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Database: PDB
Entry: 3GGR
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Original site: 3GGR 
HEADER    CELL CYCLE                              02-MAR-09   3GGR              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN RAD9-HUS1-RAD1 COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL CYCLE CHECKPOINT CONTROL PROTEIN RAD9A;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TRUNCATED HRAD9 (RESIDUES 1-270);                          
COMPND   5 SYNONYM: HRAD9, DNA REPAIR EXONUCLEASE RAD9 HOMOLOG A;               
COMPND   6 EC: 3.1.11.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CHECKPOINT PROTEIN HUS1;                                   
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: HHUS1;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CELL CYCLE CHECKPOINT PROTEIN RAD1;                        
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: HRAD1, DNA REPAIR EXONUCLEASE RAD1 HOMOLOG, RAD1-LIKE DNA   
COMPND  17 DAMAGE CHECKPOINT PROTEIN;                                           
COMPND  18 EC: 3.1.11.2;                                                        
COMPND  19 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: RAD9;                                                          
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZ C;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: HUS1;                                                          
SOURCE  15 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PPICZ C;                                  
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: RAD1;                                                          
SOURCE  24 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PPICZ C                                   
KEYWDS    PROTEIN-PROTEIN COMPLEX, DNA DAMAGE, DNA REPAIR, EXONUCLEASE,         
KEYWDS   2 HYDROLASE, NUCLEASE, NUCLEUS, PHOSPHOPROTEIN, CELL CYCLE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.XU,L.BAI,H.Y.HANG,T.JIANG                                           
REVDAT   2   12-FEB-14 3GGR    1       JRNL   VERSN                             
REVDAT   1   16-JUN-09 3GGR    0                                                
JRNL        AUTH   M.XU,L.BAI,Y.GONG,W.XIE,H.Y.HANG,T.JIANG                     
JRNL        TITL   STRUCTURE AND FUNCTIONAL IMPLICATIONS OF THE HUMAN           
JRNL        TITL 2 RAD9-HUS1-RAD1 CELL CYCLE CHECKPOINT COMPLEX                 
JRNL        REF    J.BIOL.CHEM.                  V. 284 20457 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19535328                                                     
JRNL        DOI    10.1074/JBC.C109.022384                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11575                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.291                           
REMARK   3   R VALUE            (WORKING SET) : 0.289                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1262                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 786                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6325                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.42000                                             
REMARK   3    B22 (A**2) : 8.40000                                              
