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Database: PDB
Entry: 3II6
LinkDB: 3II6
Original site: 3II6 
HEADER    LIGASE/DNA BINDING PROTEIN              31-JUL-09   3II6              
TITLE     STRUCTURE OF HUMAN XRCC4 IN COMPLEX WITH THE TANDEM BRCT              
TITLE    2 DOMAINS OF DNA LIGASEIV.                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN XRCC4;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 1-203;                                            
COMPND   5 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 4;                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA LIGASE 4;                                              
COMPND  10 CHAIN: X, Y;                                                         
COMPND  11 FRAGMENT: C-TERMINAL TANDEM BRCT DOMAINS, RESIDUES 654-911;          
COMPND  12 SYNONYM: DNA LIGASE IV, POLYDEOXYRIBONUCLEOTIDE SYNTHASE             
COMPND  13 [ATP] 4;                                                             
COMPND  14 EC: 6.5.1.1;                                                         
COMPND  15 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACYC;                                    
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;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PPROEX                                    
KEYWDS    XRCC4, DNA LIGASE IV, NHEJ, DNA REPAIR, BRCT, ALTERNATIVE             
KEYWDS   2 SPLICING, COILED COIL, DNA DAMAGE, DNA RECOMBINATION,                
KEYWDS   3 ISOPEPTIDE BOND, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, UBL          
KEYWDS   4 CONJUGATION, ATP-BINDING, CELL CYCLE, CELL DIVISION,                 
KEYWDS   5 DISEASE MUTATION, DNA REPLICATION, LIGASE, MAGNESIUM,                
KEYWDS   6 METAL-BINDING, NUCLEOTIDE-BINDING, SCID, LIGASE/DNA BINDING          
KEYWDS   7 PROTEIN COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MEESALA,M.JUNOP                                                     
REVDAT   1   11-AUG-09 3II6    0                                                
JRNL        AUTH   P.Y.WU,P.FRIT,S.MEESALA,S.DAUVILLIER,M.MODESTI,              
JRNL        AUTH 2 S.N.ANDRES,Y.HUANG,J.SEKIGUCHI,P.CALSOU,B.SALLES,            
JRNL        AUTH 3 M.S.JUNOP                                                    
JRNL        TITL   STRUCTURAL AND FUNCTIONAL INTERACTION BETWEEN THE            
JRNL        TITL 2 HUMAN DNA REPAIR PROTEINS DNA LIGASE IV AND XRCC4            
JRNL        REF    MOL.CELL.BIOL.                V.  11  3163 2009              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   19332554                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 83736                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5334                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10642                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 281                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.PARAM                              
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  3   : ION.PARAM                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3II6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054441.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-05                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : PARABOLIC COLLIMATING MIRROR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96105                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 2.790                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.75                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM/POTASSIUM PHOSPHATE,        
REMARK 280  15% PEG 8000 MME, 200MM SODIUM CHLORIDE, PH 6.0, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 9800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 10080 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, Y                               
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     ALA A   202                                                      
REMARK 465     GLN A   203                                                      
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     ALA B   202                                                      
REMARK 465     GLN B   203                                                      
REMARK 465     ALA C   202                                                      
REMARK 465     GLN C   203                                                      
REMARK 465     GLY D    77                                                      
REMARK 465     ALA D    78                                                      
REMARK 465     GLY D    79                                                      
REMARK 465     PRO D    80                                                      
REMARK 465     ALA D    81                                                      
REMARK 465     ASP D    82                                                      
REMARK 465     ALA D   202                                                      
REMARK 465     GLN D   203                                                      
REMARK 465     GLY X   649                                                      
REMARK 465     ALA X   650                                                      
REMARK 465     MET X   651                                                      
REMARK 465     GLY X   652                                                      
REMARK 465     SER X   653                                                      
REMARK 465     ASP X   671                                                      
REMARK 465     SER X   672                                                      
REMARK 465     GLY Y   649                                                      
REMARK 465     ALA Y   650                                                      
REMARK 465     MET Y   651                                                      
REMARK 465     GLY Y   652                                                      
REMARK 465     SER Y   653                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A   9   CG    HIS A   9   CD2     0.091                       
REMARK 500    HIS A   9   CE1   HIS A   9   NE2     0.122                       
REMARK 500    SER A  15   CB    SER A  15   OG      0.122                       
REMARK 500    VAL A  22   CB    VAL A  22   CG1    -0.198                       
REMARK 500    VAL A  22   CB    VAL A  22   CG2    -0.238                       
REMARK 500    SER A  92   CB    SER A  92   OG      0.102                       
REMARK 500    VAL A 104   CB    VAL A 104   CG2    -0.157                       
REMARK 500    TRP A 155   CG    TRP A 155   CD1     0.084                       
REMARK 500    VAL A 158   CB    VAL A 158   CG1     0.126                       
