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Database: PDB
Entry: 1IK9
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Original site: 1IK9 
HEADER    GENE REGULATION/LIGASE                  03-MAY-01   1IK9              
TITLE     CRYSTAL STRUCTURE OF A XRCC4-DNA LIGASE IV COMPLEX                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN XRCC4;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: XRCC4 FRAGMENT, RESIDUES 1-213;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA LIGASE IV;                                             
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: LINKER CONNECTING BRCT DOMAINS, RESIDUES 748-784;          
COMPND  11 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE;                           
COMPND  12 EC: 6.5.1.1;                                                         
COMPND  13 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: XRCC4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: LIG4;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PTYB3                                     
KEYWDS    DNA END JOINING, DOUBLE-STRAND BREAK REPAIR, V(D)J                    
KEYWDS   2 RECOMBINATION, PROTEIN-PROTEIN COMPLEX, COILED COIL, GENE            
KEYWDS   3 REGULATION/LIGASE COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.L.SIBANDA,S.E.CRITCHLOW,J.BEGUN,X.Y.PEI,S.P.JACKSON,                
AUTHOR   2 T.L.BLUNDELL,L.PELLEGRINI                                            
REVDAT   3   24-FEB-09 1IK9    1       VERSN                                    
REVDAT   2   05-DEC-01 1IK9    1       JRNL                                     
REVDAT   1   21-NOV-01 1IK9    0                                                
JRNL        AUTH   B.L.SIBANDA,S.E.CRITCHLOW,J.BEGUN,X.Y.PEI,                   
JRNL        AUTH 2 S.P.JACKSON,T.L.BLUNDELL,L.PELLEGRINI                        
JRNL        TITL   CRYSTAL STRUCTURE OF AN XRCC4-DNA LIGASE IV                  
JRNL        TITL 2 COMPLEX.                                                     
JRNL        REF    NAT.STRUCT.BIOL.              V.   8  1015 2001              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11702069                                                     
JRNL        DOI    10.1038/NSB725                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 34084                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1723                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4660                       
REMARK   3   BIN FREE R VALUE                    : 0.4670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 95                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.048                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 35.06000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : -12.72000                                            
REMARK   3    B13 (A**2) : 22.34000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.68                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.45                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL ANISOTROPIC B VALUE               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.600 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.410 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 54.13                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IK9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013360.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : 111/311 SI CRYSTAL                 
REMARK 200  OPTICS                         : MIRRORS                            
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   : 34224                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.5                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 44.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAS                          
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   (%): 71.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, MES, XYLITOL, PH 6.0,           
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       22.53100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      121.07100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.81400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      121.07100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.53100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.81400            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    77                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     PRO A    80                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     ALA B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     PRO B    80                                                      
REMARK 465     ALA B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     ALA B   202                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     GLU B   204                                                      
REMARK 465     ARG B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     ILE B   209                                                      
REMARK 465     LYS B   210                                                      
REMARK 465     GLN B   211                                                      
REMARK 465     GLU B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     PRO C   748                                                      
REMARK 465     SER C   749                                                      
REMARK 465     THR C   750                                                      
REMARK 465     LYS C   751                                                      
REMARK 465     GLU C   752                                                      
REMARK 465     HIS C   753                                                      
REMARK 465     PHE C   754                                                      
REMARK 465     ASN C   783                                                      
REMARK 465     SER C   784                                                      
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  13       65.49   -162.50                                   
REMARK 500    LYS A  26      -75.50     73.87                                   
REMARK 500    HIS A  40      -48.84   -132.63                                   
REMARK 500    ASP A 103      -10.51     63.85                                   
REMARK 500    GLU B  13       56.01   -170.14                                   
REMARK 500    LYS B  26      -78.86     72.04                                   
REMARK 500    HIS B  40      -58.89   -130.98                                   
REMARK 500    ALA B  60       30.52     87.29                                   
