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Database: PDB
Entry: 3PTF
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Original site: 3PTF 
HEADER    LIGASE                                  02-DEC-10   3PTF              
TITLE     X-RAY STRUCTURE OF THE NON-COVALENT COMPLEX BETWEEN UBCH5A AND        
TITLE    2 UBIQUITIN                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D1;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: E2;                                                        
COMPND   5 SYNONYM: STIMULATOR OF FE TRANSPORT, SFT, UBC4/5 HOMOLOG, UBCH5,     
COMPND   6 UBIQUITIN CARRIER PROTEIN D1, UBIQUITIN-CONJUGATING ENZYME E2(17)KB  
COMPND   7 1, UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 1, UBIQUITIN-PROTEIN LIGASE
COMPND   8 D1;                                                                  
COMPND   9 EC: 6.3.2.19;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: POLYUBIQUITIN-B;                                           
COMPND  13 CHAIN: C, D;                                                         
COMPND  14 FRAGMENT: UBIQUITIN;                                                 
COMPND  15 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: SFT, UBC5A, UBCH5, UBCH5A, UBE2D1;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-15B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: UBIQUITIN;                                                     
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    PROTEIN-PROTEIN COMPLEX, E2, UBIQUITIN, UBIQUITIN CONJUGATING ENZYME, 
KEYWDS   2 ALPHA/BETA, LIGASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.BOSANAC,S.G.HYMOWITZ                                                
REVDAT   2   06-SEP-23 3PTF    1       SEQADV                                   
REVDAT   1   11-MAY-11 3PTF    0                                                
JRNL        AUTH   I.BOSANAC,L.PHU,B.PAN,I.ZILBERLEYB,B.MAURER,V.M.DIXIT,       
JRNL        AUTH 2 S.G.HYMOWITZ,D.S.KIRKPATRICK                                 
JRNL        TITL   MODULATION OF K11-LINKAGE FORMATION BY VARIABLE LOOP         
JRNL        TITL 2 RESIDUES WITHIN UBCH5A.                                      
JRNL        REF    J.MOL.BIOL.                   V. 408   420 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21396940                                                     
JRNL        DOI    10.1016/J.JMB.2011.03.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13133                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 622                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 717                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.5100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3600                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.97000                                              
REMARK   3    B22 (A**2) : -1.82000                                             
REMARK   3    B33 (A**2) : 0.85000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.415         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.285         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.479        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3698 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2549 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5023 ; 1.095 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6270 ; 0.808 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   450 ; 5.649 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;33.352 ;24.753       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   654 ;15.719 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;13.739 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   560 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4022 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   677 ; 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):  2276 ; 2.619 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   886 ; 0.505 ; 2.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3717 ; 4.661 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1422 ; 3.513 ; 2.500       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1305 ; 5.951 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A      61      1                      
REMARK   3           1     B      4       B      61      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    778 ;  0.02 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):    778 ;  0.45 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C      73      4                      
REMARK   3           1     D      1       D      73      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    990 ;  0.25 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    990 ;  0.49 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2863  19.0461  33.6864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1293 T22:   0.0899                                     
REMARK   3      T33:   0.0848 T12:  -0.0039                                     
REMARK   3      T13:   0.0144 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5165 L22:   1.4066                                     
REMARK   3      L33:   3.2141 L12:   0.0598                                     
REMARK   3      L13:   0.6924 L23:   1.2531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0264 S12:   0.0290 S13:  -0.0219                       
REMARK   3      S21:   0.0688 S22:  -0.0369 S23:  -0.0557                       
REMARK   3      S31:   0.2012 S32:  -0.0078 S33:   0.0105                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0049  50.2918  10.5067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0966 T22:   0.1149                                     
REMARK   3      T33:   0.0781 T12:   0.0155                                     
REMARK   3      T13:   0.0260 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0249 L22:   3.1262                                     
REMARK   3      L33:   1.6981 L12:   0.1941                                     
