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Database: PDB
Entry: 1EUV
LinkDB: 1EUV
Original site: 1EUV 
HEADER    HYDROLASE                               17-APR-00   1EUV              
TITLE     X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN             
TITLE    2 COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ULP1 PROTEASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL PROTEASE DOMAIN;                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: UBITQUTIN-LIKE PROTEIN SMT3;                               
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: SMT3 RESIDUES 13-98;                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  10 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  11 ORGANISM_TAXID: 4932;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    SUMO HYDROLASE, UBIQUITIN-LIKE PROTEASE 1, SMT3 HYDROLASE             
KEYWDS   2 DESUMOYLATING ENZYME, CYSTEINE PROTEASE, SUMO PROCESSING             
KEYWDS   3 ENZYME, SMT3 PROCESSING ENZYME, NABH4, THIOHEMIACETAL,               
KEYWDS   4 COVALENT PROTEASE ADDUCT                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MOSSESSOVA,C.D.LIMA                                                 
REVDAT   2   24-FEB-09 1EUV    1       VERSN                                    
REVDAT   1   07-JUN-00 1EUV    0                                                
JRNL        AUTH   E.MOSSESSOVA,C.D.LIMA                                        
JRNL        TITL   ULP1-SUMO CRYSTAL STRUCTURE AND GENETIC ANALYSIS             
JRNL        TITL 2 REVEAL CONSERVED INTERACTIONS AND A REGULATORY               
JRNL        TITL 3 ELEMENT ESSENTIAL FOR CELL GROWTH IN YEAST.                  
JRNL        REF    MOL.CELL                      V.   5   865 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10882122                                                     
JRNL        DOI    10.1016/S1097-2765(00)80326-3                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.J.LI,M.HOCHSTRASSER                                        
REMARK   1  TITL   A NEW PROTEASE REQUIRED FOR CELL-CYCLE PROGRESSION           
REMARK   1  TITL 2 IN YEAST.                                                    
REMARK   1  REF    NATURE                        V. 398   246 1999              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/18457                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 47560                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5% OF THE OBSERVED DATA         
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2378                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 432                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.013 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 1.600 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
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  OTHER REFINEMENT REMARKS: USED A -LOGLIKELIHOOD RESIDUAL            
REMARK   3  DERIVED FROM RICE DISTRIBUTION FOR CENTRIC AND ACENTRIC CASES       
REMARK   3  OF FS SPARSE MATRIX PROCEDURE WITH ANISOTROPIC B-FACTOR             
REMARK   3  REFINEMENT.                                                         
REMARK   4                                                                      
REMARK   4 1EUV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010911.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.                               
REMARK 200  PH                             : 6.5                                
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) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 47875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000                            
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: NULL                         
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.5, 10% W/V                  
REMARK 280  POLYETHYLENE GLYCOL 20000, 3% W/V 1,6-HEXANDIOL, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 294K                           
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       62.88700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.58350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       62.88700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.58350            
REMARK 290   SMTRY3   4  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER CONSTRUCTED FROM        
REMARK 300 CHAIN A.                                                             
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
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 Covalent adduct formed between the proteolytic                       
REMARK 400 active site thiol and the C-terminal glycine of                      
REMARK 400 Smt3 using the reducing agent NaBH4.                                 
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     GLU B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     VAL B    18                                                      
REMARK 465     LYS B    19                                                      
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     PRO B  20    CB   CG   CD                                        
REMARK 470     GLU B  21    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     GLU B  59    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  75    CB   CG   OD1  OD2                                  
REMARK 470     GLU B  84    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  422   CB    CG    CD    NE    CZ    NH1   NH2             
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   NE   ARG A   422     O    HOH A   875              1.12            
REMARK 500   CD   ARG A   422     O    HOH A   875              2.02            
REMARK 500   NE   ARG A   422     O    HOH A   821              2.14            
REMARK 500   CZ   ARG A   422     O    HOH A   875              2.17            
REMARK 500   O    HOH A   906     O    HOH A   949              2.17            
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   625     O    HOH A   892     3548     1.28            
REMARK 500   O    HOH A   625     O    HOH A   895     3548     1.62            
REMARK 500   O    HOH A   672     O    HOH A   908     3558     1.68            
REMARK 500   O    HOH A   662     O    HOH A   931     3558     2.07            
REMARK 500   O    HOH A   642     O    HOH A   931     3558     2.18            
REMARK 500   O    HOH A   645     O    HOH A   908     3558     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 422   CA    ARG A 422   CB     -0.340                       
REMARK 500    GLY B  98   C     GLY B  98   O       0.124                       
