GenomeNet

Database: PDB
Entry: 6MBW
LinkDB: 6MBW
Original site: 6MBW 
HEADER    TRANSCRIPTION ACTIVATOR                 30-AUG-18   6MBW              
TITLE     STRUCTURE OF TRANSCRIPTION FACTOR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 5B;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 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: STAT5B;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TRANSCRIPTION FACTOR, TRANSCRIPTION ACTIVATOR                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-S.SEO,S.DHE-PAGANON                                                
REVDAT   2   08-JAN-20 6MBW    1       REMARK                                   
REVDAT   1   19-JUN-19 6MBW    0                                                
JRNL        AUTH   E.D.DE ARAUJO,F.ERDOGAN,H.A.NEUBAUER,D.MENEKSEDAG-EROL,      
JRNL        AUTH 2 P.MANASWIYOUNGKUL,M.S.ERAM,H.S.SEO,A.K.QADREE,J.ISRAELIAN,   
JRNL        AUTH 3 A.ORLOVA,T.SUSKE,H.T.T.PHAM,A.BOERSMA,S.TANGERMANN,L.KENNER, 
JRNL        AUTH 4 T.RULICKE,A.DONG,M.RAVICHANDRAN,P.J.BROWN,G.F.AUDETTE,       
JRNL        AUTH 5 S.RAUSCHER,S.DHE-PAGANON,R.MORIGGL,P.T.GUNNING               
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF THE STAT5BN642H    
JRNL        TITL 2 DRIVER MUTATION.                                             
JRNL        REF    NAT COMMUN                    V.  10  2517 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31175292                                                     
JRNL        DOI    10.1038/S41467-019-10422-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 96.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21968                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.268                           
REMARK   3   R VALUE            (WORKING SET) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.230                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1150                            
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 96.6081 -  6.5794    0.96     2716   155  0.2283 0.2209        
REMARK   3     2  6.5794 -  5.2224    0.99     2659   132  0.3058 0.3438        
REMARK   3     3  5.2224 -  4.5622    0.97     2597   139  0.2472 0.2999        
REMARK   3     4  4.5622 -  4.1451    0.99     2613   136  0.2663 0.3421        
REMARK   3     5  4.1451 -  3.8480    0.99     2585   129  0.2736 0.3411        
REMARK   3     6  3.8480 -  3.6211    0.97     2562   125  0.3169 0.4085        
REMARK   3     7  3.6211 -  3.4398    0.99     2545   175  0.3206 0.3898        
REMARK   3     8  3.4398 -  3.2900    0.99     2541   159  0.3424 0.4174        
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)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 114.2                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           7841                                  
REMARK   3   ANGLE     :  0.626          10720                                  
REMARK   3   CHIRALITY :  0.041           1259                                  
REMARK   3   PLANARITY :  0.004           1386                                  
REMARK   3   DIHEDRAL  :  3.100           4615                                  
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 6MBW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236610.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21977                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 96.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.03800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1Y1U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       67.30000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.31000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       67.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.31000            
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 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 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     SER A   132                                                      
REMARK 465     THR A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     ALA A   136                                                      
REMARK 465     MET A   137                                                      
REMARK 465     PHE A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     ASN A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     TYR A   392                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     PHE A   538                                                      
REMARK 465     ASN A   539                                                      
REMARK 465     ASN A   540                                                      
REMARK 465     ARG A   560                                                      
REMARK 465     GLU A   561                                                      
REMARK 465     PHE A   633                                                      
REMARK 465     ASP A   634                                                      
