GenomeNet

Database: PDB
Entry: 1IN1
LinkDB: 1IN1
Original site: 1IN1 
HEADER    LIGASE                                  11-MAY-01   1IN1              
TITLE     NMR STRUCTURE OF HUMAN DNA LIGASE IIIALPHA BRCT DOMAIN                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA LIGASE III;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BRCT DOMAIN;                                               
COMPND   5 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP];                     
COMPND   6 EC: 6.5.1.1;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: BL21(DE3)                                 
KEYWDS    PARALLEL BETA SHEET, LIGASE                                           
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    V.V.KRISHNAN,K.H.THORNTON,M.P.THELEN,M.COSMAN                         
REVDAT   5   23-FEB-22 1IN1    1       REMARK SEQADV                            
REVDAT   4   24-FEB-09 1IN1    1       VERSN                                    
REVDAT   3   01-APR-03 1IN1    1       JRNL                                     
REVDAT   2   09-NOV-01 1IN1    1       JRNL                                     
REVDAT   1   25-MAY-01 1IN1    0                                                
JRNL        AUTH   V.V.KRISHNAN,K.H.THORNTON,M.P.THELEN,M.COSMAN                
JRNL        TITL   SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE HUMAN DNA    
JRNL        TITL 2 LIGASE IIIALPHA BRCT DOMAIN                                  
JRNL        REF    BIOCHEMISTRY                  V.  40 13158 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11683624                                                     
JRNL        DOI    10.1021/BI010979G                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.COSMAN,V.V.KRISHNAN,K.H.THORNTON,M.P.THELEN                
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND BIOPHYSICAL CHARACTERIZATION   
REMARK   1  TITL 2 OF THE BRCT DOMAIN OF HUMAN DNA LIGASE III ALPHA             
REMARK   1  REF    PROTEIN EXPR.PURIF.           V.  21   401 2001              
REMARK   1  REFN                   ISSN 1046-5928                               
REMARK   1  DOI    10.1006/PREP.2001.1391                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : FELIX 2.3, DYANA 1.5                                 
REMARK   3   AUTHORS     : MSI INC. (FELIX), WUTHRICH ET AL. (DYANA)            
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE STRUCTURES ARE BASED ON A TOTAL OF 1072 RESTRAINTS, 979 NOE-    
REMARK   3  DERIVED                                                             
REMARK   3  DISTANCE CONSTRAINTS, 25 DIHEDRAL ANGLE RESTRAINTS, 54 H BOND       
REMARK   3  RESTRAINTS                                                          
REMARK   3  FROM HYDROGEN BONDS                                                 
REMARK   4                                                                      
REMARK   4 1IN1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013419.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 288                                
REMARK 210  PH                             : 6.6                                
REMARK 210  IONIC STRENGTH                 : 0.4-1.0 MM                         
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 50 MM NAH2PO4, 150 MM NACL, 25     
REMARK 210                                   MM D10-DTT                         
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D NOESY; 3D_13C                   
REMARK 210                                   -SEPARATED_NOESY; 3D_15N-          
REMARK 210                                   SEPARATED_NOESY; HNHA; DQF-COSY    
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE, DYANA 1.5                 
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY, SIMULATED       
REMARK 210                                   ANNEALING, TORSION ANGLE DYNAMICS  
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 299                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS, TARGET       
REMARK 210                                   FUNCTION                           
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING TRIPLE-RESONANCE NMR    
REMARK 210  SPECTROSCOPY                                                        
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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    LYS A   845     HE1  TYR A   871              0.56            
REMARK 500   CD   ARG A   855     HB   THR A   889              0.64            
REMARK 500   HG2  ARG A   855     CG2  THR A   889              0.71            
