GenomeNet

Database: PDB
Entry: 1KPS
LinkDB: 1KPS
Original site: 1KPS 
HEADER    LIGASE/PROTEIN TRANSPORT                02-JAN-02   1KPS              
TITLE     STRUCTURAL BASIS FOR E2-MEDIATED SUMO CONJUGATION REVEALED BY A       
TITLE    2 COMPLEX BETWEEN UBIQUITIN CONJUGATING ENZYME UBC9 AND RANGAP1        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-LIKE PROTEIN SUMO-1 CONJUGATING ENZYME;          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: UBC9, SUMO-1-PROTEIN LIGASE, UBIQUITIN CARRIER PROTEIN;     
COMPND   5 EC: 6.3.2.19;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RAN-GTPASE ACTIVATING PROTEIN 1;                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: RANGAP1;                                                    
COMPND  11 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: UBC9;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: RANGAP1;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28B-PSUMO                     
KEYWDS    SUMO, UBIQUITIN, E2, CONJUGATING ENZYME, LIGASE, THIOESTER, SMALL     
KEYWDS   2 UBIQUITIN-LIKE MODIFIER, LIGASE-PROTEIN TRANSPORT COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.BERNIER-VILLAMOR,D.A.SAMPSON,M.J.MATUNIS,C.D.LIMA                   
REVDAT   3   11-OCT-17 1KPS    1       REMARK                                   
REVDAT   2   24-FEB-09 1KPS    1       VERSN                                    
REVDAT   1   13-FEB-02 1KPS    0                                                
JRNL        AUTH   V.BERNIER-VILLAMOR,D.A.SAMPSON,M.J.MATUNIS,C.D.LIMA          
JRNL        TITL   STRUCTURAL BASIS FOR E2-MEDIATED SUMO CONJUGATION REVEALED   
JRNL        TITL 2 BY A COMPLEX BETWEEN UBIQUITIN-CONJUGATING ENZYME UBC9 AND   
JRNL        TITL 3 RANGAP1.                                                     
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 108   345 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11853669                                                     
JRNL        DOI    10.1016/S0092-8674(02)00630-X                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3260494.140                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 27248                          
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) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1343                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4114                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 205                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4932                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 585                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.61000                                              
REMARK   3    B22 (A**2) : -11.18000                                            
REMARK   3    B33 (A**2) : 1.57000                                              
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.52                            
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) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.940                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 37.48                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KPS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000015208.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790, 0.9793, 0.9788, 0.9712     
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27248                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 3 WAVELENGTH MAD DATASET     
REMARK 200  COLLECTED AT NSLS BEAMLINE X4A TO 2.8A                              
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM PHOSPHATE, 0.1M HEPES,     
REMARK 280  10MM CUCL2, 5% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       43.26550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.25450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.26550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.25450            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER B   419                                                      
REMARK 465     ASN B   420                                                      
REMARK 465     SER B   421                                                      
REMARK 465     GLY B   422                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     PRO B   424                                                      
REMARK 465     ALA B   425                                                      
REMARK 465     PRO B   426                                                      
REMARK 465     VAL B   427                                                      
REMARK 465     LEU B   428                                                      
