GenomeNet

Database: PDB
Entry: 4RG6
LinkDB: 4RG6
Original site: 4RG6 
HEADER    PROTEIN BINDING                         29-SEP-14   4RG6              
TITLE     CRYSTAL STRUCTURE OF APC3-APC16 COMPLEX                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CYCLE PROTEIN 27 HOMOLOG;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-180, 447-824;                               
COMPND   5 SYNONYM: ANAPHASE-PROMOTING COMPLEX SUBUNIT 3, APC3, CDC27 HOMOLOG,  
COMPND   6 CDC27HS, H-NUC;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ANAPHASE-PROMOTING COMPLEX SUBUNIT 16;                     
COMPND  10 CHAIN: S;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 74-109;                                       
COMPND  12 SYNONYM: APC16, CYCLOSOME SUBUNIT 16;                                
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: CDC27, ANAPC3, D0S1430E, D17S978E;                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ANAPC16, C10ORF104;                                            
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ASYMMETRIC COMPLEX, TPR FPLDING, PROTEIN ASSEMBLY, PROTEIN BINDING    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.YAMAGUCHI,S.YU,D.J.MILLER,B.A.SCHULMAN                              
REVDAT   4   02-AUG-17 4RG6    1       SOURCE REMARK                            
REVDAT   3   15-APR-15 4RG6    1       JRNL                                     
REVDAT   2   14-JAN-15 4RG6    1       JRNL                                     
REVDAT   1   24-DEC-14 4RG6    0                                                
JRNL        AUTH   M.YAMAGUCHI,S.YU,R.QIAO,F.WEISSMANN,D.J.MILLER,              
JRNL        AUTH 2 R.VANDERLINDEN,N.G.BROWN,J.J.FRYE,J.M.PETERS,B.A.SCHULMAN    
JRNL        TITL   STRUCTURE OF AN APC3-APC16 COMPLEX: INSIGHTS INTO ASSEMBLY   
JRNL        TITL 2 OF THE ANAPHASE-PROMOTING COMPLEX/CYCLOSOME.                 
JRNL        REF    J.MOL.BIOL.                   V. 427  1748 2015              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   25490258                                                     
JRNL        DOI    10.1016/J.JMB.2014.11.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35265                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1867                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2544                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7598                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 102.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.82000                                              
REMARK   3    B22 (A**2) : 3.82000                                              
REMARK   3    B33 (A**2) : -7.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.853         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.378         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.312         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.124        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7775 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7061 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10550 ; 1.039 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16170 ; 0.789 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   975 ; 5.748 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   354 ;35.982 ;24.153       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1222 ;17.938 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;17.098 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1160 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8929 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1865 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3921 ; 4.246 ;10.695       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3920 ; 4.243 ;10.694       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4889 ; 6.864 ;16.027       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4890 ; 6.864 ;16.028       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3854 ; 3.954 ;10.664       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3855 ; 3.953 ;10.665       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5661 ; 6.533 ;15.938       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  9216 ; 9.951 ;85.351       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9217 ; 9.950 ;85.358       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4RG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000087305.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07160                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37171                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.82900                            
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   (%): 74.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.0, 0.2M MAGNESIUM         
REMARK 280  CHLORIDE, 8% PEG6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.48600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      138.72900            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.24300            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, S                               
