GenomeNet

Database: PDB
Entry: 2UYZ
LinkDB: 2UYZ
Original site: 2UYZ 
HEADER    LIGASE                                  21-APR-07   2UYZ              
TITLE     NON-COVALENT COMPLEX BETWEEN UBC9 AND SUMO1                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUMO-CONJUGATING ENZYME UBC9;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SUMO-PROTEIN LIGASE, UBIQUITIN-CONJUGATING ENZYME E2 I,     
COMPND   5 UBIQUITIN-PROTEIN LIGASE I, UBIQUITIN CARRIER PROTEIN I, UBIQUITIN   
COMPND   6 CARRIER PROTEIN 9, MUBC9;                                            
COMPND   7 EC: 6.3.2.19;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: START METHIONINE (1) AND SECOND SERINE (2) ARE MISSING
COMPND  11 IN STRUCTURE;                                                        
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: SMALL UBIQUITIN-RELATED MODIFIER 1;                        
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: RESIDUES 20-97;                                            
COMPND  16 SYNONYM: SUMO-1, SENTRIN, UBIQUITIN-LIKE PROTEIN SMT3C, SMT3 HOMOLOG 
COMPND  17 3, UBIQUITIN-HOMOLOGY DOMAIN PROTEIN PIC1, UBIQUITIN-LIKE PROTEIN    
COMPND  18 UBL1, GAP-MODIFYING PROTEIN 1, GMP1, SUMO1;                          
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET23A;                                    
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: PET11A                                     
KEYWDS    SUMOYLATION, CELL DIVISION, NUCLEAR PROTEIN, UBIQUITIN-LIKE MODIFIER, 
KEYWDS   2 UBL CONJUGATION PATHWAY, CONJUGATING ENZYME, CHROMOSOME PARTITION,   
KEYWDS   3 E2, UBC9, SUMO1, LIGASE, MITOSIS, CELL CYCLE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.KNIPSCHEER,W.J.VAN DIJK,J.V.OLSEN,M.MANN,T.K.SIXMA                  
REVDAT   4   28-MAR-18 2UYZ    1       SOURCE AUTHOR JRNL                       
REVDAT   3   24-FEB-09 2UYZ    1       VERSN                                    
REVDAT   2   03-JUL-07 2UYZ    1       JRNL                                     
REVDAT   1   12-JUN-07 2UYZ    0                                                
JRNL        AUTH   P.KNIPSCHEER,W.J.VAN DIJK,J.V.OLSEN,M.MANN,T.K.SIXMA         
JRNL        TITL   NONCOVALENT INTERACTION BETWEEN UBC9 AND SUMO PROMOTES SUMO  
JRNL        TITL 2 CHAIN FORMATION.                                             
JRNL        REF    EMBO J.                       V.  26  2797 2007              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   17491593                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7601711                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 46681                          
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) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.141                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2482                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3398                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 163                          
REMARK   3   BIN FREE R VALUE                    : 0.2160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1893                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 408                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.30000                                             
REMARK   3    B22 (A**2) : 0.40000                                              
REMARK   3    B33 (A**2) : -0.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.20000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.066         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.031         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.668         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2206 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1596 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3014 ; 1.556 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3927 ; 0.937 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   289 ; 5.722 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;34.284 ;24.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   429 ;12.386 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;12.991 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   308 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2539 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   435 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   468 ; 0.235 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1685 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1050 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1121 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   272 ; 0.253 ; 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):     5 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    33 ; 0.222 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    40 ; 0.250 ; 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):  1336 ; 1.412 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2207 ; 2.170 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   895 ; 2.993 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   804 ; 4.382 ; 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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2UYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290032280.