REMARK 465     SER B   429                                                      
REMARK 465     SER B   430                                                      
REMARK 465     PRO B   431                                                      
REMARK 465     THR B   432                                                      
REMARK 465     PRO B   433                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     SER D   419                                                      
REMARK 465     ASN D   420                                                      
REMARK 465     SER D   421                                                      
REMARK 465     GLY D   422                                                      
REMARK 465     GLU D   423                                                      
REMARK 465     PRO D   424                                                      
REMARK 465     ALA D   425                                                      
REMARK 465     PRO D   426                                                      
REMARK 465     VAL D   427                                                      
REMARK 465     LEU D   428                                                      
REMARK 465     SER D   429                                                      
REMARK 465     SER D   430                                                      
REMARK 465     PRO D   431                                                      
REMARK 465     THR D   432                                                      
REMARK 465     PRO D   433                                                      
REMARK 465     THR D   434                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR B 434    CB   OG1  CG2                                       
REMARK 470     ASP D 435    CB   CG   OD1  OD2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   682     O    HOH B   682     2565     1.75            
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    MET A   1       77.27   -151.97                                   
REMARK 500    LEU A   6      -10.95    -49.10                                   
REMARK 500    ASP A  19      104.43   -178.25                                   
REMARK 500    PRO A  32      -18.73    -43.65                                   
REMARK 500    TYR A  68      135.86    -38.87                                   
REMARK 500    HIS A  83      129.23   -172.04                                   
REMARK 500    LYS A 101     -132.65   -133.41                                   
REMARK 500    GLN B 462       20.28    -76.30                                   
REMARK 500    SER B 466      -13.41   -148.18                                   
REMARK 500    ASN B 569        8.03    153.05                                   
REMARK 500    THR B 574     -156.04   -148.94                                   
REMARK 500    CYS B 575       41.99    -88.95                                   
REMARK 500    SER B 576      154.51    -41.29                                   
REMARK 500    ALA C  26       91.84   -165.40                                   
REMARK 500    LEU C  38       -5.39    -55.25                                   
REMARK 500    PRO C  52       -6.72    -55.31                                   
REMARK 500    HIS C  83      126.76   -170.48                                   
REMARK 500    ASP C 100       32.37    -62.76                                   
REMARK 500    LYS C 101     -125.94   -163.19                                   
REMARK 500    ASN C 140       63.44    177.73                                   
REMARK 500    PHE C 155       26.66    -78.13                                   
REMARK 500    SER D 444      147.16   -173.27                                   
REMARK 500    ARG D 450       30.62    -65.21                                   
REMARK 500    GLN D 462      -16.55    -49.75                                   
REMARK 500    THR D 465       12.47    -60.53                                   
REMARK 500    CYS D 506      104.19    -55.07                                   
REMARK 500    LYS D 530      102.13    -29.59                                   
REMARK 500    GLU D 573     -113.09    -17.92                                   
REMARK 500    THR D 574      -16.03   -168.64                                   
REMARK 500    CYS D 575      102.77    170.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 604                 
DBREF  1KPS A    1   158  UNP    P63279   UBE2I_HUMAN      1    158             
DBREF  1KPS B  420   589  UNP    P46061   RGP1_MOUSE     420    589             
DBREF  1KPS C    1   158  UNP    P63279   UBE2I_HUMAN      1    158             
DBREF  1KPS D  420   589  UNP    P46061   RGP1_MOUSE     420    589             