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    ASP A 412   CB  -  CG  -  OD1 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    SER A 421   N   -  CA  -  CB  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ARG A 422   CB  -  CA  -  C   ANGL. DEV. =  21.3 DEGREES          
REMARK 500    ARG A 422   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLU A 423   CB  -  CG  -  CD  ANGL. DEV. =  25.8 DEGREES          
REMARK 500    ARG A 446   CD  -  NE  -  CZ  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ARG A 446   NE  -  CZ  -  NH1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 446   NE  -  CZ  -  NH2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A 482   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 499   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 598   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TYR A 601   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    TYR A 601   CB  -  CG  -  CD1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 606   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 608   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  93   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 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    GLU A 423      151.65    112.62                                   
REMARK 500    GLU B  21      -84.41    -87.00                                   
REMARK 500    SER B  32      -37.68   -137.38                                   
REMARK 500    ASP B  75      -22.93    101.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 197        DISTANCE =  8.63 ANGSTROMS                       
REMARK 525    HOH A 846        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 893        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH A 906        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH A 926        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH A 938        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH A 949        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 951        DISTANCE =  5.09 ANGSTROMS                       
DBREF  1EUV A  401   621  UNP    Q02724   ULP1_YEAST     401    621             
DBREF  1EUV B   13    98  UNP    Q12306   SMT3_YEAST      13     98             
SEQADV 1EUV GLY A  401  UNP  Q02724    LYS   401 CLONING ARTIFACTS              
SEQADV 1EUV SER A  402  UNP  Q02724    LYS   402 CLONING ARTIFACTS              
SEQRES   1 A  221  GLY SER LEU VAL PRO GLU LEU ASN GLU LYS ASP ASP ASP          
SEQRES   2 A  221  GLN VAL GLN LYS ALA LEU ALA SER ARG GLU ASN THR GLN          
SEQRES   3 A  221  LEU MET ASN ARG ASP ASN ILE GLU ILE THR VAL ARG ASP          
SEQRES   4 A  221  PHE LYS THR LEU ALA PRO ARG ARG TRP LEU ASN ASP THR          
SEQRES   5 A  221  ILE ILE GLU PHE PHE MET LYS TYR ILE GLU LYS SER THR          
SEQRES   6 A  221  PRO ASN THR VAL ALA PHE ASN SER PHE PHE TYR THR ASN          
SEQRES   7 A  221  LEU SER GLU ARG GLY TYR GLN GLY VAL ARG ARG TRP MET          
SEQRES   8 A  221  LYS ARG LYS LYS THR GLN ILE ASP LYS LEU ASP LYS ILE          
SEQRES   9 A  221  PHE THR PRO ILE ASN LEU ASN GLN SER HIS TRP ALA LEU          
SEQRES  10 A  221  GLY ILE ILE ASP LEU LYS LYS LYS THR ILE GLY TYR VAL          
SEQRES  11 A  221  ASP SER LEU SER ASN GLY PRO ASN ALA MET SER PHE ALA          
SEQRES  12 A  221  ILE LEU THR ASP LEU GLN LYS TYR VAL MET GLU GLU SER          
SEQRES  13 A  221  LYS HIS THR ILE GLY GLU ASP PHE ASP LEU ILE HIS LEU          
SEQRES  14 A  221  ASP CYS PRO GLN GLN PRO ASN GLY TYR ASP CYS GLY ILE          
SEQRES  15 A  221  TYR VAL CYS MET ASN THR LEU TYR GLY SER ALA ASP ALA          
SEQRES  16 A  221  PRO LEU ASP PHE ASP TYR LYS ASP ALA ILE ARG MET ARG          
SEQRES  17 A  221  ARG PHE ILE ALA HIS LEU ILE LEU THR ASP ALA LEU LYS          
SEQRES   1 B   86  GLU VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN          
SEQRES   2 B   86  LEU LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS          
SEQRES   3 B   86  ILE LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA          
SEQRES   4 B   86  PHE ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG          
SEQRES   5 B   86  PHE LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR          
SEQRES   6 B   86  PRO GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU          
SEQRES   7 B   86  ALA HIS ARG GLU GLN ILE GLY GLY                              
FORMUL   3  HOH   *432(H2 O)                                                    
HELIX    1   1 ASN A  408  ALA A  420  1                                  13    
HELIX    2   2 VAL A  437  LYS A  441  1                                   5    
HELIX    3   3 THR A  442  ALA A  444  5                                   3    
HELIX    4   4 ASN A  450  THR A  465  1                                  16    
HELIX    5   5 SER A  473  GLY A  483  1                                  11    
HELIX    6   6 TYR A  484  VAL A  487  5                                   4    
HELIX    7   7 MET A  491  LYS A  495  5                                   5    
HELIX    8   8 GLN A  497  LEU A  501  5                                   5    
HELIX    9   9 ASN A  538  SER A  556  1                                  19    
HELIX   10  10 ASP A  579  ALA A  593  1                                  15    
HELIX   11  11 ASP A  600  THR A  617  1                                  18    
HELIX   12  12 LEU B   45  GLN B   56  1                                  12    
HELIX   13  13 GLU B   59  ASP B   61  5                                   3    
SHEET    1   A 2 GLN A 426  ARG A 430  0                                        
SHEET    2   A 2 ILE A 433  THR A 436 -1  O  ILE A 433   N  ARG A 430           
SHEET    1   B 5 THR A 468  ALA A 470  0                                        
SHEET    2   B 5 LYS A 503  LEU A 510  1  O  LYS A 503   N  VAL A 469           
SHEET    3   B 5 HIS A 514  ASP A 521 -1  O  HIS A 514   N  LEU A 510           
SHEET    4   B 5 THR A 526  VAL A 530 -1  O  THR A 526   N  ASP A 521           
SHEET    5   B 5 ASP A 565  LEU A 569  1  O  ASP A 565   N  ILE A 527           
SHEET    1   C 5 GLU B  34  LYS B  40  0                                        
SHEET    2   C 5 HIS B  23  SER B  29 -1  N  ILE B  24   O  ILE B  39           
SHEET    3   C 5 ASP B  87  ARG B  93  1  O  ASP B  87   N  LYS B  27           
SHEET    4   C 5 LEU B  63  TYR B  67 -1  N  ARG B  64   O  HIS B  92           
SHEET    5   C 5 ILE B  70  ARG B  71 -1  O  ILE B  70   N  TYR B  67           
LINK         SG  CYS A 580                 C   GLY B  98     1555   1555  1.89  
CRYST1  125.774   53.167   54.262  90.00  90.00  90.00 P 21 21 2     4          
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      0.007950  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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