REMARK 465     SER A   635                                                      
REMARK 465     GLN A   636                                                      
REMARK 465     GLU A   637                                                      
REMARK 465     ASP A   662                                                      
REMARK 465     LEU A   663                                                      
REMARK 465     VAL A   686                                                      
REMARK 465     PRO A   687                                                      
REMARK 465     CYS A   688                                                      
REMARK 465     GLU A   689                                                      
REMARK 465     SER A   690                                                      
REMARK 465     ALA A   691                                                      
REMARK 465     THR A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     LYS A   694                                                      
REMARK 465     ALA A   695                                                      
REMARK 465     VAL A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     GLY A   698                                                      
REMARK 465     TYR A   699                                                      
REMARK 465     VAL A   700                                                      
REMARK 465     LYS A   701                                                      
REMARK 465     PRO A   702                                                      
REMARK 465     GLN A   703                                                      
REMARK 465     SER B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     ALA B   136                                                      
REMARK 465     MET B   137                                                      
REMARK 465     GLN B   185                                                      
REMARK 465     PHE B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     LEU B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     GLN B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     PRO B   194                                                      
REMARK 465     GLN B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     PRO B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     THR B   388                                                      
REMARK 465     ARG B   389                                                      
REMARK 465     ASN B   390                                                      
REMARK 465     ASP B   391                                                      
REMARK 465     ARG B   426                                                      
REMARK 465     SER B   427                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     ARG B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     ALA B   432                                                      
REMARK 465     VAL B   686                                                      
REMARK 465     PRO B   687                                                      
REMARK 465     CYS B   688                                                      
REMARK 465     GLU B   689                                                      
REMARK 465     SER B   690                                                      
REMARK 465     ALA B   691                                                      
REMARK 465     THR B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     LYS B   694                                                      
REMARK 465     ALA B   695                                                      
REMARK 465     VAL B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     GLY B   698                                                      
REMARK 465     TYR B   699                                                      
REMARK 465     VAL B   700                                                      
REMARK 465     LYS B   701                                                      
REMARK 465     PRO B   702                                                      
REMARK 465     GLN B   703                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 139    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 162    CG   CD1  CD2                                       
REMARK 470     LYS A 163    CG   CD   CE   NZ                                   
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     GLN A 175    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 177    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 178    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 180    CG   CD1  CD2                                       
REMARK 470     ILE A 182    CG1  CG2  CD1                                       
REMARK 470     GLN A 183    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 185    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 189    CG   CD1  CD2                                       
