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Database: PDB
Entry: 2CYX
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Original site: 2CYX 
HEADER    LIGASE                                  08-JUL-05   2CYX              
TITLE     STRUCTURE OF HUMAN UBIQUITIN-CONJUGATING ENZYME E2 G2                 
TITLE    2 (UBE2G2/UBC7)                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 G2;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: UBIQUITIN-PROTEIN LIGASE G2, UBIQUITIN CARRIER              
COMPND   5 PROTEIN G2;                                                          
COMPND   6 EC: 6.3.2.19;                                                        
COMPND   7 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: UBE2G2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-CMBP-GATEWAY                          
KEYWDS    UBIQUITIN-CONJUGATING ENZYME (E2), UBL CONJUGATION PATHWAY,           
KEYWDS   2 LIGASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON             
KEYWDS   3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN                    
KEYWDS   4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YOSHIKAWA,R.ARAI,K.MURAYAMA,Y.IMAI,R.TAKAHASHI,M.SHIROUZU,          
AUTHOR   2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE           
AUTHOR   3 (RSGI)                                                               
REVDAT   3   24-FEB-09 2CYX    1       VERSN                                    
REVDAT   2   02-MAY-06 2CYX    1       REMARK                                   
REVDAT   1   25-APR-06 2CYX    0                                                
JRNL        AUTH   R.ARAI,S.YOSHIKAWA,K.MURAYAMA,Y.IMAI,R.TAKAHASHI,            
JRNL        AUTH 2 M.SHIROUZU,S.YOKOYAMA                                        
JRNL        TITL   STRUCTURE OF HUMAN UBIQUITIN-CONJUGATING ENZYME E2           
JRNL        TITL 2 G2 (UBE2G2/UBC7)                                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   330 2006              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   16582478                                                     
JRNL        DOI    10.1107/S1744309106009006                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1671970.030                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 28395                          
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 SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2861                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3782                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3580                       
REMARK   3   BIN FREE R VALUE                    : 0.4170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 421                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3996                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 24.74000                                             
REMARK   3    B22 (A**2) : -1.90000                                             
REMARK   3    B33 (A**2) : -22.84000                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.56                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.43                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.710 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 8.310 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 8.550 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 11.000; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 55.64                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2CYX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024779.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI DOUBLE CRYSTAL                  
REMARK 200  OPTICS                         : TWO DIMENSIONAL FOCUSING           
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28705                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.560                              
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     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.110                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2UCZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% GLYCEROL, 0.1M TRIS, 1.45M           
REMARK 280  AMMONIUM SULFATE, PH 8.1, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.76100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.70500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.80500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.70500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.76100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.80500            
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, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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    -5                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     GLY C    -5                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU C  -2   N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    PRO C 100   N   -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    PRO C 100   C   -  N   -  CA  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    GLU C 104   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