REMARK 500   HA   PHE A   851    HD11  LEU A   918              0.73            
REMARK 500  HG22  VAL A   846     HH   TYR A   871              0.77            
REMARK 500  HD11  ILE A   850     HA   ILE A   913              0.86            
REMARK 500  HD21  LEU A   858     HB3  LEU A   868              0.88            
REMARK 500  HG11  VAL A   854     HH2  TRP A   908              0.90            
REMARK 500   HG2  ARG A   855    HG21  THR A   889              0.91            
REMARK 500  HG21  ILE A   850     H    ILE A   913              0.92            
REMARK 500   O    ARG A   855     H    HIS A   890              0.92            
REMARK 500  HG21  VAL A   854     HG   LEU A   918              0.94            
REMARK 500  HD13  ILE A   850    HG13  ILE A   913              1.01            
REMARK 500   OH   TYR A   871    HD11  ILE A   913              1.01            
REMARK 500   O    MET A   885     H    ALA A   888              1.01            
REMARK 500   HG3  ARG A   855     H    THR A   889              1.05            
REMARK 500  HG23  ILE A   850     HA   ILE A   913              1.06            
REMARK 500   H    ARG A   855    HG23  THR A   889              1.07            
REMARK 500  HD13  LEU A   847     HE1  PHE A   875              1.08            
REMARK 500  HG23  ILE A   850     CA   ILE A   913              1.09            
REMARK 500  HD21  LEU A   856    HD12  LEU A   892              1.09            
REMARK 500  HD21  LEU A   841     HA   LYS A   845              1.10            
REMARK 500  HG21  ILE A   850     N    ILE A   913              1.11            
REMARK 500   SD   MET A   885     HB2  LYS A   897              1.11            
REMARK 500   HD2  ARG A   855     HB   THR A   889              1.13            
REMARK 500   HE1  PHE A   851     HA   ILE A   909              1.13            
REMARK 500   O    ILE A   850     H    THR A   852              1.14            
REMARK 500   O    ARG A   895     H    ASN A   898              1.15            
REMARK 500   H    LEU A   847     HE1  TYR A   871              1.15            
REMARK 500  HG22  VAL A   846     OH   TYR A   871              1.18            
REMARK 500   O    LYS A   845     H    LEU A   847              1.20            
REMARK 500   HZ1  LYS A   845     HB3  ARG A   867              1.21            
REMARK 500   OD1  ASP A   849     HD2  ARG A   916              1.23            
REMARK 500   O    PHE A   851     H    VAL A   854              1.23            
REMARK 500   CD1  ILE A   850     HA   ILE A   913              1.23            
REMARK 500   O    GLN A   881     H    ASP A   884              1.24            
REMARK 500   H    TYR A   857     HA   VAL A   891              1.25            
REMARK 500  HD11  LEU A   847     HE1  TYR A   871              1.27            
REMARK 500   HG2  ARG A   855     CB   THR A   889              1.29            
REMARK 500  HG23  ILE A   850     N    ILE A   913              1.29            
REMARK 500   NE   ARG A   855     HB   THR A   889              1.30            
REMARK 500   C    LYS A   845    HD21  LEU A   847              1.31            
REMARK 500   HD2  TYR A   857     HZ2  LYS A   897              1.33            
REMARK 500   O    PHE A   872     H    PHE A   875              1.33            
REMARK 500   CD2  TYR A   871     HZ   PHE A   875              1.34            
REMARK 500   CE2  TYR A   871     HZ   PHE A   875              1.36            
REMARK 500   CG2  VAL A   854     HG   LEU A   918              1.37            
REMARK 500   CG2  ILE A   850     N    ILE A   913              1.39            
REMARK 500  HD11  ILE A   850     CA   ILE A   913              1.39            
REMARK 500   O    LYS A   845    HD21  LEU A   847              1.40            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    2010 CLOSE CONTACTS                                
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  1 SER A 836      -79.82   -108.92                                   
REMARK 500  1 THR A 840      -77.12   -122.89                                   
REMARK 500  1 LEU A 841        0.29    -62.62                                   
REMARK 500  1 THR A 844      -60.38     65.80                                   
REMARK 500  1 LYS A 845      -11.70   -163.59                                   
REMARK 500  1 VAL A 846      -57.96     37.42                                   
REMARK 500  1 LEU A 847      -81.06     59.93                                   
REMARK 500  1 LEU A 848      165.72     70.97                                   
REMARK 500  1 ILE A 850      -99.76    -79.34                                   
