GenomeNet

Database: PDB
Entry: 5BPW
LinkDB: 5BPW
Original site: 5BPW 
HEADER    CELL CYCLE                              28-MAY-15   5BPW              
TITLE     ATOMIC-RESOLUTION STRUCTURES OF THE APC/C SUBUNITS APC4 AND THE APC5  
TITLE    2 N-TERMINAL DOMAIN                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANAPHASE-PROMOTING COMPLEX SUBUNIT 4;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: APC4,CYCLOSOME SUBUNIT 4;                                   
COMPND   5 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: ANAPC4, APC4;                                                  
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    APC4, APC/C, ANAPHASE PROMOTING COMPLEX, CELL CYCLE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KULKARNI,J.YANG,Z.ZHANG,D.BARFORD                                   
REVDAT   3   07-OCT-15 5BPW    1       JRNL                                     
REVDAT   2   23-SEP-15 5BPW    1       JRNL                                     
REVDAT   1   02-SEP-15 5BPW    0                                                
JRNL        AUTH   N.B.CRONIN,J.YANG,Z.ZHANG,K.KULKARNI,L.CHANG,H.YAMANO,       
JRNL        AUTH 2 D.BARFORD                                                    
JRNL        TITL   ATOMIC-RESOLUTION STRUCTURES OF THE APC/C SUBUNITS APC4 AND  
JRNL        TITL 2 THE APC5 N-TERMINAL DOMAIN.                                  
JRNL        REF    J.MOL.BIOL.                   V. 427  3300 2015              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   26343760                                                     
JRNL        DOI    10.1016/J.JMB.2015.08.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21631                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 700                             
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 51.9492 -  5.8118    0.99     4374   148  0.2140 0.2755        
REMARK   3     2  5.8118 -  4.6139    1.00     4224   136  0.1935 0.2290        
REMARK   3     3  4.6139 -  4.0310    1.00     4138   142  0.2035 0.2625        
REMARK   3     4  4.0310 -  3.6625    1.00     4107   146  0.2474 0.3100        
REMARK   3     5  3.6625 -  3.4001    0.99     4088   128  0.2870 0.3622        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.83                          
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      :  0.012           5183                                  
REMARK   3   ANGLE     :  1.828           7025                                  
REMARK   3   CHIRALITY :  0.074            833                                  
REMARK   3   PLANARITY :  0.008            878                                  
REMARK   3   DIHEDRAL  : 16.970           1854                                  
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 5BPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210343.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21671                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.18200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.1600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIN NEEDLES                                                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: APC4 CRYSTALS WERE GROWN BY VAPOUR       
REMARK 280  -DIFFUSION IN A BUFFER CONTAINING 10 MM MALIC ACID, 20 MM MES,      
REMARK 280  20 MM TRIS.HCL (PH 8.0), 160 MM NDSB 196, 10 MM EDTA AND 19% (V/    
REMARK 280  V) PEG 1500. CRYSTALS WERE INCUBATED IN A CRYOPROTECTION BUFFER     
REMARK 280  COMPRISING 10 MM MALIC ACID, 20 MM MES, 20 MM TRIS.HCL (PH 8.0),    
REMARK 280  160 MM NDSB 196, 10 MM EDTA, 22% (V/V) PEG 1500 AND 20% (V/V)       
REMARK 280  ETHYLENE GLYCOL PRIOR TO FREEZING IN LIQUID NITROGEN., VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 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   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       69.59050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       69.59050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       69.59050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       69.59050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       69.59050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.59050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       69.59050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.59050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 30410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ASN A   130                                                      
REMARK 465     ALA A   131                                                      
REMARK 465     THR A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     PHE A   290                                                      
REMARK 465     VAL A   291                                                      