REMARK 470     GLN A 191    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 192    CG   CD1  CD2                                       
REMARK 470     ARG A 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 204    CG   CD1  CD2                                       
REMARK 470     GLN A 206    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 207    CG   CD   CE   NZ                                   
REMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 231    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 232    CG   CD   CE   NZ                                   
REMARK 470     GLN A 238    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     ARG A 258    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 284    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 294    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 297    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 299    CG   CD1  CD2                                       
REMARK 470     GLN A 301    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 303    CG   CD1  CD2                                       
REMARK 470     ILE A 305    CG1  CG2  CD1                                       
REMARK 470     VAL A 309    CG1  CG2                                            
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
REMARK 470     MET A 312    CG   SD   CE                                        
REMARK 470     LYS A 347    CG   CD   CE   NZ                                   
REMARK 470     LYS A 359    CG   CD   CE   NZ                                   
REMARK 470     ASN A 361    CG   OD1  ND2                                       
REMARK 470     ASN A 365    CG   OD1  ND2                                       
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     GLN A 378    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 384    CG   CD   CE   NZ                                   
REMARK 470     ASN A 385    CG   OD1  ND2                                       
REMARK 470     GLU A 386    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 387    CG   OD1  ND2                                       
REMARK 470     THR A 388    OG1  CG2                                            
REMARK 470     ARG A 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 395    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 396    CG1  CG2  CD1                                       
REMARK 470     ASN A 398    CG   OD1  ND2                                       
REMARK 470     MET A 403    CG   SD   CE                                        
REMARK 470     GLU A 404    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 406    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 407    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     ARG A 426    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
REMARK 470     GLN A 447    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 450    CG1  CG2                                            
REMARK 470     ASN A 453    CG   OD1  ND2                                       
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 455    CG   CD1  CD2                                       
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     VAL A 470    CG1  CG2                                            
REMARK 470     GLU A 490    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 494    CG1  CG2                                            
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     VAL A 502    CG1  CG2                                            
REMARK 470     LEU A 503    CG   CD1  CD2                                       
REMARK 470     GLN A 506    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 520    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 522    CG   OD1  ND2                                       
REMARK 470     ARG A 523    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 526    OG1  CG2                                            
REMARK 470     LYS A 527    CG   CD   CE   NZ                                   
REMARK 470     GLU A 528    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 530    CG   CD1  CD2                                       
REMARK 470     VAL A 531    CG1  CG2                                            
REMARK 470     LEU A 533    CG   CD1  CD2                                       
REMARK 470     GLN A 535    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 536    CG   CD   CE   NZ                                   
REMARK 470     LEU A 537    CG   CD1  CD2                                       
REMARK 470     LEU A 545    CG   CD1  CD2                                       
REMARK 470     ASP A 547    CG   OD1  OD2                                       
REMARK 470     LEU A 551    CG   CD1  CD2                                       
REMARK 470     GLN A 557    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 562    CG   OD1  ND2                                       
