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Database: PDB
Entry: 4GGD
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HEADER    CELL CYCLE                              06-AUG-12   4GGD              
TITLE     STRUCTURAL ANALYSIS OF HUMAN CDC20 SUPPORTS MULTISITE DEGRON          
TITLE    2 RECOGNITION BY APC/C.                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CYCLE PROTEIN 20 HOMOLOG;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: P55CDC;                                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1    
COMPND   8 BETA;                                                                
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 SYNONYM: MAD3/BUB1-RELATED PROTEIN KINASE, HBUBR1, MITOTIC CHECKPOINT
COMPND  11 KINASE MAD3L, PROTEIN SSK1;                                          
COMPND  12 EC: 2.7.11.1;                                                        
COMPND  13 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: CDC20;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL CYCLE, MITOSIS, SECURIN, UBIQUITINATION, WD40                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LUO,W.TIAN,D.R.TOMCHICK                                             
REVDAT   5   21-FEB-18 4GGD    1       REMARK                                   
REVDAT   4   15-NOV-17 4GGD    1       REMARK                                   
REVDAT   3   26-OCT-16 4GGD    1       SOURCE                                   
REVDAT   2   26-DEC-12 4GGD    1       JRNL                                     
REVDAT   1   07-NOV-12 4GGD    0                                                
JRNL        AUTH   W.TIAN,B.LI,R.WARRINGTON,D.R.TOMCHICK,H.YU,X.LUO             
JRNL        TITL   STRUCTURAL ANALYSIS OF HUMAN CDC20 SUPPORTS MULTISITE DEGRON 
JRNL        TITL 2 RECOGNITION BY APC/C.                                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 18419 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23091007                                                     
JRNL        DOI    10.1073/PNAS.1213438109                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.YU                                                         
REMARK   1  TITL   CDC20: A WD40 ACTIVATOR FOR A CELL CYCLE DEGRADATION MACHINE 
REMARK   1  REF    MOL.CELL                      V.  27     3 2007              
REMARK   1  REFN                   ISSN 1097-2765                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.QI,H.YU                                                    
REMARK   1  TITL   KEN-BOX-DEPENDENT DEGRADATION OF BUB1 SPINDLE CHECKPOINT     
REMARK   1  TITL 2 KINASE BY THE ANAPHASE-PROMOTING COMPLEX/CYCLOSOME           
REMARK   1  REF    J.BIOL.CHEM.                  V. 282  3672 2007              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   Z.TANG,R.BHARADWAJ,B.LI,H.YU                                 
REMARK   1  TITL   MAD2-INDEPENDENT INHIBITION OF APC-CDC20 BY THE MITOTIC      
REMARK   1  TITL 2 CHECKPOINT PROTEIN BUBR1                                     
REMARK   1  REF    DEV.CELL                      V.   1   227 2001              
REMARK   1  REFN                   ISSN 1534-5807                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8_1062                                      
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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 36910                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1835                            
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 29.1700 -  5.7113    0.99     2827   144  0.1613 0.1757        
REMARK   3     2  5.7113 -  4.5387    0.99     2754   151  0.1197 0.1552        
REMARK   3     3  4.5387 -  3.9666    0.99     2771   144  0.1191 0.1688        
REMARK   3     4  3.9666 -  3.6046    0.99     2744   146  0.1418 0.1851        
REMARK   3     5  3.6046 -  3.3467    0.99     2749   141  0.1496 0.2194        
REMARK   3     6  3.3467 -  3.1496    0.99     2728   133  0.1666 0.2090        
REMARK   3     7  3.1496 -  2.9920    0.98     2746   147  0.1696 0.2252        
REMARK   3     8  2.9920 -  2.8619    0.98     2700   142  0.1803 0.2458        
REMARK   3     9  2.8619 -  2.7518    0.99     2694   141  0.1847 0.2676        
REMARK   3    10  2.7518 -  2.6569    0.98     2714   140  0.1880 0.2627        
REMARK   3    11  2.6569 -  2.5739    0.97     2693   149  0.1957 0.2446        
REMARK   3    12  2.5739 -  2.5004    0.99     2714   146  0.2058 0.3007        
REMARK   3    13  2.5004 -  2.4346    0.80     2241   111  0.2159 0.2600        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.90                          
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      :  0.013           5079                                  
REMARK   3   ANGLE     :  1.417           6928                                  
REMARK   3   CHIRALITY :  0.077            757                                  
REMARK   3   PLANARITY :  0.006            888                                  
