASN LEU          
SEQRES  27 C  539  LYS PHE MET ALA GLU VAL GLY THR ASN ARG GLY LEU LEU          
SEQRES  28 C  539  PRO GLU HIS PHE LEU PHE LEU ALA GLN LYS ILE PHE ASN          
SEQRES  29 C  539  ASP ASN SER LEU SER MET GLU ALA PHE GLN HIS ARG SER          
SEQRES  30 C  539  VAL SER TRP SER GLN PHE ASN LYS GLU ILE LEU LEU GLY          
SEQRES  31 C  539  ARG GLY PHE THR PHE TRP GLN TRP PHE ASP GLY VAL LEU          
SEQRES  32 C  539  ASP LEU THR LYS ARG CYS LEU ARG SER TYR TRP SER ASP          
SEQRES  33 C  539  ARG LEU ILE ILE GLY PHE ILE SER LYS GLN TYR VAL THR          
SEQRES  34 C  539  SER LEU LEU LEU ASN GLU PRO ASP GLY THR PHE LEU LEU          
SEQRES  35 C  539  ARG PHE SER ASP SER GLU ILE GLY GLY ILE THR ILE ALA          
SEQRES  36 C  539  HIS VAL ILE ARG GLY GLN ASP GLY SER PRO GLN ILE GLU          
SEQRES  37 C  539  ASN ILE GLN PRO PHE SER ALA LYS ASP LEU SER ILE ARG          
SEQRES  38 C  539  SER LEU GLY ASP ARG ILE ARG ASP LEU ALA GLN LEU LYS          
SEQRES  39 C  539  ASN LEU TYR PRO LYS LYS PRO LYS ASP GLU ALA PHE ARG          
SEQRES  40 C  539  SER HIS TYR LYS PRO GLU GLN MET GLY LYS ASP GLY ARG          
SEQRES  41 C  539  GLY PTR VAL PRO ALA THR ILE LYS MET THR VAL GLU ARG          
SEQRES  42 C  539  ASP GLN PRO LEU PRO THR                                      
SEQRES   1 D  539  SER ASN ALA TRP LYS GLN GLU GLU LEU LYS PHE LYS THR          
SEQRES   2 D  539  GLY LEU ARG ARG LEU GLN HIS ARG VAL GLY GLU ILE HIS          
SEQRES   3 D  539  LEU LEU ARG GLU ALA LEU GLN LYS GLY ALA GLU ALA GLY          
SEQRES   4 D  539  GLN VAL SER LEU HIS SER LEU ILE GLU THR PRO ALA ASN          
SEQRES   5 D  539  GLY THR GLY PRO SER GLU ALA LEU ALA MET LEU LEU GLN          
SEQRES   6 D  539  GLU THR THR GLY GLU LEU GLU ALA ALA LYS ALA LEU VAL          
SEQRES   7 D  539  LEU LYS ARG ILE GLN ILE TRP LYS ARG GLN GLN GLN LEU          
SEQRES   8 D  539  ALA GLY ASN GLY ALA PRO PHE GLU GLU SER LEU ALA PRO          
SEQRES   9 D  539  LEU GLN GLU ARG CYS GLU SER LEU VAL ASP ILE TYR SER          
SEQRES  10 D  539  GLN LEU GLN GLN GLU VAL GLY ALA ALA GLY GLY GLU LEU          
SEQRES  11 D  539  GLU PRO LYS THR ARG ALA SER LEU THR GLY ARG LEU ASP          
SEQRES  12 D  539  GLU VAL LEU ARG THR LEU VAL THR SER CYS PHE LEU VAL          
SEQRES  13 D  539  GLU LYS GLN PRO PRO GLN VAL LEU LYS THR GLN THR LYS          
SEQRES  14 D  539  PHE GLN ALA GLY VAL ARG PHE LEU LEU GLY LEU ARG PHE          
SEQRES  15 D  539  LEU GLY ALA PRO ALA LYS PRO PRO LEU VAL ARG ALA ASP          
SEQRES  16 D  539  MET VAL THR GLU LYS GLN ALA ARG GLU LEU SER VAL PRO          
SEQRES  17 D  539  GLN GLY PRO GLY ALA GLY ALA GLU SER THR GLY GLU ILE          
SEQRES  18 D  539  ILE ASN ASN THR VAL PRO LEU GLU ASN SER ILE PRO GLY          
SEQRES  19 D  539  ASN CYS CYS SER ALA LEU PHE LYS ASN LEU LEU LEU LYS          
SEQRES  20 D  539  LYS ILE LYS ARG CYS GLU ARG LYS GLY THR GLU SER VAL          
SEQRES  21 D  539  THR GLU GLU LYS CYS ALA VAL LEU PHE SER ALA SER PHE          
SEQRES  22 D  539  THR LEU GLY PRO GLY LYS LEU PRO ILE GLN LEU GLN ALA          
SEQRES  23 D  539  LEU SER LEU PRO LEU VAL VAL ILE VAL HIS GLY ASN GLN          
SEQRES  24 D  539  ASP ASN ASN ALA LYS ALA THR ILE LEU TRP ASP ASN ALA          
SEQRES  25 D  539  PHE SER GLU MET ASP ARG VAL PRO PHE VAL VAL ALA GLU          
SEQRES  26 D  539  ARG VAL PRO TRP GLU LYS MET CYS GLU THR LEU ASN LEU          
SEQRES  27 D  539  LYS PHE MET ALA GLU VAL GLY THR ASN ARG GLY LEU LEU          