REMARK 500    VAL A 158   CB    VAL A 158   CG2    -0.128                       
REMARK 500    PHE A 162   CZ    PHE A 162   CE2     0.137                       
REMARK 500    LYS A 169   CB    LYS A 169   CG     -0.209                       
REMARK 500    GLU A 173   CD    GLU A 173   OE2    -0.111                       
REMARK 500    ASP A 175   CB    ASP A 175   CG     -0.149                       
REMARK 500    ARG A 179   CZ    ARG A 179   NH1    -0.177                       
REMARK 500    PHE A 180   CG    PHE A 180   CD2     0.093                       
REMARK 500    PHE A 180   CE1   PHE A 180   CZ      0.209                       
REMARK 500    PHE A 180   CE2   PHE A 180   CD2     0.183                       
REMARK 500    GLU A 186   CG    GLU A 186   CD      0.161                       
REMARK 500    GLU A 186   CD    GLU A 186   OE1     0.109                       
REMARK 500    LEU A 199   CG    LEU A 199   CD1    -0.223                       
REMARK 500    LEU A 199   CG    LEU A 199   CD2    -0.222                       
REMARK 500    SER B  12   CB    SER B  12   OG      0.091                       
REMARK 500    SER B  50   CB    SER B  50   OG      0.116                       
REMARK 500    GLU B  60   CD    GLU B  60   OE1     0.069                       
REMARK 500    GLU B  60   CD    GLU B  60   OE2     0.067                       
REMARK 500    GLU B  60   C     GLU B  60   O       0.164                       
REMARK 500    SER B  89   CB    SER B  89   OG      0.134                       
REMARK 500    GLU B  91   CD    GLU B  91   OE1     0.165                       
REMARK 500    GLU B 121   CG    GLU B 121   CD      0.103                       
REMARK 500    GLU B 125   CD    GLU B 125   OE1     0.084                       
REMARK 500    PHE B 162   CD1   PHE B 162   CE1     0.230                       
REMARK 500    LYS B 164   CD    LYS B 164   CE      0.155                       
REMARK 500    LYS B 164   CE    LYS B 164   NZ      0.165                       
REMARK 500    GLU B 173   CB    GLU B 173   CG     -0.172                       
REMARK 500    TYR B 177   CB    TYR B 177   CG      0.126                       
REMARK 500    TYR B 177   CD1   TYR B 177   CE1     0.096                       
REMARK 500    TYR B 177   CE2   TYR B 177   CD2    -0.136                       
REMARK 500    HIS C   9   CG    HIS C   9   CD2     0.074                       
REMARK 500    SER C  15   CB    SER C  15   OG      0.146                       
REMARK 500    VAL C  22   CB    VAL C  22   CG1    -0.216                       
REMARK 500    VAL C  22   CB    VAL C  22   CG2    -0.148                       
REMARK 500    SER C  53   CB    SER C  53   OG      0.080                       
REMARK 500    GLU C  60   CD    GLU C  60   OE1     0.086                       
REMARK 500    SER C  92   CB    SER C  92   OG      0.103                       
REMARK 500    VAL C 104   CB    VAL C 104   CG2    -0.195                       
REMARK 500    GLU C 147   CD    GLU C 147   OE2    -0.119                       
REMARK 500    ASP C 154   CG    ASP C 154   OD1    -0.156                       
REMARK 500    TRP C 155   CG    TRP C 155   CD1     0.102                       
REMARK 500    VAL C 158   CB    VAL C 158   CG1     0.131                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     143 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A  22   CG1 -  CB  -  CG2 ANGL. DEV. = -12.3 DEGREES          
REMARK 500    MET A  61   CG  -  SD  -  CE  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    GLU A  62   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    LEU A 101   O   -  C   -  N   ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ASP A 103   CB  -  CG  -  OD1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    GLU A 147   OE1 -  CD  -  OE2 ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 153   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 154   OD1 -  CG  -  OD2 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP A 154   CB  -  CG  -  OD1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ASP A 157   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    GLU A 163   OE1 -  CD  -  OE2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    LYS A 169   CD  -  CE  -  NZ  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ASP A 175   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG A 179   NH1 -  CZ  -  NH2 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    ARG A 179   NE  -  CZ  -  NH2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    LYS B  26   CB  -  CA  -  C   ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ASP B 157   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B 157   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    LEU B 172   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ASP B 175   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    TYR B 177   CD1 -  CE1 -  CZ  ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    ARG B 179   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    LEU B 184   CB  -  CG  -  CD2 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    LYS B 190   CD  -  CE  -  NZ  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    SER B 193   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    ARG C   3   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    VAL C  22   CG1 -  CB  -  CG2 ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ILE C  34   CG1 -  CB  -  CG2 ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLU C  62   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    GLU C  62   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LYS C  63   O   -  C   -  N   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ARG C  71   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL C 104   CG1 -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LEU C 108   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ARG C 124   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    GLU C 147   OE1 -  CD  -  OE2 ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ARG C 153   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG C 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP C 154   CB  -  CG  -  OD2 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ASP C 157   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    VAL C 158   CA  -  CB  -  CG2 ANGL. DEV. = -12.6 DEGREES          
REMARK 500    GLU C 163   OE1 -  CD  -  OE2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    THR C 174   OG1 -  CB  -  CG2 ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASP C 175   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     145 ANGLE DEVIATIONS.                             