REMARK   3   DIHEDRAL  : 14.424           1766                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 202 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1463  12.2023 -55.5632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1962 T22:   0.3181                                     
REMARK   3      T33:   0.2692 T12:   0.0542                                     
REMARK   3      T13:  -0.0341 T23:   0.1815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4995 L22:   0.7663                                     
REMARK   3      L33:   0.3115 L12:   0.3922                                     
REMARK   3      L13:   0.1356 L23:   0.1952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0590 S12:   0.3076 S13:   0.4331                       
REMARK   3      S21:   0.0775 S22:  -0.0066 S23:   0.0443                       
REMARK   3      S31:  -0.0822 S32:   0.0917 S33:  -0.3162                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9958  -1.6915 -54.7155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1338 T22:   0.3386                                     
REMARK   3      T33:   0.1469 T12:  -0.0132                                     
REMARK   3      T13:  -0.0565 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1266 L22:   0.9289                                     
REMARK   3      L33:   0.4171 L12:  -0.3356                                     
REMARK   3      L13:  -0.0195 L23:   0.0572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:   0.3202 S13:  -0.1100                       
REMARK   3      S21:   0.0112 S22:   0.0759 S23:   0.3067                       
REMARK   3      S31:   0.1944 S32:  -0.2200 S33:  -0.0109                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 359 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7197  -8.1820 -41.4999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1883 T22:   0.1357                                     
REMARK   3      T33:   0.1690 T12:   0.0069                                     
REMARK   3      T13:  -0.0027 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1692 L22:   0.0698                                     
REMARK   3      L33:   0.0961 L12:   0.0239                                     
REMARK   3      L13:  -0.0194 L23:  -0.0830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0698 S12:  -0.0833 S13:  -0.2656                       
REMARK   3      S21:   0.1089 S22:   0.0220 S23:   0.0444                       
REMARK   3      S31:   0.0378 S32:  -0.0276 S33:   0.0003                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 360 THROUGH 476 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8468  10.1311 -49.1967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2108 T22:   0.2183                                     
REMARK   3      T33:   0.3259 T12:   0.0103                                     
REMARK   3      T13:  -0.0326 T23:   0.1068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3201 L22:   0.2671                                     
REMARK   3      L33:   0.1264 L12:   0.1116                                     
REMARK   3      L13:  -0.0763 L23:  -0.0851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1009 S12:   0.2655 S13:   0.4244                       
REMARK   3      S21:   0.1764 S22:  -0.0919 S23:  -0.1818                       
REMARK   3      S31:  -0.0788 S32:   0.1791 S33:  -0.0151                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5612  -8.4054  -2.3752              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1071 T22:   0.2858                                     
REMARK   3      T33:   0.1575 T12:  -0.0588                                     
REMARK   3      T13:   0.0546 T23:   0.1401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4101 L22:   0.8151                                     
REMARK   3      L33:   0.6800 L12:  -0.2844                                     
REMARK   3      L13:  -0.1439 L23:   0.3127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0185 S12:  -0.4593 S13:  -0.2651                       
REMARK   3      S21:  -0.0274 S22:  -0.0827 S23:   0.1015                       
REMARK   3      S31:  -0.0370 S32:  -0.1553 S33:  -0.4401                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7718   3.8902 -13.6300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1256 T22:   0.1075                                     
REMARK   3      T33:   0.1347 T12:  -0.0161                                     
REMARK   3      T13:   0.0021 T23:  -0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3454 L22:   0.2031                                     
REMARK   3      L33:   0.1968 L12:   0.1409                                     
REMARK   3      L13:  -0.0940 L23:  -0.1725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0639 S12:  -0.0538 S13:   0.1114                       
REMARK   3      S21:  -0.0525 S22:  -0.0339 S23:   0.0660                       
