GenomeNet

Database: PDB
Entry: 1Y6L
LinkDB: 1Y6L
Original site: 1Y6L 
HEADER    LIGASE                                  06-DEC-04   1Y6L              
TITLE     HUMAN UBIQUITIN CONJUGATING ENZYME E2E2                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2E2;                         
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: RESIDUES 55-201;                                           
COMPND   5 SYNONYM: UBIQUITIN-PROTEIN LIGASE E2, UBIQUITIN CARRIER PROTEIN E2,  
COMPND   6 UBCH8;                                                               
COMPND   7 EC: 6.3.2.19;                                                        
COMPND   8 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: UBE2E2, UBCH8;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, UBIQUITIN, UBIQUITIN-CONJUGATING      
KEYWDS   2 ENZYME, LIGASE, SGC                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,G.V.AVVAKUMOV,E.M.NEWMAN,F.MACKENZIE,I.KOZIERADZKI,        
AUTHOR   2 A.BOCHKAREV,M.SUNDSTROM,C.ARROWSMITH,A.EDWARDS,S.DHE-PAGANON,        
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   6   23-AUG-23 1Y6L    1       SEQADV                                   
REVDAT   5   28-NOV-12 1Y6L    1       JRNL   VERSN                             
REVDAT   4   24-FEB-09 1Y6L    1       VERSN                                    
REVDAT   3   10-OCT-06 1Y6L    1       AUTHOR KEYWDS DBREF  SEQADV              
REVDAT   2   24-JAN-06 1Y6L    1       JRNL                                     
REVDAT   1   11-JAN-05 1Y6L    0                                                
JRNL        AUTH   Y.SHENG,J.H.HONG,R.DOHERTY,T.SRIKUMAR,J.SHLOUSH,             
JRNL        AUTH 2 G.V.AVVAKUMOV,J.R.WALKER,S.XUE,D.NECULAI,J.W.WAN,S.K.KIM,    
JRNL        AUTH 3 C.H.ARROWSMITH,B.RAUGHT,S.DHE-PAGANON                        
JRNL        TITL   A HUMAN UBIQUITIN CONJUGATING ENZYME (E2)-HECT E3 LIGASE     
JRNL        TITL 2 STRUCTURE-FUNCTION SCREEN.                                   
JRNL        REF    MOL CELL PROTEOMICS           V.  11   329 2012              
JRNL        REFN                   ISSN 1535-9476                               
JRNL        PMID   22496338                                                     
JRNL        DOI    10.1074/MCP.O111.013706                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 37014                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1995                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2773                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.43                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3486                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 369                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.34000                                             
REMARK   3    B22 (A**2) : 2.13000                                              
REMARK   3    B33 (A**2) : -0.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.13000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.158         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.315         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3579 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4881 ; 1.588 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   441 ; 5.673 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   147 ;35.318 ;23.469       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   585 ;15.655 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.507 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   546 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2715 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1797 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2473 ; 0.315 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   302 ; 0.179 ; 0.200       
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):    80 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.163 ; 0.200       
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):  2300 ; 1.058 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3651 ; 1.723 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1485 ; 2.762 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1230 ; 4.285 ; 4.500       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1Y6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000031180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39009                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.2800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1QCQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 0.1M TRIS, PH 8.5, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.05450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.05500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.05450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.05500            
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 300 REMARK: THE BIOLOGICAL UNIT IS EXPECTED TO BE A MONOMER.             