REMARK   3    B33 (A**2) : -7.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.34000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.876                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.851                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6439 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8707 ; 1.728 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   803 ; 8.759 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   285 ;41.618 ;24.596       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1166 ;24.413 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;20.002 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1013 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4769 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3470 ; 0.290 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4150 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   216 ; 0.207 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   123 ; 0.280 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.249 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4022 ; 7.698 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6514 ;10.507 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2417 ; 0.027 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2193 ; 0.035 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GGR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051839.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-07; 29-JUN-08               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SPRING-8; SLS                      
REMARK 200  BEAMLINE                       : BL41XU; X06SA                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00716; 1.0063, 1.0092            
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; MARMOSAIC 225   
REMARK 200                                   MM CCD                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13010                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 2000 MME, 100MM TRIS-HCL,200MM    
REMARK 280  TRIMETHYLAMINE N-OXIDE DIHYDRATE, PH 8.0, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.58200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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     MET A     1                                                      
REMARK 465     SER A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     ASP A   269                                                      
REMARK 465     SER A   270                                                      
REMARK 465     MET B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     MET C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     ILE C     8                                                      
REMARK 465     GLN C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     VAL C   277                                                      
REMARK 465     PRO C   278                                                      
REMARK 465     GLU C   279                                                      
REMARK 465     SER C   280                                                      
REMARK 465     GLU C   281                                                      
REMARK 465     SER C   282                                                      
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    PRO B 154   C   -  N   -  CD  ANGL. DEV. = -20.6 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    SER A  21        1.34    -68.77                                   
REMARK 500    LEU A  32      139.89   -176.80                                   
REMARK 500    THR A  40      140.59   -178.60                                   
REMARK 500    ASN A  42      147.67    -17.93                                   
REMARK 500    ALA A  63       34.37   -154.47                                   
REMARK 500    PRO A  66      124.86    -36.23                                   
REMARK 500    LEU A  70       93.46    -64.07                                   
REMARK 500    LEU A  87      -78.14   -114.64                                   
REMARK 500    MET A  89       -8.96    -52.98                                   
REMARK 500    LEU A  90       50.96    -97.01                                   