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    LYS A   4      106.11   -171.40                                   
REMARK 500    SER A  23      136.75   -174.28                                   
REMARK 500    TRP A  24     -165.11   -177.41                                   
REMARK 500    ILE A  34       81.23   -164.74                                   
REMARK 500    HIS A  40      -21.96   -143.70                                   
REMARK 500    ALA A  42      119.22   -169.32                                   
REMARK 500    THR A  44     -158.44   -129.58                                   
REMARK 500    GLU A  55      -54.40    -27.23                                   
REMARK 500    GLU A  62      129.78    -37.28                                   
REMARK 500    LYS A  65      -52.98    -27.94                                   
REMARK 500    ALA A  81      -75.30    -47.92                                   
REMARK 500    ASP A  82      114.72    -36.73                                   
REMARK 500    CYS A  93       54.41     32.42                                   
REMARK 500    LEU A 101     -105.87   -109.93                                   
REMARK 500    ASP A 103       16.69     52.26                                   
REMARK 500    SER B   6      117.84   -161.73                                   
REMARK 500    LYS B  26      -19.77     58.03                                   
REMARK 500    HIS B  40      -50.83   -125.59                                   
REMARK 500    SER B  50      -33.65    161.05                                   
REMARK 500    LYS B  63      -24.75    -39.99                                   
REMARK 500    TYR B  66      -79.11    -93.47                                   
REMARK 500    VAL B  67      -58.33    -25.48                                   
REMARK 500    LEU B  74      -51.23   -124.30                                   
REMARK 500    LEU B  75       34.92    -83.84                                   
REMARK 500    CYS B  93       -4.94     98.43                                   
REMARK 500    ASP B 103       -2.81     60.09                                   
REMARK 500    SER B 110       91.71   -173.89                                   
REMARK 500    LYS B 115      174.48    -59.30                                   
REMARK 500    LYS C   4      107.54   -166.80                                   
REMARK 500    SER C  23      136.23    179.18                                   
REMARK 500    TRP C  24     -153.21   -167.52                                   
REMARK 500    ILE C  34       78.06   -161.80                                   
REMARK 500    HIS C  40      -46.47   -163.79                                   
REMARK 500    ALA C  42      114.76   -174.06                                   
REMARK 500    THR C  44     -158.95   -130.60                                   
REMARK 500    GLU C  55      -56.51    -26.76                                   
REMARK 500    GLU C  62      127.20    -38.44                                   
REMARK 500    ALA C  81      -72.51    -49.55                                   
REMARK 500    CYS C  93       71.11     22.09                                   
REMARK 500    LYS C 102       29.14     43.31                                   
REMARK 500    ASN C 200     -164.40    -69.98                                   
REMARK 500    LYS D  26      -17.24     58.13                                   
REMARK 500    SER D  48     -158.64   -104.24                                   
REMARK 500    GLU D  49       36.21    -73.80                                   
REMARK 500    SER D  50      -19.38   -158.90                                   
REMARK 500    GLU D  60      -11.52    104.13                                   
REMARK 500    GLU D  62      110.72    -35.31                                   
REMARK 500    LYS D  63      -11.50    -49.72                                   
REMARK 500    TYR D  66      -80.22    -77.00                                   
REMARK 500    VAL D  67      -58.12    -27.69                                   
REMARK 500    LEU D  74      -57.88   -131.39                                   
REMARK 500    LEU D  75       37.17    -78.78                                   
REMARK 500    CYS D  93        3.86     94.80                                   
REMARK 500    ASP D 103      -11.30     65.77                                   
REMARK 500    SER D 110       91.72   -173.73                                   
REMARK 500    LEU D 113     -179.85    -62.30                                   
REMARK 500    GLU D 114       84.45   -155.43                                   
REMARK 500    LYS D 115     -176.15    -54.90                                   
REMARK 500    SER X 656      168.51    174.58                                   
REMARK 500    CYS X 747      140.32    -14.97                                   
REMARK 500    THR X 769     -167.65    -72.81                                   
REMARK 500    ASN X 772      -71.98    -38.75                                   
REMARK 500    ILE X 781      -17.27   -154.15                                   
REMARK 500    LYS X 782      126.70    -37.65                                   
REMARK 500    ASN X 783     -148.70    -92.05                                   
REMARK 500    SER X 784      154.33    171.23                                   
