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Database: PDB
Entry: 4P0Q
LinkDB: 4P0Q
Original site: 4P0Q 
HEADER    HYDROLASE/DNA                           22-FEB-14   4P0Q              
TITLE     CRYSTAL STRUCTURE OF HUMAN MUS81-EME1 IN COMPLEX WITH 5'-FLAP DNA     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CROSSOVER JUNCTION ENDONUCLEASE MUS81;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.22.-;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CROSSOVER JUNCTION ENDONUCLEASE EME1;                      
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: MMS4 HOMOLOG,HMMS4;                                         
COMPND  10 EC: 3.1.22.-;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA GAATGTGTGTCTCAATC;                                     
COMPND  14 CHAIN: E;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: DNA GGATTG;                                                
COMPND  18 CHAIN: F;                                                            
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: DNA TAACCAGACACACATT;                                      
COMPND  22 CHAIN: G;                                                            
COMPND  23 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: MUS81;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: EME1, MMS4;                                                    
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  20 ORGANISM_TAXID: 32630;                                               
SOURCE  21 MOL_ID: 4;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  24 ORGANISM_TAXID: 32630;                                               
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  28 ORGANISM_TAXID: 32630                                                
KEYWDS    RESOLVASE, HYDROLASE-DNA COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.H.GWON,K.BAEK,Y.CHO                                                 
REVDAT   2   14-JAN-15 4P0Q    1       DBREF                                    
REVDAT   1   28-MAY-14 4P0Q    0                                                
JRNL        AUTH   G.H.GWON,A.JO,K.BAEK,K.S.JIN,Y.FU,J.B.LEE,Y.KIM,Y.CHO        
JRNL        TITL   CRYSTAL STRUCTURES OF THE STRUCTURE-SELECTIVE NUCLEASE       
JRNL        TITL 2 MUS81-EME1 BOUND TO FLAP DNA SUBSTRATES.                     
JRNL        REF    EMBO J.                       V.  33  1061 2014              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   24733841                                                     
JRNL        DOI    10.1002/EMBJ.201487820                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24741                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1269                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.4562 -  5.9252    0.92     2622   130  0.2397 0.2769        
REMARK   3     2  5.9252 -  4.7050    0.99     2677   161  0.2508 0.2753        
REMARK   3     3  4.7050 -  4.1108    1.00     2643   144  0.2167 0.2682        
REMARK   3     4  4.1108 -  3.7352    1.00     2638   140  0.2360 0.2624        
REMARK   3     5  3.7352 -  3.4676    1.00     2613   144  0.2420 0.2537        
REMARK   3     6  3.4676 -  3.2632    1.00     2596   144  0.2573 0.2966        
REMARK   3     7  3.2632 -  3.0999    1.00     2603   141  0.2706 0.3005        
REMARK   3     8  3.0999 -  2.9650    1.00     2603   132  0.2865 0.3133        
REMARK   3     9  2.9650 -  2.8508    0.94     2477   133  0.3012 0.3402        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           5336                                  
REMARK   3   ANGLE     :  0.732           7359                                  
REMARK   3   CHIRALITY :  0.045            848                                  
REMARK   3   PLANARITY :  0.003            830                                  
REMARK   3   DIHEDRAL  : 20.078           2054                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4P0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200444.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, ETHANOL, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
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       43.20450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      114.18850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.20450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      114.18850            
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 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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, G, F                         
