GenomeNet

Database: PDB
Entry: 1LDD
LinkDB: 1LDD
Original site: 1LDD 
HEADER    LIGASE                                  08-APR-02   1LDD              
TITLE     STRUCTURE OF THE CUL1-RBX1-SKP1-F BOXSKP2 SCF UBIQUITIN               
TITLE    2 LIGASE COMPLEX                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANAPHASE PROMOTING COMPLEX;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 773-846;                                          
COMPND   5 SYNONYM: APC2WHB;                                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX4T3                                   
KEYWDS    UBIQUITIN, LIGASE, UBIQUITINATION, RING FINGER, WINGED-HELIX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.ZHENG,B.A.SCHULMAN,L.SONG,J.J.MILLER,P.D.JEFFREY,P.WANG,            
AUTHOR   2 C.CHU,D.M.KOEPP,S.J.ELLEDGE,M.PAGANO,R.C.CONAWAY,                    
AUTHOR   3 J.W.CONAWAY,J.W.HARPER,N.P.PAVLETICH                                 
REVDAT   2   24-FEB-09 1LDD    1       VERSN                                    
REVDAT   1   08-MAY-02 1LDD    0                                                
JRNL        AUTH   N.ZHENG,B.A.SCHULMAN,L.SONG,J.J.MILLER,P.D.JEFFREY,          
JRNL        AUTH 2 P.WANG,C.CHU,D.M.KOEPP,S.J.ELLEDGE,M.PAGANO,                 
JRNL        AUTH 3 R.C.CONAWAY,J.W.CONAWAY,J.W.HARPER,N.P.PAVLETICH             
JRNL        TITL   STRUCTURE OF THE CUL1-RBX1-SKP1-F BOXSKP2 SCF                
JRNL        TITL 2 UBIQUITIN LIGASE COMPLEX.                                    
JRNL        REF    NATURE                        V. 416   703 2002              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   11961546                                                     
JRNL        DOI    10.1038/416703A                                              
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 40867                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2972                                    
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LDD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015856.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 170                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9747                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40867                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4K, PH 8.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
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       27.35000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.35000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.45000            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     LYS A  773                                                       
REMARK 475     ALA A  839                                                       
REMARK 475     ASN A  840                                                       
REMARK 475     ALA B  839                                                       
REMARK 475     ASN B  840                                                       
REMARK 475     LYS C  773                                                       
REMARK 475     ALA C  839                                                       
REMARK 475     ASN C  840                                                       
REMARK 475     LYS D  773                                                       
REMARK 475     ALA D  839                                                       
REMARK 475     ASN D  840                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     VAL A  846   OXT                                                 
REMARK 480     LYS B  773   N     CA    C     O     CB                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TYR D   837     O    SER D   842              1.98            
REMARK 500   O    TYR C   837     O    SER C   842              2.06            
REMARK 500   O    TYR B   837     O    SER B   842              2.07            
REMARK 500   O    TYR A   837     O    SER A   842              2.14            
REMARK 500   O    ALA B   830     O    GLU B   832              2.18            
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    TYR A 814      -34.44     98.72                                   
REMARK 500    GLU A 832     -149.54    -72.88                                   
REMARK 500    TYR A 837      -92.33    -59.03                                   
REMARK 500    ILE A 838      101.42    104.49                                   
REMARK 500    ALA A 839      150.41    -29.49                                   
REMARK 500    ASN A 840      -14.35     86.88                                   
REMARK 500    TYR B 814      -30.83     91.31                                   
REMARK 500    GLU B 832     -164.00    -71.92                                   
REMARK 500    TYR B 837      -91.18    -55.83                                   
REMARK 500    ILE B 838      105.46    103.48                                   
REMARK 500    ALA B 839      150.84    -34.31                                   
REMARK 500    ASN B 840      -17.61     86.71                                   
REMARK 500    TYR C 814      -32.30     93.79                                   
REMARK 500    GLU C 832     -163.60    -74.31                                   
REMARK 500    TYR C 837      -93.23    -53.93                                   
REMARK 500    ILE C 838      103.16    105.46                                   
REMARK 500    ALA C 839      148.73    -30.58                                   
REMARK 500    ASN C 840      -13.19     86.91                                   
REMARK 500    TYR D 814      -32.70     88.52                                   
REMARK 500    GLU D 832     -161.12    -68.56                                   
