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Database: PDB
Entry: 3K75
LinkDB: 3K75
Original site: 3K75 
HEADER    DNA-BINDING PROTEIN                     12-OCT-09   3K75              
TITLE     X-RAY CRYSTAL STRUCTURE OF REDUCED XRCC1 BOUND TO DNA POL BETA        
TITLE    2 CATALYTIC DOMAIN                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN XRCC1;                                  
COMPND   3 CHAIN: B, C;                                                         
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 1 TO 183);                 
COMPND   5 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 1;                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA POLYMERASE BETA;                                       
COMPND   9 CHAIN: D, E;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 91 TO 335;                                    
COMPND  11 EC: 2.7.7.7, 4.2.99.-;                                               
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: HUMAN;                                                       
SOURCE   6 GENE: XRCC1;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21A;                                   
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  14 ORGANISM_COMMON: RAT;                                                
SOURCE  15 ORGANISM_TAXID: 10116;                                               
SOURCE  16 STRAIN: RATTUS;                                                      
SOURCE  17 GENE: POLB;                                                          
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ALLOSTERIC DISULFIDE, XRCC1, POL BETA, DNA DAMAGE, DNA REPAIR,        
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, DNA REPLICATION, DNA SYNTHESIS, DNA-        
KEYWDS   3 BINDING, DNA-DIRECTED DNA POLYMERASE, LYASE, MAGNESIUM, METAL-       
KEYWDS   4 BINDING, METHYLATION, NUCLEOTIDYLTRANSFERASE, TRANSFERASE, DNA-      
KEYWDS   5 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.CUNEO,R.E.LONDON                                                  
REVDAT   2   05-SEP-12 3K75    1       VERSN                                    
REVDAT   1   28-APR-10 3K75    0                                                
JRNL        AUTH   M.J.CUNEO,R.E.LONDON                                         
JRNL        TITL   OXIDATION STATE OF THE XRCC1 N-TERMINAL DOMAIN REGULATES DNA 
JRNL        TITL 2 POLYMERASE BETA BINDING AFFINITY.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107  6805 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20351257                                                     
JRNL        DOI    10.1073/PNAS.0914077107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 19123                          
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) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 957                             
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) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1287                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.4510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6282                                    
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) : 41.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.06000                                              
REMARK   3    B22 (A**2) : 0.48000                                              
REMARK   3    B33 (A**2) : -1.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.35000                                              
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): 0.523         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.417         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.195        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.880                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.813                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6481 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5836 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8747 ; 0.842 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13618 ; 0.789 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   801 ; 5.394 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   316 ;34.414 ;23.576       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1164 ;15.602 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;15.717 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   946 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7239 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1334 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3986 ; 2.544 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1617 ; 1.325 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6454 ; 4.682 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2495 ; 3.251 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2293 ; 4.514 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 12317 ; 4.119 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 12185 ;11.941 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      6       B     140      4                      
REMARK   3           1     C      6       C     140      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1904 ; 0.700 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1904 ; 6.790 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : D E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     95       D     330      4                      
REMARK   3           1     E     95       E     330      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    D    (A):   3696 ; 0.320 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    D (A**2):   3696 ; 3.960 ; 2.000           
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   : 1.40                                          