SEQRES  28 D  539  PRO GLU HIS PHE LEU PHE LEU ALA GLN LYS ILE PHE ASN          
SEQRES  29 D  539  ASP ASN SER LEU SER MET GLU ALA PHE GLN HIS ARG SER          
SEQRES  30 D  539  VAL SER TRP SER GLN PHE ASN LYS GLU ILE LEU LEU GLY          
SEQRES  31 D  539  ARG GLY PHE THR PHE TRP GLN TRP PHE ASP GLY VAL LEU          
SEQRES  32 D  539  ASP LEU THR LYS ARG CYS LEU ARG SER TYR TRP SER ASP          
SEQRES  33 D  539  ARG LEU ILE ILE GLY PHE ILE SER LYS GLN TYR VAL THR          
SEQRES  34 D  539  SER LEU LEU LEU ASN GLU PRO ASP GLY THR PHE LEU LEU          
SEQRES  35 D  539  ARG PHE SER ASP SER GLU ILE GLY GLY ILE THR ILE ALA          
SEQRES  36 D  539  HIS VAL ILE ARG GLY GLN ASP GLY SER PRO GLN ILE GLU          
SEQRES  37 D  539  ASN ILE GLN PRO PHE SER ALA LYS ASP LEU SER ILE ARG          
SEQRES  38 D  539  SER LEU GLY ASP ARG ILE ARG ASP LEU ALA GLN LEU LYS          
SEQRES  39 D  539  ASN LEU TYR PRO LYS LYS PRO LYS ASP GLU ALA PHE ARG          
SEQRES  40 D  539  SER HIS TYR LYS PRO GLU GLN MET GLY LYS ASP GLY ARG          
SEQRES  41 D  539  GLY PTR VAL PRO ALA THR ILE LYS MET THR VAL GLU ARG          
SEQRES  42 D  539  ASP GLN PRO LEU PRO THR                                      
SEQRES   1 N   21   DT  DC  DT  DG  DT  DC  DT  DT  DC  DC  DA  DG  DG          
SEQRES   2 N   21   DA  DA  DA  DT  DC  DC  DA  DT                              
SEQRES   1 M   21   DA  DT  DG  DG  DA  DT  DT  DT  DC  DC  DT  DG  DG          
SEQRES   2 M   21   DA  DA  DG  DA  DC  DA  DG  DA                              
SEQRES   1 E   21   DA  DT  DG  DG  DA  DT  DT  DT  DC  DC  DT  DG  DG          
SEQRES   2 E   21   DA  DA  DG  DA  DC  DA  DG  DA                              
SEQRES   1 F   21   DT  DC  DT  DG  DT  DC  DT  DT  DC  DC  DA  DG  DG          
SEQRES   2 F   21   DA  DA  DA  DT  DC  DC  DA  DT                              
MODRES 5D39 PTR A  641  TYR  MODIFIED RESIDUE                                   
MODRES 5D39 PTR B  641  TYR  MODIFIED RESIDUE                                   
MODRES 5D39 PTR C  641  TYR  MODIFIED RESIDUE                                   
MODRES 5D39 PTR D  641  TYR  MODIFIED RESIDUE                                   
HET    PTR  A 641      16                                                       
HET    PTR  B 641      16                                                       
HET    PTR  C 641      16                                                       
HET    PTR  D 641      16                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   9  HOH   *206(H2 O)                                                    
HELIX    1 AA1 GLN A  125  ARG A  148  1                                  24    
HELIX    2 AA2 GLU A  149  LEU A  151  5                                   3    
HELIX    3 AA3 MET A  181  THR A  187  1                                   7    
HELIX    4 AA4 GLU A  189  GLY A  212  1                                  24    
HELIX    5 AA5 LEU A  221  ALA A  244  1                                  24    
HELIX    6 AA6 GLU A  250  SER A  271  1                                  22    
HELIX    7 AA7 LEU A  297  LEU A  302  1                                   6    
HELIX    8 AA8 GLU A  318  GLU A  323  1                                   6    
HELIX    9 AA9 SER A  378  GLU A  382  5                                   5    
HELIX   10 AB1 HIS A  415  ASN A  417  5                                   3    
HELIX   11 AB2 GLN A  418  SER A  433  1                                  16    