REMARK 500    TYR D 837      -86.59    -59.37                                   
REMARK 500    ILE D 838      105.94     99.66                                   
REMARK 500    ALA D 839      150.24    -35.69                                   
REMARK 500    ASN D 840      -18.51     87.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 814         0.07    SIDE_CHAIN                              
REMARK 500    TYR C 814         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LDJ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE CUL1-RBX1-SKP1-F BOXSKP2 SCF UBIQUITIN              
REMARK 900 LIGASE COMPLEX                                                       
REMARK 900 RELATED ID: 1LDK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE CUL1-RBX1-SKP1-F BOXSKP2 SCF UBIQUITIN              
REMARK 900 LIGASE COMPLEX                                                       
DBREF  1LDD A  773   846  UNP    Q12440   APC2_YEAST     773    846             
DBREF  1LDD B  773   846  UNP    Q12440   APC2_YEAST     773    846             
DBREF  1LDD C  773   846  UNP    Q12440   APC2_YEAST     773    846             
DBREF  1LDD D  773   846  UNP    Q12440   APC2_YEAST     773    846             
SEQRES   1 A   74  LYS TYR GLU LEU THR LEU GLN ARG SER LEU PRO PHE ILE          
SEQRES   2 A   74  GLU GLY MET LEU THR ASN LEU GLY ALA MET LYS LEU HIS          
SEQRES   3 A   74  LYS ILE HIS SER PHE LEU LYS ILE THR VAL PRO LYS ASP          
SEQRES   4 A   74  TRP GLY TYR ASN ARG ILE THR LEU GLN GLN LEU GLU GLY          
SEQRES   5 A   74  TYR LEU ASN THR LEU ALA ASP GLU GLY ARG LEU LYS TYR          
SEQRES   6 A   74  ILE ALA ASN GLY SER TYR GLU ILE VAL                          
SEQRES   1 B   74  LYS TYR GLU LEU THR LEU GLN ARG SER LEU PRO PHE ILE          
SEQRES   2 B   74  GLU GLY MET LEU THR ASN LEU GLY ALA MET LYS LEU HIS          
SEQRES   3 B   74  LYS ILE HIS SER PHE LEU LYS ILE THR VAL PRO LYS ASP          
SEQRES   4 B   74  TRP GLY TYR ASN ARG ILE THR LEU GLN GLN LEU GLU GLY          
SEQRES   5 B   74  TYR LEU ASN THR LEU ALA ASP GLU GLY ARG LEU LYS TYR          
SEQRES   6 B   74  ILE ALA ASN GLY SER TYR GLU ILE VAL                          
SEQRES   1 C   74  LYS TYR GLU LEU THR LEU GLN ARG SER LEU PRO PHE ILE          
SEQRES   2 C   74  GLU GLY MET LEU THR ASN LEU GLY ALA MET LYS LEU HIS          
SEQRES   3 C   74  LYS ILE HIS SER PHE LEU LYS ILE THR VAL PRO LYS ASP          
SEQRES   4 C   74  TRP GLY TYR ASN ARG ILE THR LEU GLN GLN LEU GLU GLY          
SEQRES   5 C   74  TYR LEU ASN THR LEU ALA ASP GLU GLY ARG LEU LYS TYR          
SEQRES   6 C   74  ILE ALA ASN GLY SER TYR GLU ILE VAL                          
SEQRES   1 D   74  LYS TYR GLU LEU THR LEU GLN ARG SER LEU PRO PHE ILE          
SEQRES   2 D   74  GLU GLY MET LEU THR ASN LEU GLY ALA MET LYS LEU HIS          
SEQRES   3 D   74  LYS ILE HIS SER PHE LEU LYS ILE THR VAL PRO LYS ASP          
SEQRES   4 D   74  TRP GLY TYR ASN ARG ILE THR LEU GLN GLN LEU GLU GLY          
SEQRES   5 D   74  TYR LEU ASN THR LEU ALA ASP GLU GLY ARG LEU LYS TYR          
SEQRES   6 D   74  ILE ALA ASN GLY SER TYR GLU ILE VAL                          
HELIX    1   1 TYR A  774  GLY A  793  1                                  20    
HELIX    2   2 LEU A  797  VAL A  808  1                                  12    
HELIX    3   3 PRO A  809  GLY A  813  5                                   5    
HELIX    4   4 THR A  818  GLU A  832  1                                  15    
HELIX    5   5 TYR B  774  GLY B  793  1                                  20    
HELIX    6   6 LEU B  797  VAL B  808  1                                  12    
HELIX    7   7 PRO B  809  GLY B  813  5                                   5    
HELIX    8   8 THR B  818  GLU B  832  1                                  15    
HELIX    9   9 TYR C  774  SER C  781  1                                   8    
HELIX   10  10 SER C  781  GLY C  793  1                                  13    
HELIX   11  11 LEU C  797  VAL C  808  1                                  12    
HELIX   12  12 PRO C  809  GLY C  813  5                                   5    
HELIX   13  13 THR C  818  GLU C  832  1                                  15    
HELIX   14  14 TYR D  774  SER D  781  1                                   8    
HELIX   15  15 SER D  781  GLY D  793  1                                  13    
HELIX   16  16 LEU D  797  VAL D  808  1                                  12    
HELIX   17  17 PRO D  809  GLY D  813  5                                   5    
HELIX   18  18 THR D  818  GLU D  832  1                                  15    
SHEET    1   A 3 MET A 795  LYS A 796  0                                        
SHEET    2   A 3 SER A 842  ILE A 845 -1  O  TYR A 843   N  MET A 795           
SHEET    3   A 3 LEU A 835  LYS A 836 -1  N  LYS A 836   O  GLU A 844           
SHEET    1   B 3 MET B 795  LYS B 796  0                                        
SHEET    2   B 3 SER B 842  ILE B 845 -1  O  TYR B 843   N  MET B 795           
SHEET    3   B 3 LEU B 835  LYS B 836 -1  N  LYS B 836   O  GLU B 844           
SHEET    1   C 3 MET C 795  LYS C 796  0                                        
SHEET    2   C 3 SER C 842  ILE C 845 -1  O  TYR C 843   N  MET C 795           
SHEET    3   C 3 LEU C 835  LYS C 836 -1  N  LYS C 836   O  GLU C 844           
SHEET    1   D 3 MET D 795  LYS D 796  0                                        
SHEET    2   D 3 SER D 842  ILE D 845 -1  O  TYR D 843   N  MET D 795           
SHEET    3   D 3 LEU D 835  LYS D 836 -1  N  LYS D 836   O  GLU D 844           
CRYST1   54.700   72.900   79.800  90.00  90.00  90.00 P 21 21 21   16          
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      0.018282  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system