REMARK 500    ASN X 785       -9.12   -144.89                                   
REMARK 500    GLU X 786       -4.52    -28.33                                   
REMARK 500    HIS X 848       31.23    -95.32                                   
REMARK 500    ASP X 868      105.45    -59.23                                   
REMARK 500    CYS X 901       21.93     46.87                                   
REMARK 500    ASN Y 657       30.52   -143.30                                   
REMARK 500    THR Y 670     -112.39   -115.68                                   
REMARK 500    ASP Y 671      -86.89   -139.01                                   
REMARK 500    SER Y 672     -122.73     36.16                                   
REMARK 500    LEU Y 714      -33.78   -134.28                                   
REMARK 500    ASN Y 716       68.55    -63.28                                   
REMARK 500    THR Y 732      -39.46    -37.82                                   
REMARK 500    ARG Y 741      -27.92    -33.14                                   
REMARK 500    HIS Y 753      -70.98    -53.68                                   
REMARK 500    SER Y 804       30.95     72.47                                   
REMARK 500    LEU Y 810       13.28    -66.16                                   
REMARK 500    SER Y 811       15.53   -148.17                                   
REMARK 500    PHE Y 813       30.77    -99.75                                   
REMARK 500    ALA Y 824      -16.39    -49.33                                   
REMARK 500    ILE Y 826      135.17    -31.83                                   
REMARK 500    ASN Y 827       -8.81     70.19                                   
REMARK 500    LEU Y 829        6.10    -32.26                                   
REMARK 500    SER Y 830       48.50   -158.54                                   
REMARK 500    LYS Y 832      109.10    -19.79                                   
REMARK 500    GLU Y 834      172.72    -58.20                                   
REMARK 500    LEU Y 856       47.94    -79.11                                   
REMARK 500    ALA Y 857     -175.73    -69.88                                   
REMARK 500    GLU Y 858       30.13    -70.94                                   
REMARK 500    ARG Y 880      -56.35    -27.01                                   
REMARK 500    CYS Y 901       27.73     48.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   25     LYS A   26                 -101.05                    
REMARK 500 LYS A   26     THR A   27                  117.43                    
REMARK 500 GLY A   39     HIS A   40                 -142.00                    
REMARK 500 ASP B   82     VAL B   83                 -100.90                    
REMARK 500 VAL B   83     TYR B   84                  145.76                    
REMARK 500 GLU C   25     LYS C   26                 -116.73                    
REMARK 500 LYS C   26     THR C   27                  104.54                    
REMARK 500 ILE C  127     CYS C  128                  148.91                    
REMARK 500 GLU D   60     MET D   61                 -138.97                    
REMARK 500 SER X  668     GLY X  669                  -82.67                    
REMARK 500 GLY X  669     THR X  670                  -72.45                    
REMARK 500 GLN X  673     PRO X  674                 -131.46                    
REMARK 500 ILE X  701     ALA X  702                 -147.62                    
REMARK 500 MET X  746     CYS X  747                  140.09                    
REMARK 500 ILE X  781     LYS X  782                 -140.62                    
REMARK 500 ASN X  783     SER X  784                  -97.97                    
REMARK 500 SER X  784     ASN X  785                 -120.14                    
REMARK 500 ASN X  785     GLU X  786                  146.93                    
REMARK 500 ARG X  884     LYS X  885                  142.36                    
REMARK 500 GLU X  905     GLU X  906                 -123.81                    
REMARK 500 LEU X  910     ILE X  911                  136.80                    
REMARK 500 SER Y  668     GLY Y  669                  132.13                    
REMARK 500 THR Y  670     ASP Y  671                 -119.40                    
REMARK 500 ASP Y  671     SER Y  672                   80.06                    
REMARK 500 ILE Y  713     LEU Y  714                 -140.93                    
REMARK 500 LEU Y  714     SER Y  715                  144.96                    
REMARK 500 THR Y  817     VAL Y  818                 -148.81                    
REMARK 500 SER Y  830     THR Y  831                  138.26                    
REMARK 500 ASN Y  833     GLU Y  834                 -139.30                    
REMARK 500 GLY Y  859     VAL Y  860                 -141.45                    
REMARK 500 THR Y  881     PHE Y  882                 -148.36                    
REMARK 500 LEU Y  903     GLN Y  904                  144.97                    
REMARK 500 GLU Y  905     GLU Y  906                 -134.27                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    PHE X 813         0.08    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP X 759        -10.43                                           