SEQADV 1KPS SER A    0  UNP  P63279              CLONING ARTIFACT               
SEQADV 1KPS SER C    0  UNP  P63279              CLONING ARTIFACT               
SEQADV 1KPS SER B  419  UNP  P46061              CLONING ARTIFACT               
SEQADV 1KPS SER D  419  UNP  P46061              CLONING ARTIFACT               
SEQRES   1 A  159  SER MET SER GLY ILE ALA LEU SER ARG LEU ALA GLN GLU          
SEQRES   2 A  159  ARG LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY PHE VAL          
SEQRES   3 A  159  ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET ASN LEU          
SEQRES   4 A  159  MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS GLY THR          
SEQRES   5 A  159  PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET LEU PHE          
SEQRES   6 A  159  LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS LYS PHE          
SEQRES   7 A  159  GLU PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO SER GLY          
SEQRES   8 A  159  THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS ASP TRP          
SEQRES   9 A  159  ARG PRO ALA ILE THR ILE LYS GLN ILE LEU LEU GLY ILE          
SEQRES  10 A  159  GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP PRO ALA          
SEQRES  11 A  159  GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN ARG VAL          
SEQRES  12 A  159  GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS LYS PHE          
SEQRES  13 A  159  ALA PRO SER                                                  
SEQRES   1 B  171  SER ASN SER GLY GLU PRO ALA PRO VAL LEU SER SER PRO          
SEQRES   2 B  171  THR PRO THR ASP LEU SER THR PHE LEU SER PHE PRO SER          
SEQRES   3 B  171  PRO GLU LYS LEU LEU ARG LEU GLY PRO LYS VAL SER VAL          
SEQRES   4 B  171  LEU ILE VAL GLN GLN THR ASP THR SER ASP PRO GLU LYS          
SEQRES   5 B  171  VAL VAL SER ALA PHE LEU LYS VAL ALA SER VAL PHE ARG          
SEQRES   6 B  171  ASP ASP ALA SER VAL LYS THR ALA VAL LEU ASP ALA ILE          
SEQRES   7 B  171  ASP ALA LEU MET LYS LYS ALA PHE SER CYS SER SER PHE          
SEQRES   8 B  171  ASN SER ASN THR PHE LEU THR ARG LEU LEU ILE HIS MET          
SEQRES   9 B  171  GLY LEU LEU LYS SER GLU ASP LYS ILE LYS ALA ILE PRO          
SEQRES  10 B  171  SER LEU HIS GLY PRO LEU MET VAL LEU ASN HIS VAL VAL          
SEQRES  11 B  171  ARG GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU LEU          
SEQRES  12 B  171  LEU ALA PHE VAL THR LYS PRO ASN GLY ALA LEU GLU THR          
SEQRES  13 B  171  CYS SER PHE ALA ARG HIS ASN LEU LEU GLN THR LEU TYR          
SEQRES  14 B  171  ASN ILE                                                      
SEQRES   1 C  159  SER MET SER GLY ILE ALA LEU SER ARG LEU ALA GLN GLU          
SEQRES   2 C  159  ARG LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY PHE VAL          
SEQRES   3 C  159  ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET ASN LEU          
SEQRES   4 C  159  MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS GLY THR          
SEQRES   5 C  159  PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET LEU PHE          
SEQRES   6 C  159  LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS LYS PHE          
SEQRES   7 C  159  GLU PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO SER GLY          
SEQRES   8 C  159  THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS ASP TRP          
SEQRES   9 C  159  ARG PRO ALA ILE THR ILE LYS GLN ILE LEU LEU GLY ILE          
SEQRES  10 C  159  GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP PRO ALA          
SEQRES  11 C  159  GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN ARG VAL          
SEQRES  12 C  159  GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS LYS PHE          
SEQRES  13 C  159  ALA PRO SER                                                  
SEQRES   1 D  171  SER ASN SER GLY GLU PRO ALA PRO VAL LEU SER SER PRO          
SEQRES   2 D  171  THR PRO THR ASP LEU SER THR PHE LEU SER PHE PRO SER          
SEQRES   3 D  171  PRO GLU LYS LEU LEU ARG LEU GLY PRO LYS VAL SER VAL          
SEQRES   4 D  171  LEU ILE VAL GLN GLN THR ASP THR SER ASP PRO GLU LYS          
SEQRES   5 D  171  VAL VAL SER ALA PHE LEU LYS VAL ALA SER VAL PHE ARG          
SEQRES   6 D  171  ASP ASP ALA SER VAL LYS THR ALA VAL LEU ASP ALA ILE          
SEQRES   7 D  171  ASP ALA LEU MET LYS LYS ALA PHE SER CYS SER SER PHE          
SEQRES   8 D  171  ASN SER ASN THR PHE LEU THR ARG LEU LEU ILE HIS MET          
SEQRES   9 D  171  GLY LEU LEU LYS SER GLU ASP LYS ILE LYS ALA ILE PRO          
SEQRES  10 D  171  SER LEU HIS GLY PRO LEU MET VAL LEU ASN HIS VAL VAL          
SEQRES  11 D  171  ARG GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU LEU          
SEQRES  12 D  171  LEU ALA PHE VAL THR LYS PRO ASN GLY ALA LEU GLU THR          