REMARK 470     LEU A 563    CG   CD1  CD2                                       
REMARK 470     ARG A 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 567    CG   OD1  ND2                                       
REMARK 470     GLN A 572    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 594    CG1  CG2  CD1                                       
REMARK 470     LEU A 595    CG   CD1  CD2                                       
REMARK 470     PHE A 597    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 598    CG1  CG2                                            
REMARK 470     ASN A 599    CG   OD1  ND2                                       
REMARK 470     LYS A 600    CG   CD   CE   NZ                                   
REMARK 470     GLN A 601    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 602    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 607    CG   CD1  CD2                                       
REMARK 470     ILE A 608    CG1  CG2  CD1                                       
REMARK 470     ASN A 609    CG   OD1  ND2                                       
REMARK 470     LYS A 610    CG   CD   CE   NZ                                   
REMARK 470     LEU A 617    CG   CD1  CD2                                       
REMARK 470     ARG A 618    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 632    CG   CD   CE   NZ                                   
REMARK 470     ARG A 638    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 639    CG   SD   CE                                        
REMARK 470     PHE A 640    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 659    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 666    CG   CD1  CD2                                       
REMARK 470     PHE A 670    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 673    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 677    CG   CD   OE1  OE2                                  
REMARK 470     SER A 680    OG                                                  
REMARK 470     LYS A 681    CG   CD   CE   NZ                                   
REMARK 470     GLN B 139    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 142    CG   CD1  CD2                                       
REMARK 470     GLN B 146    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 150    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 197    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 198    CG   CD1  CD2                                       
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 202    OG1  CG2                                            
REMARK 470     GLN B 205    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 206    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 232    CG   CD   CE   NZ                                   
REMARK 470     ARG B 294    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 301    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 311    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 315    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 322    CG   OD1  OD2                                       
REMARK 470     LYS B 336    CG   CD   CE   NZ                                   
REMARK 470     LEU B 342    CG   CD1  CD2                                       
REMARK 470     LYS B 343    CG   CD   CE   NZ                                   
REMARK 470     GLN B 345    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     ILE B 373    CG1  CG2  CD1                                       
REMARK 470     ILE B 374    CG1  CG2  CD1                                       
REMARK 470     SER B 375    OG                                                  
REMARK 470     GLU B 376    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 377    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 378    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 380    CG   CD   CE   NZ                                   
REMARK 470     LEU B 383    CG   CD1  CD2                                       
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     ASN B 385    CG   OD1  ND2                                       
REMARK 470     GLU B 386    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 387    CG   OD1  ND2                                       
REMARK 470     TYR B 392    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 393    OG                                                  
REMARK 470     GLU B 395    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 396    CG1  CG2  CD1                                       
REMARK 470     ASN B 399    CG   OD1  ND2                                       
REMARK 470     MET B 403    CG   SD   CE                                        
REMARK 470     GLU B 404    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 407    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 417    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 418    CG   OD1  ND2                                       
REMARK 470     SER B 420    OG                                                  