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    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A   172                                                      
REMARK 465     LEU A   173                                                      
REMARK 465     GLN A   174                                                      
REMARK 465     ASN A   175                                                      
REMARK 465     PHE A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     CYS A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     GLN A   454                                                      
REMARK 465     ILE A   455                                                      
REMARK 465     GLN A   456                                                      
REMARK 465     ALA A   457                                                      
REMARK 465     PHE A   458                                                      
REMARK 465     ASN A   459                                                      
REMARK 465     LYS A   689                                                      
REMARK 465     LYS A   690                                                      
REMARK 465     SER A   691                                                      
REMARK 465     GLU A   692                                                      
REMARK 465     LYS A   693                                                      
REMARK 465     ALA A   694                                                      
REMARK 465     LEU A   695                                                      
REMARK 465     ASP A   696                                                      
REMARK 465     LYS A   775                                                      
REMARK 465     GLY A   776                                                      
REMARK 465     ALA A   777                                                      
REMARK 465     ASN A   778                                                      
REMARK 465     ASN A   779                                                      
REMARK 465     GLN A   780                                                      
REMARK 465     ILE A   781                                                      
REMARK 465     LYS A   782                                                      
REMARK 465     GLU A   783                                                      
REMARK 465     ALA A   784                                                      
REMARK 465     ILE A   785                                                      
REMARK 465     ASP A   786                                                      
REMARK 465     LYS A   787                                                      
REMARK 465     ARG A   788                                                      
REMARK 465     TYR A   789                                                      
REMARK 465     LEU A   790                                                      
REMARK 465     PRO A   791                                                      
REMARK 465     ASP A   792                                                      
REMARK 465     ASP A   793                                                      
REMARK 465     GLU A   794                                                      
REMARK 465     GLU A   795                                                      
REMARK 465     PRO A   796                                                      
REMARK 465     ILE A   797                                                      
REMARK 465     THR A   798                                                      
REMARK 465     GLN A   799                                                      
REMARK 465     GLU A   800                                                      
REMARK 465     GLU A   801                                                      
REMARK 465     GLN A   802                                                      
REMARK 465     ILE A   803                                                      
REMARK 465     MET A   804                                                      
REMARK 465     GLY A   805                                                      
REMARK 465     THR A   806                                                      
REMARK 465     ASP A   807                                                      
REMARK 465     GLU A   808                                                      
REMARK 465     SER A   809                                                      
REMARK 465     GLN A   810                                                      
REMARK 465     GLU A   811                                                      
REMARK 465     SER A   812                                                      
REMARK 465     SER A   813                                                      
REMARK 465     MET A   814                                                      
REMARK 465     THR A   815                                                      
REMARK 465     ASP A   816                                                      