REMARK 500    THR A  93      -41.57   -136.80                                   
REMARK 500    VAL A  94      121.72    176.97                                   
REMARK 500    ARG A 104      -70.17    -68.11                                   
REMARK 500    SER A 105      -98.92   -106.33                                   
REMARK 500    CYS A 114       59.58   -144.75                                   
REMARK 500    LYS A 115     -140.85     51.78                                   
REMARK 500    SER A 125       67.27   -101.94                                   
REMARK 500    PHE A 126     -163.57    -66.50                                   
REMARK 500    ASP A 128       90.34    -15.30                                   
REMARK 500    LEU A 132      141.01   -173.95                                   
REMARK 500    GLN A 133      147.61    173.53                                   
REMARK 500    PHE A 136       73.58   -103.52                                   
REMARK 500    PRO A 138     -163.50    -69.93                                   
REMARK 500    ALA A 139       44.44    -64.81                                   
REMARK 500    PHE A 159       52.61    -97.78                                   
REMARK 500    PRO A 161      -19.65    -40.94                                   
REMARK 500    ARG A 174       90.13   -174.25                                   
REMARK 500    ALA A 186       58.00   -155.64                                   
REMARK 500    ASP A 187     -161.25   -107.88                                   
REMARK 500    SER A 188      -50.09    -24.64                                   
REMARK 500    ALA A 192      122.60    175.41                                   
REMARK 500    GLU A 211      119.81    -26.83                                   
REMARK 500    PHE A 222      -70.25    -54.60                                   
REMARK 500    ARG A 223      -43.92    -26.44                                   
REMARK 500    PHE A 228       48.77    -80.28                                   
REMARK 500    ALA A 229       44.31    -97.37                                   
REMARK 500    ALA A 242     -161.93     60.85                                   
REMARK 500    PRO A 243      -81.53    -90.94                                   
REMARK 500    LEU A 255      -31.20   -146.94                                   
REMARK 500    ASP B   9      -39.08   -133.56                                   
REMARK 500    SER B  35     -151.03   -133.42                                   
REMARK 500    PRO B  36     -161.67    -75.69                                   
REMARK 500    ASP B  37       -6.62    -59.49                                   
REMARK 500    ASP B  45       90.31    172.61                                   
REMARK 500    LEU B  47     -147.16     53.71                                   
REMARK 500    ASN B  49     -146.26     53.29                                   
REMARK 500    VAL B  52     -145.48     51.74                                   
REMARK 500    SER B  53      116.14   -164.62                                   
REMARK 500    GLU B  61      -47.40    -26.46                                   
REMARK 500    PHE B  63       70.69   -104.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     118 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG B  99        21.5      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 112        24.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 151        24.3      L          L   OUTSIDE RANGE           
REMARK 500    CYS C 272        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3GGR A    1   270  UNP    Q99638   RAD9A_HUMAN      1    270             
DBREF  3GGR B    2   280  UNP    O60921   HUS1_HUMAN       2    280             
DBREF  3GGR C    1   282  UNP    O60671   RAD1_HUMAN       1    282             
