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Database: PDB
Entry: 4GGA
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Original site: 4GGA 
HEADER    CELL CYCLE                              06-AUG-12   4GGA              
TITLE     STRUCTURAL ANALYSIS OF HUMAN CDC20 SUPPORTS MULTI-SITE DEGRON         
TITLE    2 RECOGNITION BY APC/C                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CYCLE PROTEIN 20 HOMOLOG;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: P55CDC;                                                     
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: 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                                  
KEYWDS    CELL CYCLE, MITOSIS, SECURIN, UBIQUITINATION, WD40                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LUO,W.TIAN,D.R.TOMCHICK                                             
REVDAT   4   21-FEB-18 4GGA    1       REMARK                                   
REVDAT   3   15-NOV-17 4GGA    1       REMARK                                   
REVDAT   2   26-DEC-12 4GGA    1       JRNL                                     
REVDAT   1   07-NOV-12 4GGA    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.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1239                            
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 38.3536 -  4.2509    0.99     2877   154  0.1405 0.1594        
REMARK   3     2  4.2509 -  3.3747    0.99     2743   144  0.1216 0.1699        
REMARK   3     3  3.3747 -  2.9483    0.99     2707   143  0.1467 0.2091        
REMARK   3     4  2.9483 -  2.6788    0.99     2687   143  0.1588 0.2033        
REMARK   3     5  2.6788 -  2.4868    0.99     2672   141  0.1626 0.2487        
REMARK   3     6  2.4868 -  2.3402    0.97     2620   134  0.1763 0.2352        
REMARK   3     7  2.3402 -  2.2231    0.94     2515   128  0.1771 0.2733        
REMARK   3     8  2.2231 -  2.1263    0.89     2383   129  0.1760 0.2389        
REMARK   3     9  2.1263 -  2.0444    0.84     2231   123  0.1792 0.2320        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.35                          
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      :  0.011           2509                                  
REMARK   3   ANGLE     :  1.327           3429                                  
REMARK   3   CHIRALITY :  0.080            373                                  
REMARK   3   PLANARITY :  0.006            441                                  
REMARK   3   DIHEDRAL  : 13.338            872                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4070 -15.5020  29.8225              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0853                                     
REMARK   3      T33:   0.0338 T12:   0.0238                                     
REMARK   3      T13:  -0.0032 T23:  -0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2550 L22:   0.4871                                     
REMARK   3      L33:   0.2412 L12:   0.1249                                     
REMARK   3      L13:   0.0227 L23:   0.2547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0452 S12:  -0.1441 S13:   0.0083                       
REMARK   3      S21:   0.1752 S22:   0.0527 S23:  -0.0475                       
REMARK   3      S31:   0.0162 S32:   0.0148 S33:  -0.0006                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 359 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.9054 -27.1325  14.1041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0842 T22:   0.0719                                     
REMARK   3      T33:   0.0754 T12:  -0.0172                                     
REMARK   3      T13:   0.0051 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1754 L22:   0.1358                                     
REMARK   3      L33:   0.1828 L12:  -0.1508                                     
REMARK   3      L13:  -0.0755 L23:   0.0137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0369 S12:  -0.0221 S13:  -0.0437                       
REMARK   3      S21:  -0.0263 S22:   0.0108 S23:  -0.0731                       
REMARK   3      S31:   0.0634 S32:   0.0225 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 360 THROUGH 478 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.8168  -9.4664  11.3438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0447 T22:   0.0446                                     
REMARK   3      T33:   0.0585 T12:  -0.0025                                     
REMARK   3      T13:   0.0006 T23:  -0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2609 L22:   0.3610                                     
REMARK   3      L33:   0.1201 L12:  -0.1248                                     
REMARK   3      L13:   0.0976 L23:  -0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0220 S12:  -0.0155 S13:   0.0515                       
REMARK   3      S21:  -0.0325 S22:  -0.0011 S23:   0.0243                       
REMARK   3      S31:  -0.0370 S32:  -0.0418 S33:  -0.0007                       
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 4GGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074145.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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   : 24684                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.044                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.589                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.22200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900                            
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   (%): 42.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA CITRATE, 15 % (W/V) PEG        