REMARK 465     ALA A   817                                                      
REMARK 465     ASP A   818                                                      
REMARK 465     ASP A   819                                                      
REMARK 465     THR A   820                                                      
REMARK 465     GLN A   821                                                      
REMARK 465     LEU A   822                                                      
REMARK 465     HIS A   823                                                      
REMARK 465     ALA A   824                                                      
REMARK 465     ALA A   825                                                      
REMARK 465     GLU A   826                                                      
REMARK 465     SER A   827                                                      
REMARK 465     ASP A   828                                                      
REMARK 465     GLU A   829                                                      
REMARK 465     PHE A   830                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     SER B   172                                                      
REMARK 465     LEU B   173                                                      
REMARK 465     GLN B   174                                                      
REMARK 465     ASN B   175                                                      
REMARK 465     PHE B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     ASN B   178                                                      
REMARK 465     CYS B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     PRO B   453                                                      
REMARK 465     GLN B   454                                                      
REMARK 465     ILE B   455                                                      
REMARK 465     GLN B   456                                                      
REMARK 465     ALA B   457                                                      
REMARK 465     PHE B   458                                                      
REMARK 465     ASN B   459                                                      
REMARK 465     LEU B   460                                                      
REMARK 465     LYS B   689                                                      
REMARK 465     LYS B   690                                                      
REMARK 465     SER B   691                                                      
REMARK 465     GLU B   692                                                      
REMARK 465     LYS B   693                                                      
REMARK 465     ALA B   694                                                      
REMARK 465     LEU B   695                                                      
REMARK 465     ASP B   696                                                      
REMARK 465     LYS B   775                                                      
REMARK 465     GLY B   776                                                      
REMARK 465     ALA B   777                                                      
REMARK 465     ASN B   778                                                      
REMARK 465     ASN B   779                                                      
REMARK 465     GLN B   780                                                      
REMARK 465     ILE B   781                                                      
REMARK 465     LYS B   782                                                      
REMARK 465     GLU B   783                                                      
REMARK 465     ALA B   784                                                      
REMARK 465     ILE B   785                                                      
REMARK 465     ASP B   786                                                      
REMARK 465     LYS B   787                                                      
REMARK 465     ARG B   788                                                      
REMARK 465     TYR B   789                                                      
REMARK 465     LEU B   790                                                      
REMARK 465     PRO B   791                                                      
REMARK 465     ASP B   792                                                      
REMARK 465     ASP B   793                                                      
REMARK 465     GLU B   794                                                      
REMARK 465     GLU B   795                                                      
REMARK 465     PRO B   796                                                      
REMARK 465     ILE B   797                                                      
REMARK 465     THR B   798                                                      
REMARK 465     GLN B   799                                                      
REMARK 465     GLU B   800                                                      
REMARK 465     GLU B   801                                                      
REMARK 465     GLN B   802                                                      