REMARK 470     LEU B 421    CG   CD1  CD2                                       
REMARK 470     LYS B 422    CG   CD   CE   NZ                                   
REMARK 470     ARG B 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     GLU B 433    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 435    CG1  CG2                                            
REMARK 470     ASN B 453    CG   OD1  ND2                                       
REMARK 470     GLU B 454    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 455    CG   CD1  CD2                                       
REMARK 470     LYS B 460    CG   CD   CE   NZ                                   
REMARK 470     ILE B 469    CG1  CG2  CD1                                       
REMARK 470     VAL B 470    CG1  CG2                                            
REMARK 470     GLN B 474    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 477    CG   OD1  ND2                                       
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 501    CG   CD   CE   NZ                                   
REMARK 470     GLU B 509    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 528    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 560    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 562    CG   OD1  ND2                                       
REMARK 470     ARG B 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 567    CG   OD1  ND2                                       
REMARK 470     THR B 569    OG1  CG2                                            
REMARK 470     GLN B 572    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 582    CG   CD   CE   NZ                                   
REMARK 470     LYS B 586    CG   CD   CE   NZ                                   
REMARK 470     ASP B 591    CG   OD1  OD2                                       
REMARK 470     LYS B 600    CG   CD   CE   NZ                                   
REMARK 470     GLN B 601    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 609    CG   OD1  ND2                                       
REMARK 470     GLU B 623    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 624    CG1  CG2  CD1                                       
REMARK 470     LYS B 632    CG   CD   CE   NZ                                   
REMARK 470     PHE B 633    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 634    CG   OD1  OD2                                       
REMARK 470     SER B 635    OG                                                  
REMARK 470     GLN B 636    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 637    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 638    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 639    CG   SD   CE                                        
REMARK 470     ARG B 649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 653    CG1  CG2  CD1                                       
REMARK 470     ARG B 654    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 658    CG   OD1  OD2                                       
REMARK 470     ILE B 667    CG1  CG2  CD1                                       
REMARK 470     ASP B 672    CG   OD1  OD2                                       
REMARK 470     ARG B 673    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 677    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 681    CG   CD   CE   NZ                                   
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    LEU B   327     OG1  THR B   331              2.08            
REMARK 500   O    GLU A   315     N    ASN A   317              2.15            
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    GLN A 216      -22.57     73.82                                   
REMARK 500    GLU A 315     -141.06    -66.98                                   
REMARK 500    VAL A 316      -30.67    -20.81                                   
REMARK 500    GLN A 340     -171.48    -69.20                                   
REMARK 500    VAL A 341      122.92    -31.10                                   
REMARK 500    ASN A 361       13.08     58.79                                   
REMARK 500    GLU A 395     -176.73   -171.09                                   
REMARK 500    LEU A 563       86.84   -158.75                                   
REMARK 500    ASN A 567        4.74    -68.63                                   
REMARK 500    GLN A 601       -6.59     71.99                                   
REMARK 500    PRO A 611     -177.67    -69.57                                   
REMARK 500    PHE A 670       85.68     43.72                                   
REMARK 500    PRO A 671      174.07    -38.40                                   
REMARK 500    ASP A 672      112.81    -34.48                                   
REMARK 500    GLN B 183       37.04   -143.86                                   
REMARK 500    LEU B 272       -2.88     68.54                                   
REMARK 500    SER B 375     -150.90   -142.40                                   