REMARK   3      S31:  -0.0542 S32:  -0.0100 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 476 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5664 -14.0262  -8.1723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1930 T22:   0.2107                                     
REMARK   3      T33:   0.3691 T12:  -0.0382                                     
REMARK   3      T13:   0.0524 T23:   0.2523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1803 L22:   0.1173                                     
REMARK   3      L33:   0.3430 L12:  -0.0147                                     
REMARK   3      L13:  -0.0575 L23:  -0.0703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:  -0.2729 S13:  -0.5210                       
REMARK   3      S21:  -0.0903 S22:  -0.0941 S23:  -0.2193                       
REMARK   3      S31:   0.1368 S32:   0.2707 S33:   0.0599                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9130  10.6371 -33.9571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4867 T22:   0.4271                                     
REMARK   3      T33:   0.3447 T12:   0.1405                                     
REMARK   3      T13:  -0.0236 T23:  -0.1619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0009 L22:   0.0020                                     
REMARK   3      L33:   0.0025 L12:  -0.0001                                     
REMARK   3      L13:   0.0014 L23:   0.0012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0255 S12:  -0.0077 S13:  -0.0022                       
REMARK   3      S21:   0.0134 S22:   0.0275 S23:   0.0283                       
REMARK   3      S31:   0.0238 S32:   0.0125 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4582 -12.5557 -24.7615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2912 T22:   0.1836                                     
REMARK   3      T33:   0.2185 T12:  -0.0699                                     
REMARK   3      T13:   0.0055 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0036 L22:   0.0004                                     
REMARK   3      L33:   0.0006 L12:   0.0012                                     
REMARK   3      L13:  -0.0016 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0163 S12:   0.0358 S13:   0.0281                       
REMARK   3      S21:   0.0072 S22:   0.0943 S23:   0.0276                       
REMARK   3      S31:   0.0451 S32:   0.0032 S33:  -0.0000                       
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 4GGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074148.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97937                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36910                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.435                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM CAPSO, 5% (W/V) PEG 6000, AND      
REMARK 280  15.5 % MPD, PH 9.3, SITTING-DROP VAPOR DIFFUSION, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       44.06450            
REMARK 290   SMTRY3   2  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     GLY A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     LYS A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     GLY A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     TYR A    79                                                      
REMARK 465     ILE A    80                                                      
REMARK 465     PRO A    81                                                      
REMARK 465     HIS A    82                                                      
REMARK 465     ARG A    83                                                      
REMARK 465     SER A    84                                                      
REMARK 465     ALA A    85                                                      
REMARK 465     ALA A    86                                                      
REMARK 465     GLN A    87                                                      
REMARK 465     MET A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     SER A    92                                                      
REMARK 465     PHE A    93                                                      
REMARK 465     LEU A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     SER A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     GLU A    98                                                      
REMARK 465     ASN A    99                                                      
REMARK 465     GLN A   100                                                      
REMARK 465     PRO A   101                                                      
REMARK 465     GLU A   102                                                      
REMARK 465     ASN A   103                                                      
REMARK 465     SER A   104                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     THR A   106                                                      
REMARK 465     PRO A   107                                                      
REMARK 465     THR A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     GLU A   111                                                      