REMARK 465     ILE B   803                                                      
REMARK 465     MET B   804                                                      
REMARK 465     GLY B   805                                                      
REMARK 465     THR B   806                                                      
REMARK 465     ASP B   807                                                      
REMARK 465     GLU B   808                                                      
REMARK 465     SER B   809                                                      
REMARK 465     GLN B   810                                                      
REMARK 465     GLU B   811                                                      
REMARK 465     SER B   812                                                      
REMARK 465     SER B   813                                                      
REMARK 465     MET B   814                                                      
REMARK 465     THR B   815                                                      
REMARK 465     ASP B   816                                                      
REMARK 465     ALA B   817                                                      
REMARK 465     ASP B   818                                                      
REMARK 465     ASP B   819                                                      
REMARK 465     THR B   820                                                      
REMARK 465     GLN B   821                                                      
REMARK 465     LEU B   822                                                      
REMARK 465     HIS B   823                                                      
REMARK 465     ALA B   824                                                      
REMARK 465     ALA B   825                                                      
REMARK 465     GLU B   826                                                      
REMARK 465     SER B   827                                                      
REMARK 465     ASP B   828                                                      
REMARK 465     GLU B   829                                                      
REMARK 465     PHE B   830                                                      
REMARK 465     SER S   108                                                      
REMARK 465     SER S   109                                                      
REMARK 465     GLU S   110                                                      
REMARK 465     ASN S   111                                                      
REMARK 465     LEU S   112                                                      
REMARK 465     TYR S   113                                                      
REMARK 465     PHE S   114                                                      
REMARK 465     GLN S   115                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   5    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  99    CG   CD   CE   NZ                                   
REMARK 470     LYS A 127    CG   CD   CE   NZ                                   
REMARK 470     LEU A 131    CG   CD1  CD2                                       
REMARK 470     LYS A 161    CG   CD   CE   NZ                                   
REMARK 470     ASP A 163    CG   OD1  OD2                                       
REMARK 470     LYS A 169    CG   CD   CE   NZ                                   
REMARK 470     PHE A 170    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 171    OG1  CG2                                            
REMARK 470     LEU A 460    CG   CD1  CD2                                       
REMARK 470     GLN A 461    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 462    CG   CD   CE   NZ                                   
REMARK 470     GLU A 466    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 468    CG   CD1  CD2                                       
REMARK 470     LEU A 471    CG   CD1  CD2                                       
REMARK 470     GLU A 474    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 477    CE   NZ                                             
REMARK 470     LYS A 488    CG   CD   CE   NZ                                   
REMARK 470     ASN A 492    CG   OD1  ND2                                       
REMARK 470     HIS A 496    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 497    CG   CD1  CD2                                       
REMARK 470     ARG A 513    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 520    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 587    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 621    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 623    CG   CD1  CD2                                       
REMARK 470     LEU A 627    CG   CD1  CD2                                       
REMARK 470     LYS A 656    CG   CD   CE   NZ                                   
REMARK 470     MET A 662    CG   SD   CE                                        
REMARK 470     LYS A 666    CG   CD   CE   NZ                                   