REMARK 500    GLU B 376     -171.22    -55.01                                   
REMARK 500    GLN B 377      -22.39    -30.56                                   
REMARK 500    THR B 436       49.58    -83.87                                   
REMARK 500    PHE B 538     -169.63   -118.60                                   
REMARK 500    LEU B 563      151.84    -49.87                                   
REMARK 500    ALA B 593       -6.14     67.65                                   
REMARK 500    PHE B 597       31.36    -95.75                                   
REMARK 500    LEU B 607       14.06   -140.63                                   
REMARK 500    ASP B 650        0.65    -68.20                                   
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  315     VAL A  316                 -143.25                    
REMARK 500 GLN A  340     VAL A  341                 -131.77                    
REMARK 500 PHE A  670     PRO A  671                 -133.39                    
REMARK 500 PRO A  671     ASP A  672                 -121.39                    
REMARK 500 ILE B  374     SER B  375                 -149.62                    
REMARK 500 GLU B  376     GLN B  377                 -143.20                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6MBW A  136   703  UNP    P51692   STA5B_HUMAN    136    703             
DBREF  6MBW B  136   703  UNP    P51692   STA5B_HUMAN    136    703             
SEQADV 6MBW SER A  132  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW THR A  133  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW GLY A  134  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW SER A  135  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW SER B  132  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW THR B  133  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW GLY B  134  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBW SER B  135  UNP  P51692              EXPRESSION TAG                 
SEQRES   1 A  572  SER THR GLY SER ALA MET SER GLN LYS HIS LEU GLN ILE          
SEQRES   2 A  572  ASN GLN THR PHE GLU GLU LEU ARG LEU VAL THR GLN ASP          
SEQRES   3 A  572  THR GLU ASN GLU LEU LYS LYS LEU GLN GLN THR GLN GLU          
SEQRES   4 A  572  TYR PHE ILE ILE GLN TYR GLN GLU SER LEU ARG ILE GLN          
SEQRES   5 A  572  ALA GLN PHE GLY PRO LEU ALA GLN LEU SER PRO GLN GLU          
SEQRES   6 A  572  ARG LEU SER ARG GLU THR ALA LEU GLN GLN LYS GLN VAL          
SEQRES   7 A  572  SER LEU GLU ALA TRP LEU GLN ARG GLU ALA GLN THR LEU          
SEQRES   8 A  572  GLN GLN TYR ARG VAL GLU LEU ALA GLU LYS HIS GLN LYS          
SEQRES   9 A  572  THR LEU GLN LEU LEU ARG LYS GLN GLN THR ILE ILE LEU          
SEQRES  10 A  572  ASP ASP GLU LEU ILE GLN TRP LYS ARG ARG GLN GLN LEU          
SEQRES  11 A  572  ALA GLY ASN GLY GLY PRO PRO GLU GLY SER LEU ASP VAL          
SEQRES  12 A  572  LEU GLN SER TRP CYS GLU LYS LEU ALA GLU ILE ILE TRP          
SEQRES  13 A  572  GLN ASN ARG GLN GLN ILE ARG ARG ALA GLU HIS LEU CYS          
SEQRES  14 A  572  GLN GLN LEU PRO ILE PRO GLY PRO VAL GLU GLU MET LEU          
SEQRES  15 A  572  ALA GLU VAL ASN ALA THR ILE THR ASP ILE ILE SER ALA          
SEQRES  16 A  572  LEU VAL THR SER THR PHE ILE ILE GLU LYS GLN PRO PRO          
SEQRES  17 A  572  GLN VAL LEU LYS THR GLN THR LYS PHE ALA ALA THR VAL          
SEQRES  18 A  572  ARG LEU LEU VAL GLY GLY LYS LEU ASN VAL HIS MET ASN          
SEQRES  19 A  572  PRO PRO GLN VAL LYS ALA THR ILE ILE SER GLU GLN GLN          
SEQRES  20 A  572  ALA LYS SER LEU LEU LYS ASN GLU ASN THR ARG ASN ASP          
SEQRES  21 A  572  TYR SER GLY GLU ILE LEU ASN ASN CYS CYS VAL MET GLU          
SEQRES  22 A  572  TYR HIS GLN ALA THR GLY THR LEU SER ALA HIS PHE ARG          
SEQRES  23 A  572  ASN MET SER LEU LYS ARG ILE LYS ARG SER ASP ARG ARG          
SEQRES  24 A  572  GLY ALA GLU SER VAL THR GLU GLU LYS PHE THR ILE LEU          
SEQRES  25 A  572  PHE GLU SER GLN PHE SER VAL GLY GLY ASN GLU LEU VAL          
SEQRES  26 A  572  PHE GLN VAL LYS THR LEU SER LEU PRO VAL VAL VAL ILE          
SEQRES  27 A  572  VAL HIS GLY SER GLN ASP ASN ASN ALA THR ALA THR VAL          
SEQRES  28 A  572  LEU TRP ASP ASN ALA PHE ALA GLU PRO GLY ARG VAL PRO          
SEQRES  29 A  572  PHE ALA VAL PRO ASP LYS VAL LEU TRP PRO GLN LEU CYS          
SEQRES  30 A  572  GLU ALA LEU ASN MET LYS PHE LYS ALA GLU VAL GLN SER          
SEQRES  31 A  572  ASN ARG GLY LEU THR LYS GLU ASN LEU VAL PHE LEU ALA          
SEQRES  32 A  572  GLN LYS LEU PHE ASN ASN SER SER SER HIS LEU GLU ASP          
SEQRES  33 A  572  TYR SER GLY LEU SER VAL SER TRP SER GLN PHE ASN ARG          
SEQRES  34 A  572  GLU ASN LEU PRO GLY ARG ASN TYR THR PHE TRP GLN TRP          
SEQRES  35 A  572  PHE ASP GLY VAL MET GLU VAL LEU LYS LYS HIS LEU LYS          
SEQRES  36 A  572  PRO HIS TRP ASN ASP GLY ALA ILE LEU GLY PHE VAL ASN          
SEQRES  37 A  572  LYS GLN GLN ALA HIS ASP LEU LEU ILE ASN LYS PRO ASP          