SEQRES  13 D  171  CYS SER PHE ALA ARG HIS ASN LEU LEU GLN THR LEU TYR          
SEQRES  14 D  171  ASN ILE                                                      
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    SO4  C 602       5                                                       
HET    SO4  D 601       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *585(H2 O)                                                    
HELIX    1   1 ILE A    4  ASP A   19  1                                  16    
HELIX    2   2 LEU A   94  GLU A   98  5                                   5    
HELIX    3   3 THR A  108  GLU A  122  1                                  15    
HELIX    4   4 GLN A  130  ASN A  140  1                                  11    
HELIX    5   5 ASN A  140  PHE A  155  1                                  16    
HELIX    6   6 ASP B  435  PHE B  442  1                                   8    
HELIX    7   7 SER B  444  LEU B  451  1                                   8    
HELIX    8   8 LYS B  454  GLN B  462  1                                   9    
HELIX    9   9 ASP B  467  VAL B  481  1                                  15    
HELIX   10  10 ASP B  485  CYS B  506  1                                  22    
HELIX   11  11 ASN B  510  MET B  522  1                                  13    
HELIX   12  12 LEU B  537  GLN B  550  1                                  14    
HELIX   13  13 PRO B  554  ALA B  556  5                                   3    
HELIX   14  14 LEU B  557  THR B  566  1                                  10    
HELIX   15  15 SER B  576  ILE B  589  1                                  14    
HELIX   16  16 ILE C    4  ASP C   19  1                                  16    
HELIX   17  17 LEU C   94  GLU C   98  5                                   5    
HELIX   18  18 THR C  108  GLU C  122  1                                  15    
HELIX   19  19 GLN C  130  ASN C  140  1                                  11    
HELIX   20  20 ASN C  140  PHE C  155  1                                  16    
HELIX   21  21 ASP D  435  PHE D  442  1                                   8    
HELIX   22  22 SER D  444  ARG D  450  1                                   7    
HELIX   23  23 LEU D  451  PRO D  453  5                                   3    
HELIX   24  24 LYS D  454  THR D  463  1                                  10    
HELIX   25  25 ASP D  467  VAL D  481  1                                  15    
HELIX   26  26 ASP D  485  CYS D  506  1                                  22    
HELIX   27  27 ASN D  510  MET D  522  1                                  13    
HELIX   28  28 LEU D  537  GLN D  550  1                                  14    
HELIX   29  29 PRO D  554  ALA D  556  5                                   3    
HELIX   30  30 LEU D  557  THR D  566  1                                  10    
HELIX   31  31 SER D  576  ILE D  589  1                                  14    
SHEET    1   A 4 VAL A  25  LYS A  30  0                                        
SHEET    2   A 4 MET A  36  PRO A  46 -1  O  GLU A  42   N  VAL A  27           
SHEET    3   A 4 LEU A  57  LEU A  63 -1  O  PHE A  58   N  ILE A  45           
SHEET    4   A 4 LYS A  74  PHE A  77 -1  O  LYS A  76   N  ARG A  61           
SHEET    1   B 4 VAL C  25  LYS C  30  0                                        
SHEET    2   B 4 MET C  36  PRO C  46 -1  O  ASN C  37   N  THR C  29           
SHEET    3   B 4 LEU C  57  LEU C  63 -1  O  PHE C  58   N  ILE C  45           
SHEET    4   B 4 LYS C  74  PHE C  77 -1  O  LYS C  76   N  ARG C  61           
SSBOND   1 CYS A  138    CYS D  575                          1555   1555  2.04  
SSBOND   2 CYS B  575    CYS C  138                          1555   1555  2.02  
CISPEP   1 TYR A   68    PRO A   69          0        -0.09                     
CISPEP   2 GLU A   78    PRO A   79          0         0.04                     
CISPEP   3 TYR C   68    PRO C   69          0         0.95                     
CISPEP   4 GLU C   78    PRO C   79          0        -0.29                     
SITE     1 AC1  4 SER D 536  LEU D 537  HIS D 538  HOH D 681                    
SITE     1 AC2  6 GLY C  47  LYS C  48  LYS C  49  GLN C 117                    
SITE     2 AC2  6 HOH C 656  HOH C 724                                          
SITE     1 AC3  3 SER B 536  LEU B 537  HIS B 538                               
SITE     1 AC4  4 LYS B 502  HOH B 660  HOH B 683  LYS D 502                    
CRYST1   86.531  126.509   72.639  90.00  90.00  90.00 P 21 21 2     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      0.011557  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013767        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system