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 U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3K75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055630.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19123                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 3350, 0.2-0.3M TRI-           
REMARK 280  POTASSIUM CITRATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       70.38500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.02500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.38500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.02500            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E                                  
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 B     1                                                      
REMARK 465     TYR B    30                                                      
REMARK 465     ASP B   154                                                      
REMARK 465     LYS B   155                                                      
REMARK 465     ASP B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ALA B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     PRO B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     VAL B   165                                                      
REMARK 465     THR B   166                                                      
REMARK 465     VAL B   167                                                      
REMARK 465     THR B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     LEU B   170                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     GLN B   172                                                      
REMARK 465     PHE B   173                                                      
REMARK 465     ARG B   174                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     LYS B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     ASP B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     ALA B   182                                                      
REMARK 465     ASN B   183                                                      
REMARK 465     HIS B   184                                                      
REMARK 465     HIS B   185                                                      
REMARK 465     HIS B   186                                                      
REMARK 465     HIS B   187                                                      
REMARK 465     HIS B   188                                                      
REMARK 465     HIS B   189                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C    29                                                      
REMARK 465     TYR C    30                                                      
REMARK 465     PRO C   153                                                      
REMARK 465     ASP C   154                                                      
REMARK 465     LYS C   155                                                      
REMARK 465     ASP C   156                                                      
REMARK 465     GLU C   157                                                      
REMARK 465     ALA C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     ALA C   160                                                      
REMARK 465     PRO C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     LYS C   164                                                      
REMARK 465     VAL C   165                                                      
REMARK 465     THR C   166                                                      
REMARK 465     VAL C   167                                                      
REMARK 465     THR C   168                                                      
REMARK 465     LYS C   169                                                      
REMARK 465     LEU C   170                                                      
REMARK 465     GLY C   171                                                      
REMARK 465     GLN C   172                                                      
REMARK 465     PHE C   173                                                      
REMARK 465     ARG C   174                                                      
REMARK 465     VAL C   175                                                      
REMARK 465     LYS C   176                                                      
REMARK 465     GLU C   177                                                      
REMARK 465     GLU C   178                                                      
REMARK 465     ASP C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     SER C   181                                                      
REMARK 465     ALA C   182                                                      
REMARK 465     ASN C   183                                                      
REMARK 465     HIS C   184                                                      
REMARK 465     HIS C   185                                                      
REMARK 465     HIS C   186                                                      
REMARK 465     HIS C   187                                                      
REMARK 465     HIS C   188                                                      
REMARK 465     HIS C   189                                                      
REMARK 465     MET D    90                                                      
REMARK 465     HIS D   339                                                      
REMARK 465     HIS D   340                                                      
REMARK 465     HIS D   341                                                      
REMARK 465     MET E    90                                                      
REMARK 465     ASP E    91                                                      