SEQADV 3GGR MET B   -5  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B   -4  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B   -3  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B   -2  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B   -1  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B    0  UNP  O60921              EXPRESSION TAG                 
SEQADV 3GGR HIS B    1  UNP  O60921              EXPRESSION TAG                 
SEQRES   1 A  270  MET LYS CYS LEU VAL THR GLY GLY ASN VAL LYS VAL LEU          
SEQRES   2 A  270  GLY LYS ALA VAL HIS SER LEU SER ARG ILE GLY ASP GLU          
SEQRES   3 A  270  LEU TYR LEU GLU PRO LEU GLU ASP GLY LEU SER LEU ARG          
SEQRES   4 A  270  THR VAL ASN SER SER ARG SER ALA TYR ALA CYS PHE LEU          
SEQRES   5 A  270  PHE ALA PRO LEU PHE PHE GLN GLN TYR GLN ALA ALA THR          
SEQRES   6 A  270  PRO GLY GLN ASP LEU LEU ARG CYS LYS ILE LEU MET LYS          
SEQRES   7 A  270  SER PHE LEU SER VAL PHE ARG SER LEU ALA MET LEU GLU          
SEQRES   8 A  270  LYS THR VAL GLU LYS CYS CYS ILE SER LEU ASN GLY ARG          
SEQRES   9 A  270  SER SER ARG LEU VAL VAL GLN LEU HIS CYS LYS PHE GLY          
SEQRES  10 A  270  VAL ARG LYS THR HIS ASN LEU SER PHE GLN ASP CYS GLU          
SEQRES  11 A  270  SER LEU GLN ALA VAL PHE ASP PRO ALA SER CYS PRO HIS          
SEQRES  12 A  270  MET LEU ARG ALA PRO ALA ARG VAL LEU GLY GLU ALA VAL          
SEQRES  13 A  270  LEU PRO PHE SER PRO ALA LEU ALA GLU VAL THR LEU GLY          
SEQRES  14 A  270  ILE GLY ARG GLY ARG ARG VAL ILE LEU ARG SER TYR HIS          
SEQRES  15 A  270  GLU GLU GLU ALA ASP SER THR ALA LYS ALA MET VAL THR          
SEQRES  16 A  270  GLU MET CYS LEU GLY GLU GLU ASP PHE GLN GLN LEU GLN          
SEQRES  17 A  270  ALA GLN GLU GLY VAL ALA ILE THR PHE CYS LEU LYS GLU          
SEQRES  18 A  270  PHE ARG GLY LEU LEU SER PHE ALA GLU SER ALA ASN LEU          
SEQRES  19 A  270  ASN LEU SER ILE HIS PHE ASP ALA PRO GLY ARG PRO ALA          
SEQRES  20 A  270  ILE PHE THR ILE LYS ASP SER LEU LEU ASP GLY HIS PHE          
SEQRES  21 A  270  VAL LEU ALA THR LEU SER ASP THR ASP SER                      
SEQRES   1 B  286  MET HIS HIS HIS HIS HIS HIS LYS PHE ARG ALA LYS ILE          
SEQRES   2 B  286  VAL ASP GLY ALA CYS LEU ASN HIS PHE THR ARG ILE SER          
SEQRES   3 B  286  ASN MET ILE ALA LYS LEU ALA LYS THR CYS THR LEU ARG          
SEQRES   4 B  286  ILE SER PRO ASP LYS LEU ASN PHE ILE LEU CYS ASP LYS          
SEQRES   5 B  286  LEU ALA ASN GLY GLY VAL SER MET TRP CYS GLU LEU GLU          
SEQRES   6 B  286  GLN GLU ASN PHE PHE ASN GLU PHE GLN MET GLU GLY VAL          
SEQRES   7 B  286  SER ALA GLU ASN ASN GLU ILE TYR LEU GLU LEU THR SER          
SEQRES   8 B  286  GLU ASN LEU SER ARG ALA LEU LYS THR ALA GLN ASN ALA          
SEQRES   9 B  286  ARG ALA LEU LYS ILE LYS LEU THR ASN LYS HIS PHE PRO          
SEQRES  10 B  286  CYS LEU THR VAL SER VAL GLU LEU LEU SER MET SER SER          
SEQRES  11 B  286  SER SER ARG ILE VAL THR HIS ASP ILE PRO ILE LYS VAL          
SEQRES  12 B  286  ILE PRO ARG LYS LEU TRP LYS ASP LEU GLN GLU PRO VAL          
SEQRES  13 B  286  VAL PRO ASP PRO ASP VAL SER ILE TYR LEU PRO VAL LEU          
SEQRES  14 B  286  LYS THR MET LYS SER VAL VAL GLU LYS MET LYS ASN ILE          
SEQRES  15 B  286  SER ASN HIS LEU VAL ILE GLU ALA ASN LEU ASP GLY GLU          
SEQRES  16 B  286  LEU ASN LEU LYS ILE GLU THR GLU LEU VAL CYS VAL THR          
SEQRES  17 B  286  THR HIS PHE LYS ASP LEU GLY ASN PRO PRO LEU ALA SER          
SEQRES  18 B  286  GLU SER THR HIS GLU ASP ARG ASN VAL GLU HIS MET ALA          
SEQRES  19 B  286  GLU VAL HIS ILE ASP ILE ARG LYS LEU LEU GLN PHE LEU          
SEQRES  20 B  286  ALA GLY GLN GLN VAL ASN PRO THR LYS ALA LEU CYS ASN          
SEQRES  21 B  286  ILE VAL ASN ASN LYS MET VAL HIS PHE ASP LEU LEU HIS          