REMARK 280  6000, AND 4% MPD, PH 5.6, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.43250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.47700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.62900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.47700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.43250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.62900            
REMARK 290   SMTRY3   4  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 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     GLY 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     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 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    GLU A 180       11.90     81.91                                   
REMARK 500    ASN A 196       38.56     74.52                                   
REMARK 500    ASP A 203     -110.20     53.07                                   
REMARK 500    SER A 278     -123.40     54.11                                   
REMARK 500    LYS A 412       73.43     57.27                                   
REMARK 500    ASP A 476       70.87     51.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GGC   RELATED DB: PDB                                   
DBREF  4GGA A   81   499  UNP    Q12834   CDC20_HUMAN     81    499             
SEQADV 4GGA GLY A   80  UNP  Q12834              EXPRESSION TAG                 
SEQRES   1 A  420  GLY PRO HIS ARG SER ALA ALA GLN MET GLU VAL ALA SER          
SEQRES   2 A  420  PHE LEU LEU SER LYS GLU ASN GLN PRO GLU ASN SER GLN          
SEQRES   3 A  420  THR PRO THR LYS LYS GLU HIS GLN LYS ALA TRP ALA LEU          
SEQRES   4 A  420  ASN LEU ASN GLY PHE ASP VAL GLU GLU ALA LYS ILE LEU          
SEQRES   5 A  420  ARG LEU SER GLY LYS PRO GLN ASN ALA PRO GLU GLY TYR          
SEQRES   6 A  420  GLN ASN ARG LEU LYS VAL LEU TYR SER GLN LYS ALA THR          
SEQRES   7 A  420  PRO GLY SER SER ARG LYS THR CYS ARG TYR ILE PRO SER          
SEQRES   8 A  420  LEU PRO ASP ARG ILE LEU ASP ALA PRO GLU ILE ARG ASN          
SEQRES   9 A  420  ASP TYR TYR LEU ASN LEU VAL ASP TRP SER SER GLY ASN          
SEQRES  10 A  420  VAL LEU ALA VAL ALA LEU ASP ASN SER VAL TYR LEU TRP          
SEQRES  11 A  420  SER ALA SER SER GLY ASP ILE LEU GLN LEU LEU GLN MET          
SEQRES  12 A  420  GLU GLN PRO GLY GLU TYR ILE SER SER VAL ALA TRP ILE          
SEQRES  13 A  420  LYS GLU GLY ASN TYR LEU ALA VAL GLY THR SER SER ALA          
SEQRES  14 A  420  GLU VAL GLN LEU TRP ASP VAL GLN GLN GLN LYS ARG LEU          
SEQRES  15 A  420  ARG ASN MET THR SER HIS SER ALA ARG VAL GLY SER LEU          
SEQRES  16 A  420  SER TRP ASN SER TYR ILE LEU SER SER GLY SER ARG SER          
SEQRES  17 A  420  GLY HIS ILE HIS HIS HIS ASP VAL ARG VAL ALA GLU HIS          
SEQRES  18 A  420  HIS VAL ALA THR LEU SER GLY HIS SER GLN GLU VAL CYS          
SEQRES  19 A  420  GLY LEU ARG TRP ALA PRO ASP GLY ARG HIS LEU ALA SER          
SEQRES  20 A  420  GLY GLY ASN ASP ASN LEU VAL ASN VAL TRP PRO SER ALA          
SEQRES  21 A  420  PRO GLY GLU GLY GLY TRP VAL PRO LEU GLN THR PHE THR          
SEQRES  22 A  420  GLN HIS GLN GLY ALA VAL LYS ALA VAL ALA TRP CYS PRO          
SEQRES  23 A  420  TRP GLN SER ASN VAL LEU ALA THR GLY GLY GLY THR SER          
SEQRES  24 A  420  ASP ARG HIS ILE ARG ILE TRP ASN VAL CYS SER GLY ALA          
SEQRES  25 A  420  CYS LEU SER ALA VAL ASP ALA HIS SER GLN VAL CYS SER          
SEQRES  26 A  420  ILE LEU TRP SER PRO HIS TYR LYS GLU LEU ILE SER GLY          
SEQRES  27 A  420  HIS GLY PHE ALA GLN ASN GLN LEU VAL ILE TRP LYS TYR          
SEQRES  28 A  420  PRO THR MET ALA LYS VAL ALA GLU LEU LYS GLY HIS THR          
SEQRES  29 A  420  SER ARG VAL LEU SER LEU THR MET SER PRO ASP GLY ALA          
SEQRES  30 A  420  THR VAL ALA SER ALA ALA ALA ASP GLU THR LEU ARG LEU          
SEQRES  31 A  420  TRP ARG CYS PHE GLU LEU ASP PRO ALA ARG ARG ARG GLU          
SEQRES  32 A  420  ARG GLU LYS ALA SER ALA ALA LYS SER SER LEU ILE HIS          
SEQRES  33 A  420  GLN GLY ILE ARG                                              
FORMUL   2  HOH   *247(H2 O)                                                    
SHEET    1   A 4 ARG A 174  ASP A 177  0                                        
SHEET    2   A 4 THR A 466  TRP A 470 -1  O  LEU A 469   N  ARG A 174           
SHEET    3   A 4 VAL A 458  ALA A 462 -1  N  VAL A 458   O  TRP A 470           
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  TRP A 209   N  LEU A 198           
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 VAL A 250  ASP A 254 -1  O  GLN A 251   N  VAL A 243           
SHEET    4   C 4 LYS A 259  MET A 264 -1  O  LYS A 259   N  ASP A 254           
SHEET    1   D 4 VAL A 271  ASN A 277  0                                        
SHEET    2   D 4 ILE A 280  SER A 285 -1  O  ILE A 280   N  ASN A 277           
SHEET    3   D 4 HIS A 289  ASP A 294 -1  O  HIS A 291   N  SER A 283           
SHEET    4   D 4 HIS A 301  SER A 306 -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  GLN A 349   N  VAL A 335           
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 ALA A 391  ASP A 397 -1  O  LEU A 393   N  ILE A 384           
SHEET    1   G 4 VAL A 402  SER A 408  0                                        
SHEET    2   G 4 GLU A 413  HIS A 418 -1  O  GLU A 413   N  SER A 408           
SHEET    3   G 4 LEU A 425  LYS A 429 -1  O  TRP A 428   N  LEU A 414           
SHEET    4   G 4 LYS A 435  LEU A 439 -1  O  VAL A 436   N  ILE A 427           
CISPEP   1 PHE A  420    ALA A  421          0         8.35                     
CISPEP   2 TYR A  430    PRO A  431          0         4.84                     
CRYST1   40.865   87.258  110.954  90.00  90.00  90.00 P 21 21 21    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      0.024471  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009013        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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