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49557                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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 1U9A, 2BF8                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.5 % (W/V) PEG3350 100 MM BISTRIS PH   
REMARK 280  5.5 15 % (W/V) GLYCEROL, PH 5.50                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       17.51500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 93 TO SER                         
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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY B    97                                                      
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 B  2127     O    HOH B  2128              1.58            
REMARK 500   O    HOH A  2039     O    HOH A  2110              1.74            
REMARK 500   NZ   LYS A    18     O    HOH A  2036              1.83            
REMARK 500   NZ   LYS A    48     O    HOH A  2094              1.92            
REMARK 500   OD1  ASP A   127     O    HOH A  2207              1.94            
REMARK 500   OE1  GLN B    29     O    HOH B  2039              1.98            
REMARK 500   O    HOH A  2031     O    HOH B  2130              2.02            
REMARK 500   O    HOH A  2148     O    HOH A  2157              2.03            
REMARK 500   O    HOH B  2046     O    HOH B  2047              2.05            
REMARK 500   O    HOH A  2147     O    HOH A  2154              2.09            
REMARK 500   O    HOH A  2236     O    HOH A  2239              2.15            
REMARK 500   O    PRO A   157     O    HOH A  2259              2.17            
REMARK 500   O    HOH B  2122     O    HOH B  2124              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A  2129     O    HOH A  2171     2456     1.92            
REMARK 500   O    HOH A  2196     O    HOH B  2054     1455     2.14            
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    ASP A  19      115.83   -161.22                                   
REMARK 500    ASP A  19      117.26   -170.08                                   
REMARK 500    HIS A  83      139.51   -170.27                                   
REMARK 500    LYS A 101     -106.86   -112.15                                   
REMARK 500    ASN A 140       76.92   -155.29                                   
REMARK 500    ASP B  30        8.38    -62.49                                   
REMARK 500    SER B  31        4.89     81.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1159  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2140   O                                                      
REMARK 620 2 HOH A2154   O    88.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1159                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1U9A   RELATED DB: PDB                                   
REMARK 900 HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9                              
REMARK 900 RELATED ID: 1U9B   RELATED DB: PDB                                   
REMARK 900 MURINE/HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9                       
REMARK 900 RELATED ID: 1A5R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN -RELATED MODIFIER     
REMARK 900 SUMO-1, NMR, 10 STRUCTURES                                           
REMARK 900 RELATED ID: 1TGZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN SENP2 IN COMPLEX WITH SUMO-1                      
REMARK 900 RELATED ID: 1WYW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SUMO1-CONJUGATED THYMINE DNAGLYCOSYLASE         
REMARK 900 RELATED ID: 1Y8R   RELATED DB: PDB                                   
REMARK 900 SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1- MG-ATP COMPLEX            
REMARK 900 RELATED ID: 1Z5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN UBC9 , SUMO-1,RANGAP1 AND     
REMARK 900 NUP358/RANBP2                                                        
REMARK 900 RELATED ID: 2ASQ   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF SUMO-1 IN COMPLEX WITH A SUMO-BINDINGMOTIF     
REMARK 900 (SBM)                                                                
REMARK 900 RELATED ID: 2BF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-  
REMARK 900 25K                                                                  