SEQRES  38 A  572  GLY THR PHE LEU LEU ARG PHE SER ASP SER GLU ILE GLY          
SEQRES  39 A  572  GLY ILE THR ILE ALA TRP LYS PHE ASP SER GLN GLU ARG          
SEQRES  40 A  572  MET PHE TRP ASN LEU MET PRO PHE THR THR ARG ASP PHE          
SEQRES  41 A  572  SER ILE ARG SER LEU ALA ASP ARG LEU GLY ASP LEU ASN          
SEQRES  42 A  572  TYR LEU ILE TYR VAL PHE PRO ASP ARG PRO LYS ASP GLU          
SEQRES  43 A  572  VAL TYR SER LYS TYR TYR THR PRO VAL PRO CYS GLU SER          
SEQRES  44 A  572  ALA THR ALA LYS ALA VAL ASP GLY TYR VAL LYS PRO GLN          
SEQRES   1 B  572  SER THR GLY SER ALA MET SER GLN LYS HIS LEU GLN ILE          
SEQRES   2 B  572  ASN GLN THR PHE GLU GLU LEU ARG LEU VAL THR GLN ASP          
SEQRES   3 B  572  THR GLU ASN GLU LEU LYS LYS LEU GLN GLN THR GLN GLU          
SEQRES   4 B  572  TYR PHE ILE ILE GLN TYR GLN GLU SER LEU ARG ILE GLN          
SEQRES   5 B  572  ALA GLN PHE GLY PRO LEU ALA GLN LEU SER PRO GLN GLU          
SEQRES   6 B  572  ARG LEU SER ARG GLU THR ALA LEU GLN GLN LYS GLN VAL          
SEQRES   7 B  572  SER LEU GLU ALA TRP LEU GLN ARG GLU ALA GLN THR LEU          
SEQRES   8 B  572  GLN GLN TYR ARG VAL GLU LEU ALA GLU LYS HIS GLN LYS          
SEQRES   9 B  572  THR LEU GLN LEU LEU ARG LYS GLN GLN THR ILE ILE LEU          
SEQRES  10 B  572  ASP ASP GLU LEU ILE GLN TRP LYS ARG ARG GLN GLN LEU          
SEQRES  11 B  572  ALA GLY ASN GLY GLY PRO PRO GLU GLY SER LEU ASP VAL          
SEQRES  12 B  572  LEU GLN SER TRP CYS GLU LYS LEU ALA GLU ILE ILE TRP          
SEQRES  13 B  572  GLN ASN ARG GLN GLN ILE ARG ARG ALA GLU HIS LEU CYS          
SEQRES  14 B  572  GLN GLN LEU PRO ILE PRO GLY PRO VAL GLU GLU MET LEU          
SEQRES  15 B  572  ALA GLU VAL ASN ALA THR ILE THR ASP ILE ILE SER ALA          
SEQRES  16 B  572  LEU VAL THR SER THR PHE ILE ILE GLU LYS GLN PRO PRO          
SEQRES  17 B  572  GLN VAL LEU LYS THR GLN THR LYS PHE ALA ALA THR VAL          
SEQRES  18 B  572  ARG LEU LEU VAL GLY GLY LYS LEU ASN VAL HIS MET ASN          
SEQRES  19 B  572  PRO PRO GLN VAL LYS ALA THR ILE ILE SER GLU GLN GLN          
SEQRES  20 B  572  ALA LYS SER LEU LEU LYS ASN GLU ASN THR ARG ASN ASP          
SEQRES  21 B  572  TYR SER GLY GLU ILE LEU ASN ASN CYS CYS VAL MET GLU          
SEQRES  22 B  572  TYR HIS GLN ALA THR GLY THR LEU SER ALA HIS PHE ARG          
SEQRES  23 B  572  ASN MET SER LEU LYS ARG ILE LYS ARG SER ASP ARG ARG          
SEQRES  24 B  572  GLY ALA GLU SER VAL THR GLU GLU LYS PHE THR ILE LEU          
SEQRES  25 B  572  PHE GLU SER GLN PHE SER VAL GLY GLY ASN GLU LEU VAL          
SEQRES  26 B  572  PHE GLN VAL LYS THR LEU SER LEU PRO VAL VAL VAL ILE          
SEQRES  27 B  572  VAL HIS GLY SER GLN ASP ASN ASN ALA THR ALA THR VAL          
SEQRES  28 B  572  LEU TRP ASP ASN ALA PHE ALA GLU PRO GLY ARG VAL PRO          
SEQRES  29 B  572  PHE ALA VAL PRO ASP LYS VAL LEU TRP PRO GLN LEU CYS          
SEQRES  30 B  572  GLU ALA LEU ASN MET LYS PHE LYS ALA GLU VAL GLN SER          
SEQRES  31 B  572  ASN ARG GLY LEU THR LYS GLU ASN LEU VAL PHE LEU ALA          
SEQRES  32 B  572  GLN LYS LEU PHE ASN ASN SER SER SER HIS LEU GLU ASP          
SEQRES  33 B  572  TYR SER GLY LEU SER VAL SER TRP SER GLN PHE ASN ARG          
SEQRES  34 B  572  GLU ASN LEU PRO GLY ARG ASN TYR THR PHE TRP GLN TRP          
SEQRES  35 B  572  PHE ASP GLY VAL MET GLU VAL LEU LYS LYS HIS LEU LYS          
SEQRES  36 B  572  PRO HIS TRP ASN ASP GLY ALA ILE LEU GLY PHE VAL ASN          
SEQRES  37 B  572  LYS GLN GLN ALA HIS ASP LEU LEU ILE ASN LYS PRO ASP          
SEQRES  38 B  572  GLY THR PHE LEU LEU ARG PHE SER ASP SER GLU ILE GLY          
SEQRES  39 B  572  GLY ILE THR ILE ALA TRP LYS PHE ASP SER GLN GLU ARG          
SEQRES  40 B  572  MET PHE TRP ASN LEU MET PRO PHE THR THR ARG ASP PHE          
SEQRES  41 B  572  SER ILE ARG SER LEU ALA ASP ARG LEU GLY ASP LEU ASN          
SEQRES  42 B  572  TYR LEU ILE TYR VAL PHE PRO ASP ARG PRO LYS ASP GLU          
SEQRES  43 B  572  VAL TYR SER LYS TYR TYR THR PRO VAL PRO CYS GLU SER          
SEQRES  44 B  572  ALA THR ALA LYS ALA VAL ASP GLY TYR VAL LYS PRO GLN          
FORMUL   3  HOH   *3(H2 O)                                                      
HELIX    1 AA1 SER A  138  GLN A  183  1                                  46    
HELIX    2 AA2 SER A  193  GLY A  263  1                                  71    
HELIX    3 AA3 VAL A  274  GLN A  302  1                                  29    
HELIX    4 AA4 PRO A  308  GLU A  315  1                                   8    
HELIX    5 AA5 VAL A  316  THR A  331  1                                  16    
HELIX    6 AA6 VAL A  356  LYS A  359  5                                   4    
HELIX    7 AA7 GLU A  376  LYS A  384  1                                   9    
HELIX    8 AA8 HIS A  471  SER A  473  5                                   3    
HELIX    9 AA9 GLN A  474  ALA A  489  1                                  16    
HELIX   10 AB1 TRP A  504  VAL A  519  1                                  16    
HELIX   11 AB2 THR A  526  LEU A  537  1                                  12    