REMARK 465     GLN A   292                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     MET A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     LEU A   309                                                      
REMARK 465     TRP A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     SER A   314                                                      
REMARK 465     ALA A   315                                                      
REMARK 465     GLU A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     ASP A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     VAL A   433                                                      
REMARK 465     LEU A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     LEU A   437                                                      
REMARK 465     ASN A   438                                                      
REMARK 465     LYS A   439                                                      
REMARK 465     MET A   440                                                      
REMARK 465     THR A   441                                                      
REMARK 465     GLN A   442                                                      
REMARK 465     LYS A   443                                                      
REMARK 465     ASP A   444                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     PRO A   460                                                      
REMARK 465     ASP A   461                                                      
REMARK 465     LEU A   462                                                      
REMARK 465     TYR A   463                                                      
REMARK 465     ASN A   464                                                      
REMARK 465     ARG A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     GLY A   467                                                      
REMARK 465     LYS A   468                                                      
REMARK 465     TYR A   469                                                      
REMARK 465     PHE A   470                                                      
REMARK 465     ASN A   471                                                      
REMARK 465     VAL A   472                                                      
REMARK 465     LYS A   480                                                      
REMARK 465     ASP A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     ASP A   483                                                      
REMARK 465     ASP A   484                                                      
REMARK 465     ASP A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     VAL A   487                                                      
REMARK 465     SER A   488                                                      
REMARK 465     PRO A   489                                                      
REMARK 465     PRO A   490                                                      
REMARK 465     ASN A   491                                                      
REMARK 465     THR A   492                                                      
REMARK 465     GLU A   493                                                      
REMARK 465     GLY A   494                                                      
REMARK 465     ASN A   495                                                      
REMARK 465     GLN A   496                                                      
REMARK 465     TRP A   497                                                      
REMARK 465     TYR A   498                                                      
REMARK 465     ASP A   499                                                      
REMARK 465     PHE A   500                                                      
REMARK 465     LEU A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     ASN A   503                                                      
REMARK 465     SER A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     HIS A   506                                                      
REMARK 465     LEU A   507                                                      
REMARK 465     LYS A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     PRO A   511                                                      
REMARK 465     LEU A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     PHE A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     TYR A   516                                                      
REMARK 465     TYR A   517                                                      
REMARK 465     PRO A   518                                                      
REMARK 465     ARG A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     SER A   758                                                      