HELIX   12 AB3 TRP A  448  GLY A  464  1                                  17    
HELIX   13 AB4 LEU A  470  ASN A  483  1                                  14    
HELIX   14 AB5 TRP A  499  LYS A  504  1                                   6    
HELIX   15 AB6 THR A  513  LEU A  529  1                                  17    
HELIX   16 AB7 LEU A  529  ASP A  535  1                                   7    
HELIX   17 AB8 SER A  543  ASN A  553  1                                  11    
HELIX   18 AB9 SER A  593  ARG A  600  1                                   8    
HELIX   19 AC1 SER A  601  LEU A  609  1                                   9    
HELIX   20 AC2 LYS A  621  ARG A  626  1                                   6    
HELIX   21 AC3 SER A  627  TYR A  629  5                                   3    
HELIX   22 AC4 GLU B  126  ARG B  148  1                                  23    
HELIX   23 AC5 GLU B  149  LEU B  151  5                                   3    
HELIX   24 AC6 LEU B  182  THR B  187  1                                   6    
HELIX   25 AC7 GLU B  189  ASN B  213  1                                  25    
HELIX   26 AC8 LEU B  221  ALA B  244  1                                  24    
HELIX   27 AC9 GLU B  250  SER B  271  1                                  22    
HELIX   28 AD1 GLU B  318  ARG B  322  1                                   5    
HELIX   29 AD2 SER B  378  GLU B  382  5                                   5    
HELIX   30 AD3 HIS B  415  ASN B  417  5                                   3    
HELIX   31 AD4 GLN B  418  SER B  433  1                                  16    
HELIX   32 AD5 TRP B  448  GLY B  464  1                                  17    
HELIX   33 AD6 LEU B  470  ASN B  483  1                                  14    
HELIX   34 AD7 TRP B  499  LYS B  504  1                                   6    
HELIX   35 AD8 THR B  513  LEU B  529  1                                  17    
HELIX   36 AD9 LEU B  529  ASP B  535  1                                   7    
HELIX   37 AE1 SER B  543  ASN B  553  1                                  11    
HELIX   38 AE2 SER B  593  ARG B  600  1                                   8    
HELIX   39 AE3 SER B  601  LEU B  609  1                                   9    
HELIX   40 AE4 PRO B  620  ARG B  626  1                                   7    
HELIX   41 AE5 SER B  627  TYR B  629  5                                   3    
HELIX   42 AE6 GLU C  126  LEU C  151  1                                  26    
HELIX   43 AE7 ALA C  178  GLU C  185  1                                   8    
HELIX   44 AE8 GLU C  185  GLY C  212  1                                  28    
HELIX   45 AE9 LEU C  221  GLY C  246  1                                  26    
HELIX   46 AF1 GLU C  250  CYS C  272  1                                  23    
HELIX   47 AF2 LEU C  297  PHE C  301  5                                   5    
HELIX   48 AF3 GLU C  318  GLU C  323  1                                   6    
HELIX   49 AF4 SER C  378  GLU C  381  5                                   4    
HELIX   50 AF5 HIS C  415  ASN C  417  5                                   3    
HELIX   51 AF6 GLN C  418  SER C  433  1                                  16    
HELIX   52 AF7 TRP C  448  GLY C  464  1                                  17    
HELIX   53 AF8 LEU C  470  ASN C  483  1                                  14    
HELIX   54 AF9 TRP C  499  LYS C  504  1                                   6    