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    SER A  -3       92.82    -62.10                                   
REMARK 500    GLU A  -2       38.68    -78.04                                   
REMARK 500    ASN A  30      116.14    175.89                                   
REMARK 500    ASP A  46       59.11   -110.12                                   
REMARK 500    ASP A  98      -76.23    -31.95                                   
REMARK 500    PRO A 100       84.27     47.86                                   
REMARK 500    MET A 101      123.18    -20.25                                   
REMARK 500    GLU A 104        5.12    -57.34                                   
REMARK 500    ASP A 132        1.70    -57.26                                   
REMARK 500    SER A 134      103.21   -161.87                                   
REMARK 500    ASP A 146      -87.53    -88.92                                   
REMARK 500    GLU B  -2       23.96    -71.30                                   
REMARK 500    ASN B  30      113.79    174.66                                   
REMARK 500    GLU B  45      -75.78    -45.42                                   
REMARK 500    ASP B  46       50.94    -99.37                                   
REMARK 500    PHE B  51       -8.75     81.23                                   
REMARK 500    PRO B  65       31.38    -96.16                                   
REMARK 500    ASP B  99       65.95   -168.08                                   
REMARK 500    TYR B 103        5.17    -46.70                                   
REMARK 500    ALA B 107      -27.45   -155.33                                   
REMARK 500    ASP B 132       -2.75    -52.19                                   
REMARK 500    GLU B 133       58.16    -91.29                                   
REMARK 500    SER B 134      105.98   -163.06                                   
REMARK 500    ASP B 146      -87.21    -86.58                                   
REMARK 500    ASN C  30      114.35    175.63                                   
REMARK 500    GLU C  45      -82.04    -39.30                                   
REMARK 500    ASP C  46       61.16   -108.06                                   
REMARK 500    PHE C  51       -2.02     73.73                                   
REMARK 500    ASP C  99       67.21   -158.21                                   
REMARK 500    PRO C 100     -169.10   -117.12                                   
REMARK 500    TYR C 103      -68.85    -97.90                                   
REMARK 500    ASP C 132        6.30    -60.51                                   
REMARK 500    SER C 134      101.19   -160.04                                   
REMARK 500    ASP C 146      -87.31    -86.92                                   
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 103         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: AR_001000136.1   RELATED DB: TARGETDB                    
DBREF  2CYX A    1   165  UNP    P60604   UB2G2_HUMAN      1    165             
DBREF  2CYX B    1   165  UNP    P60604   UB2G2_HUMAN      1    165             
DBREF  2CYX C    1   165  UNP    P60604   UB2G2_HUMAN      1    165             
SEQADV 2CYX GLY A   -5  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLY A   -4  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX SER A   -3  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLU A   -2  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX PHE A   -1  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLY B   -5  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLY B   -4  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX SER B   -3  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLU B   -2  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX PHE B   -1  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLY C   -5  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLY C   -4  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX SER C   -3  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX GLU C   -2  UNP  P60604              CLONING ARTIFACT               
SEQADV 2CYX PHE C   -1  UNP  P60604              CLONING ARTIFACT               
SEQRES   1 A  170  GLY GLY SER GLU PHE MET ALA GLY THR ALA LEU LYS ARG          
SEQRES   2 A  170  LEU MET ALA GLU TYR LYS GLN LEU THR LEU ASN PRO PRO          
SEQRES   3 A  170  GLU GLY ILE VAL ALA GLY PRO MET ASN GLU GLU ASN PHE          
SEQRES   4 A  170  PHE GLU TRP GLU ALA LEU ILE MET GLY PRO GLU ASP THR          
SEQRES   5 A  170  CYS PHE GLU PHE GLY VAL PHE PRO ALA ILE LEU SER PHE          
SEQRES   6 A  170  PRO LEU ASP TYR PRO LEU SER PRO PRO LYS MET ARG PHE          
SEQRES   7 A  170  THR CYS GLU MET PHE HIS PRO ASN ILE TYR PRO ASP GLY          
SEQRES   8 A  170  ARG VAL CYS ILE SER ILE LEU HIS ALA PRO GLY ASP ASP          
SEQRES   9 A  170  PRO MET GLY TYR GLU SER SER ALA GLU ARG TRP SER PRO          
SEQRES  10 A  170  VAL GLN SER VAL GLU LYS ILE LEU LEU SER VAL VAL SER          
SEQRES  11 A  170  MET LEU ALA GLU PRO ASN ASP GLU SER GLY ALA ASN VAL          
SEQRES  12 A  170  ASP ALA SER LYS MET TRP ARG ASP ASP ARG GLU GLN PHE          
SEQRES  13 A  170  TYR LYS ILE ALA LYS GLN ILE VAL GLN LYS SER LEU GLY          
SEQRES  14 A  170  LEU                                                          