REMARK   3      L13:  -0.0838 L23:   0.0599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2224 S12:  -0.0511 S13:  -0.0381                       
REMARK   3      S21:  -0.1340 S22:   0.2316 S23:  -0.0582                       
REMARK   3      S31:  -0.0331 S32:   0.1883 S33:  -0.0092                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6131  42.4372  33.0572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0175 T22:   0.0461                                     
REMARK   3      T33:   0.1027 T12:  -0.0127                                     
REMARK   3      T13:   0.0233 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9410 L22:   3.5983                                     
REMARK   3      L33:   4.8786 L12:   0.0594                                     
REMARK   3      L13:   0.8408 L23:   0.1209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0811 S12:   0.0728 S13:  -0.0202                       
REMARK   3      S21:   0.0780 S22:  -0.0698 S23:   0.0397                       
REMARK   3      S31:  -0.0654 S32:  -0.0299 S33:  -0.0112                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3371  61.8829 -10.3491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1126 T22:   0.0710                                     
REMARK   3      T33:   0.0705 T12:  -0.0322                                     
REMARK   3      T13:   0.0359 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3677 L22:   5.2689                                     
REMARK   3      L33:   4.9335 L12:  -0.9046                                     
REMARK   3      L13:  -0.0959 L23:  -0.9290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0906 S12:   0.1105 S13:   0.1599                       
REMARK   3      S21:  -0.0783 S22:  -0.1136 S23:  -0.1075                       
REMARK   3      S31:  -0.1206 S32:  -0.1498 S33:   0.0230                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3PTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062791.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: 1UBQ, 1X23                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE COMPLEX WERE GROWN BY    
REMARK 280  HANGING-DROP VAPOR DIFFUSION AT 19 C BY COMBINING 1.5 UL OF         
REMARK 280  PROTEIN SOLUTION (20 MM MES PH 6.0, 150 MM NACL AND 0.5 MM TCEP)    
REMARK 280  AT 20 MG/ML WITH 1.5 UL OF RESERVOIR SOLUTION (0.1 M TRIS PH 8.5    
REMARK 280  AND 24% PEG 10,000), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  292K                                                                
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       13.73100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.90300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.45150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.90300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       13.73100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.45150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    -5                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     ARG C    74                                                      
REMARK 465     GLY C    75                                                      
REMARK 465     GLY C    76                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     ARG D    74                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     GLY D    76                                                      
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    SER A  -4      -66.64    -20.35                                   
REMARK 500    ILE A  88       -7.44    -59.14                                   
REMARK 500    ARG A  90     -106.08   -134.95                                   
REMARK 500    ASP A 130       79.07   -160.06                                   
REMARK 500    ARG B  90     -111.59   -138.01                                   
REMARK 500    ALA C  46       54.95     28.43                                   
REMARK 500    LYS C  63      125.30    -38.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3PTF A    1   147  UNP    P51668   UB2D1_HUMAN      1    147             
DBREF  3PTF B    1   147  UNP    P51668   UB2D1_HUMAN      1    147             
DBREF  3PTF C    1    76  UNP    P0CG47   UBB_HUMAN        1     76             
DBREF  3PTF D    1    76  UNP    P0CG47   UBB_HUMAN        1     76             
SEQADV 3PTF GLY A   -5  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF SER A   -4  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF HIS A   -3  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF MET A   -2  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF LEU A   -1  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF GLU A    0  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF GLY B   -5  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF SER B   -4  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF HIS B   -3  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF MET B   -2  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF LEU B   -1  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF GLU B    0  UNP  P51668              EXPRESSION TAG                 
SEQADV 3PTF GLY C   -2  UNP  P0CG47              EXPRESSION TAG                 
SEQADV 3PTF SER C   -1  UNP  P0CG47              EXPRESSION TAG                 
SEQADV 3PTF HIS C    0  UNP  P0CG47              EXPRESSION TAG                 
SEQADV 3PTF GLY D   -2  UNP  P0CG47              EXPRESSION TAG                 
SEQADV 3PTF SER D   -1  UNP  P0CG47              EXPRESSION TAG                 
SEQADV 3PTF HIS D    0  UNP  P0CG47              EXPRESSION TAG                 
SEQRES   1 A  153  GLY SER HIS MET LEU GLU MET ALA LEU LYS ARG ILE GLN          
SEQRES   2 A  153  LYS GLU LEU SER ASP LEU GLN ARG ASP PRO PRO ALA HIS          
SEQRES   3 A  153  CYS SER ALA GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP          
SEQRES   4 A  153  GLN ALA THR ILE MET GLY PRO PRO ASP SER ALA TYR GLN          
SEQRES   5 A  153  GLY GLY VAL PHE PHE LEU THR VAL HIS PHE PRO THR ASP          