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 A   246                                                      
REMARK 465     ALA A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     GLY A   281                                                      
REMARK 465     ASN A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     GLU A   440                                                      
REMARK 465     SER A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     ALA A   443                                                      
REMARK 465     MET A   444                                                      
REMARK 465     THR A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     GLN B   179                                                      
REMARK 465     SER B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     ALA B   184                                                      
REMARK 465     VAL B   185                                                      
REMARK 465     THR B   186                                                      
REMARK 465     LYS B   187                                                      
REMARK 465     THR B   188                                                      
REMARK 465     ASN B   189                                                      
REMARK 465     SER B   190                                                      
REMARK 465     ASP B   191                                                      
REMARK 465     ILE B   192                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     PRO B   194                                                      
REMARK 465     PRO B   195                                                      
REMARK 465     GLN B   196                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     THR B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     PRO B   201                                                      
REMARK 465     SER B   202                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     VAL B   205                                                      
REMARK 465     GLN B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     ARG B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     SER B   210                                                      
REMARK 465     HIS B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     CYS B   213                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     GLN B   215                                                      
REMARK 465     GLN B   216                                                      
REMARK 465     ARG B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     ARG B   220                                                      
REMARK 465     GLN B   221                                                      
REMARK 465     LYS B   222                                                      
REMARK 465     GLU B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     LEU B   226                                                      
REMARK 465     ARG B   227                                                      
REMARK 465     ARG B   228                                                      
REMARK 465     GLN B   229                                                      
REMARK 465     GLU B   230                                                      
REMARK 465     ARG B   231                                                      
REMARK 465     LYS B   232                                                      
REMARK 465     GLN B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     LEU B   333                                                      
REMARK 465     ASP B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     MET B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     LYS B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     SER B   371                                                      
REMARK 465     ALA B   372                                                      
REMARK 465     GLN B   373                                                      
REMARK 465     ASN B   374                                                      
REMARK 465     PRO B   375                                                      
REMARK 465     PRO B   376                                                      
REMARK 465     ARG B   377                                                      
REMARK 465     ARG B   378                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     LYS B   380                                                      