REMARK 465     ASP A   759                                                      
REMARK 465     GLU A   760                                                      
REMARK 465     GLU A   761                                                      
REMARK 465     GLU A   762                                                      
REMARK 465     GLU A   763                                                      
REMARK 465     ALA A   764                                                      
REMARK 465     SER A   765                                                      
REMARK 465     ASN A   766                                                      
REMARK 465     LYS A   767                                                      
REMARK 465     PRO A   768                                                      
REMARK 465     VAL A   769                                                      
REMARK 465     LYS A   770                                                      
REMARK 465     ILE A   771                                                      
REMARK 465     LYS A   772                                                      
REMARK 465     GLU A   773                                                      
REMARK 465     GLU A   774                                                      
REMARK 465     VAL A   775                                                      
REMARK 465     LEU A   776                                                      
REMARK 465     SER A   777                                                      
REMARK 465     GLU A   778                                                      
REMARK 465     SER A   779                                                      
REMARK 465     GLU A   780                                                      
REMARK 465     ALA A   781                                                      
REMARK 465     GLU A   782                                                      
REMARK 465     ASN A   783                                                      
REMARK 465     GLN A   784                                                      
REMARK 465     GLN A   785                                                      
REMARK 465     ALA A   786                                                      
REMARK 465     GLY A   787                                                      
REMARK 465     ALA A   788                                                      
REMARK 465     ALA A   789                                                      
REMARK 465     ALA A   790                                                      
REMARK 465     LEU A   791                                                      
REMARK 465     ALA A   792                                                      
REMARK 465     PRO A   793                                                      
REMARK 465     GLU A   794                                                      
REMARK 465     ILE A   795                                                      
REMARK 465     VAL A   796                                                      
REMARK 465     ILE A   797                                                      
REMARK 465     LYS A   798                                                      
REMARK 465     VAL A   799                                                      
REMARK 465     GLU A   800                                                      
REMARK 465     LYS A   801                                                      
REMARK 465     LEU A   802                                                      
REMARK 465     ASP A   803                                                      
REMARK 465     PRO A   804                                                      
REMARK 465     GLU A   805                                                      
REMARK 465     LEU A   806                                                      
REMARK 465     ASP A   807                                                      
REMARK 465     SER A   808                                                      
REMARK 465     GLU A   809                                                      
REMARK 465     ASN A   810                                                      
REMARK 465     LEU A   811                                                      
REMARK 465     TYR A   812                                                      
REMARK 465     PHE A   813                                                      
REMARK 465     GLN A   814                                                      
REMARK 465     SER A   815                                                      
REMARK 465     TRP A   816                                                      
REMARK 465     SER A   817                                                      
REMARK 465     HIS A   818                                                      