REMARK 465     ASP E    92                                                      
REMARK 465     HIS E   336                                                      
REMARK 465     HIS E   337                                                      
REMARK 465     HIS E   338                                                      
REMARK 465     HIS E   339                                                      
REMARK 465     HIS E   340                                                      
REMARK 465     HIS E   341                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  48    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 138    CG   CD   CE   NZ                                   
REMARK 470     ASP D  91    CG   OD1  OD2                                       
REMARK 470     ASP D  92    CG   OD1  OD2                                       
REMARK 470     GLU D 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 167    CG   CD   CE   NZ                                   
REMARK 470     GLU E 144    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     VAL B  128   N    CA   C    O    CB   CG1  CG2                   
REMARK 480     VAL C  128   N    CA   C    O    CB   CG1  CG2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN D   245     OD1  ASP D   246              1.67            
REMARK 500   O    THR E   273     O    GLY E   274              1.77            
REMARK 500   OH   TYR D   142     OD1  ASP D   226              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG B     7     OD1  ASP B   139     4445     2.07            
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    ARG B   7      -74.68    -79.95                                   
REMARK 500    CYS B  12      114.68   -164.13                                   
REMARK 500    HIS B  19       61.26   -104.35                                   
REMARK 500    ASP B  28     -162.94    144.16                                   
REMARK 500    ALA B  79      100.22   -163.40                                   
REMARK 500    GLU B  81      -77.45    -63.71                                   
REMARK 500    GLN B  82       34.78    -96.36                                   
REMARK 500    MET B  94      119.14   -171.91                                   
REMARK 500    ASP B 126       14.04   -145.20                                   
REMARK 500    GLN B 134       89.11   -170.65                                   
REMARK 500    ARG C   7      -72.96    -76.14                                   
REMARK 500    ALA C  38      -27.34     82.03                                   
REMARK 500    GLU C  40     -138.55     52.33                                   
REMARK 500    LYS C  41      -54.23   -179.30                                   
REMARK 500    LEU C  49      108.61   -161.32                                   
REMARK 500    ASP C  63       59.77   -147.44                                   
REMARK 500    ASP C  83       50.67    -97.43                                   
REMARK 500    THR C  90      109.09    -50.99                                   
REMARK 500    MET C  94      135.65    175.17                                   
REMARK 500    ARG C 118       -4.54    -58.98                                   
REMARK 500    ASP C 126      -16.35   -144.35                                   
REMARK 500    GLN C 134       84.38   -168.86                                   
REMARK 500    ASP C 139      137.61    117.74                                   
REMARK 500    SER C 140       97.45     60.55                                   
REMARK 500    PRO C 141       27.33    -71.47                                   
REMARK 500    PHE C 142      171.63     36.58                                   
REMARK 500    CYS D 178     -147.18   -116.73                                   
REMARK 500    VAL D 221       10.28    -66.30                                   
REMARK 500    ASP D 246        2.51     84.40                                   
REMARK 500    ARG D 333       57.22   -101.36                                   
REMARK 500    SER D 334     -159.03    -83.88                                   
REMARK 500    TYR E 142       41.78   -109.65                                   
REMARK 500    CYS E 178     -162.62   -101.05                                   
REMARK 500    LYS E 230       75.05   -111.23                                   
REMARK 500    SER E 243       59.84   -140.85                                   
REMARK 500    THR E 273      -63.47    -91.41                                   
REMARK 500    GLU E 295      -35.29    -31.36                                   
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 D  244     ASN D  245                 -139.86                    
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    LYS B 129        19.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS C 129        14.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K76   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K77   RELATED DB: PDB                                   
DBREF  3K75 B    1   183  UNP    P18887   XRCC1_HUMAN      1    183             
DBREF  3K75 C    1   183  UNP    P18887   XRCC1_HUMAN      1    183             
DBREF  3K75 D   91   335  UNP    P06766   DPOLB_RAT       91    335             
DBREF  3K75 E   91   335  UNP    P06766   DPOLB_RAT       91    335             
SEQADV 3K75 HIS B  184  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS B  185  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS B  186  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS B  187  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS B  188  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS B  189  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  184  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  185  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  186  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  187  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  188  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 HIS C  189  UNP  P18887              EXPRESSION TAG                 