SEQRES   1 B  170  GLY GLY SER GLU PHE MET ALA GLY THR ALA LEU LYS ARG          
SEQRES   2 B  170  LEU MET ALA GLU TYR LYS GLN LEU THR LEU ASN PRO PRO          
SEQRES   3 B  170  GLU GLY ILE VAL ALA GLY PRO MET ASN GLU GLU ASN PHE          
SEQRES   4 B  170  PHE GLU TRP GLU ALA LEU ILE MET GLY PRO GLU ASP THR          
SEQRES   5 B  170  CYS PHE GLU PHE GLY VAL PHE PRO ALA ILE LEU SER PHE          
SEQRES   6 B  170  PRO LEU ASP TYR PRO LEU SER PRO PRO LYS MET ARG PHE          
SEQRES   7 B  170  THR CYS GLU MET PHE HIS PRO ASN ILE TYR PRO ASP GLY          
SEQRES   8 B  170  ARG VAL CYS ILE SER ILE LEU HIS ALA PRO GLY ASP ASP          
SEQRES   9 B  170  PRO MET GLY TYR GLU SER SER ALA GLU ARG TRP SER PRO          
SEQRES  10 B  170  VAL GLN SER VAL GLU LYS ILE LEU LEU SER VAL VAL SER          
SEQRES  11 B  170  MET LEU ALA GLU PRO ASN ASP GLU SER GLY ALA ASN VAL          
SEQRES  12 B  170  ASP ALA SER LYS MET TRP ARG ASP ASP ARG GLU GLN PHE          
SEQRES  13 B  170  TYR LYS ILE ALA LYS GLN ILE VAL GLN LYS SER LEU GLY          
SEQRES  14 B  170  LEU                                                          
SEQRES   1 C  170  GLY GLY SER GLU PHE MET ALA GLY THR ALA LEU LYS ARG          
SEQRES   2 C  170  LEU MET ALA GLU TYR LYS GLN LEU THR LEU ASN PRO PRO          
SEQRES   3 C  170  GLU GLY ILE VAL ALA GLY PRO MET ASN GLU GLU ASN PHE          
SEQRES   4 C  170  PHE GLU TRP GLU ALA LEU ILE MET GLY PRO GLU ASP THR          
SEQRES   5 C  170  CYS PHE GLU PHE GLY VAL PHE PRO ALA ILE LEU SER PHE          
SEQRES   6 C  170  PRO LEU ASP TYR PRO LEU SER PRO PRO LYS MET ARG PHE          
SEQRES   7 C  170  THR CYS GLU MET PHE HIS PRO ASN ILE TYR PRO ASP GLY          
SEQRES   8 C  170  ARG VAL CYS ILE SER ILE LEU HIS ALA PRO GLY ASP ASP          
SEQRES   9 C  170  PRO MET GLY TYR GLU SER SER ALA GLU ARG TRP SER PRO          
SEQRES  10 C  170  VAL GLN SER VAL GLU LYS ILE LEU LEU SER VAL VAL SER          
SEQRES  11 C  170  MET LEU ALA GLU PRO ASN ASP GLU SER GLY ALA ASN VAL          
SEQRES  12 C  170  ASP ALA SER LYS MET TRP ARG ASP ASP ARG GLU GLN PHE          
SEQRES  13 C  170  TYR LYS ILE ALA LYS GLN ILE VAL GLN LYS SER LEU GLY          
SEQRES  14 C  170  LEU                                                          
FORMUL   4  HOH   *23(H2 O)                                                     
HELIX    1   1 GLU A   -2  ASN A   19  1                                  21    
HELIX    2   2 ILE A   90  HIS A   94  5                                   5    
HELIX    3   3 GLU A  104  ARG A  109  1                                   6    
HELIX    4   4 SER A  115  GLU A  129  1                                  15    
HELIX    5   5 SER A  134  ALA A  136  5                                   3    
HELIX    6   6 ASN A  137  ASP A  146  1                                  10    
HELIX    7   7 ASP A  147  LEU A  163  1                                  17    
HELIX    8   8 GLU B   -2  ASN B   19  1                                  21    
HELIX    9   9 ILE B   90  HIS B   94  5                                   5    
HELIX   10  10 SER B  115  GLU B  129  1                                  15    
HELIX   11  11 ASN B  137  ASP B  146  1                                  10    
HELIX   12  12 ASP B  147  LEU B  163  1                                  17    
HELIX   13  13 GLU C   -2  ASN C   19  1                                  21    
HELIX   14  14 ILE C   90  HIS C   94  5                                   5    
HELIX   15  15 GLU C  104  ARG C  109  1                                   6    
HELIX   16  16 SER C  115  GLU C  129  1                                  15    
HELIX   17  17 SER C  134  ALA C  136  5                                   3    
HELIX   18  18 ASN C  137  ASP C  146  1                                  10    
HELIX   19  19 ASP C  147  LEU C  163  1                                  17    
SHEET    1   A 4 ILE A  24  PRO A  28  0                                        
SHEET    2   A 4 GLU A  36  MET A  42 -1  O  GLU A  38   N  GLY A  27           
SHEET    3   A 4 VAL A  53  SER A  59 -1  O  LEU A  58   N  TRP A  37           
SHEET    4   A 4 LYS A  70  PHE A  73 -1  O  LYS A  70   N  SER A  59           
SHEET    1   B 4 ILE B  24  PRO B  28  0                                        
SHEET    2   B 4 GLU B  36  MET B  42 -1  O  GLU B  38   N  GLY B  27           
SHEET    3   B 4 VAL B  53  SER B  59 -1  O  PHE B  54   N  ILE B  41           
SHEET    4   B 4 LYS B  70  PHE B  73 -1  O  LYS B  70   N  SER B  59           
SHEET    1   C 4 ILE C  24  PRO C  28  0                                        
SHEET    2   C 4 GLU C  36  MET C  42 -1  O  GLU C  38   N  GLY C  27           
SHEET    3   C 4 VAL C  53  SER C  59 -1  O  LEU C  58   N  TRP C  37           
SHEET    4   C 4 LYS C  70  PHE C  73 -1  O  LYS C  70   N  SER C  59           
CISPEP   1 TYR A   64    PRO A   65          0        -1.93                     
CISPEP   2 TYR B   64    PRO B   65          0         1.74                     
CISPEP   3 TYR C   64    PRO C   65          0        -0.29                     
CRYST1   63.522   87.610  157.410  90.00  90.00  90.00 P 21 21 21   12          
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      0.015743  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006353        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system