REMARK 465     HIS A   112                                                      
REMARK 465     GLN A   113                                                      
REMARK 465     LYS A   114                                                      
REMARK 465     ALA A   115                                                      
REMARK 465     TRP A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     ASN A   119                                                      
REMARK 465     LEU A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     GLY A   122                                                      
REMARK 465     PHE A   123                                                      
REMARK 465     ASP A   124                                                      
REMARK 465     VAL A   125                                                      
REMARK 465     GLU A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     ALA A   128                                                      
REMARK 465     LYS A   129                                                      
REMARK 465     ILE A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     ARG A   132                                                      
REMARK 465     LEU A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     GLN A   138                                                      
REMARK 465     ASN A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     GLU A   142                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     GLN A   145                                                      
REMARK 465     ASN A   146                                                      
REMARK 465     ARG A   147                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     VAL A   150                                                      
REMARK 465     LEU A   151                                                      
REMARK 465     TYR A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     GLN A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     THR A   157                                                      
REMARK 465     PRO A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     LYS A   163                                                      
REMARK 465     THR A   164                                                      
REMARK 465     PRO A   477                                                      
REMARK 465     ALA A   478                                                      
REMARK 465     ARG A   479                                                      
REMARK 465     ARG A   480                                                      
REMARK 465     ARG A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     ARG A   483                                                      
REMARK 465     GLU A   484                                                      
REMARK 465     LYS A   485                                                      
REMARK 465     ALA A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     SER A   492                                                      
REMARK 465     LEU A   493                                                      
REMARK 465     ILE A   494                                                      
REMARK 465     HIS A   495                                                      
REMARK 465     GLN A   496                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     ILE A   498                                                      
REMARK 465     ARG A   499                                                      
REMARK 465     GLY B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     PRO B    71                                                      
REMARK 465     SER B    72                                                      
REMARK 465     LYS B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     ASP B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     TYR B    79                                                      
REMARK 465     ILE B    80                                                      
REMARK 465     PRO B    81                                                      
REMARK 465     HIS B    82                                                      
REMARK 465     ARG B    83                                                      
REMARK 465     SER B    84                                                      
REMARK 465     ALA B    85                                                      
REMARK 465     ALA B    86                                                      
REMARK 465     GLN B    87                                                      
REMARK 465     MET B    88                                                      
REMARK 465     GLU B    89                                                      
REMARK 465     VAL B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     SER B    92                                                      
REMARK 465     PHE B    93                                                      