REMARK 500    ASP B 103       -0.24     79.97                                   
REMARK 500    ASP B 157      -71.01    -53.77                                   
REMARK 500    CYS C 760      -18.67    -48.43                                   
REMARK 500    ASP C 768      162.48    -49.89                                   
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 265        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH B 271        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH B 282        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 287        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 304        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 312        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A 315        DISTANCE =  5.10 ANGSTROMS                       
DBREF  1IK9 A    1   213  UNP    Q13426   XRCC4_HUMAN      1    213             
DBREF  1IK9 B    1   213  UNP    Q13426   XRCC4_HUMAN      1    213             
DBREF  1IK9 C  748   784  UNP    P49917   DNL4_HUMAN     748    784             
SEQADV 1IK9 ALA A   93  UNP  Q13426    CYS    93 ENGINEERED                     
SEQADV 1IK9 ALA A  128  UNP  Q13426    CYS   128 ENGINEERED                     
SEQADV 1IK9 ALA A  130  UNP  Q13426    CYS   130 ENGINEERED                     
SEQADV 1IK9 ALA A  165  UNP  Q13426    CYS   165 ENGINEERED                     
SEQADV 1IK9 ALA B   93  UNP  Q13426    CYS    93 ENGINEERED                     
SEQADV 1IK9 ALA B  128  UNP  Q13426    CYS   128 ENGINEERED                     
SEQADV 1IK9 ALA B  130  UNP  Q13426    CYS   130 ENGINEERED                     
SEQADV 1IK9 ALA B  165  UNP  Q13426    CYS   165 ENGINEERED                     
SEQRES   1 A  213  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 A  213  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 A  213  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 A  213  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 A  213  SER GLN GLU ALA ASP ASP MET ALA MET GLU LYS GLY LYS          
SEQRES   6 A  213  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 A  213  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 A  213  SER ALA TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 A  213  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 A  213  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ALA TYR ALA          
SEQRES  11 A  213  LEU ASP THR ILE ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 A  213  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 A  213  ASP VAL GLN GLY ARG PHE GLU LYS ALA VAL SER ALA LYS          
SEQRES  14 A  213  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 A  213  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 A  213  ASN LYS LEU LEU ASN ALA ALA GLN GLU ARG GLU LYS ASP          
SEQRES  17 A  213  ILE LYS GLN GLU GLY                                          
SEQRES   1 B  213  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 B  213  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 B  213  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 B  213  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 B  213  SER GLN GLU ALA ASP ASP MET ALA MET GLU LYS GLY LYS          
SEQRES   6 B  213  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 B  213  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 B  213  SER ALA TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 B  213  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 B  213  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ALA TYR ALA          
SEQRES  11 B  213  LEU ASP THR ILE ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 B  213  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 B  213  ASP VAL GLN GLY ARG PHE GLU LYS ALA VAL SER ALA LYS          
SEQRES  14 B  213  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 B  213  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 B  213  ASN LYS LEU LEU ASN ALA ALA GLN GLU ARG GLU LYS ASP          
SEQRES  17 B  213  ILE LYS GLN GLU GLY                                          
SEQRES   1 C   37  PRO SER THR LYS GLU HIS PHE ALA ARG GLU TYR ASP CYS          
SEQRES   2 C   37  TYR GLY ASP SER TYR PHE ILE ASP THR ASP LEU ASN GLN          
SEQRES   3 C   37  LEU LYS GLU VAL PHE SER GLY ILE LYS ASN SER                  
FORMUL   4  HOH   *224(H2 O)                                                    
HELIX    1   1 THR A   27  GLU A   29  5                                   3    
HELIX    2   2 GLU A   49  MET A   59  1                                  11    
HELIX    3   3 GLU A   62  LEU A   75  1                                  14    
HELIX    4   4 ASN A  118  GLN A  211  1                                  94    
HELIX    5   5 THR B   27  GLU B   29  5                                   3    
HELIX    6   6 GLU B   49  ALA B   60  1                                  12    
HELIX    7   7 GLU B   62  LEU B   75  1                                  14    
HELIX    8   8 ASN B  118  GLU B  170  1                                  53    
HELIX    9   9 ALA B  171  ALA B  201  1                                  31    
HELIX   10  10 ASP C  770  GLY C  780  1                                  11    
SHEET    1   A 5 GLU A   2  LEU A  10  0                                        
SHEET    2   A 5 GLU A  13  TRP A  24 -1  N  GLU A  13   O  LEU A  10           
SHEET    3   A 5 GLY A  31  THR A  37 -1  N  VAL A  33   O  SER A  23           
SHEET    4   A 5 ALA A  42  SER A  48 -1  O  TRP A  43   N  LEU A  36           
SHEET    5   A 5 GLU A 114  LYS A 115 -1  O  GLU A 114   N  THR A  44           
SHEET    1   B 3 TYR A  84  PHE A  88  0                                        
SHEET    2   B 3 TYR A  94  ASN A 100 -1  O  PHE A  96   N  ASN A  87           
SHEET    3   B 3 SER A 105  ASN A 112 -1  O  PHE A 106   N  LYS A  99           
SHEET    1   C 5 GLU B   2  ILE B   8  0                                        
SHEET    2   C 5 HIS B  18  TRP B  24 -1  O  HIS B  18   N  ILE B   8           
SHEET    3   C 5 GLY B  31  THR B  37 -1  N  VAL B  33   O  SER B  23           
SHEET    4   C 5 ALA B  42  SER B  48 -1  O  TRP B  43   N  LEU B  36           
SHEET    5   C 5 GLU B 114  LYS B 115 -1  N  GLU B 114   O  THR B  44           
SHEET    1   D 3 TYR B  84  PHE B  88  0                                        
SHEET    2   D 3 TYR B  94  LEU B 101 -1  O  PHE B  96   N  ASN B  87           
SHEET    3   D 3 VAL B 104  ASN B 112 -1  O  VAL B 104   N  LEU B 101           
CRYST1   45.062   79.628  242.142  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022192  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004130        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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