REMARK 465     GLN B   381                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     ASN B   384                                                      
REMARK 465     LYS B   385                                                      
REMARK 465     GLN B   386                                                      
REMARK 465     THR B   387                                                      
REMARK 465     LYS B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     GLN B   390                                                      
REMARK 465     GLN B   391                                                      
REMARK 465     GLN B   392                                                      
REMARK 465     ARG B   393                                                      
REMARK 465     GLN B   394                                                      
REMARK 465     PRO B   395                                                      
REMARK 465     GLU B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     ILE B   399                                                      
REMARK 465     GLY B   400                                                      
REMARK 465     SER B   401                                                      
REMARK 465     MET B   402                                                      
REMARK 465     GLY B   535                                                      
REMARK 465     GLU B   536                                                      
REMARK 465     GLY B   537                                                      
REMARK 465     VAL B   538                                                      
REMARK 465     THR B   539                                                      
REMARK 465     SER B   540                                                      
REMARK 465     ASP B   567                                                      
REMARK 465     SER B   568                                                      
REMARK 465     ALA B   569                                                      
REMARK 465     ASP B   570                                                      
REMARK 465      DT G    23                                                      
REMARK 465      DA G    24                                                      
REMARK 465      DA G    25                                                      
REMARK 465      DC G    26                                                      
REMARK 465      DC G    27                                                      
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     GLY A 533    O                                                   
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    LEU B   256     O    HOH B   610              2.02            
REMARK 500   OG   SER A   486     OP1   DA G    34              2.16            
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     DG E   1   C3' -  C2' -  C1' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DG E   1   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DC E  13   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DG G  29   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA G  30   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DA G  34   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA G  36   O4' -  C1' -  N9  ANGL. DEV. =   2.9 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    PRO A 259      113.29    -32.48                                   
REMARK 500    HIS A 283       34.58    -85.71                                   
REMARK 500    GLU A 370       72.75     46.57                                   
REMARK 500    GLU B 367      -72.87   -143.83                                   
REMARK 500    LYS B 368      -75.19    -71.27                                   
REMARK 500    SER B 463     -119.11     55.25                                   
REMARK 500    ALA B 474     -150.57    -88.00                                   
REMARK 500    PRO B 505       23.48    -69.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P0P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P0R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P0S   RELATED DB: PDB                                   
DBREF  4P0Q A  246   551  UNP    Q96NY9   MUS81_HUMAN    246    551             
DBREF  4P0Q B  178   570  UNP    Q96AY2   EME1_HUMAN     178    570             
DBREF  4P0Q E    1    17  PDB    4P0Q     4P0Q             1     17             
DBREF  4P0Q F   21    26  PDB    4P0Q     4P0Q            21     26             
DBREF  4P0Q G   23    38  PDB    4P0Q     4P0Q            23     38             
SEQRES   1 A  306  SER ALA GLU LEU ALA SER GLU ALA GLY VAL GLN GLN GLN          