REMARK 465     LEU B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     SER B    96                                                      
REMARK 465     LYS B    97                                                      
REMARK 465     GLU B    98                                                      
REMARK 465     ASN B    99                                                      
REMARK 465     GLN B   100                                                      
REMARK 465     PRO B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     ASN B   103                                                      
REMARK 465     SER B   104                                                      
REMARK 465     GLN B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     PRO B   107                                                      
REMARK 465     THR B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     LYS B   110                                                      
REMARK 465     GLU B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     GLN B   113                                                      
REMARK 465     LYS B   114                                                      
REMARK 465     ALA B   115                                                      
REMARK 465     TRP B   116                                                      
REMARK 465     ALA B   117                                                      
REMARK 465     LEU B   118                                                      
REMARK 465     ASN B   119                                                      
REMARK 465     LEU B   120                                                      
REMARK 465     ASN B   121                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     PHE B   123                                                      
REMARK 465     ASP B   124                                                      
REMARK 465     VAL B   125                                                      
REMARK 465     GLU B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     ALA B   128                                                      
REMARK 465     LYS B   129                                                      
REMARK 465     ILE B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     ARG B   132                                                      
REMARK 465     LEU B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     GLN B   138                                                      
REMARK 465     ASN B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     GLU B   142                                                      
REMARK 465     GLY B   143                                                      
REMARK 465     TYR B   144                                                      
REMARK 465     GLN B   145                                                      
REMARK 465     ASN B   146                                                      
REMARK 465     ARG B   147                                                      
REMARK 465     LEU B   148                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     VAL B   150                                                      
REMARK 465     LEU B   151                                                      
REMARK 465     TYR B   152                                                      
REMARK 465     SER B   153                                                      
REMARK 465     GLN B   154                                                      
REMARK 465     LYS B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     THR B   157                                                      
REMARK 465     PRO B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     SER B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     ARG B   162                                                      
REMARK 465     LYS B   163                                                      
REMARK 465     THR B   164                                                      
REMARK 465     PRO B   477                                                      
REMARK 465     ALA B   478                                                      
REMARK 465     ARG B   479                                                      
REMARK 465     ARG B   480                                                      
REMARK 465     ARG B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     ARG B   483                                                      
REMARK 465     GLU B   484                                                      
REMARK 465     LYS B   485                                                      
REMARK 465     ALA B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     ALA B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     LYS B   490                                                      
REMARK 465     SER B   491                                                      
REMARK 465     SER B   492                                                      