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 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: (11X,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     LYS A  63        22.8      L          L   OUTSIDE RANGE          
REMARK 500     TYR A 177        24.8      L          L   OUTSIDE RANGE          
REMARK 500     ALA A 201        24.7      L          L   OUTSIDE RANGE          
REMARK 500     SER B  48        24.7      L          L   OUTSIDE RANGE          
REMARK 500     ASP B 103        23.4      L          L   OUTSIDE RANGE          
REMARK 500     MET D  59        20.2      L          L   OUTSIDE RANGE          
REMARK 500     VAL D  83        23.8      L          L   OUTSIDE RANGE          
REMARK 500     ASP D 103        22.0      L          L   OUTSIDE RANGE          
REMARK 500     ASN D 148        24.1      L          L   OUTSIDE RANGE          
REMARK 500     ILE X 655        21.0      L          L   OUTSIDE RANGE          
REMARK 500     ASN X 657        24.4      L          L   OUTSIDE RANGE          
REMARK 500     GLN X 691        24.0      L          L   OUTSIDE RANGE          
REMARK 500     ASN X 706        22.2      L          L   OUTSIDE RANGE          
REMARK 500     ILE X 707        21.0      L          L   OUTSIDE RANGE          
REMARK 500     ASP X 719        55.6      L          L   OUTSIDE RANGE          
REMARK 500     LYS X 722        21.0      L          L   OUTSIDE RANGE          
REMARK 500     ILE X 744        16.8      L          L   OUTSIDE RANGE          
REMARK 500     ILE X 781        22.2      L          L   OUTSIDE RANGE          
REMARK 500     LYS X 782        14.1      L          L   OUTSIDE RANGE          
REMARK 500     ASN X 785        45.8      L          L   OUTSIDE RANGE          
REMARK 500     GLN X 787        23.9      L          L   OUTSIDE RANGE          
REMARK 500     LEU X 843        23.3      L          L   OUTSIDE RANGE          
REMARK 500     GLU X 905        23.3      L          L   OUTSIDE RANGE          
REMARK 500     ILE X 911         7.1      L          D   EXPECTING SP3          
REMARK 500     GLN Y 691        24.2      L          L   OUTSIDE RANGE          
REMARK 500     LEU Y 714        45.1      L          L   OUTSIDE RANGE          
REMARK 500     SER Y 715        45.1      L          L   OUTSIDE RANGE          
REMARK 500     ASP Y 759        48.0      L          L   OUTSIDE RANGE          
REMARK 500     TYR Y 761        48.3      L          L   OUTSIDE RANGE          
REMARK 500     SER Y 779        21.5      L          L   OUTSIDE RANGE          
REMARK 500     ARG Y 802        24.8      L          L   OUTSIDE RANGE          
REMARK 500     PHE Y 813        24.9      L          L   OUTSIDE RANGE          
REMARK 500     ASP Y 828        24.4      L          L   OUTSIDE RANGE          
REMARK 500     SER Y 830        14.9      L          L   OUTSIDE RANGE          
REMARK 500     VAL Y 872        24.7      L          L   OUTSIDE RANGE          
REMARK 500     GLU Y 905        13.1      L          L   OUTSIDE RANGE          
REMARK 500     ASN Y 907        22.9      L          L   OUTSIDE RANGE          
REMARK 500     ILE Y 911        21.1      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL Y 301                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL Y 302                  
DBREF  3II6 A    1   203  UNP    Q13426   XRCC4_HUMAN      1    203             
DBREF  3II6 B    1   203  UNP    Q13426   XRCC4_HUMAN      1    203             
DBREF  3II6 C    1   203  UNP    Q13426   XRCC4_HUMAN      1    203             
DBREF  3II6 D    1   203  UNP    Q13426   XRCC4_HUMAN      1    203             
DBREF  3II6 X  654   911  UNP    P49917   DNLI4_HUMAN    654    911             
DBREF  3II6 Y  654   911  UNP    P49917   DNLI4_HUMAN    654    911             
SEQADV 3II6 GLU A   60  UNP  Q13426    ALA    60 ENGINEERED                     
SEQADV 3II6 THR A  134  UNP  Q13426    ILE   134 ENGINEERED                     
SEQADV 3II6 GLU B   60  UNP  Q13426    ALA    60 ENGINEERED                     
SEQADV 3II6 THR B  134  UNP  Q13426    ILE   134 ENGINEERED                     
SEQADV 3II6 GLU C   60  UNP  Q13426    ALA    60 ENGINEERED                     
SEQADV 3II6 THR C  134  UNP  Q13426    ILE   134 ENGINEERED                     
SEQADV 3II6 GLU D   60  UNP  Q13426    ALA    60 ENGINEERED                     
SEQADV 3II6 THR D  134  UNP  Q13426    ILE   134 ENGINEERED                     
SEQADV 3II6 GLY X  649  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 ALA X  650  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 MET X  651  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 GLY X  652  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 SER X  653  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 GLY Y  649  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 ALA Y  650  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 MET Y  651  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 GLY Y  652  UNP  P49917              EXPRESSION TAG                 
SEQADV 3II6 SER Y  653  UNP  P49917              EXPRESSION TAG                 
SEQRES   1 A  203  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 A  203  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 A  203  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 A  203  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 A  203  SER GLN GLU ALA ASP ASP MET GLU MET GLU LYS GLY LYS          