REMARK 470     HIS A 686    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 688    CG   CD1  CD2                                       
REMARK 470     THR A 697    OG1  CG2                                            
REMARK 470     LEU A 698    CG   CD1  CD2                                       
REMARK 470     ASN A 699    CG   OD1  ND2                                       
REMARK 470     LYS A 700    CG   CD   CE   NZ                                   
REMARK 470     ILE A 702    CG1  CG2  CD1                                       
REMARK 470     VAL A 703    CG1  CG2                                            
REMARK 470     ILE A 704    CG1  CG2  CD1                                       
REMARK 470     ASP A 705    CG   OD1  OD2                                       
REMARK 470     PRO A 706    CG   CD                                             
REMARK 470     LYS A 712    CG   CD   CE   NZ                                   
REMARK 470     ARG A 715    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 724    CE   NZ                                             
REMARK 470     LYS A 726    CG   CD   CE   NZ                                   
REMARK 470     LEU A 735    CG   CD1  CD2                                       
REMARK 470     LYS A 741    CG   CD   CE   NZ                                   
REMARK 470     LEU A 744    CG   CD1  CD2                                       
REMARK 470     PHE A 747    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 754    CG   CD   CE   NZ                                   
REMARK 470     LYS A 755    CG   CD   CE   NZ                                   
REMARK 470     PRO A 774    CG   CD                                             
REMARK 470     GLN B   5    CG   CD   OE1  NE2                                  
REMARK 470     GLN B   9    CG   CD   OE1  NE2                                  
REMARK 470     VAL B  96    CG1  CG2                                            
REMARK 470     LYS B  99    CE   NZ                                             
REMARK 470     LYS B 161    CE   NZ                                             
REMARK 470     THR B 171    OG1  CG2                                            
REMARK 470     GLN B 461    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 462    CG   CD   CE   NZ                                   
REMARK 470     LEU B 468    CG   CD1  CD2                                       
REMARK 470     LYS B 477    CG   CD   CE   NZ                                   
REMARK 470     LYS B 488    CG   CD   CE   NZ                                   
REMARK 470     LYS B 563    CG   CD   CE   NZ                                   
REMARK 470     LYS B 594    CG   CD   CE   NZ                                   
REMARK 470     THR B 697    OG1  CG2                                            
REMARK 470     ASN B 699    CG   OD1  ND2                                       
REMARK 470     LYS B 700    CG   CD   CE   NZ                                   
REMARK 470     ILE B 702    CG1  CG2  CD1                                       
REMARK 470     VAL B 703    CG1  CG2                                            
REMARK 470     ILE B 704    CG1  CG2  CD1                                       
REMARK 470     ASP B 705    CG   OD1  OD2                                       
REMARK 470     PRO B 706    CG   CD                                             
REMARK 470     LYS B 707    CG   CD   CE   NZ                                   
REMARK 470     LYS B 712    CG   CD   CE   NZ                                   
REMARK 470     LYS B 726    CG   CD   CE   NZ                                   
REMARK 470     LYS B 741    CG   CD   CE   NZ                                   
REMARK 470     LEU B 744    CG   CD1  CD2                                       
REMARK 470     LYS B 754    CG   CD   CE   NZ                                   
REMARK 470     HIS B 760    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP B 768    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 768    CZ3  CH2                                            
REMARK 470     MET B 770    CG   SD   CE                                        
REMARK 470     PRO B 774    CG   CD                                             
REMARK 470     MET S  73    CG   SD   CE                                        
REMARK 470     GLU S  80    CG   CD   OE1  OE2                                  
REMARK 470     GLU S  87    CG   CD   OE1  OE2                                  
REMARK 470     PRO S 107    CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CA   LEU A   668     O    ASN A   671              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  36       32.18    -85.92                                   
REMARK 500    SER A  51        1.27    -68.20                                   
REMARK 500    LYS A  84       59.40    -91.76                                   
REMARK 500    PHE A 110       40.56    -94.87                                   
REMARK 500    LYS A 462       56.06   -141.64                                   
REMARK 500    ASN A 536       -4.37     83.40                                   
REMARK 500    GLN A 586       88.43    -69.90                                   