HELIX   55 AG1 THR C  513  LEU C  529  1                                  17    
HELIX   56 AG2 LEU C  529  ASP C  535  1                                   7    
HELIX   57 AG3 SER C  543  ASN C  553  1                                  11    
HELIX   58 AG4 SER C  593  ARG C  600  1                                   8    
HELIX   59 AG5 SER C  601  LEU C  609  1                                   9    
HELIX   60 AG6 LYS C  621  PHE C  625  1                                   5    
HELIX   61 AG7 ARG C  626  TYR C  629  5                                   4    
HELIX   62 AG8 GLU D  126  GLN D  152  1                                  27    
HELIX   63 AG9 LEU D  182  GLU D  185  5                                   4    
HELIX   64 AH1 THR D  186  GLY D  212  1                                  27    
HELIX   65 AH2 LEU D  221  ALA D  244  1                                  24    
HELIX   66 AH3 PRO D  251  CYS D  272  1                                  22    
HELIX   67 AH4 LEU D  297  PHE D  301  5                                   5    
HELIX   68 AH5 GLU D  318  GLU D  323  1                                   6    
HELIX   69 AH6 HIS D  415  ASN D  417  5                                   3    
HELIX   70 AH7 GLN D  418  SER D  433  1                                  16    
HELIX   71 AH8 TRP D  448  GLY D  464  1                                  17    
HELIX   72 AH9 LEU D  470  ASN D  483  1                                  14    
HELIX   73 AI1 TRP D  499  LYS D  504  1                                   6    
HELIX   74 AI2 THR D  513  LEU D  529  1                                  17    
HELIX   75 AI3 LEU D  529  ASP D  535  1                                   7    
HELIX   76 AI4 SER D  543  ASN D  553  1                                  11    
HELIX   77 AI5 SER D  593  ARG D  600  1                                   8    
HELIX   78 AI6 SER D  601  LEU D  609  1                                   9    
HELIX   79 AI7 LYS D  621  PHE D  625  1                                   5    
HELIX   80 AI8 ARG D  626  TYR D  629  5                                   4    
SHEET    1 AA1 4 PHE A 273  LYS A 277  0                                        
SHEET    2 AA1 4 ALA A 291  PHE A 295 -1  O  GLY A 292   N  LYS A 277           
SHEET    3 AA1 4 CYS A 355  PHE A 360 -1  O  PHE A 360   N  ALA A 291           
SHEET    4 AA1 4 GLU A 348  SER A 350 -1  N  SER A 350   O  CYS A 355           
SHEET    1 AA2 2 VAL A 282  LYS A 284  0                                        
SHEET    2 AA2 2 VAL A 411  ILE A 413  1  O  ILE A 413   N  LEU A 283           
SHEET    1 AA3 3 ALA A 313  THR A 317  0                                        
SHEET    2 AA3 3 CYS A 384  PHE A 392 -1  O  ALA A 385   N  VAL A 316           
SHEET    3 AA3 3 ILE A 401  LEU A 406 -1  O  ALA A 405   N  PHE A 388           
SHEET    1 AA4 2 ILE A 340  ILE A 341  0                                        
SHEET    2 AA4 2 LEU A 364  LEU A 365 -1  O  LEU A 364   N  ILE A 341           
SHEET    1 AA5 2 ARG A 445  PRO A 447  0                                        
SHEET    2 AA5 2 SER A 496  SER A 498 -1  O  VAL A 497   N  VAL A 446           
SHEET    1 AA6 6 LYS A 619  PRO A 620  0                                        
SHEET    2 AA6 6 ASN A 614  LEU A 615 -1  N  LEU A 615   O  LYS A 619           
SHEET    3 AA6 6 THR A 558  PHE A 563  1  N  PHE A 559   O  ASN A 614           
SHEET    4 AA6 6 ILE A 571  ILE A 577 -1  O  THR A 572   N  ARG A 562           