SEQRES   6 A  203  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 A  203  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 A  203  SER CYS TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 A  203  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 A  203  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE CYS TYR CYS          
SEQRES  11 A  203  LEU ASP THR THR ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 A  203  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 A  203  ASP VAL GLN GLY ARG PHE GLU LYS CYS VAL SER ALA LYS          
SEQRES  14 A  203  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 A  203  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 A  203  ASN LYS LEU LEU ASN ALA ALA GLN                              
SEQRES   1 B  203  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 B  203  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 B  203  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 B  203  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 B  203  SER GLN GLU ALA ASP ASP MET GLU MET GLU LYS GLY LYS          
SEQRES   6 B  203  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 B  203  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 B  203  SER CYS TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 B  203  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 B  203  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE CYS TYR CYS          
SEQRES  11 B  203  LEU ASP THR THR ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 B  203  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 B  203  ASP VAL GLN GLY ARG PHE GLU LYS CYS VAL SER ALA LYS          
SEQRES  14 B  203  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 B  203  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 B  203  ASN LYS LEU LEU ASN ALA ALA GLN                              
SEQRES   1 C  203  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 C  203  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 C  203  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 C  203  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 C  203  SER GLN GLU ALA ASP ASP MET GLU MET GLU LYS GLY LYS          
SEQRES   6 C  203  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 C  203  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 C  203  SER CYS TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 C  203  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 C  203  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE CYS TYR CYS          
SEQRES  11 C  203  LEU ASP THR THR ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 C  203  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 C  203  ASP VAL GLN GLY ARG PHE GLU LYS CYS VAL SER ALA LYS          
SEQRES  14 C  203  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 C  203  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 C  203  ASN LYS LEU LEU ASN ALA ALA GLN                              
SEQRES   1 D  203  MET GLU ARG LYS ILE SER ARG ILE HIS LEU VAL SER GLU          
SEQRES   2 D  203  PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP GLU LYS          
SEQRES   3 D  203  THR LEU GLU SER GLY PHE VAL ILE THR LEU THR ASP GLY          
SEQRES   4 D  203  HIS SER ALA TRP THR GLY THR VAL SER GLU SER GLU ILE          
SEQRES   5 D  203  SER GLN GLU ALA ASP ASP MET GLU MET GLU LYS GLY LYS          
SEQRES   6 D  203  TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER GLY ALA          
SEQRES   7 D  203  GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER LYS GLU          
SEQRES   8 D  203  SER CYS TYR PHE PHE PHE GLU LYS ASN LEU LYS ASP VAL          
SEQRES   9 D  203  SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS VAL GLU          
SEQRES  10 D  203  ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE CYS TYR CYS          
SEQRES  11 D  203  LEU ASP THR THR ALA GLU ASN GLN ALA LYS ASN GLU HIS          
SEQRES  12 D  203  LEU GLN LYS GLU ASN GLU ARG LEU LEU ARG ASP TRP ASN          
SEQRES  13 D  203  ASP VAL GLN GLY ARG PHE GLU LYS CYS VAL SER ALA LYS          
SEQRES  14 D  203  GLU ALA LEU GLU THR ASP LEU TYR LYS ARG PHE ILE LEU          
SEQRES  15 D  203  VAL LEU ASN GLU LYS LYS THR LYS ILE ARG SER LEU HIS          
SEQRES  16 D  203  ASN LYS LEU LEU ASN ALA ALA GLN                              
SEQRES   1 X  263  GLY ALA MET GLY SER LYS ILE SER ASN ILE PHE GLU ASP          
SEQRES   2 X  263  VAL GLU PHE CYS VAL MET SER GLY THR ASP SER GLN PRO          
SEQRES   3 X  263  LYS PRO ASP LEU GLU ASN ARG ILE ALA GLU PHE GLY GLY          
SEQRES   4 X  263  TYR ILE VAL GLN ASN PRO GLY PRO ASP THR TYR CYS VAL          
SEQRES   5 X  263  ILE ALA GLY SER GLU ASN ILE ARG VAL LYS ASN ILE ILE          
SEQRES   6 X  263  LEU SER ASN LYS HIS ASP VAL VAL LYS PRO ALA TRP LEU          
SEQRES   7 X  263  LEU GLU CYS PHE LYS THR LYS SER PHE VAL PRO TRP GLN          
SEQRES   8 X  263  PRO ARG PHE MET ILE HIS MET CYS PRO SER THR LYS GLU          
SEQRES   9 X  263  HIS PHE ALA ARG GLU TYR ASP CYS TYR GLY ASP SER TYR          
SEQRES  10 X  263  PHE ILE ASP THR ASP LEU ASN GLN LEU LYS GLU VAL PHE          
SEQRES  11 X  263  SER GLY ILE LYS ASN SER ASN GLU GLN THR PRO GLU GLU          
SEQRES  12 X  263  MET ALA SER LEU ILE ALA ASP LEU GLU TYR ARG TYR SER          