REMARK 500  1 PHE A 851       31.86    -53.00                                   
REMARK 500  1 THR A 852      104.54    -39.33                                   
REMARK 500  1 SER A 866      -76.56    -27.62                                   
REMARK 500  1 ARG A 869      -89.20    -68.14                                   
REMARK 500  1 TYR A 871      -76.07    -38.62                                   
REMARK 500  1 PHE A 872      -94.49    -38.02                                   
REMARK 500  1 VAL A 873      -39.45    -29.14                                   
REMARK 500  1 ASP A 876        9.88    149.50                                   
REMARK 500  1 GLU A 882      -71.10    -26.21                                   
REMARK 500  1 PHE A 883       12.96    -63.24                                   
REMARK 500  1 MET A 885      -35.95   -146.81                                   
REMARK 500  1 THR A 886      -51.72     -8.75                                   
REMARK 500  1 ALA A 888      179.03    -45.44                                   
REMARK 500  1 SER A 894      166.25     84.50                                   
REMARK 500  1 ARG A 895      -33.56   -144.80                                   
REMARK 500  1 ASP A 896      -76.70    -13.61                                   
REMARK 500  1 LYS A 897      -33.71    -32.41                                   
REMARK 500  1 ALA A 901     -155.39    -91.34                                   
REMARK 500  1 SER A 905     -168.09   -129.30                                   
REMARK 500  1 CYS A 912      -72.92    -73.63                                   
REMARK 500  1 ARG A 916       13.97     53.28                                   
REMARK 500  1 VAL A 919     -160.60   -101.33                                   
REMARK 500  2 SER A 836      -60.94    -94.74                                   
REMARK 500  2 CYS A 842       -6.91    -53.97                                   
REMARK 500  2 GLN A 843       68.32   -116.34                                   
REMARK 500  2 THR A 844      -71.17     67.30                                   
REMARK 500  2 LYS A 845       -1.33   -156.00                                   
REMARK 500  2 VAL A 846      119.17     41.69                                   
REMARK 500  2 LEU A 847       74.27   -150.41                                   
REMARK 500  2 ASP A 849       47.36    -77.62                                   
REMARK 500  2 ILE A 850      -92.17    -70.61                                   
REMARK 500  2 PHE A 851       25.37    -58.27                                   
REMARK 500  2 THR A 852      107.94    -39.79                                   
REMARK 500  2 SER A 866      -80.39    -27.30                                   
REMARK 500  2 ARG A 869      -83.12    -62.66                                   
REMARK 500  2 PHE A 872      -93.02    -49.00                                   
REMARK 500  2 VAL A 873      -35.47    -30.57                                   
REMARK 500  2 ASP A 876        7.93    142.96                                   
REMARK 500  2 GLU A 882      -70.55    -26.55                                   
REMARK 500  2 PHE A 883       12.41    -64.61                                   
REMARK 500  2 MET A 885      -35.71   -145.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     610 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1IN1 A  835   922  UNP    P49916   DNL3_HUMAN     835    922             
SEQADV 1IN1 GLY A  835  UNP  P49916    LYS   835 CLONING ARTIFACT               
SEQADV 1IN1 SER A  836  UNP  P49916    ALA   836 CLONING ARTIFACT               
SEQRES   1 A   88  GLY SER ALA ASP GLU THR LEU CYS GLN THR LYS VAL LEU          
SEQRES   2 A   88  LEU ASP ILE PHE THR GLY VAL ARG LEU TYR LEU PRO PRO          
SEQRES   3 A   88  SER THR PRO ASP PHE SER ARG LEU ARG ARG TYR PHE VAL          
SEQRES   4 A   88  ALA PHE ASP GLY ASP LEU VAL GLN GLU PHE ASP MET THR          
SEQRES   5 A   88  SER ALA THR HIS VAL LEU GLY SER ARG ASP LYS ASN PRO          
SEQRES   6 A   88  ALA ALA GLN GLN VAL SER PRO GLU TRP ILE TRP ALA CYS          
SEQRES   7 A   88  ILE ARG LYS ARG ARG LEU VAL ALA PRO CYS                      
HELIX    1   1 SER A  836  THR A  840  5                                   5    
HELIX    2   2 ASP A  864  ASP A  876  1                                  13    
HELIX    3   3 SER A  905  LYS A  915  1                                  11    
SHEET    1   A 2 VAL A 891  LEU A 892  0                                        
SHEET    2   A 2 GLN A 903  VAL A 904  1  N  VAL A 904   O  VAL A 891           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system