SEQRES  22 B  286  GLU ASP VAL SER LEU GLN TYR PHE ILE PRO ALA LEU SER          
SEQRES   1 C  282  MET PRO LEU LEU THR GLN GLN ILE GLN ASP GLU ASP ASP          
SEQRES   2 C  282  GLN TYR SER LEU VAL ALA SER LEU ASP ASN VAL ARG ASN          
SEQRES   3 C  282  LEU SER THR ILE LEU LYS ALA ILE HIS PHE ARG GLU HIS          
SEQRES   4 C  282  ALA THR CYS PHE ALA THR LYS ASN GLY ILE LYS VAL THR          
SEQRES   5 C  282  VAL GLU ASN ALA LYS CYS VAL GLN ALA ASN ALA PHE ILE          
SEQRES   6 C  282  GLN ALA GLY ILE PHE GLN GLU PHE LYS VAL GLN GLU GLU          
SEQRES   7 C  282  SER VAL THR PHE ARG ILE ASN LEU THR VAL LEU LEU ASP          
SEQRES   8 C  282  CYS LEU SER ILE PHE GLY SER SER PRO MET PRO GLY THR          
SEQRES   9 C  282  LEU THR ALA LEU ARG MET CYS TYR GLN GLY TYR GLY TYR          
SEQRES  10 C  282  PRO LEU MET LEU PHE LEU GLU GLU GLY GLY VAL VAL THR          
SEQRES  11 C  282  VAL CYS LYS ILE ASN THR GLN GLU PRO GLU GLU THR LEU          
SEQRES  12 C  282  ASP PHE ASP PHE CYS SER THR ASN VAL ILE ASN LYS ILE          
SEQRES  13 C  282  ILE LEU GLN SER GLU GLY LEU ARG GLU ALA PHE SER GLU          
SEQRES  14 C  282  LEU ASP MET THR SER GLU VAL LEU GLN ILE THR MET SER          
SEQRES  15 C  282  PRO ASP LYS PRO TYR PHE ARG LEU SER THR PHE GLY ASN          
SEQRES  16 C  282  ALA GLY SER SER HIS LEU ASP TYR PRO LYS ASP SER ASP          
SEQRES  17 C  282  LEU MET GLU ALA PHE HIS CYS ASN GLN THR GLN VAL ASN          
SEQRES  18 C  282  ARG TYR LYS ILE SER LEU LEU LYS PRO SER THR LYS ALA          
SEQRES  19 C  282  LEU VAL LEU SER CYS LYS VAL SER ILE ARG THR ASP ASN          
SEQRES  20 C  282  ARG GLY PHE LEU SER LEU GLN TYR MET ILE ARG ASN GLU          
SEQRES  21 C  282  ASP GLY GLN ILE CYS PHE VAL GLU TYR TYR CYS CYS PRO          
SEQRES  22 C  282  ASP GLU GLU VAL PRO GLU SER GLU SER                          
HELIX    1   1 GLY A    8  SER A   21  1                                  14    
HELIX    2   2 PRO A   55  PHE A   58  5                                   4    
HELIX    3   3 MET A   77  ARG A   85  1                                   9    
HELIX    4   4 ALA A  149  LEU A  157  1                                   9    
HELIX    5   5 CYS A  218  PHE A  228  1                                  11    
HELIX    6   6 ALA B   11  LYS B   25  1                                  15    
HELIX    7   7 THR B   84  LYS B   93  1                                  10    
HELIX    8   8 LEU B  142  GLN B  147  1                                   6    
HELIX    9   9 LYS B  164  SER B  177  1                                  14    
HELIX   10  10 ARG B  235  ALA B  242  1                                   8    
HELIX   11  11 VAL C   24  ALA C   33  1                                  10    
HELIX   12  12 GLY C   68  PHE C   70  5                                   3    
HELIX   13  13 LEU C   86  ASP C   91  1                                   6    
HELIX   14  14 GLN C  159  PHE C  167  1                                   9    
HELIX   15  15 ILE C  225  VAL C  236  1                                  12    
SHEET    1   A 7 GLN A  60  TYR A  61  0                                        
SHEET    2   A 7 CYS A   3  THR A   6 -1  N  LEU A   4   O  GLN A  60           
SHEET    3   A 7 LYS A  96  LEU A 101 -1  O  CYS A  97   N  VAL A   5           
SHEET    4   A 7 LEU A 108  HIS A 113 -1  O  VAL A 109   N  SER A 100           
SHEET    5   A 7 VAL A 118  ASN A 123 -1  O  ARG A 119   N  LEU A 112           
SHEET    6   A 7 GLY C 197  ASP C 202 -1  O  SER C 198   N  HIS A 122           
SHEET    7   A 7 ARG C 189  GLY C 194 -1  N  LEU C 190   O  LEU C 201           
SHEET    1   B 9 CYS A  73  LEU A  76  0                                        
SHEET    2   B 9 GLU A  26  GLU A  30 -1  N  LEU A  27   O  ILE A  75           