REMARK 900 RELATED ID: 2G4D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SENP1 MUTANT ( C603S) IN COMPLEXWITH      
REMARK 900 SUMO-1                                                               
REMARK 900 RELATED ID: 2IO2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SENP2 IN COMPLEX WITH RANGAP1-SUMO-1      
REMARK 900 RELATED ID: 2IY0   RELATED DB: PDB                                   
REMARK 900 SENP1 (MUTANT) SUMO1 RANGAP                                          
REMARK 900 RELATED ID: 2IY1   RELATED DB: PDB                                   
REMARK 900 SENP1 (MUTANT) FULL LENGTH SUMO1                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 C93S MUTANT                                                          
DBREF  2UYZ A    1   158  UNP    P63280   UBC9_MOUSE       1    158             
DBREF  2UYZ B   19    19  PDB    2UYZ     2UYZ            19     19             
DBREF  2UYZ B   20    97  UNP    P63165   SUMO1_HUMAN     20     97             
SEQADV 2UYZ SER A   93  UNP  P63280    CYS    93 ENGINEERED MUTATION            
SEQRES   1 A  158  MET SER GLY ILE ALA LEU SER ARG LEU ALA GLN GLU ARG          
SEQRES   2 A  158  LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY PHE VAL ALA          
SEQRES   3 A  158  VAL PRO THR LYS ASN PRO ASP GLY THR MET ASN LEU MET          
SEQRES   4 A  158  ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS GLY THR PRO          
SEQRES   5 A  158  TRP GLU GLY GLY LEU PHE LYS LEU ARG MET LEU PHE LYS          
SEQRES   6 A  158  ASP ASP TYR PRO SER SER PRO PRO LYS CYS LYS PHE GLU          
SEQRES   7 A  158  PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO SER GLY THR          
SEQRES   8 A  158  VAL SER LEU SER ILE LEU GLU GLU ASP LYS ASP TRP ARG          
SEQRES   9 A  158  PRO ALA ILE THR ILE LYS GLN ILE LEU LEU GLY ILE GLN          
SEQRES  10 A  158  GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP PRO ALA GLN          
SEQRES  11 A  158  ALA GLU ALA TYR THR ILE TYR CYS GLN ASN ARG VAL GLU          
SEQRES  12 A  158  TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS LYS PHE ALA          
SEQRES  13 A  158  PRO SER                                                      
SEQRES   1 B   79  MET GLU TYR ILE LYS LEU LYS VAL ILE GLY GLN ASP SER          
SEQRES   2 B   79  SER GLU ILE HIS PHE LYS VAL LYS MET THR THR HIS LEU          
SEQRES   3 B   79  LYS LYS LEU LYS GLU SER TYR CYS GLN ARG GLN GLY VAL          
SEQRES   4 B   79  PRO MET ASN SER LEU ARG PHE LEU PHE GLU GLY GLN ARG          
SEQRES   5 B   79  ILE ALA ASP ASN HIS THR PRO LYS GLU LEU GLY MET GLU          
SEQRES   6 B   79  GLU GLU ASP VAL ILE GLU VAL TYR GLN GLU GLN THR GLY          
SEQRES   7 B   79  GLY                                                          
HET     NA  A1159       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  HOH   *408(H2 O)                                                    
HELIX    1   1 GLY A    3  ASP A   19  1                                  17    
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 LEU B   44  GLY B   56  1                                  13    
HELIX    7   7 PRO B   58  ASN B   60  5                                   3    
HELIX    8   8 THR B   76  GLY B   81  1                                   6    
SHEET    1  AA 4 VAL A  25  LYS A  30  0                                        
SHEET    2  AA 4 MET A  36  PRO A  46 -1  N  ASN A  37   O  THR A  29           
SHEET    3  AA 4 LEU A  57  LEU A  63 -1  O  PHE A  58   N  ILE A  45           
SHEET    4  AA 4 LYS A  74  PHE A  77 -1  O  LYS A  74   N  LEU A  63           
SHEET    1  BA 5 GLU B  33  LYS B  39  0                                        
SHEET    2  BA 5 TYR B  21  ILE B  27 -1  O  ILE B  22   N  VAL B  38           
SHEET    3  BA 5 ASP B  86  GLN B  92  1  O  ASP B  86   N  LYS B  25           
SHEET    4  BA 5 LEU B  62  PHE B  66 -1  O  ARG B  63   N  TYR B  91           
SHEET    5  BA 5 GLN B  69  ARG B  70 -1  O  GLN B  69   N  PHE B  66           
LINK        NA    NA A1159                 O   HOH A2140     1555   1555  2.15  
LINK        NA    NA A1159                 O   HOH A2154     1555   1555  2.28  
CISPEP   1 TYR A   68    PRO A   69          0         6.53                     
CISPEP   2 GLU A   78    PRO A   79          0         1.61                     
CISPEP   3 THR B   95    GLY B   96          0        -1.26                     
SITE     1 AC1  6 TYR A  87  SER A  93  GLU A  98  HOH A2140                    
SITE     2 AC1  6 HOH A2154  HOH A2157                                          
CRYST1   49.481   35.030   72.915  90.00  93.41  90.00 P 1 21 1      2          
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      0.020210  0.000000  0.001204        0.00000                         
SCALE2      0.000000  0.028547  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013739        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system