SHEET    5 AA6 6 GLN A 585  ILE A 589 -1  O  GLN A 585   N  ILE A 577           
SHEET    6 AA6 6 PTR C 641  VAL C 642  1  O  VAL C 642   N  ASN A 588           
SHEET    1 AA7 6 PTR A 641  VAL A 642  0                                        
SHEET    2 AA7 6 ILE C 586  ILE C 589  1  O  ASN C 588   N  VAL A 642           
SHEET    3 AA7 6 ILE C 571  VAL C 576 -1  N  HIS C 575   O  GLU C 587           
SHEET    4 AA7 6 THR C 558  PHE C 563 -1  N  ARG C 562   O  THR C 572           
SHEET    5 AA7 6 ASN C 614  LEU C 615  1  O  ASN C 614   N  PHE C 559           
SHEET    6 AA7 6 LYS C 619  PRO C 620 -1  O  LYS C 619   N  LEU C 615           
SHEET    1 AA8 2 THR A 645  THR A 649  0                                        
SHEET    2 AA8 2 THR C 645  THR C 649 -1  O  THR C 649   N  THR A 645           
SHEET    1 AA9 4 PHE B 273  LYS B 277  0                                        
SHEET    2 AA9 4 LYS B 288  PHE B 295 -1  O  ARG B 294   N  LEU B 274           
SHEET    3 AA9 4 CYS B 355  LEU B 365 -1  O  PHE B 360   N  ALA B 291           
SHEET    4 AA9 4 ILE B 340  ILE B 341 -1  N  ILE B 341   O  LEU B 364           
SHEET    1 AB1 4 PHE B 273  LYS B 277  0                                        
SHEET    2 AB1 4 LYS B 288  PHE B 295 -1  O  ARG B 294   N  LEU B 274           
SHEET    3 AB1 4 CYS B 355  LEU B 365 -1  O  PHE B 360   N  ALA B 291           
SHEET    4 AB1 4 GLU B 348  SER B 350 -1  N  GLU B 348   O  SER B 357           
SHEET    1 AB2 2 VAL B 282  LYS B 284  0                                        
SHEET    2 AB2 2 VAL B 411  ILE B 413  1  O  ILE B 413   N  LEU B 283           
SHEET    1 AB3 3 ARG B 312  THR B 317  0                                        
SHEET    2 AB3 3 CYS B 384  PHE B 392 -1  O  ALA B 385   N  VAL B 316           
SHEET    3 AB3 3 ILE B 401  LEU B 406 -1  O  ALA B 405   N  PHE B 388           
SHEET    1 AB4 2 ARG B 445  PRO B 447  0                                        
SHEET    2 AB4 2 SER B 496  SER B 498 -1  O  VAL B 497   N  VAL B 446           
SHEET    1 AB5 5 ASN B 614  LEU B 615  0                                        
SHEET    2 AB5 5 THR B 558  PHE B 563  1  N  PHE B 559   O  ASN B 614           
SHEET    3 AB5 5 ILE B 571  ILE B 577 -1  O  THR B 572   N  ARG B 562           
SHEET    4 AB5 5 GLN B 585  ILE B 589 -1  O  GLN B 585   N  ILE B 577           
SHEET    5 AB5 5 PTR D 641  VAL D 642  1  O  VAL D 642   N  ASN B 588           
SHEET    1 AB6 2 THR B 645  THR B 649  0                                        
SHEET    2 AB6 2 THR D 645  THR D 649 -1  O  THR D 649   N  THR B 645           
SHEET    1 AB7 4 PHE C 273  LYS C 277  0                                        
SHEET    2 AB7 4 LYS C 288  PHE C 295 -1  O  ARG C 294   N  LEU C 274           
SHEET    3 AB7 4 CYS C 355  LEU C 365 -1  O  PHE C 360   N  ALA C 291           
SHEET    4 AB7 4 ILE C 340  ILE C 341 -1  N  ILE C 341   O  LEU C 364           
SHEET    1 AB8 4 PHE C 273  LYS C 277  0                                        
SHEET    2 AB8 4 LYS C 288  PHE C 295 -1  O  ARG C 294   N  LEU C 274           
SHEET    3 AB8 4 CYS C 355  LEU C 365 -1  O  PHE C 360   N  ALA C 291           
SHEET    4 AB8 4 GLU C 348  SER C 350 -1  N  SER C 350   O  CYS C 355           
SHEET    1 AB9 5 VAL C 282  LYS C 284  0                                        
SHEET    2 AB9 5 LEU C 410  ILE C 413  1  O  VAL C 411   N  LEU C 283           
SHEET    3 AB9 5 LYS C 383  PHE C 392 -1  N  CYS C 384   O  LEU C 410           