REMARK 500    ARG A 587       98.41    -62.35                                   
REMARK 500    ASP A 603       99.16   -162.28                                   
REMARK 500    GLU A 622       51.47   -103.19                                   
REMARK 500    HIS B  36       26.11    -78.84                                   
REMARK 500    LYS B  84       71.30   -109.85                                   
REMARK 500    PHE B  97      -63.90    -97.94                                   
REMARK 500    ASN B  98       -8.94   -147.44                                   
REMARK 500    ASN B 145       86.98   -167.00                                   
REMARK 500    PHE B 168       77.77   -107.64                                   
REMARK 500    LYS B 554       74.96   -111.94                                   
REMARK 500    GLU B 622       66.31   -107.60                                   
REMARK 500    ASN B 708       75.74   -102.79                                   
REMARK 500    GLN B 758       96.81    -65.10                                   
REMARK 500    ASP B 773       68.21   -110.12                                   
REMARK 500    PHE S 105      -70.61    -76.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RG9   RELATED DB: PDB                                   
DBREF  4RG6 A    1   180  UNP    P30260   CDC27_HUMAN      1    180             
DBREF  4RG6 A  453   830  UNP    P30260   CDC27_HUMAN    447    824             
DBREF  4RG6 B    1   180  UNP    P30260   CDC27_HUMAN      1    180             
DBREF  4RG6 B  453   830  UNP    P30260   CDC27_HUMAN    447    824             
DBREF  4RG6 S   74   109  UNP    Q96DE5   APC16_HUMAN     74    109             
SEQADV 4RG6 GLY A   -1  UNP  P30260              EXPRESSION TAG                 
SEQADV 4RG6 SER A    0  UNP  P30260              EXPRESSION TAG                 
SEQADV 4RG6 GLY B   -1  UNP  P30260              EXPRESSION TAG                 
SEQADV 4RG6 SER B    0  UNP  P30260              EXPRESSION TAG                 
SEQADV 4RG6 MET S   73  UNP  Q96DE5              INITIATING METHIONINE          
SEQADV 4RG6 GLU S  110  UNP  Q96DE5              EXPRESSION TAG                 
SEQADV 4RG6 ASN S  111  UNP  Q96DE5              EXPRESSION TAG                 
SEQADV 4RG6 LEU S  112  UNP  Q96DE5              EXPRESSION TAG                 
SEQADV 4RG6 TYR S  113  UNP  Q96DE5              EXPRESSION TAG                 
SEQADV 4RG6 PHE S  114  UNP  Q96DE5              EXPRESSION TAG                 
SEQADV 4RG6 GLN S  115  UNP  Q96DE5              EXPRESSION TAG                 
SEQRES   1 A  560  GLY SER MET THR VAL LEU GLN GLU PRO VAL GLN ALA ALA          
SEQRES   2 A  560  ILE TRP GLN ALA LEU ASN HIS TYR ALA TYR ARG ASP ALA          
SEQRES   3 A  560  VAL PHE LEU ALA GLU ARG LEU TYR ALA GLU VAL HIS SER          
SEQRES   4 A  560  GLU GLU ALA LEU PHE LEU LEU ALA THR CYS TYR TYR ARG          
SEQRES   5 A  560  SER GLY LYS ALA TYR LYS ALA TYR ARG LEU LEU LYS GLY          
SEQRES   6 A  560  HIS SER CYS THR THR PRO GLN CYS LYS TYR LEU LEU ALA          
SEQRES   7 A  560  LYS CYS CYS VAL ASP LEU SER LYS LEU ALA GLU GLY GLU          
SEQRES   8 A  560  GLN ILE LEU SER GLY GLY VAL PHE ASN LYS GLN LYS SER          
SEQRES   9 A  560  HIS ASP ASP ILE VAL THR GLU PHE GLY ASP SER ALA CYS          
SEQRES  10 A  560  PHE THR LEU SER LEU LEU GLY HIS VAL TYR CYS LYS THR          
SEQRES  11 A  560  ASP ARG LEU ALA LYS GLY SER GLU CYS TYR GLN LYS SER          
SEQRES  12 A  560  LEU SER LEU ASN PRO PHE LEU TRP SER PRO PHE GLU SER          
SEQRES  13 A  560  LEU CYS GLU ILE GLY GLU LYS PRO ASP PRO ASP GLN THR          
SEQRES  14 A  560  PHE LYS PHE THR SER LEU GLN ASN PHE SER ASN CYS LEU          
SEQRES  15 A  560  PRO GLN ILE GLN ALA PHE ASN LEU GLN LYS ALA ALA ALA          
SEQRES  16 A  560  GLU GLY LEU MET SER LEU LEU ARG GLU MET GLY LYS GLY          
SEQRES  17 A  560  TYR LEU ALA LEU CYS SER TYR ASN CYS LYS GLU ALA ILE          
SEQRES  18 A  560  ASN ILE LEU SER HIS LEU PRO SER HIS HIS TYR ASN THR          
SEQRES  19 A  560  GLY TRP VAL LEU CYS GLN ILE GLY ARG ALA TYR PHE GLU          
SEQRES  20 A  560  LEU SER GLU TYR MET GLN ALA GLU ARG ILE PHE SER GLU          
SEQRES  21 A  560  VAL ARG ARG ILE GLU ASN TYR ARG VAL GLU GLY MET GLU          
SEQRES  22 A  560  ILE TYR SER THR THR LEU TRP HIS LEU GLN LYS ASP VAL          
SEQRES  23 A  560  ALA LEU SER VAL LEU SER LYS ASP LEU THR ASP MET ASP          
SEQRES  24 A  560  LYS ASN SER PRO GLU ALA TRP CYS ALA ALA GLY ASN CYS          
SEQRES  25 A  560  PHE SER LEU GLN ARG GLU HIS ASP ILE ALA ILE LYS PHE          
SEQRES  26 A  560  PHE GLN ARG ALA ILE GLN VAL ASP PRO ASN TYR ALA TYR          
SEQRES  27 A  560  ALA TYR THR LEU LEU GLY HIS GLU PHE VAL LEU THR GLU          
SEQRES  28 A  560  GLU LEU ASP LYS ALA LEU ALA CYS PHE ARG ASN ALA ILE          
SEQRES  29 A  560  ARG VAL ASN PRO ARG HIS TYR ASN ALA TRP TYR GLY LEU          
SEQRES  30 A  560  GLY MET ILE TYR TYR LYS GLN GLU LYS PHE SER LEU ALA          
SEQRES  31 A  560  GLU MET HIS PHE GLN LYS ALA LEU ASP ILE ASN PRO GLN          
SEQRES  32 A  560  SER SER VAL LEU LEU CYS HIS ILE GLY VAL VAL GLN HIS          