REMARK 465     LEU B   493                                                      
REMARK 465     ILE B   494                                                      
REMARK 465     HIS B   495                                                      
REMARK 465     GLN B   496                                                      
REMARK 465     GLY B   497                                                      
REMARK 465     ILE B   498                                                      
REMARK 465     ARG B   499                                                      
REMARK 465     ASP C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     TRP C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     LEU C    13                                                      
REMARK 465     ARG C    14                                                      
REMARK 465     GLN C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     ILE C    18                                                      
REMARK 465     MET C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     THR C    21                                                      
REMARK 465     LEU C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     TRP D     3                                                      
REMARK 465     PRO D    12                                                      
REMARK 465     LEU D    13                                                      
REMARK 465     ARG D    14                                                      
REMARK 465     GLN D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     ARG D    17                                                      
REMARK 465     ILE D    18                                                      
REMARK 465     MET D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     THR D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     GLN D    23                                                      
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    ASP A 203     -102.53     46.28                                   
REMARK 500    SER A 212      -72.32    -64.34                                   
REMARK 500    SER A 266      -36.05    171.24                                   
REMARK 500    SER A 278     -120.76     63.20                                   
REMARK 500    ASP A 379      -61.68   -120.45                                   
REMARK 500    SER A 394      143.20   -176.97                                   
REMARK 500    HIS A 410      -55.99    -25.89                                   
REMARK 500    LEU A 475     -158.60   -101.18                                   
REMARK 500    ASP B 203     -103.48     49.12                                   
REMARK 500    SER B 266      -34.40    180.00                                   
REMARK 500    SER B 278     -114.46     58.90                                   
REMARK 500    GLU B 342      -53.53     61.01                                   
REMARK 500    SER B 394      142.87   -177.36                                   
REMARK 500    LYS B 412       70.49     45.20                                   
REMARK 500    LYS C   7      -44.52    -26.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GGA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GGC   RELATED DB: PDB                                   
DBREF  4GGD A   71   499  UNP    Q12834   CDC20_HUMAN     71    499             
DBREF  4GGD B   71   499  UNP    Q12834   CDC20_HUMAN     71    499             
DBREF  4GGD C    1    23  UNP    O60566   BUB1B_HUMAN     20     42             
DBREF  4GGD D    1    23  UNP    O60566   BUB1B_HUMAN     20     42             
SEQADV 4GGD GLY A   69  UNP  Q12834              EXPRESSION TAG                 
SEQADV 4GGD ALA A   70  UNP  Q12834              EXPRESSION TAG                 
SEQADV 4GGD GLY B   69  UNP  Q12834              EXPRESSION TAG                 
SEQADV 4GGD ALA B   70  UNP  Q12834              EXPRESSION TAG                 
SEQRES   1 A  431  GLY ALA PRO SER LYS PRO GLY GLY ASP ARG TYR ILE PRO          
SEQRES   2 A  431  HIS ARG SER ALA ALA GLN MET GLU VAL ALA SER PHE LEU          
SEQRES   3 A  431  LEU SER LYS GLU ASN GLN PRO GLU ASN SER GLN THR PRO          
SEQRES   4 A  431  THR LYS LYS GLU HIS GLN LYS ALA TRP ALA LEU ASN LEU          
SEQRES   5 A  431  ASN GLY PHE ASP VAL GLU GLU ALA LYS ILE LEU ARG LEU          
SEQRES   6 A  431  SER GLY LYS PRO GLN ASN ALA PRO GLU GLY TYR GLN ASN          
SEQRES   7 A  431  ARG LEU LYS VAL LEU TYR SER GLN LYS ALA THR PRO GLY          
SEQRES   8 A  431  SER SER ARG LYS THR CYS ARG TYR ILE PRO SER LEU PRO          
SEQRES   9 A  431  ASP ARG ILE LEU ASP ALA PRO GLU ILE ARG ASN ASP TYR          
SEQRES  10 A  431  TYR LEU ASN LEU VAL ASP TRP SER SER GLY ASN VAL LEU          
SEQRES  11 A  431  ALA VAL ALA LEU ASP ASN SER VAL TYR LEU TRP SER ALA          
SEQRES  12 A  431  SER SER GLY ASP ILE LEU GLN LEU LEU GLN MET GLU GLN          
SEQRES  13 A  431  PRO GLY GLU TYR ILE SER SER VAL ALA TRP ILE LYS GLU          
SEQRES  14 A  431  GLY ASN TYR LEU ALA VAL GLY THR SER SER ALA GLU VAL          