SEQRES   2 A  306  PRO LEU GLU LEU ARG PRO GLY GLU TYR ARG VAL LEU LEU          
SEQRES   3 A  306  CYS VAL ASP ILE GLY GLU THR ARG GLY GLY GLY HIS ARG          
SEQRES   4 A  306  PRO GLU LEU LEU ARG GLU LEU GLN ARG LEU HIS VAL THR          
SEQRES   5 A  306  HIS THR VAL ARG LYS LEU HIS VAL GLY ASP PHE VAL TRP          
SEQRES   6 A  306  VAL ALA GLN GLU THR ASN PRO ARG ASP PRO ALA ASN PRO          
SEQRES   7 A  306  GLY GLU LEU VAL LEU ASP HIS ILE VAL GLU ARG LYS ARG          
SEQRES   8 A  306  LEU ASP ASP LEU CYS SER SER ILE ILE ASP GLY ARG PHE          
SEQRES   9 A  306  ARG GLU GLN LYS PHE ARG LEU LYS ARG CYS GLY LEU GLU          
SEQRES  10 A  306  ARG ARG VAL TYR LEU VAL GLU GLU HIS GLY SER VAL HIS          
SEQRES  11 A  306  ASN LEU SER LEU PRO GLU SER THR LEU LEU GLN ALA VAL          
SEQRES  12 A  306  THR ASN THR GLN VAL ILE ASP GLY PHE PHE VAL LYS ARG          
SEQRES  13 A  306  THR ALA ASP ILE LYS GLU SER ALA ALA TYR LEU ALA LEU          
SEQRES  14 A  306  LEU THR ARG GLY LEU GLN ARG LEU TYR GLN GLY HIS THR          
SEQRES  15 A  306  LEU ARG SER ARG PRO TRP GLY THR PRO GLY ASN PRO GLU          
SEQRES  16 A  306  SER GLY ALA MET THR SER PRO ASN PRO LEU CYS SER LEU          
SEQRES  17 A  306  LEU THR PHE SER ASP PHE ASN ALA GLY ALA ILE LYS ASN          
SEQRES  18 A  306  LYS ALA GLN SER VAL ARG GLU VAL PHE ALA ARG GLN LEU          
SEQRES  19 A  306  MET GLN VAL ARG GLY VAL SER GLY GLU LYS ALA ALA ALA          
SEQRES  20 A  306  LEU VAL ASP ARG TYR SER THR PRO ALA SER LEU LEU ALA          
SEQRES  21 A  306  ALA TYR ASP ALA CYS ALA THR PRO LYS GLU GLN GLU THR          
SEQRES  22 A  306  LEU LEU SER THR ILE LYS CYS GLY ARG LEU GLN ARG ASN          
SEQRES  23 A  306  LEU GLY PRO ALA LEU SER ARG THR LEU SER GLN LEU TYR          
SEQRES  24 A  306  CYS SER TYR GLY PRO LEU THR                                  
SEQRES   1 B  393  GLY GLN SER SER SER LEU ALA VAL THR LYS THR ASN SER          
SEQRES   2 B  393  ASP ILE LEU PRO PRO GLN LYS LYS THR LYS PRO SER GLN          
SEQRES   3 B  393  LYS VAL GLN GLY ARG GLY SER HIS GLY CYS ARG GLN GLN          
SEQRES   4 B  393  ARG GLN ALA ARG GLN LYS GLU SER THR LEU ARG ARG GLN          
SEQRES   5 B  393  GLU ARG LYS ASN ALA ALA LEU VAL THR ARG MET LYS ALA          
SEQRES   6 B  393  GLN ARG PRO GLU GLU CYS LEU LYS HIS ILE ILE VAL VAL          
SEQRES   7 B  393  LEU ASP PRO VAL LEU LEU GLN MET GLU GLY GLY GLY GLN          
SEQRES   8 B  393  LEU LEU GLY ALA LEU GLN THR MET GLU CYS ARG CYS VAL          
SEQRES   9 B  393  ILE GLU ALA GLN ALA VAL PRO CYS SER VAL THR TRP ARG          
SEQRES  10 B  393  ARG ARG ALA GLY PRO SER GLU ASP ARG GLU ASP TRP VAL          
SEQRES  11 B  393  GLU GLU PRO THR VAL LEU VAL LEU LEU ARG ALA GLU ALA          
SEQRES  12 B  393  PHE VAL SER MET ILE ASP ASN GLY LYS GLN GLY SER LEU          
SEQRES  13 B  393  ASP SER THR MET LYS GLY LYS GLU THR LEU GLN GLY PHE          
SEQRES  14 B  393  VAL THR ASP ILE THR ALA LYS THR ALA GLY LYS ALA LEU          
SEQRES  15 B  393  SER LEU VAL ILE VAL ASP GLN GLU LYS CYS PHE SER ALA          
SEQRES  16 B  393  GLN ASN PRO PRO ARG ARG GLY LYS GLN GLY ALA ASN LYS          
SEQRES  17 B  393  GLN THR LYS LYS GLN GLN GLN ARG GLN PRO GLU ALA SER          
SEQRES  18 B  393  ILE GLY SER MET VAL SER ARG VAL ASP ALA GLU GLU ALA          
SEQRES  19 B  393  LEU VAL ASP LEU GLN LEU HIS THR GLU ALA GLN ALA GLN          
SEQRES  20 B  393  ILE VAL GLN SER TRP LYS GLU LEU ALA ASP PHE THR CYS          
SEQRES  21 B  393  ALA PHE THR LYS ALA VAL ALA GLU ALA PRO PHE LYS LYS          
SEQRES  22 B  393  LEU ARG ASP GLU THR THR PHE SER PHE CYS LEU GLU SER          
SEQRES  23 B  393  ASP TRP ALA GLY GLY VAL LYS VAL ASP LEU ALA GLY ARG          
SEQRES  24 B  393  GLY LEU ALA LEU VAL TRP ARG ARG GLN ILE GLN GLN LEU          
SEQRES  25 B  393  ASN ARG VAL SER LEU GLU MET ALA SER ALA VAL VAL ASN          
SEQRES  26 B  393  ALA TYR PRO SER PRO GLN LEU LEU VAL GLN ALA TYR GLN          
SEQRES  27 B  393  GLN CYS PHE SER ASP LYS GLU ARG GLN ASN LEU LEU ALA          
SEQRES  28 B  393  ASP ILE GLN VAL ARG ARG GLY GLU GLY VAL THR SER THR          
SEQRES  29 B  393  SER ARG ARG ILE GLY PRO GLU LEU SER ARG ARG ILE TYR          
SEQRES  30 B  393  LEU GLN MET THR THR LEU GLN PRO HIS LEU SER LEU ASP          
SEQRES  31 B  393  SER ALA ASP                                                  
SEQRES   1 E   17   DG  DA  DA  DT  DG  DT  DG  DT  DG  DT  DC  DT  DC          
SEQRES   2 E   17   DA  DA  DT  DC                                              
SEQRES   1 F    6   DG  DG  DA  DT  DT  DG                                      