REMARK 465     PRO A   819                                                      
REMARK 465     GLN A   820                                                      
REMARK 465     PHE A   821                                                      
REMARK 465     GLU A   822                                                      
REMARK 465     LYS A   823                                                      
REMARK 465     GLY A   824                                                      
REMARK 465     GLY A   825                                                      
REMARK 465     GLY A   826                                                      
REMARK 465     SER A   827                                                      
REMARK 465     GLY A   828                                                      
REMARK 465     GLY A   829                                                      
REMARK 465     GLY A   830                                                      
REMARK 465     SER A   831                                                      
REMARK 465     GLY A   832                                                      
REMARK 465     GLY A   833                                                      
REMARK 465     GLY A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     TRP A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     HIS A   838                                                      
REMARK 465     PRO A   839                                                      
REMARK 465     GLN A   840                                                      
REMARK 465     PHE A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
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     PHE A 128    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 129    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 132    CD   OE1  OE2                                       
REMARK 470     ASP A 133    CG   OD1  OD2                                       
REMARK 470     ASN A 136    CG   OD1  ND2                                       
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     ASN A 148    CG   OD1  ND2                                       
REMARK 470     TYR A 149    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 151    CG   OD1  ND2                                       
REMARK 470     THR A 152    OG1  CG2                                            
REMARK 470     LYS A 154    CG   CD   CE   NZ                                   
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 160    CG   OD1  ND2                                       
REMARK 470     GLU A 277    CG   CD   OE1  OE2                                  
REMARK 470     MET A 281    CG   SD   CE                                        
REMARK 470     GLN A 282    CD   OE1  NE2                                       
REMARK 470     ARG A 286    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     GLN A 318    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 346    CG   CD   CE   NZ                                   
REMARK 470     GLN A 374    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 399    CG   CD   CE   NZ                                   
REMARK 470     GLU A 402    CG   CD   OE1  OE2                                  
REMARK 470     MET A 411    CG   SD   CE                                        
REMARK 470     LYS A 412    CG   CD   CE   NZ                                   
REMARK 470     PHE A 418    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 427    CD   NE   CZ   NH1  NH2                             
REMARK 470     MET A 428    CG   SD   CE                                        
REMARK 470     GLU A 450    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 451    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LEU A 452    CG   CD1  CD2                                       
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 455    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE A 456    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 477    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 478    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 479    CG   CD1  CD2                                       
REMARK 470     LEU A 522    CG   CD1  CD2                                       
REMARK 470     ARG A 567    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 659    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 660    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 662    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 756    CG   CD   OE1  OE2                                  
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    THR A   453     ND2  ASN A   457              1.83            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG1  THR A   446     OG1  THR A   446     7737     1.81            