SHEET    3   B 9 LEU A  36  ARG A  39 -1  O  SER A  37   N  GLU A  30           
SHEET    4   B 9 ALA A  47  PHE A  53 -1  O  PHE A  51   N  LEU A  38           
SHEET    5   B 9 LEU A 256  LEU A 262 -1  O  ASP A 257   N  LEU A  52           
SHEET    6   B 9 ALA A 247  LYS A 252 -1  N  PHE A 249   O  PHE A 260           
SHEET    7   B 9 LEU A 234  HIS A 239 -1  N  ILE A 238   O  ILE A 248           
SHEET    8   B 9 HIS A 143  PRO A 148 -1  N  LEU A 145   O  SER A 237           
SHEET    9   B 9 GLN A 206  LEU A 207 -1  O  GLN A 206   N  ARG A 146           
SHEET    1   C 9 ALA A 214  THR A 216  0                                        
SHEET    2   C 9 LEU A 168  ILE A 170 -1  N  GLY A 169   O  ILE A 215           
SHEET    3   C 9 ILE A 177  SER A 180 -1  O  LEU A 178   N  ILE A 170           
SHEET    4   C 9 THR A 195  LEU A 199 -1  O  LEU A 199   N  ILE A 177           
SHEET    5   C 9 ILE B 128  ASP B 132 -1  O  VAL B 129   N  CYS A 198           
SHEET    6   C 9 LEU B 113  LEU B 119 -1  N  VAL B 117   O  THR B 130           
SHEET    7   C 9 ALA B 100  LEU B 105 -1  N  LYS B 102   O  SER B 116           
SHEET    8   C 9 ARG B   4  VAL B   8 -1  N  LYS B   6   O  ILE B 103           
SHEET    9   C 9 PHE B  67  MET B  69 -1  O  GLN B  68   N  ALA B   5           
SHEET    1   D 8 LYS B 136  VAL B 137  0                                        
SHEET    2   D 8 ILE B  79  LEU B  83 -1  N  GLU B  82   O  VAL B 137           
SHEET    3   D 8 THR B  31  ILE B  34 -1  N  LEU B  32   O  LEU B  81           
SHEET    4   D 8 ASN B  40  LEU B  43 -1  O  LEU B  43   N  THR B  31           
SHEET    5   D 8 MET B  54  LEU B  58 -1  O  LEU B  58   N  ASN B  40           
SHEET    6   D 8 VAL B 270  PHE B 275 -1  O  GLN B 273   N  TRP B  55           
SHEET    7   D 8 MET B 260  HIS B 267 -1  N  LEU B 265   O  LEU B 272           
SHEET    8   D 8 ILE B 255  VAL B 256 -1  O  VAL B 256   N  MET B 260           
SHEET    1   E 9 ILE B 232  ASP B 233  0                                        
SHEET    2   E 9 LEU B 180  ALA B 184 -1  N  LEU B 180   O  ASP B 233           
SHEET    3   E 9 LEU B 190  GLU B 195 -1  O  LYS B 193   N  VAL B 181           
SHEET    4   E 9 VAL B 199  HIS B 204 -1  O  VAL B 201   N  ILE B 194           
SHEET    5   E 9 VAL C 129  GLN C 137 -1  O  VAL C 131   N  HIS B 204           
SHEET    6   E 9 GLY C 116  GLU C 124 -1  N  LEU C 121   O  CYS C 132           
SHEET    7   E 9 LEU C 105  CYS C 111 -1  N  LEU C 108   O  MET C 120           
SHEET    8   E 9 LEU C  17  SER C  20 -1  N  LEU C  17   O  CYS C 111           
SHEET    9   E 9 GLU C  72  VAL C  75 -1  O  LYS C  74   N  VAL C  18           
SHEET    1   F 6 ARG C  83  ASN C  85  0                                        
SHEET    2   F 6 HIS C  39  THR C  45 -1  N  ALA C  40   O  ILE C  84           
SHEET    3   F 6 GLY C  48  GLU C  54 -1  O  THR C  52   N  THR C  41           
SHEET    4   F 6 GLN C  60  GLN C  66 -1  O  ILE C  65   N  ILE C  49           
SHEET    5   F 6 CYS C 265  CYS C 271 -1  O  GLU C 268   N  ASN C  62           
SHEET    6   F 6 SER C 252  MET C 256 -1  N  SER C 252   O  CYS C 271           
SHEET    1   G 3 PHE C 213  HIS C 214  0                                        
SHEET    2   G 3 LYS C 155  ILE C 157 -1  N  LYS C 155   O  HIS C 214           
SHEET    3   G 3 VAL C 241  ILE C 243 -1  O  SER C 242   N  ILE C 156           
SHEET    1   H 2 SER C 174  ILE C 179  0                                        
SHEET    2   H 2 GLN C 219  LYS C 224 -1  O  TYR C 223   N  GLU C 175           
CRYST1   71.029   67.164   83.405  90.00  97.58  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014079  0.000000  0.001874        0.00000                         
SCALE2      0.000000  0.014889  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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