SEQRES  33 A  560  ALA LEU LYS LYS SER GLU LYS ALA LEU ASP THR LEU ASN          
SEQRES  34 A  560  LYS ALA ILE VAL ILE ASP PRO LYS ASN PRO LEU CYS LYS          
SEQRES  35 A  560  PHE HIS ARG ALA SER VAL LEU PHE ALA ASN GLU LYS TYR          
SEQRES  36 A  560  LYS SER ALA LEU GLN GLU LEU GLU GLU LEU LYS GLN ILE          
SEQRES  37 A  560  VAL PRO LYS GLU SER LEU VAL TYR PHE LEU ILE GLY LYS          
SEQRES  38 A  560  VAL TYR LYS LYS LEU GLY GLN THR HIS LEU ALA LEU MET          
SEQRES  39 A  560  ASN PHE SER TRP ALA MET ASP LEU ASP PRO LYS GLY ALA          
SEQRES  40 A  560  ASN ASN GLN ILE LYS GLU ALA ILE ASP LYS ARG TYR LEU          
SEQRES  41 A  560  PRO ASP ASP GLU GLU PRO ILE THR GLN GLU GLU GLN ILE          
SEQRES  42 A  560  MET GLY THR ASP GLU SER GLN GLU SER SER MET THR ASP          
SEQRES  43 A  560  ALA ASP ASP THR GLN LEU HIS ALA ALA GLU SER ASP GLU          
SEQRES  44 A  560  PHE                                                          
SEQRES   1 B  560  GLY SER MET THR VAL LEU GLN GLU PRO VAL GLN ALA ALA          
SEQRES   2 B  560  ILE TRP GLN ALA LEU ASN HIS TYR ALA TYR ARG ASP ALA          
SEQRES   3 B  560  VAL PHE LEU ALA GLU ARG LEU TYR ALA GLU VAL HIS SER          
SEQRES   4 B  560  GLU GLU ALA LEU PHE LEU LEU ALA THR CYS TYR TYR ARG          
SEQRES   5 B  560  SER GLY LYS ALA TYR LYS ALA TYR ARG LEU LEU LYS GLY          
SEQRES   6 B  560  HIS SER CYS THR THR PRO GLN CYS LYS TYR LEU LEU ALA          
SEQRES   7 B  560  LYS CYS CYS VAL ASP LEU SER LYS LEU ALA GLU GLY GLU          
SEQRES   8 B  560  GLN ILE LEU SER GLY GLY VAL PHE ASN LYS GLN LYS SER          
SEQRES   9 B  560  HIS ASP ASP ILE VAL THR GLU PHE GLY ASP SER ALA CYS          
SEQRES  10 B  560  PHE THR LEU SER LEU LEU GLY HIS VAL TYR CYS LYS THR          
SEQRES  11 B  560  ASP ARG LEU ALA LYS GLY SER GLU CYS TYR GLN LYS SER          
SEQRES  12 B  560  LEU SER LEU ASN PRO PHE LEU TRP SER PRO PHE GLU SER          
SEQRES  13 B  560  LEU CYS GLU ILE GLY GLU LYS PRO ASP PRO ASP GLN THR          
SEQRES  14 B  560  PHE LYS PHE THR SER LEU GLN ASN PHE SER ASN CYS LEU          
SEQRES  15 B  560  PRO GLN ILE GLN ALA PHE ASN LEU GLN LYS ALA ALA ALA          
SEQRES  16 B  560  GLU GLY LEU MET SER LEU LEU ARG GLU MET GLY LYS GLY          
SEQRES  17 B  560  TYR LEU ALA LEU CYS SER TYR ASN CYS LYS GLU ALA ILE          
SEQRES  18 B  560  ASN ILE LEU SER HIS LEU PRO SER HIS HIS TYR ASN THR          
SEQRES  19 B  560  GLY TRP VAL LEU CYS GLN ILE GLY ARG ALA TYR PHE GLU          
SEQRES  20 B  560  LEU SER GLU TYR MET GLN ALA GLU ARG ILE PHE SER GLU          
SEQRES  21 B  560  VAL ARG ARG ILE GLU ASN TYR ARG VAL GLU GLY MET GLU          
SEQRES  22 B  560  ILE TYR SER THR THR LEU TRP HIS LEU GLN LYS ASP VAL          
SEQRES  23 B  560  ALA LEU SER VAL LEU SER LYS ASP LEU THR ASP MET ASP          
SEQRES  24 B  560  LYS ASN SER PRO GLU ALA TRP CYS ALA ALA GLY ASN CYS          
SEQRES  25 B  560  PHE SER LEU GLN ARG GLU HIS ASP ILE ALA ILE LYS PHE          
SEQRES  26 B  560  PHE GLN ARG ALA ILE GLN VAL ASP PRO ASN TYR ALA TYR          
SEQRES  27 B  560  ALA TYR THR LEU LEU GLY HIS GLU PHE VAL LEU THR GLU          
SEQRES  28 B  560  GLU LEU ASP LYS ALA LEU ALA CYS PHE ARG ASN ALA ILE          
SEQRES  29 B  560  ARG VAL ASN PRO ARG HIS TYR ASN ALA TRP TYR GLY LEU          
SEQRES  30 B  560  GLY MET ILE TYR TYR LYS GLN GLU LYS PHE SER LEU ALA          
SEQRES  31 B  560  GLU MET HIS PHE GLN LYS ALA LEU ASP ILE ASN PRO GLN          
SEQRES  32 B  560  SER SER VAL LEU LEU CYS HIS ILE GLY VAL VAL GLN HIS          
SEQRES  33 B  560  ALA LEU LYS LYS SER GLU LYS ALA LEU ASP THR LEU ASN          
SEQRES  34 B  560  LYS ALA ILE VAL ILE ASP PRO LYS ASN PRO LEU CYS LYS          
SEQRES  35 B  560  PHE HIS ARG ALA SER VAL LEU PHE ALA ASN GLU LYS TYR          
SEQRES  36 B  560  LYS SER ALA LEU GLN GLU LEU GLU GLU LEU LYS GLN ILE          
SEQRES  37 B  560  VAL PRO LYS GLU SER LEU VAL TYR PHE LEU ILE GLY LYS          
SEQRES  38 B  560  VAL TYR LYS LYS LEU GLY GLN THR HIS LEU ALA LEU MET          
SEQRES  39 B  560  ASN PHE SER TRP ALA MET ASP LEU ASP PRO LYS GLY ALA          
SEQRES  40 B  560  ASN ASN GLN ILE LYS GLU ALA ILE ASP LYS ARG TYR LEU          
SEQRES  41 B  560  PRO ASP ASP GLU GLU PRO ILE THR GLN GLU GLU GLN ILE          
SEQRES  42 B  560  MET GLY THR ASP GLU SER GLN GLU SER SER MET THR ASP          
SEQRES  43 B  560  ALA ASP ASP THR GLN LEU HIS ALA ALA GLU SER ASP GLU          
SEQRES  44 B  560  PHE                                                          
SEQRES   1 S   43  MET GLN GLN VAL ALA ARG MET GLU LYS LEU ALA GLY LEU          
SEQRES   2 S   43  VAL GLU GLU LEU GLU ALA ASP GLU TRP ARG PHE LYS PRO          
SEQRES   3 S   43  ILE GLU GLN LEU LEU GLY PHE THR PRO SER SER GLU ASN          
SEQRES   4 S   43  LEU TYR PHE GLN                                              
HELIX    1   1 PRO A    7  HIS A   18  1                                  12    
HELIX    2   2 ALA A   20  VAL A   35  1                                  16    
HELIX    3   3 SER A   37  SER A   51  1                                  15    
HELIX    4   4 LYS A   53  HIS A   64  1                                  12    