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 A 236   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    LEU A 321   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    PRO A 378   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    LEU A 381   CA  -  CB  -  CG  ANGL. DEV. =  16.0 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    PHE A  52       61.04     39.40                                   
REMARK 500    ASN A  61     -167.60   -169.99                                   
REMARK 500    PRO A 109      152.67    -49.02                                   
REMARK 500    ASN A 151     -116.44     56.73                                   
REMARK 500    ILE A 155      -61.89   -130.59                                   
REMARK 500    TYR A 190       -1.50     66.05                                   
REMARK 500    MET A 192      -63.56   -130.29                                   
REMARK 500    TYR A 242      -71.58    -76.03                                   
REMARK 500    GLN A 324      -63.85   -131.71                                   
REMARK 500    HIS A 351      -65.23    -97.13                                   
REMARK 500    GLU A 377       59.84   -115.43                                   
REMARK 500    THR A 429      -76.39   -107.32                                   
REMARK 500    HIS A 523      -68.43    -90.51                                   
REMARK 500    LEU A 556      -64.38   -102.55                                   
REMARK 500    LEU A 569      -13.85     75.04                                   
REMARK 500    ASN A 582       70.98     52.90                                   
REMARK 500    GLU A 592      -75.73   -107.84                                   
REMARK 500    GLU A 678      -72.12    -76.32                                   
REMARK 500    HIS A 710       70.55     54.81                                   
REMARK 500    LYS A 718        2.27     83.11                                   
REMARK 500    GLN A 720      -57.26   -122.21                                   
REMARK 500    PHE A 727      -70.70    -95.59                                   
REMARK 500    LEU A 738       -2.33     67.42                                   
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 LEU A  320     LEU A  321                  128.32                    
REMARK 500 GLU A  377     PRO A  378                  128.69                    
REMARK 500 HIS A  523     PHE A  524                 -147.75                    
REMARK 500 GLU A  629     LYS A  630                  149.23                    
REMARK 500 GLY A  658     ARG A  659                 -143.53                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5BPW A    1   808  UNP    Q9UJX5   APC4_HUMAN       1    808             
SEQADV 5BPW GLU A  809  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW ASN A  810  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW LEU A  811  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW TYR A  812  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW PHE A  813  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLN A  814  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  815  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW TRP A  816  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  817  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW HIS A  818  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW PRO A  819  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLN A  820  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW PHE A  821  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLU A  822  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW LYS A  823  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  824  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  825  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  826  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  827  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  828  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  829  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  830  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  831  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  832  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  833  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLY A  834  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  835  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW TRP A  836  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW SER A  837  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW HIS A  838  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW PRO A  839  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLN A  840  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW PHE A  841  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW GLU A  842  UNP  Q9UJX5              EXPRESSION TAG                 