SHEET    4 AB9 5 LEU C 310  THR C 317 -1  N  VAL C 316   O  ALA C 385           
SHEET    5 AB9 5 THR C 344  PRO C 346 -1  O  VAL C 345   N  VAL C 311           
SHEET    1 AC1 4 VAL C 282  LYS C 284  0                                        
SHEET    2 AC1 4 LEU C 410  ILE C 413  1  O  VAL C 411   N  LEU C 283           
SHEET    3 AC1 4 LYS C 383  PHE C 392 -1  N  CYS C 384   O  LEU C 410           
SHEET    4 AC1 4 ILE C 401  LEU C 406 -1  O  ALA C 405   N  PHE C 388           
SHEET    1 AC2 2 ARG C 445  PRO C 447  0                                        
SHEET    2 AC2 2 SER C 496  SER C 498 -1  O  VAL C 497   N  VAL C 446           
SHEET    1 AC3 4 PHE D 273  LYS D 277  0                                        
SHEET    2 AC3 4 LYS D 288  PHE D 295 -1  O  ARG D 294   N  LEU D 274           
SHEET    3 AC3 4 CYS D 355  LEU D 365 -1  O  PHE D 360   N  ALA D 291           
SHEET    4 AC3 4 ILE D 340  ILE D 341 -1  N  ILE D 341   O  LEU D 364           
SHEET    1 AC4 4 PHE D 273  LYS D 277  0                                        
SHEET    2 AC4 4 LYS D 288  PHE D 295 -1  O  ARG D 294   N  LEU D 274           
SHEET    3 AC4 4 CYS D 355  LEU D 365 -1  O  PHE D 360   N  ALA D 291           
SHEET    4 AC4 4 GLU D 348  SER D 350 -1  N  SER D 350   O  CYS D 355           
SHEET    1 AC5 5 VAL D 282  LYS D 284  0                                        
SHEET    2 AC5 5 LEU D 410  ILE D 413  1  O  ILE D 413   N  LEU D 283           
SHEET    3 AC5 5 LYS D 383  PHE D 392 -1  N  CYS D 384   O  LEU D 410           
SHEET    4 AC5 5 LEU D 310  THR D 317 -1  N  VAL D 316   O  ALA D 385           
SHEET    5 AC5 5 THR D 344  PRO D 346 -1  O  VAL D 345   N  VAL D 311           
SHEET    1 AC6 4 VAL D 282  LYS D 284  0                                        
SHEET    2 AC6 4 LEU D 410  ILE D 413  1  O  ILE D 413   N  LEU D 283           
SHEET    3 AC6 4 LYS D 383  PHE D 392 -1  N  CYS D 384   O  LEU D 410           
SHEET    4 AC6 4 ILE D 401  LEU D 406 -1  O  ALA D 405   N  PHE D 388           
SHEET    1 AC7 2 ARG D 445  PRO D 447  0                                        
SHEET    2 AC7 2 SER D 496  SER D 498 -1  O  VAL D 497   N  VAL D 446           
SHEET    1 AC8 5 GLN D 585  ASN D 588  0                                        
SHEET    2 AC8 5 ILE D 571  ILE D 577 -1  N  ILE D 577   O  GLN D 585           
SHEET    3 AC8 5 THR D 558  PHE D 563 -1  N  ARG D 562   O  THR D 572           
SHEET    4 AC8 5 ASN D 614  LEU D 615  1  O  ASN D 614   N  PHE D 559           
SHEET    5 AC8 5 LYS D 619  PRO D 620 -1  O  LYS D 619   N  LEU D 615           
LINK         C   GLY A 640                 N   PTR A 641     1555   1555  1.33  
LINK         C   PTR A 641                 N   VAL A 642     1555   1555  1.33  
LINK         OD1 ASP B 637                 CZ  ARG B 639     1555   1555  1.39  
LINK         C   GLY B 640                 N   PTR B 641     1555   1555  1.33  
LINK         C   PTR B 641                 N   VAL B 642     1555   1555  1.33  
LINK         C   GLY C 640                 N   PTR C 641     1555   1555  1.33  
LINK         C   PTR C 641                 N   VAL C 642     1555   1555  1.33  
LINK         C   GLY D 640                 N   PTR D 641     1555   1555  1.33  
LINK         C   PTR D 641                 N   VAL D 642     1555   1555  1.33  
CISPEP   1 GLU A  323    LEU A  324          0        -3.11                     
CISPEP   2 PHE A  392    THR A  393          0        21.64                     