HELIX    5   5 THR A   68  LEU A   82  1                                  15    
HELIX    6   6 LYS A   84  GLY A   94  1                                  11    
HELIX    7   7 SER A  102  PHE A  110  1                                   9    
HELIX    8   8 SER A  113  THR A  128  1                                  16    
HELIX    9   9 ARG A  130  ASN A  145  1                                  16    
HELIX   10  10 LEU A  148  GLY A  159  1                                  12    
HELIX   11  11 ASP A  163  PHE A  168  1                                   6    
HELIX   12  12 LYS A  462  SER A  484  1                                  23    
HELIX   13  13 ASN A  486  HIS A  496  1                                  11    
HELIX   14  14 SER A  499  THR A  504  1                                   6    
HELIX   15  15 THR A  504  SER A  519  1                                  16    
HELIX   16  16 GLU A  520  GLU A  535  1                                  16    
HELIX   17  17 GLY A  541  LEU A  552  1                                  12    
HELIX   18  18 LYS A  554  ASP A  569  1                                  16    
HELIX   19  19 SER A  572  GLN A  586  1                                  15    
HELIX   20  20 GLU A  588  VAL A  602  1                                  15    
HELIX   21  21 TYR A  606  THR A  620  1                                  15    
HELIX   22  22 GLU A  622  ASN A  637  1                                  16    
HELIX   23  23 HIS A  640  GLN A  654  1                                  15    
HELIX   24  24 LYS A  656  ASN A  671  1                                  16    
HELIX   25  25 SER A  674  LEU A  688  1                                  15    
HELIX   26  26 LEU A  698  ASN A  708  1                                  11    
HELIX   27  27 ASN A  708  ASN A  722  1                                  15    
HELIX   28  28 LYS A  724  VAL A  739  1                                  16    
HELIX   29  29 GLU A  742  LYS A  755  1                                  14    
HELIX   30  30 GLN A  758  LEU A  772  1                                  15    
HELIX   31  31 GLU B    6  HIS B   18  1                                  13    
HELIX   32  32 ALA B   20  VAL B   35  1                                  16    
HELIX   33  33 SER B   37  SER B   51  1                                  15    
HELIX   34  34 LYS B   53  GLY B   63  1                                  11    
HELIX   35  35 THR B   68  LEU B   82  1                                  15    
HELIX   36  36 LYS B   84  GLY B   94  1                                  11    
HELIX   37  37 SER B  102  GLY B  111  1                                  10    
HELIX   38  38 SER B  113  THR B  128  1                                  16    
HELIX   39  39 ARG B  130  ASN B  145  1                                  16    
HELIX   40  40 TRP B  149  ILE B  158  1                                  10    
HELIX   41  41 ASP B  163  PHE B  168  1                                   6    
HELIX   42  42 LYS B  462  SER B  484  1                                  23    
HELIX   43  43 ASN B  486  SER B  495  1                                  10    
HELIX   44  44 PRO B  498  ASN B  503  1                                   6    
HELIX   45  45 THR B  504  LEU B  518  1                                  15    
HELIX   46  46 GLU B  520  GLU B  535  1                                  16    
HELIX   47  47 GLY B  541  LEU B  552  1                                  12    
HELIX   48  48 LYS B  554  ASP B  567  1                                  14    
HELIX   49  49 SER B  572  GLN B  586  1                                  15    
HELIX   50  50 GLU B  588  ASP B  603  1                                  16    
HELIX   51  51 TYR B  606  THR B  620  1                                  15    
HELIX   52  52 GLU B  622  ASN B  637  1                                  16    
HELIX   53  53 HIS B  640  GLN B  654  1                                  15    
HELIX   54  54 LYS B  656  ASN B  671  1                                  16    
HELIX   55  55 SER B  674  LEU B  688  1                                  15    
HELIX   56  56 LEU B  698  ASP B  705  1                                   8    
HELIX   57  57 ASN B  708  ASN B  722  1                                  15    
HELIX   58  58 LYS B  724  VAL B  739  1                                  16    
HELIX   59  59 GLU B  742  GLY B  757  1                                  16    
HELIX   60  60 GLN B  758  ASP B  773  1                                  16    
HELIX   61  61 GLN S   74  GLY S   84  1                                  11    
HELIX   62  62 GLY S   84  ASP S   92  1                                   9    
HELIX   63  63 GLU S   93  PHE S   96  5                                   4    
HELIX   64  64 PRO S   98  LEU S  103  1                                   6    
CRYST1  116.660  116.660  184.972  90.00  90.00  90.00 P 43          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008572  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008572  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005406        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system