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 193  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY C    -1                                                      
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    HOH C   180     O    HOH C   254              2.07            
REMARK 500   NH2  ARG A     5     O    PRO A    95              2.15            
REMARK 500   NH2  ARG B     5     O    LEU B    97              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A   5   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 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    LYS A  90     -103.03   -132.33                                   
REMARK 500    LYS B  90     -120.72   -129.98                                   
REMARK 500    ASN B 130       63.52   -151.49                                   
REMARK 500    LYS C  90     -117.61   -131.34                                   
REMARK 500    ASN C 130       67.46   -152.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1Y6L A    1   147  UNP    Q96LR5   UB2E2_HUMAN     55    201             
DBREF  1Y6L B    1   147  UNP    Q96LR5   UB2E2_HUMAN     55    201             
DBREF  1Y6L C    1   147  UNP    Q96LR5   UB2E2_HUMAN     55    201             
SEQADV 1Y6L GLY A   -1  UNP  Q96LR5              CLONING ARTIFACT               
SEQADV 1Y6L SER A    0  UNP  Q96LR5              CLONING ARTIFACT               
SEQADV 1Y6L GLY B   -1  UNP  Q96LR5              CLONING ARTIFACT               
SEQADV 1Y6L SER B    0  UNP  Q96LR5              CLONING ARTIFACT               
SEQADV 1Y6L GLY C   -1  UNP  Q96LR5              CLONING ARTIFACT               
SEQADV 1Y6L SER C    0  UNP  Q96LR5              CLONING ARTIFACT               
SEQRES   1 A  149  GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA          
SEQRES   2 A  149  GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY          
SEQRES   3 A  149  PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE          
SEQRES   4 A  149  LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE          
SEQRES   5 A  149  PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS          
SEQRES   6 A  149  PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS          
SEQRES   7 A  149  ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU          
SEQRES   8 A  149  LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 A  149  LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO          
SEQRES  10 A  149  ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET          
SEQRES  11 A  149  THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP          
SEQRES  12 A  149  THR LYS ARG TYR ALA THR                                      
SEQRES   1 B  149  GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA          
SEQRES   2 B  149  GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY          
SEQRES   3 B  149  PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE          
SEQRES   4 B  149  LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE          
SEQRES   5 B  149  PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS          
SEQRES   6 B  149  PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS          
SEQRES   7 B  149  ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU          
SEQRES   8 B  149  LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 B  149  LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO          
SEQRES  10 B  149  ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET          
SEQRES  11 B  149  THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP          
SEQRES  12 B  149  THR LYS ARG TYR ALA THR                                      
SEQRES   1 C  149  GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA          
SEQRES   2 C  149  GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY          
SEQRES   3 C  149  PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE          
SEQRES   4 C  149  LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE          
SEQRES   5 C  149  PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS          
SEQRES   6 C  149  PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS          
SEQRES   7 C  149  ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU          
SEQRES   8 C  149  LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 C  149  LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO          
SEQRES  10 C  149  ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET          
SEQRES  11 C  149  THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP          
SEQRES  12 C  149  THR LYS ARG TYR ALA THR                                      
FORMUL   4  HOH   *369(H2 O)                                                    
HELIX    1   1 THR A    1  ASP A   16  1                                  16    
HELIX    2   2 LEU A   86  LYS A   90  5                                   5    
HELIX    3   3 THR A   98  ASP A  112  1                                  15    
HELIX    4   4 VAL A  120  ASN A  130  1                                  11    
HELIX    5   5 ASN A  130  ALA A  146  1                                  17    
HELIX    6   6 THR B    1  ASP B   16  1                                  16    
HELIX    7   7 LEU B   86  LYS B   90  5                                   5    
HELIX    8   8 THR B   98  ASP B  112  1                                  15    
HELIX    9   9 VAL B  120  ASN B  130  1                                  11    
HELIX   10  10 ASN B  130  ALA B  146  1                                  17    
HELIX   11  11 THR C    1  ASP C   16  1                                  16    
HELIX   12  12 LEU C   86  LYS C   90  5                                   5    
HELIX   13  13 THR C   98  ASP C  112  1                                  15    
HELIX   14  14 VAL C  120  ASN C  130  1                                  11    
HELIX   15  15 ASN C  130  ALA C  146  1                                  17    
SHEET    1   A 4 CYS A  21  PRO A  25  0                                        
SHEET    2   A 4 GLU A  32  LEU A  38 -1  O  ARG A  34   N  GLY A  24           
SHEET    3   A 4 VAL A  49  THR 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  THR A  55           
SHEET    1   B 4 CYS B  21  PRO B  25  0                                        
SHEET    2   B 4 GLU B  32  LEU B  38 -1  O  ARG B  34   N  GLY B  24           
SHEET    3   B 4 VAL B  49  THR B  55 -1  O  PHE B  50   N  ILE B  37           
SHEET    4   B 4 LYS B  66  PHE B  69 -1  O  LYS B  66   N  THR B  55           
SHEET    1   C 4 CYS C  21  PRO C  25  0                                        
SHEET    2   C 4 GLU C  32  LEU C  38 -1  O  ARG C  34   N  GLY C  24           
SHEET    3   C 4 VAL C  49  THR C  55 -1  O  PHE C  50   N  ILE C  37           
SHEET    4   C 4 LYS C  66  PHE C  69 -1  O  LYS C  66   N  THR C  55           
CISPEP   1 TYR A   60    PRO A   61          0         8.31                     
CISPEP   2 TYR B   60    PRO B   61          0         9.06                     
CISPEP   3 TYR C   60    PRO C   61          0         8.23                     
CRYST1  108.109   36.110  130.568  90.00  99.92  90.00 C 1 2 1      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      0.009250  0.000000  0.001618        0.00000                         
SCALE2      0.000000  0.027693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007775        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system