SEQRES  15 A  431  GLN LEU TRP ASP VAL GLN GLN GLN LYS ARG LEU ARG ASN          
SEQRES  16 A  431  MET THR SER HIS SER ALA ARG VAL GLY SER LEU SER TRP          
SEQRES  17 A  431  ASN SER TYR ILE LEU SER SER GLY SER ARG SER GLY HIS          
SEQRES  18 A  431  ILE HIS HIS HIS ASP VAL ARG VAL ALA GLU HIS HIS VAL          
SEQRES  19 A  431  ALA THR LEU SER GLY HIS SER GLN GLU VAL CYS GLY LEU          
SEQRES  20 A  431  ARG TRP ALA PRO ASP GLY ARG HIS LEU ALA SER GLY GLY          
SEQRES  21 A  431  ASN ASP ASN LEU VAL ASN VAL TRP PRO SER ALA PRO GLY          
SEQRES  22 A  431  GLU GLY GLY TRP VAL PRO LEU GLN THR PHE THR GLN HIS          
SEQRES  23 A  431  GLN GLY ALA VAL LYS ALA VAL ALA TRP CYS PRO TRP GLN          
SEQRES  24 A  431  SER ASN VAL LEU ALA THR GLY GLY GLY THR SER ASP ARG          
SEQRES  25 A  431  HIS ILE ARG ILE TRP ASN VAL CYS SER GLY ALA CYS LEU          
SEQRES  26 A  431  SER ALA VAL ASP ALA HIS SER GLN VAL CYS SER ILE LEU          
SEQRES  27 A  431  TRP SER PRO HIS TYR LYS GLU LEU ILE SER GLY HIS GLY          
SEQRES  28 A  431  PHE ALA GLN ASN GLN LEU VAL ILE TRP LYS TYR PRO THR          
SEQRES  29 A  431  MET ALA LYS VAL ALA GLU LEU LYS GLY HIS THR SER ARG          
SEQRES  30 A  431  VAL LEU SER LEU THR MET SER PRO ASP GLY ALA THR VAL          
SEQRES  31 A  431  ALA SER ALA ALA ALA ASP GLU THR LEU ARG LEU TRP ARG          
SEQRES  32 A  431  CYS PHE GLU LEU ASP PRO ALA ARG ARG ARG GLU ARG GLU          
SEQRES  33 A  431  LYS ALA SER ALA ALA LYS SER SER LEU ILE HIS GLN GLY          
SEQRES  34 A  431  ILE ARG                                                      
SEQRES   1 B  431  GLY ALA PRO SER LYS PRO GLY GLY ASP ARG TYR ILE PRO          
SEQRES   2 B  431  HIS ARG SER ALA ALA GLN MET GLU VAL ALA SER PHE LEU          
SEQRES   3 B  431  LEU SER LYS GLU ASN GLN PRO GLU ASN SER GLN THR PRO          
SEQRES   4 B  431  THR LYS LYS GLU HIS GLN LYS ALA TRP ALA LEU ASN LEU          
SEQRES   5 B  431  ASN GLY PHE ASP VAL GLU GLU ALA LYS ILE LEU ARG LEU          
SEQRES   6 B  431  SER GLY LYS PRO GLN ASN ALA PRO GLU GLY TYR GLN ASN          
SEQRES   7 B  431  ARG LEU LYS VAL LEU TYR SER GLN LYS ALA THR PRO GLY          
SEQRES   8 B  431  SER SER ARG LYS THR CYS ARG TYR ILE PRO SER LEU PRO          
SEQRES   9 B  431  ASP ARG ILE LEU ASP ALA PRO GLU ILE ARG ASN ASP TYR          
SEQRES  10 B  431  TYR LEU ASN LEU VAL ASP TRP SER SER GLY ASN VAL LEU          
SEQRES  11 B  431  ALA VAL ALA LEU ASP ASN SER VAL TYR LEU TRP SER ALA          
SEQRES  12 B  431  SER SER GLY ASP ILE LEU GLN LEU LEU GLN MET GLU GLN          
SEQRES  13 B  431  PRO GLY GLU TYR ILE SER SER VAL ALA TRP ILE LYS GLU          
SEQRES  14 B  431  GLY ASN TYR LEU ALA VAL GLY THR SER SER ALA GLU VAL          
SEQRES  15 B  431  GLN LEU TRP ASP VAL GLN GLN GLN LYS ARG LEU ARG ASN          
SEQRES  16 B  431  MET THR SER HIS SER ALA ARG VAL GLY SER LEU SER TRP          
SEQRES  17 B  431  ASN SER TYR ILE LEU SER SER GLY SER ARG SER GLY HIS          
SEQRES  18 B  431  ILE HIS HIS HIS ASP VAL ARG VAL ALA GLU HIS HIS VAL          
SEQRES  19 B  431  ALA THR LEU SER GLY HIS SER GLN GLU VAL CYS GLY LEU          
SEQRES  20 B  431  ARG TRP ALA PRO ASP GLY ARG HIS LEU ALA SER GLY GLY          
SEQRES  21 B  431  ASN ASP ASN LEU VAL ASN VAL TRP PRO SER ALA PRO GLY          
SEQRES  22 B  431  GLU GLY GLY TRP VAL PRO LEU GLN THR PHE THR GLN HIS          
SEQRES  23 B  431  GLN GLY ALA VAL LYS ALA VAL ALA TRP CYS PRO TRP GLN          
SEQRES  24 B  431  SER ASN VAL LEU ALA THR GLY GLY GLY THR SER ASP ARG          
SEQRES  25 B  431  HIS ILE ARG ILE TRP ASN VAL CYS SER GLY ALA CYS LEU          
SEQRES  26 B  431  SER ALA VAL ASP ALA HIS SER GLN VAL CYS SER ILE LEU          
SEQRES  27 B  431  TRP SER PRO HIS TYR LYS GLU LEU ILE SER GLY HIS GLY          
SEQRES  28 B  431  PHE ALA GLN ASN GLN LEU VAL ILE TRP LYS TYR PRO THR          
SEQRES  29 B  431  MET ALA LYS VAL ALA GLU LEU LYS GLY HIS THR SER ARG          
SEQRES  30 B  431  VAL LEU SER LEU THR MET SER PRO ASP GLY ALA THR VAL          
SEQRES  31 B  431  ALA SER ALA ALA ALA ASP GLU THR LEU ARG LEU TRP ARG          
SEQRES  32 B  431  CYS PHE GLU LEU ASP PRO ALA ARG ARG ARG GLU ARG GLU          
SEQRES  33 B  431  LYS ALA SER ALA ALA LYS SER SER LEU ILE HIS GLN GLY          
SEQRES  34 B  431  ILE ARG                                                      
SEQRES   1 C   23  ASP GLU TRP GLU LEU SER LYS GLU ASN VAL GLN PRO LEU          
SEQRES   2 C   23  ARG GLN GLY ARG ILE MET SER THR LEU GLN                      
SEQRES   1 D   23  ASP GLU TRP GLU LEU SER LYS GLU ASN VAL GLN PRO LEU          
SEQRES   2 D   23  ARG GLN GLY ARG ILE MET SER THR LEU GLN                      
FORMUL   5  HOH   *185(H2 O)                                                    
HELIX    1   1 PRO B  409  TYR B  411  5                                   3    
HELIX    2   2 SER D    6  VAL D   10  5                                   5    
SHEET    1   A 4 ARG A 174  ASP A 177  0                                        
SHEET    2   A 4 THR A 466  ARG A 471 -1  O  LEU A 467   N  LEU A 176           