CISPEP   3 GLY A  395    PRO A  396          0        14.83                     
CISPEP   4 GLY A  397    LYS A  398          0        -3.32                     
CISPEP   5 PRO A  439    PHE A  440          0        -5.43                     
CISPEP   6 ILE A  577    ARG A  578          0         7.22                     
CISPEP   7 TYR A  616    PRO A  617          0         7.98                     
CISPEP   8 ASP A  637    GLY A  638          0       -10.60                     
CISPEP   9 GLY A  638    ARG A  639          0        -1.01                     
CISPEP  10 LEU B  249    GLU B  250          0       -11.16                     
CISPEP  11 GLU B  323    LEU B  324          0         3.14                     
CISPEP  12 PHE B  392    THR B  393          0         9.26                     
CISPEP  13 GLY B  395    PRO B  396          0         9.76                     
CISPEP  14 GLY B  397    LYS B  398          0        -1.32                     
CISPEP  15 PRO B  439    PHE B  440          0        -6.83                     
CISPEP  16 TYR B  616    PRO B  617          0       -10.31                     
CISPEP  17 ASP B  637    GLY B  638          0       -17.05                     
CISPEP  18 GLY B  638    ARG B  639          0        -8.55                     
CISPEP  19 GLY C  246    GLY C  247          0       -13.56                     
CISPEP  20 GLU C  323    LEU C  324          0         3.05                     
CISPEP  21 GLU C  377    SER C  378          0        -5.30                     
CISPEP  22 PHE C  392    THR C  393          0        15.76                     
CISPEP  23 GLY C  395    PRO C  396          0        10.15                     
CISPEP  24 GLY C  397    LYS C  398          0        -2.63                     
CISPEP  25 PRO C  439    PHE C  440          0        -7.42                     
CISPEP  26 ILE C  577    ARG C  578          0        -6.78                     
CISPEP  27 ARG C  578    GLY C  579          0        17.23                     
CISPEP  28 TYR C  616    PRO C  617          0       -12.29                     
CISPEP  29 GLN C  633    MET C  634          0        13.22                     
CISPEP  30 ASP C  637    GLY C  638          0       -11.29                     
CISPEP  31 GLY C  638    ARG C  639          0        -1.48                     
CISPEP  32 ALA D  245    GLY D  246          0        18.23                     
CISPEP  33 GLU D  323    LEU D  324          0         0.74                     
CISPEP  34 GLY D  395    PRO D  396          0         8.36                     
CISPEP  35 GLY D  397    LYS D  398          0        -4.38                     
CISPEP  36 PRO D  439    PHE D  440          0        -8.00                     
CISPEP  37 ILE D  577    ARG D  578          0        -6.98                     
CISPEP  38 TYR D  616    PRO D  617          0       -12.40                     
CISPEP  39 ASP D  637    GLY D  638          0       -14.59                     
CISPEP  40 GLY D  638    ARG D  639          0        -4.19                     
CRYST1   68.395   94.697  145.642  79.62  78.31  89.58 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014621 -0.000108 -0.003056        0.00000                         
SCALE2      0.000000  0.010560 -0.001960        0.00000                         
SCALE3      0.000000  0.000000  0.007131        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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