SEQRES   1 G   16   DT  DA  DA  DC  DC  DA  DG  DA  DC  DA  DC  DA  DC          
SEQRES   2 G   16   DA  DT  DT                                                  
FORMUL   6  HOH   *33(H2 O)                                                     
HELIX    1 AA1 ARG A  284  LEU A  294  1                                  11    
HELIX    2 AA2 ARG A  336  ASP A  346  1                                  11    
HELIX    3 AA3 GLY A  347  ARG A  358  1                                  12    
HELIX    4 AA4 PRO A  380  ILE A  394  1                                  15    
HELIX    5 AA5 ASP A  404  TYR A  423  1                                  20    
HELIX    6 AA6 PHE A  456  ALA A  463  1                                   8    
HELIX    7 AA7 SER A  470  MET A  480  1                                  11    
HELIX    8 AA8 SER A  486  TYR A  497  1                                  12    
HELIX    9 AA9 THR A  499  ALA A  509  1                                  11    
HELIX   10 AB1 THR A  512  THR A  518  1                                   7    
HELIX   11 AB2 PRO A  534  SER A  546  1                                  13    
HELIX   12 AB3 ALA B  234  ARG B  244  1                                  11    
HELIX   13 AB4 CYS B  248  LYS B  250  5                                   3    
HELIX   14 AB5 ASP B  257  GLN B  262  1                                   6    
HELIX   15 AB6 GLY B  265  MET B  276  1                                  12    
HELIX   16 AB7 ALA B  318  LYS B  329  1                                  12    
HELIX   17 AB8 LEU B  343  ALA B  355  1                                  13    
HELIX   18 AB9 SER B  404  THR B  419  1                                  16    
HELIX   19 AC1 LYS B  430  THR B  456  1                                  27    
HELIX   20 AC2 SER B  458  GLU B  462  5                                   5    
HELIX   21 AC3 GLY B  477  GLN B  488  1                                  12    
HELIX   22 AC4 SER B  493  TYR B  504  1                                  12    
HELIX   23 AC5 SER B  506  CYS B  517  1                                  12    
HELIX   24 AC6 GLU B  548  THR B  559  1                                  12    
SHEET    1 AA1 7 GLU A 261  LEU A 262  0                                        
SHEET    2 AA1 7 LEU A 428  SER A 430 -1  O  LEU A 428   N  LEU A 262           
SHEET    3 AA1 7 SER A 452  THR A 455  1  O  LEU A 453   N  ARG A 429           
SHEET    4 AA1 7 GLU A 325  LYS A 335 -1  N  VAL A 327   O  LEU A 454           
SHEET    5 AA1 7 PHE A 308  GLU A 314 -1  N  ALA A 312   O  LEU A 326           
SHEET    6 AA1 7 TYR A 267  ASP A 274 -1  N  CYS A 272   O  VAL A 309           
SHEET    7 AA1 7 HIS A 298  ARG A 301  1  O  THR A 299   N  VAL A 273           
SHEET    1 AA2 6 GLU A 261  LEU A 262  0                                        
SHEET    2 AA2 6 LEU A 428  SER A 430 -1  O  LEU A 428   N  LEU A 262           
SHEET    3 AA2 6 SER A 452  THR A 455  1  O  LEU A 453   N  ARG A 429           
SHEET    4 AA2 6 GLU A 325  LYS A 335 -1  N  VAL A 327   O  LEU A 454           
SHEET    5 AA2 6 ARG A 363  VAL A 368  1  O  LEU A 367   N  LYS A 335           
SHEET    6 AA2 6 PHE A 398  ARG A 401  1  O  PHE A 398   N  TYR A 366           
SHEET    1 AA3 2 LYS A 524  CYS A 525  0                                        
SHEET    2 AA3 2 ARG A 530  ASN A 531 -1  O  ARG A 530   N  CYS A 525           
SHEET    1 AA4 4 ARG B 279  ILE B 282  0                                        
SHEET    2 AA4 4 ILE B 252  LEU B 256  1  N  VAL B 254   O  ARG B 279           
SHEET    3 AA4 4 SER B 290  ARG B 295 -1  O  THR B 292   N  VAL B 255           
SHEET    4 AA4 4 VAL B 307  GLU B 308 -1  O  VAL B 307   N  ARG B 295           
SHEET    1 AA5 6 ARG B 279  ILE B 282  0                                        
SHEET    2 AA5 6 ILE B 252  LEU B 256  1  N  VAL B 254   O  ARG B 279           
SHEET    3 AA5 6 SER B 290  ARG B 295 -1  O  THR B 292   N  VAL B 255           
SHEET    4 AA5 6 THR B 311  ARG B 317 -1  O  LEU B 313   N  VAL B 291           
SHEET    5 AA5 6 ALA B 358  VAL B 364  1  O  VAL B 362   N  LEU B 316           
SHEET    6 AA5 6 GLN B 422  VAL B 426  1  O  GLN B 422   N  LEU B 361           
CISPEP   1 ASN A  448    PRO A  449          0        -5.55                     
CISPEP   2 LEU A  528    GLN A  529          0        -1.19                     
CRYST1   86.409  228.377   52.637  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      0.011573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004379  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018998        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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