SHEET    3   A 4 THR A 457  ALA A 462 -1  N  SER A 460   O  ARG A 468           
SHEET    4   A 4 VAL A 446  MET A 451 -1  N  LEU A 447   O  ALA A 461           
SHEET    1   B 4 VAL A 190  TRP A 192  0                                        
SHEET    2   B 4 VAL A 197  LEU A 202 -1  O  ALA A 199   N  ASP A 191           
SHEET    3   B 4 SER A 205  SER A 210 -1  O  TYR A 207   N  VAL A 200           
SHEET    4   B 4 ILE A 216  GLN A 221 -1  O  LEU A 217   N  LEU A 208           
SHEET    1   C 4 ILE A 229  TRP A 234  0                                        
SHEET    2   C 4 TYR A 240  THR A 245 -1  O  ALA A 242   N  ALA A 233           
SHEET    3   C 4 GLU A 249  ASP A 254 -1  O  GLN A 251   N  VAL A 243           
SHEET    4   C 4 LYS A 259  THR A 265 -1  O  MET A 264   N  VAL A 250           
SHEET    1   D 4 VAL A 271  ASN A 277  0                                        
SHEET    2   D 4 ILE A 280  SER A 285 -1  O  SER A 282   N  SER A 275           
SHEET    3   D 4 ILE A 290  ASP A 294 -1  O  HIS A 293   N  LEU A 281           
SHEET    4   D 4 HIS A 301  LEU A 305 -1  O  LEU A 305   N  ILE A 290           
SHEET    1   E 4 VAL A 312  TRP A 317  0                                        
SHEET    2   E 4 HIS A 323  GLY A 328 -1  O  ALA A 325   N  ARG A 316           
SHEET    3   E 4 VAL A 333  PRO A 337 -1  O  TRP A 336   N  LEU A 324           
SHEET    4   E 4 GLN A 349  PHE A 351 -1  O  PHE A 351   N  VAL A 333           
SHEET    1   F 4 VAL A 358  TRP A 363  0                                        
SHEET    2   F 4 VAL A 370  GLY A 375 -1  O  ALA A 372   N  ALA A 362           
SHEET    3   F 4 HIS A 381  ASN A 386 -1  O  TRP A 385   N  LEU A 371           
SHEET    4   F 4 CYS A 392  ASP A 397 -1  O  VAL A 396   N  ILE A 382           
SHEET    1   G 4 VAL A 402  SER A 408  0                                        
SHEET    2   G 4 GLU A 413  HIS A 418 -1  O  ILE A 415   N  LEU A 406           
SHEET    3   G 4 LEU A 425  LYS A 429 -1  O  TRP A 428   N  LEU A 414           
SHEET    4   G 4 ALA A 434  LEU A 439 -1  O  VAL A 436   N  ILE A 427           
SHEET    1   H 4 ARG B 174  ASP B 177  0                                        
SHEET    2   H 4 THR B 466  ARG B 471 -1  O  LEU B 467   N  LEU B 176           
SHEET    3   H 4 THR B 457  ALA B 462 -1  N  SER B 460   O  ARG B 468           
SHEET    4   H 4 VAL B 446  MET B 451 -1  N  THR B 450   O  ALA B 459           
SHEET    1   I 4 VAL B 190  TRP B 192  0                                        
SHEET    2   I 4 VAL B 197  LEU B 202 -1  O  ALA B 199   N  ASP B 191           
SHEET    3   I 4 SER B 205  SER B 210 -1  O  TYR B 207   N  VAL B 200           
SHEET    4   I 4 ILE B 216  GLN B 221 -1  O  LEU B 217   N  LEU B 208           
SHEET    1   J 4 ILE B 229  TRP B 234  0                                        
SHEET    2   J 4 TYR B 240  THR B 245 -1  O  GLY B 244   N  SER B 230           
SHEET    3   J 4 GLU B 249  ASP B 254 -1  O  TRP B 253   N  LEU B 241           
SHEET    4   J 4 LYS B 259  THR B 265 -1  O  LEU B 261   N  LEU B 252           
SHEET    1   K 4 SER B 273  ASN B 277  0                                        
SHEET    2   K 4 ILE B 280  GLY B 284 -1  O  SER B 282   N  SER B 275           
SHEET    3   K 4 ILE B 290  ASP B 294 -1  O  HIS B 293   N  LEU B 281           
SHEET    4   K 4 HIS B 301  LEU B 305 -1  O  LEU B 305   N  ILE B 290           
SHEET    1   L 4 VAL B 312  TRP B 317  0                                        
SHEET    2   L 4 HIS B 323  GLY B 328 -1  O  ALA B 325   N  ARG B 316           
SHEET    3   L 4 VAL B 333  PRO B 337 -1  O  TRP B 336   N  LEU B 324           
SHEET    4   L 4 GLN B 349  PHE B 351 -1  O  GLN B 349   N  VAL B 335           
SHEET    1   M 4 ALA B 360  TRP B 363  0                                        
SHEET    2   M 4 VAL B 370  GLY B 374 -1  O  ALA B 372   N  ALA B 362           
SHEET    3   M 4 HIS B 381  ASN B 386 -1  O  TRP B 385   N  LEU B 371           
SHEET    4   M 4 CYS B 392  ASP B 397 -1  O  VAL B 396   N  ILE B 382           
SHEET    1   N 4 VAL B 402  SER B 408  0                                        
SHEET    2   N 4 GLU B 413  HIS B 418 -1  O  GLU B 413   N  SER B 408           
SHEET    3   N 4 LEU B 425  LYS B 429 -1  O  TRP B 428   N  LEU B 414           
SHEET    4   N 4 ALA B 434  LEU B 439 -1  O  LEU B 439   N  LEU B 425           
CISPEP   1 PHE A  420    ALA A  421          0        14.69                     
CISPEP   2 TYR A  430    PRO A  431          0        10.52                     
CISPEP   3 PHE B  420    ALA B  421          0         5.63                     
CISPEP   4 TYR B  430    PRO B  431          0        10.19                     
CRYST1   49.826   88.129  118.351  90.00  99.66  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020070  0.000000  0.003418        0.00000                         
SCALE2      0.000000  0.011347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008571        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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