SEQRES  13 X  263  TRP ASP CYS SER PRO LEU SER MET PHE ARG ARG HIS THR          
SEQRES  14 X  263  VAL TYR LEU ASP SER TYR ALA VAL ILE ASN ASP LEU SER          
SEQRES  15 X  263  THR LYS ASN GLU GLY THR ARG LEU ALA ILE LYS ALA LEU          
SEQRES  16 X  263  GLU LEU ARG PHE HIS GLY ALA LYS VAL VAL SER CYS LEU          
SEQRES  17 X  263  ALA GLU GLY VAL SER HIS VAL ILE ILE GLY GLU ASP HIS          
SEQRES  18 X  263  SER ARG VAL ALA ASP PHE LYS ALA PHE ARG ARG THR PHE          
SEQRES  19 X  263  LYS ARG LYS PHE LYS ILE LEU LYS GLU SER TRP VAL THR          
SEQRES  20 X  263  ASP SER ILE ASP LYS CYS GLU LEU GLN GLU GLU ASN GLN          
SEQRES  21 X  263  TYR LEU ILE                                                  
SEQRES   1 Y  263  GLY ALA MET GLY SER LYS ILE SER ASN ILE PHE GLU ASP          
SEQRES   2 Y  263  VAL GLU PHE CYS VAL MET SER GLY THR ASP SER GLN PRO          
SEQRES   3 Y  263  LYS PRO ASP LEU GLU ASN ARG ILE ALA GLU PHE GLY GLY          
SEQRES   4 Y  263  TYR ILE VAL GLN ASN PRO GLY PRO ASP THR TYR CYS VAL          
SEQRES   5 Y  263  ILE ALA GLY SER GLU ASN ILE ARG VAL LYS ASN ILE ILE          
SEQRES   6 Y  263  LEU SER ASN LYS HIS ASP VAL VAL LYS PRO ALA TRP LEU          
SEQRES   7 Y  263  LEU GLU CYS PHE LYS THR LYS SER PHE VAL PRO TRP GLN          
SEQRES   8 Y  263  PRO ARG PHE MET ILE HIS MET CYS PRO SER THR LYS GLU          
SEQRES   9 Y  263  HIS PHE ALA ARG GLU TYR ASP CYS TYR GLY ASP SER TYR          
SEQRES  10 Y  263  PHE ILE ASP THR ASP LEU ASN GLN LEU LYS GLU VAL PHE          
SEQRES  11 Y  263  SER GLY ILE LYS ASN SER ASN GLU GLN THR PRO GLU GLU          
SEQRES  12 Y  263  MET ALA SER LEU ILE ALA ASP LEU GLU TYR ARG TYR SER          
SEQRES  13 Y  263  TRP ASP CYS SER PRO LEU SER MET PHE ARG ARG HIS THR          
SEQRES  14 Y  263  VAL TYR LEU ASP SER TYR ALA VAL ILE ASN ASP LEU SER          
SEQRES  15 Y  263  THR LYS ASN GLU GLY THR ARG LEU ALA ILE LYS ALA LEU          
SEQRES  16 Y  263  GLU LEU ARG PHE HIS GLY ALA LYS VAL VAL SER CYS LEU          
SEQRES  17 Y  263  ALA GLU GLY VAL SER HIS VAL ILE ILE GLY GLU ASP HIS          
SEQRES  18 Y  263  SER ARG VAL ALA ASP PHE LYS ALA PHE ARG ARG THR PHE          
SEQRES  19 Y  263  LYS ARG LYS PHE LYS ILE LEU LYS GLU SER TRP VAL THR          
SEQRES  20 Y  263  ASP SER ILE ASP LYS CYS GLU LEU GLN GLU GLU ASN GLN          
SEQRES  21 Y  263  TYR LEU ILE                                                  
HET     CL  Y 301       1                                                       
HET     CL  Y 302       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   9  HOH   *281(H2 O)                                                    
HELIX    1   1 GLU A   49  MET A   59  1                                  11    
HELIX    2   2 GLU A   62  LEU A   75  1                                  14    
HELIX    3   3 ASN A  118  ALA A  201  1                                  84    
HELIX    4   4 GLN B   54  MET B   59  1                                   6    
HELIX    5   5 LYS B   63  LEU B   75  1                                  13    
HELIX    6   6 ASN B  118  ALA B  201  1                                  84    
HELIX    7   7 GLU C   49  MET C   59  1                                  11    
HELIX    8   8 GLY C   64  LEU C   75  1                                  12    
HELIX    9   9 ASN C  118  ASN C  200  1                                  83    
HELIX   10  10 GLN D   54  MET D   59  1                                   6    
HELIX   11  11 GLU D   62  LEU D   75  1                                  14    
HELIX   12  12 ALA D  120  ASN D  200  1                                  81    
HELIX   13  13 PRO X  674  PHE X  685  1                                  12    
HELIX   14  14 ASN X  706  SER X  715  1                                  10    
HELIX   15  15 LYS X  722  LYS X  733  1                                  12    
HELIX   16  16 GLN X  739  ARG X  741  5                                   3    
HELIX   17  17 CYS X  747  PHE X  754  1                                   8    
HELIX   18  18 ASP X  770  GLY X  780  1                                  11    
HELIX   19  19 THR X  788  TYR X  803  1                                  16    
HELIX   20  20 SER X  808  MET X  812  5                                   5    
HELIX   21  21 ASP X  828  LYS X  832  5                                   5    
HELIX   22  22 THR X  836  HIS X  848  1                                  13    
HELIX   23  23 ARG X  871  THR X  881  1                                  11    
HELIX   24  24 GLU X  891  LYS X  900  1                                  10    
HELIX   25  25 GLU X  905  TYR X  909  5                                   5    
HELIX   26  26 PRO Y  674  PHE Y  685  1                                  12    
HELIX   27  27 ASN Y  706  ILE Y  713  1                                   8    
HELIX   28  28 LYS Y  722  LYS Y  733  1                                  12    
HELIX   29  29 GLN Y  739  ARG Y  741  5                                   3    
HELIX   30  30 CYS Y  747  TYR Y  758  1                                  12    
HELIX   31  31 ASP Y  770  ILE Y  781  1                                  12    
HELIX   32  32 THR Y  788  TYR Y  803  1                                  16    
HELIX   33  33 SER Y  804  MET Y  812  5                                   9    
HELIX   34  34 THR Y  836  HIS Y  848  1                                  13    