SEQADV 5BPW LYS A  843  UNP  Q9UJX5              EXPRESSION TAG                 
SEQRES   1 A  843  MET LEU ARG PHE PRO THR CYS PHE PRO SER PHE ARG VAL          
SEQRES   2 A  843  VAL GLY GLU LYS GLN LEU PRO GLN GLU ILE ILE PHE LEU          
SEQRES   3 A  843  VAL TRP SER PRO LYS ARG ASP LEU ILE ALA LEU ALA ASN          
SEQRES   4 A  843  THR ALA GLY GLU VAL LEU LEU HIS ARG LEU ALA SER PHE          
SEQRES   5 A  843  HIS ARG VAL TRP SER PHE PRO PRO ASN GLU ASN THR GLY          
SEQRES   6 A  843  LYS GLU VAL THR CYS LEU ALA TRP ARG PRO ASP GLY LYS          
SEQRES   7 A  843  LEU LEU ALA PHE ALA LEU ALA ASP THR LYS LYS ILE VAL          
SEQRES   8 A  843  LEU CYS ASP VAL GLU LYS PRO GLU SER LEU HIS SER PHE          
SEQRES   9 A  843  SER VAL GLU ALA PRO VAL SER CYS MET HIS TRP MET GLU          
SEQRES  10 A  843  VAL THR VAL GLU SER SER VAL LEU THR SER PHE TYR ASN          
SEQRES  11 A  843  ALA GLU ASP GLU SER ASN LEU LEU LEU PRO LYS LEU PRO          
SEQRES  12 A  843  THR LEU PRO LYS ASN TYR SER ASN THR SER LYS ILE PHE          
SEQRES  13 A  843  SER GLU GLU ASN SER ASP GLU ILE ILE LYS LEU LEU GLY          
SEQRES  14 A  843  ASP VAL ARG LEU ASN ILE LEU VAL LEU GLY GLY SER SER          
SEQRES  15 A  843  GLY PHE ILE GLU LEU TYR ALA TYR GLY MET PHE LYS ILE          
SEQRES  16 A  843  ALA ARG VAL THR GLY ILE ALA GLY THR CYS LEU ALA LEU          
SEQRES  17 A  843  CYS LEU SER SER ASP LEU LYS SER LEU SER VAL VAL THR          
SEQRES  18 A  843  GLU VAL SER THR ASN GLY ALA SER GLU VAL SER TYR PHE          
SEQRES  19 A  843  GLN LEU GLU THR ASN LEU LEU TYR SER PHE LEU PRO GLU          
SEQRES  20 A  843  VAL THR ARG MET ALA ARG LYS PHE THR HIS ILE SER ALA          
SEQRES  21 A  843  LEU LEU GLN TYR ILE ASN LEU SER LEU THR CYS MET CYS          
SEQRES  22 A  843  GLU ALA TRP GLU GLU ILE LEU MET GLN MET ASP SER ARG          
SEQRES  23 A  843  LEU THR LYS PHE VAL GLN GLU LYS ASN THR THR THR SER          
SEQRES  24 A  843  VAL GLN ASP GLU PHE MET HIS LEU LEU LEU TRP GLY LYS          
SEQRES  25 A  843  ALA SER ALA GLU LEU GLN THR LEU LEU MET ASN GLN LEU          
SEQRES  26 A  843  THR VAL LYS GLY LEU LYS LYS LEU GLY GLN SER ILE GLU          
SEQRES  27 A  843  SER SER TYR SER SER ILE GLN LYS LEU VAL ILE SER HIS          
SEQRES  28 A  843  LEU GLN SER GLY SER GLU SER LEU LEU TYR HIS LEU SER          
SEQRES  29 A  843  GLU LEU LYS GLY MET ALA SER TRP LYS GLN LYS TYR GLU          
SEQRES  30 A  843  PRO LEU GLY LEU ASP ALA ALA GLY ILE GLU GLU ALA ILE          
SEQRES  31 A  843  THR ALA VAL GLY SER PHE ILE LEU LYS ALA ASN GLU LEU          
SEQRES  32 A  843  LEU GLN VAL ILE ASP SER SER MET LYS ASN PHE LYS ALA          
SEQRES  33 A  843  PHE PHE ARG TRP LEU TYR VAL ALA MET LEU ARG MET THR          
SEQRES  34 A  843  GLU ASP HIS VAL LEU PRO GLU LEU ASN LYS MET THR GLN          
SEQRES  35 A  843  LYS ASP ILE THR PHE VAL ALA GLU PHE LEU THR GLU HIS          
SEQRES  36 A  843  PHE ASN GLU ALA PRO ASP LEU TYR ASN ARG LYS GLY LYS          
SEQRES  37 A  843  TYR PHE ASN VAL GLU ARG VAL GLY GLN TYR LEU LYS ASP          
SEQRES  38 A  843  GLU ASP ASP ASP LEU VAL SER PRO PRO ASN THR GLU GLY          
SEQRES  39 A  843  ASN GLN TRP TYR ASP PHE LEU GLN ASN SER SER HIS LEU          
SEQRES  40 A  843  LYS GLU SER PRO LEU LEU PHE PRO TYR TYR PRO ARG LYS          
SEQRES  41 A  843  SER LEU HIS PHE VAL LYS ARG ARG MET GLU ASN ILE ILE          
SEQRES  42 A  843  ASP GLN CYS LEU GLN LYS PRO ALA ASP VAL ILE GLY LYS          
SEQRES  43 A  843  SER MET ASN GLN ALA ILE CYS ILE PRO LEU TYR ARG ASP          
SEQRES  44 A  843  THR ARG SER GLU ASP SER THR ARG ARG LEU PHE LYS PHE          
SEQRES  45 A  843  PRO PHE LEU TRP ASN ASN LYS THR SER ASN LEU HIS TYR          
SEQRES  46 A  843  LEU LEU PHE THR ILE LEU GLU ASP SER LEU TYR LYS MET          
SEQRES  47 A  843  CYS ILE LEU ARG ARG HIS THR ASP ILE SER GLN SER VAL          
SEQRES  48 A  843  SER ASN GLY LEU ILE ALA ILE LYS PHE GLY SER PHE THR          
SEQRES  49 A  843  TYR ALA THR THR GLU LYS VAL ARG ARG SER ILE TYR SER          
SEQRES  50 A  843  CYS LEU ASP ALA GLN PHE TYR ASP ASP GLU THR VAL THR          
SEQRES  51 A  843  VAL VAL LEU LYS ASP THR VAL GLY ARG GLU GLY ARG ASP          
SEQRES  52 A  843  ARG LEU LEU VAL GLN LEU PRO LEU SER LEU VAL TYR ASN          
SEQRES  53 A  843  SER GLU ASP SER ALA GLU TYR GLN PHE THR GLY THR TYR          
SEQRES  54 A  843  SER THR ARG LEU ASP GLU GLN CYS SER ALA ILE PRO THR          
SEQRES  55 A  843  ARG THR MET HIS PHE GLU LYS HIS TRP ARG LEU LEU GLU          
SEQRES  56 A  843  SER MET LYS ALA GLN TYR VAL ALA GLY ASN GLY PHE ARG          
SEQRES  57 A  843  LYS VAL SER CYS VAL LEU SER SER ASN LEU ARG HIS VAL          
SEQRES  58 A  843  ARG VAL PHE GLU MET ASP ILE ASP ASP GLU TRP GLU LEU          