SEQRES   6 A  153  TYR PRO PHE LYS PRO PRO LYS ILE ALA PHE THR THR LYS          
SEQRES   7 A  153  ILE TYR HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS          
SEQRES   8 A  153  LEU ASP ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR          
SEQRES   9 A  153  VAL SER LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS          
SEQRES  10 A  153  ASP PRO ASN PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA          
SEQRES  11 A  153  GLN ILE TYR LYS SER ASP LYS GLU LYS TYR ASN ARG HIS          
SEQRES  12 A  153  ALA ARG GLU TRP THR GLN LYS TYR ALA MET                      
SEQRES   1 B  153  GLY SER HIS MET LEU GLU MET ALA LEU LYS ARG ILE GLN          
SEQRES   2 B  153  LYS GLU LEU SER ASP LEU GLN ARG ASP PRO PRO ALA HIS          
SEQRES   3 B  153  CYS SER ALA GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP          
SEQRES   4 B  153  GLN ALA THR ILE MET GLY PRO PRO ASP SER ALA TYR GLN          
SEQRES   5 B  153  GLY GLY VAL PHE PHE LEU THR VAL HIS PHE PRO THR ASP          
SEQRES   6 B  153  TYR PRO PHE LYS PRO PRO LYS ILE ALA PHE THR THR LYS          
SEQRES   7 B  153  ILE TYR HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS          
SEQRES   8 B  153  LEU ASP ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR          
SEQRES   9 B  153  VAL SER LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS          
SEQRES  10 B  153  ASP PRO ASN PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA          
SEQRES  11 B  153  GLN ILE TYR LYS SER ASP LYS GLU LYS TYR ASN ARG HIS          
SEQRES  12 B  153  ALA ARG GLU TRP THR GLN LYS TYR ALA MET                      
SEQRES   1 C   79  GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY          
SEQRES   2 C   79  LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE          
SEQRES   3 C   79  GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE          
SEQRES   4 C   79  PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN          
SEQRES   5 C   79  LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN          
SEQRES   6 C   79  LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY          
SEQRES   7 C   79  GLY                                                          
SEQRES   1 D   79  GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY          
SEQRES   2 D   79  LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE          
SEQRES   3 D   79  GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE          
SEQRES   4 D   79  PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN          
SEQRES   5 D   79  LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN          
SEQRES   6 D   79  LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY          
SEQRES   7 D   79  GLY                                                          
FORMUL   5  HOH   *40(H2 O)                                                     
HELIX    1   1 GLY A   -5  ASP A   16  1                                  22    
HELIX    2   2 LEU A   86  ARG A   90  5                                   5    
HELIX    3   3 THR A   98  ASP A  112  1                                  15    
HELIX    4   4 VAL A  120  ASP A  130  1                                  11    
HELIX    5   5 ASP A  130  ALA A  146  1                                  17    
HELIX    6   6 SER B   -4  ASP B   16  1                                  21    
HELIX    7   7 LEU B   86  ARG B   90  5                                   5    
HELIX    8   8 THR B   98  ASP B  112  1                                  15    
HELIX    9   9 VAL B  120  ASP B  130  1                                  11    
HELIX   10  10 ASP B  130  ALA B  146  1                                  17    
HELIX   11  11 THR C   22  GLY C   35  1                                  14    
HELIX   12  12 PRO C   37  ASP C   39  5                                   3    
HELIX   13  13 LEU C   56  ASN C   60  5                                   5    
HELIX   14  14 THR D   22  GLY D   35  1                                  14    
HELIX   15  15 PRO D   37  ASP D   39  5                                   3    
SHEET    1   A 4 CYS A  21  PRO A  25  0                                        
SHEET    2   A 4 HIS A  32  MET A  38 -1  O  THR A  36   N  SER A  22           
SHEET    3   A 4 VAL A  49  HIS A  55 -1  O  PHE A  50   N  ILE A  37           
SHEET    4   A 4 LYS A  66  PHE A  69 -1  O  LYS A  66   N  HIS A  55           
SHEET    1   B 4 CYS B  21  PRO B  25  0                                        
SHEET    2   B 4 HIS B  32  MET B  38 -1  O  THR B  36   N  SER B  22           
SHEET    3   B 4 VAL B  49  HIS B  55 -1  O  PHE B  50   N  ILE B  37           
SHEET    4   B 4 LYS B  66  PHE B  69 -1  O  ALA B  68   N  THR B  53           
SHEET    1   C 5 THR C  12  GLU C  16  0                                        
SHEET    2   C 5 GLN C   2  LYS C   6 -1  N  VAL C   5   O  ILE C  13           
SHEET    3   C 5 THR C  66  LEU C  71  1  O  LEU C  67   N  LYS C   6           
SHEET    4   C 5 GLN C  41  PHE C  45 -1  N  ARG C  42   O  VAL C  70           
SHEET    5   C 5 LYS C  48  GLN C  49 -1  O  LYS C  48   N  PHE C  45           
SHEET    1   D 5 THR D  12  VAL D  17  0                                        
SHEET    2   D 5 MET D   1  LYS D   6 -1  N  VAL D   5   O  ILE D  13           
SHEET    3   D 5 THR D  66  LEU D  71  1  O  LEU D  69   N  LYS D   6           
SHEET    4   D 5 GLN D  41  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    5   D 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
CISPEP   1 TYR A   60    PRO A   61          0        10.01                     
CISPEP   2 TYR B   60    PRO B   61          0         8.97                     
CRYST1   27.462  102.903  159.806  90.00  90.00  90.00 P 21 21 21    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      0.036414  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009718  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006258        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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