HELIX   12 AB3 GLU A  546  GLY A  550  5                                   5    
HELIX   13 AB4 TRP A  555  ASN A  559  1                                   5    
HELIX   14 AB5 THR A  569  HIS A  584  1                                  16    
HELIX   15 AB6 LEU A  585  ASP A  591  1                                   7    
HELIX   16 AB7 ALA A  603  LEU A  607  5                                   5    
HELIX   17 AB8 THR A  647  ARG A  654  1                                   8    
HELIX   18 AB9 SER A  655  LEU A  660  1                                   6    
HELIX   19 AC1 PRO A  674  SER A  680  1                                   7    
HELIX   20 AC2 LYS A  681  TYR A  683  5                                   3    
HELIX   21 AC3 LYS B  140  ILE B  182  1                                  43    
HELIX   22 AC4 LEU B  198  GLY B  263  1                                  66    
HELIX   23 AC5 LEU B  272  LEU B  303  1                                  32    
HELIX   24 AC6 VAL B  309  THR B  331  1                                  23    
HELIX   25 AC7 GLN B  377  LYS B  384  1                                   8    
HELIX   26 AC8 HIS B  471  SER B  473  5                                   3    
HELIX   27 AC9 GLN B  474  ALA B  489  1                                  16    
HELIX   28 AD1 LEU B  503  GLN B  520  1                                  18    
HELIX   29 AD2 THR B  526  PHE B  538  1                                  13    
HELIX   30 AD3 HIS B  544  SER B  549  1                                   6    
HELIX   31 AD4 SER B  554  ARG B  560  1                                   7    
HELIX   32 AD5 THR B  569  HIS B  584  1                                  16    
HELIX   33 AD6 LEU B  585  ASP B  591  1                                   7    
HELIX   34 AD7 ASN B  599  ASP B  605  1                                   7    
HELIX   35 AD8 THR B  648  ARG B  654  1                                   7    
HELIX   36 AD9 SER B  655  LEU B  663  1                                   9    
HELIX   37 AE1 LYS B  675  SER B  680  1                                   6    
HELIX   38 AE2 LYS B  681  TYR B  683  5                                   3    
SHEET    1 AA1 4 PHE A 332  LYS A 336  0                                        
SHEET    2 AA1 4 PHE A 348  LEU A 354 -1  O  ARG A 353   N  ILE A 333           
SHEET    3 AA1 4 THR A 411  MET A 419 -1  O  LEU A 412   N  LEU A 354           
SHEET    4 AA1 4 GLU A 404  HIS A 406 -1  N  HIS A 406   O  THR A 411           
SHEET    1 AA2 2 LEU A 342  LYS A 343  0                                        
SHEET    2 AA2 2 VAL A 468  ILE A 469  1  O  ILE A 469   N  LEU A 342           
SHEET    1 AA3 4 CYS A 400  VAL A 402  0                                        
SHEET    2 AA3 4 GLN A 368  SER A 375 -1  N  VAL A 369   O  CYS A 401           
SHEET    3 AA3 4 PHE A 440  VAL A 450 -1  O  GLU A 445   N  LYS A 370           
SHEET    4 AA3 4 LEU A 455  LEU A 462 -1  O  PHE A 457   N  PHE A 448           
SHEET    1 AA4 2 GLU A 395  ILE A 396  0                                        
SHEET    2 AA4 2 ARG A 423  ILE A 424 -1  O  ARG A 423   N  ILE A 396           
SHEET    1 AA5 2 LYS A 501  LEU A 503  0                                        
SHEET    2 AA5 2 SER A 552  SER A 554 -1  O  VAL A 553   N  VAL A 502           
SHEET    1 AA6 2 THR A 614  PHE A 615  0                                        
SHEET    2 AA6 2 TYR A 668  VAL A 669  1  O  TYR A 668   N  PHE A 615           
SHEET    1 AA7 2 ARG A 618  PHE A 619  0                                        
SHEET    2 AA7 2 ILE A 627  THR A 628 -1  O  THR A 628   N  ARG A 618           
SHEET    1 AA8 4 PHE B 332  LYS B 336  0                                        
SHEET    2 AA8 4 ALA B 350  LEU B 354 -1  O  ARG B 353   N  ILE B 333           
SHEET    3 AA8 4 THR B 411  PHE B 416 -1  O  LEU B 412   N  LEU B 354           
SHEET    4 AA8 4 GLU B 404  HIS B 406 -1  N  HIS B 406   O  THR B 411           
SHEET    1 AA9 2 VAL B 341  LYS B 343  0                                        
SHEET    2 AA9 2 VAL B 467  ILE B 469  1  O  VAL B 467   N  LEU B 342           
SHEET    1 AB1 4 CYS B 400  VAL B 402  0                                        
SHEET    2 AB1 4 GLN B 368  THR B 372 -1  N  VAL B 369   O  CYS B 401           
SHEET    3 AB1 4 LEU B 443  VAL B 450 -1  O  GLU B 445   N  LYS B 370           
SHEET    4 AB1 4 LEU B 455  LEU B 462 -1  O  PHE B 457   N  PHE B 448           
SHEET    1 AB2 5 TRP B 641  ASN B 642  0                                        
SHEET    2 AB2 5 ILE B 627  LYS B 632 -1  N  TRP B 631   O  TRP B 641           
SHEET    3 AB2 5 THR B 614  PHE B 619 -1  N  LEU B 616   O  ALA B 630           
SHEET    4 AB2 5 TYR B 668  VAL B 669  1  O  TYR B 668   N  PHE B 615           
SHEET    5 AB2 5 ARG B 673  PRO B 674 -1  O  ARG B 673   N  VAL B 669           
CRYST1  134.600  138.620   76.500  90.00  90.00  90.00 P 21 21 2     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      0.007429  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system