SEQRES  59 A  843  ASP GLU SER SER ASP GLU GLU GLU GLU ALA SER ASN LYS          
SEQRES  60 A  843  PRO VAL LYS ILE LYS GLU GLU VAL LEU SER GLU SER GLU          
SEQRES  61 A  843  ALA GLU ASN GLN GLN ALA GLY ALA ALA ALA LEU ALA PRO          
SEQRES  62 A  843  GLU ILE VAL ILE LYS VAL GLU LYS LEU ASP PRO GLU LEU          
SEQRES  63 A  843  ASP SER GLU ASN LEU TYR PHE GLN SER TRP SER HIS PRO          
SEQRES  64 A  843  GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY          
SEQRES  65 A  843  GLY GLY SER TRP SER HIS PRO GLN PHE GLU LYS                  
HELIX    1 AA1 ALA A   50  PHE A   52  5                                   3    
HELIX    2 AA2 ASP A  133  LEU A  137  1                                   5    
HELIX    3 AA3 SER A  161  ASP A  170  1                                  10    
HELIX    4 AA4 THR A  238  PHE A  244  1                                   7    
HELIX    5 AA5 PHE A  244  SER A  285  1                                  42    
HELIX    6 AA6 THR A  326  HIS A  351  1                                  26    
HELIX    7 AA7 HIS A  351  SER A  371  1                                  21    
HELIX    8 AA8 TRP A  372  GLU A  377  1                                   6    
HELIX    9 AA9 ASP A  382  ARG A  427  1                                  46    
HELIX   10 AB1 PHE A  447  ASN A  457  1                                  11    
HELIX   11 AB2 ARG A  474  LEU A  479  1                                   6    
HELIX   12 AB3 VAL A  525  MET A  548  1                                  24    
HELIX   13 AB4 SER A  672  VAL A  674  5                                   3    
HELIX   14 AB5 GLU A  678  TYR A  683  5                                   6    
SHEET    1 AA1 4 ARG A  12  GLN A  18  0                                        
SHEET    2 AA1 4 HIS A 740  GLU A 745 -1  O  VAL A 743   N  GLY A  15           
SHEET    3 AA1 4 VAL A 730  LEU A 734 -1  N  VAL A 733   O  ARG A 742           
SHEET    4 AA1 4 TYR A 721  GLY A 724 -1  N  ALA A 723   O  CYS A 732           
SHEET    1 AA2 4 ILE A  23  TRP A  28  0                                        
SHEET    2 AA2 4 LEU A  34  ASN A  39 -1  O  ALA A  36   N  VAL A  27           
SHEET    3 AA2 4 VAL A  44  ARG A  48 -1  O  LEU A  45   N  LEU A  37           
SHEET    4 AA2 4 ARG A  54  PHE A  58 -1  O  VAL A  55   N  LEU A  46           
SHEET    1 AA3 4 VAL A  68  TRP A  73  0                                        
SHEET    2 AA3 4 LEU A  79  LEU A  84 -1  O  ALA A  81   N  ALA A  72           
SHEET    3 AA3 4 LYS A  89  ASP A  94 -1  O  LYS A  89   N  LEU A  84           
SHEET    4 AA3 4 SER A 100  SER A 105 -1  O  HIS A 102   N  LEU A  92           
SHEET    1 AA4 4 CYS A 112  GLU A 117  0                                        
SHEET    2 AA4 4 ASN A 174  GLY A 179 -1  O  VAL A 177   N  HIS A 114           
SHEET    3 AA4 4 PHE A 184  ALA A 189 -1  O  GLU A 186   N  LEU A 178           
SHEET    4 AA4 4 LYS A 194  THR A 199 -1  O  VAL A 198   N  ILE A 185           
SHEET    1 AA5 4 THR A 204  LEU A 210  0                                        
SHEET    2 AA5 4 SER A 216  VAL A 223 -1  O  SER A 218   N  CYS A 209           
SHEET    3 AA5 4 SER A 229  GLU A 237 -1  O  LEU A 236   N  LEU A 217           
SHEET    4 AA5 4 ALA A 551  ASP A 559 -1  O  ILE A 554   N  TYR A 233           
SHEET    1 AA6 5 PHE A 574  ASN A 578  0                                        
SHEET    2 AA6 5 LEU A 583  LEU A 591 -1  O  TYR A 585   N  TRP A 576           
SHEET    3 AA6 5 TYR A 596  HIS A 604 -1  O  CYS A 599   N  PHE A 588           
SHEET    4 AA6 5 LEU A 615  THR A 624 -1  O  ILE A 616   N  ILE A 600           
SHEET    5 AA6 5 VAL A 631  ARG A 632 -1  O  ARG A 632   N  PHE A 623           
SHEET    1 AA7 5 PHE A 574  ASN A 578  0                                        
SHEET    2 AA7 5 LEU A 583  LEU A 591 -1  O  TYR A 585   N  TRP A 576           
SHEET    3 AA7 5 TYR A 596  HIS A 604 -1  O  CYS A 599   N  PHE A 588           
SHEET    4 AA7 5 LEU A 615  THR A 624 -1  O  ILE A 616   N  ILE A 600           
SHEET    5 AA7 5 THR A 702  PHE A 707  1  O  PHE A 707   N  SER A 622           
SHEET    1 AA8 4 TYR A 636  ASP A 645  0                                        
SHEET    2 AA8 4 THR A 648  ASP A 655 -1  O  LYS A 654   N  SER A 637           
SHEET    3 AA8 4 ARG A 664  PRO A 670 -1  O  VAL A 667   N  VAL A 651           
SHEET    4 AA8 4 TRP A 711  LEU A 713 -1  O  ARG A 712   N  LEU A 666           
CISPEP   1 PHE A  572    PRO A  573          0        -1.42                     
CRYST1  139.181  139.181  156.106  90.00  90.00  90.00 P 4 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      0.007185  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007185  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006406        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system