HELIX   35  35 ARG Y  871  PHE Y  882  1                                  12    
HELIX   36  36 GLU Y  891  LYS Y  900  1                                  10    
HELIX   37  37 GLU Y  905  TYR Y  909  5                                   5    
SHEET    1   A 4 ARG A   3  LEU A  10  0                                        
SHEET    2   A 4 GLU A  13  SER A  23 -1  O  VAL A  22   N  LYS A   4           
SHEET    3   A 4 GLY A  31  THR A  37 -1  O  THR A  35   N  GLN A  21           
SHEET    4   A 4 THR A  46  SER A  48 -1  O  VAL A  47   N  PHE A  32           
SHEET    1   B 5 ARG A   3  LEU A  10  0                                        
SHEET    2   B 5 GLU A  13  SER A  23 -1  O  VAL A  22   N  LYS A   4           
SHEET    3   B 5 GLY A  31  THR A  37 -1  O  THR A  35   N  GLN A  21           
SHEET    4   B 5 ALA A  42  THR A  44 -1  O  TRP A  43   N  LEU A  36           
SHEET    5   B 5 GLU A 114  LYS A 115 -1  O  GLU A 114   N  THR A  44           
SHEET    1   C 3 TYR A  84  PHE A  88  0                                        
SHEET    2   C 3 TYR A  94  ASN A 100 -1  O  PHE A  96   N  ASN A  87           
SHEET    3   C 3 SER A 105  ASN A 112 -1  O  LEU A 108   N  PHE A  97           
SHEET    1   D 4 GLU B   2  ILE B   8  0                                        
SHEET    2   D 4 HIS B  18  TRP B  24 -1  O  LEU B  20   N  SER B   6           
SHEET    3   D 4 PHE B  32  THR B  37 -1  O  VAL B  33   N  SER B  23           
SHEET    4   D 4 ALA B  42  TRP B  43 -1  O  TRP B  43   N  LEU B  36           
SHEET    1   E 3 PHE B  86  PHE B  88  0                                        
SHEET    2   E 3 TYR B  94  PHE B  97 -1  O  PHE B  96   N  ASN B  87           
SHEET    3   E 3 GLY B 109  ASN B 112 -1  O  PHE B 111   N  PHE B  95           
SHEET    1   F 4 ARG C   3  LEU C  10  0                                        
SHEET    2   F 4 GLU C  13  SER C  23 -1  O  VAL C  22   N  LYS C   4           
SHEET    3   F 4 GLY C  31  THR C  37 -1  O  THR C  35   N  GLN C  21           
SHEET    4   F 4 THR C  46  SER C  48 -1  O  VAL C  47   N  PHE C  32           
SHEET    1   G 5 ARG C   3  LEU C  10  0                                        
SHEET    2   G 5 GLU C  13  SER C  23 -1  O  VAL C  22   N  LYS C   4           
SHEET    3   G 5 GLY C  31  THR C  37 -1  O  THR C  35   N  GLN C  21           
SHEET    4   G 5 ALA C  42  THR C  44 -1  O  TRP C  43   N  LEU C  36           
SHEET    5   G 5 GLU C 114  LYS C 115 -1  O  GLU C 114   N  THR C  44           
SHEET    1   H 3 TYR C  84  SER C  89  0                                        
SHEET    2   H 3 TYR C  94  LEU C 101 -1  O  GLU C  98   N  THR C  85           
SHEET    3   H 3 VAL C 104  ASN C 112 -1  O  PHE C 111   N  PHE C  95           
SHEET    1   I 4 GLU D   2  ILE D   8  0                                        
SHEET    2   I 4 HIS D  18  TRP D  24 -1  O  LEU D  20   N  SER D   6           
SHEET    3   I 4 GLY D  31  THR D  37 -1  O  VAL D  33   N  SER D  23           
SHEET    4   I 4 ALA D  42  SER D  48 -1  O  GLY D  45   N  ILE D  34           
SHEET    1   J 3 PHE D  86  PHE D  88  0                                        
SHEET    2   J 3 TYR D  94  PHE D  97 -1  O  PHE D  96   N  ASN D  87           
SHEET    3   J 3 GLY D 109  ASN D 112 -1  O  PHE D 111   N  PHE D  95           
SHEET    1   K 5 TYR X 688  ILE X 689  0                                        
SHEET    2   K 5 GLU X 663  VAL X 666  1  N  PHE X 664   O  TYR X 688           
SHEET    3   K 5 THR X 697  ILE X 701  1  O  TYR X 698   N  GLU X 663           
SHEET    4   K 5 VAL X 720  VAL X 721  1  O  VAL X 721   N  VAL X 700           
SHEET    5   K 5 MET X 743  HIS X 745 -1  O  HIS X 745   N  VAL X 720           
SHEET    1   L 4 LYS X 851  VAL X 853  0                                        
SHEET    2   L 4 THR X 817  LEU X 820  1  N  VAL X 818   O  LYS X 851           
SHEET    3   L 4 HIS X 862  ILE X 865  1  O  ILE X 864   N  TYR X 819           
SHEET    4   L 4 LYS X 887  LYS X 890  1  O  LEU X 889   N  VAL X 863           
SHEET    1   M 5 TYR Y 688  ILE Y 689  0                                        
SHEET    2   M 5 GLU Y 663  VAL Y 666  1  N  PHE Y 664   O  TYR Y 688           
SHEET    3   M 5 THR Y 697  ILE Y 701  1  O  TYR Y 698   N  GLU Y 663           
SHEET    4   M 5 VAL Y 720  VAL Y 721  1  O  VAL Y 721   N  VAL Y 700           
SHEET    5   M 5 MET Y 743  HIS Y 745 -1  O  HIS Y 745   N  VAL Y 720           
SHEET    1   N 4 LYS Y 851  VAL Y 853  0                                        
SHEET    2   N 4 THR Y 817  LEU Y 820  1  N  VAL Y 818   O  LYS Y 851           
SHEET    3   N 4 HIS Y 862  ILE Y 865  1  O  ILE Y 864   N  TYR Y 819           
SHEET    4   N 4 LYS Y 887  LYS Y 890  1  O  LYS Y 887   N  VAL Y 863           
SITE     1 AC1  2 GLY Y 669  LYS Y 675                                          
SITE     1 AC2  1 TRP Y 738                                                     
CRYST1   67.243   85.982  111.608  67.34  82.86  74.52 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014871 -0.004119 -0.000373        0.00000                         
SCALE2      0.000000  0.012068 -0.004779        0.00000                         
SCALE3      0.000000  0.000000  0.009712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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