SEQADV 3K75 MET D   90  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  336  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  337  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  338  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  339  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  340  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS D  341  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 MET E   90  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  336  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  337  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  338  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  339  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  340  UNP  P06766              EXPRESSION TAG                 
SEQADV 3K75 HIS E  341  UNP  P06766              EXPRESSION TAG                 
SEQRES   1 B  189  MET PRO GLU ILE ARG LEU ARG HIS VAL VAL SER CYS SER          
SEQRES   2 B  189  SER GLN ASP SER THR HIS CYS ALA GLU ASN LEU LEU LYS          
SEQRES   3 B  189  ALA ASP THR TYR ARG LYS TRP ARG ALA ALA LYS ALA GLY          
SEQRES   4 B  189  GLU LYS THR ILE SER VAL VAL LEU GLN LEU GLU LYS GLU          
SEQRES   5 B  189  GLU GLN ILE HIS SER VAL ASP ILE GLY ASN ASP GLY SER          
SEQRES   6 B  189  ALA PHE VAL GLU VAL LEU VAL GLY SER SER ALA GLY GLY          
SEQRES   7 B  189  ALA GLY GLU GLN ASP TYR GLU VAL LEU LEU VAL THR SER          
SEQRES   8 B  189  SER PHE MET SER PRO SER GLU SER ARG SER GLY SER ASN          
SEQRES   9 B  189  PRO ASN ARG VAL ARG MET PHE GLY PRO ASP LYS LEU VAL          
SEQRES  10 B  189  ARG ALA ALA ALA GLU LYS ARG TRP ASP ARG VAL LYS ILE          
SEQRES  11 B  189  VAL CYS SER GLN PRO TYR SER LYS ASP SER PRO PHE GLY          
SEQRES  12 B  189  LEU SER PHE VAL ARG PHE HIS SER PRO PRO ASP LYS ASP          
SEQRES  13 B  189  GLU ALA GLU ALA PRO SER GLN LYS VAL THR VAL THR LYS          
SEQRES  14 B  189  LEU GLY GLN PHE ARG VAL LYS GLU GLU ASP GLU SER ALA          
SEQRES  15 B  189  ASN HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  189  MET PRO GLU ILE ARG LEU ARG HIS VAL VAL SER CYS SER          
SEQRES   2 C  189  SER GLN ASP SER THR HIS CYS ALA GLU ASN LEU LEU LYS          
SEQRES   3 C  189  ALA ASP THR TYR ARG LYS TRP ARG ALA ALA LYS ALA GLY          
SEQRES   4 C  189  GLU LYS THR ILE SER VAL VAL LEU GLN LEU GLU LYS GLU          
SEQRES   5 C  189  GLU GLN ILE HIS SER VAL ASP ILE GLY ASN ASP GLY SER          
SEQRES   6 C  189  ALA PHE VAL GLU VAL LEU VAL GLY SER SER ALA GLY GLY          
SEQRES   7 C  189  ALA GLY GLU GLN ASP TYR GLU VAL LEU LEU VAL THR SER          
SEQRES   8 C  189  SER PHE MET SER PRO SER GLU SER ARG SER GLY SER ASN          
SEQRES   9 C  189  PRO ASN ARG VAL ARG MET PHE GLY PRO ASP LYS LEU VAL          
SEQRES  10 C  189  ARG ALA ALA ALA GLU LYS ARG TRP ASP ARG VAL LYS ILE          
SEQRES  11 C  189  VAL CYS SER GLN PRO TYR SER LYS ASP SER PRO PHE GLY          
SEQRES  12 C  189  LEU SER PHE VAL ARG PHE HIS SER PRO PRO ASP LYS ASP          
SEQRES  13 C  189  GLU ALA GLU ALA PRO SER GLN LYS VAL THR VAL THR LYS          
SEQRES  14 C  189  LEU GLY GLN PHE ARG VAL LYS GLU GLU ASP GLU SER ALA          
SEQRES  15 C  189  ASN HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 D  252  MET ASP ASP THR SER SER SER ILE ASN PHE LEU THR ARG          
SEQRES   2 D  252  VAL THR GLY ILE GLY PRO SER ALA ALA ARG LYS LEU VAL          
SEQRES   3 D  252  ASP GLU GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN          
SEQRES   4 D  252  GLU ASP LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS          
SEQRES   5 D  252  TYR PHE GLU ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU          
SEQRES   6 D  252  MET LEU GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS          
SEQRES   7 D  252  LYS LEU ASP PRO GLU TYR ILE ALA THR VAL CYS GLY SER          
SEQRES   8 D  252  PHE ARG ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL          
SEQRES   9 D  252  LEU LEU THR HIS PRO ASN PHE THR SER GLU SER SER LYS          
SEQRES  10 D  252  GLN PRO LYS LEU LEU HIS ARG VAL VAL GLU GLN LEU GLN          
SEQRES  11 D  252  LYS VAL ARG PHE ILE THR ASP THR LEU SER LYS GLY GLU          
SEQRES  12 D  252  THR LYS PHE MET GLY VAL CYS GLN LEU PRO SER GLU ASN          
SEQRES  13 D  252  ASP GLU ASN GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG          
SEQRES  14 D  252  LEU ILE PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR          
SEQRES  15 D  252  PHE THR GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA          
SEQRES  16 D  252  HIS ALA LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR          
SEQRES  17 D  252  ILE ARG PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO          
SEQRES  18 D  252  LEU PRO VAL ASP SER GLU GLN ASP ILE PHE ASP TYR ILE          
SEQRES  19 D  252  GLN TRP ARG TYR ARG GLU PRO LYS ASP ARG SER GLU HIS          
SEQRES  20 D  252  HIS HIS HIS HIS HIS                                          
SEQRES   1 E  252  MET ASP ASP THR SER SER SER ILE ASN PHE LEU THR ARG          
SEQRES   2 E  252  VAL THR GLY ILE GLY PRO SER ALA ALA ARG LYS LEU VAL          
SEQRES   3 E  252  ASP GLU GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN          
SEQRES   4 E  252  GLU ASP LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS          
SEQRES   5 E  252  TYR PHE GLU ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU          
SEQRES   6 E  252  MET LEU GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS          
SEQRES   7 E  252  LYS LEU ASP PRO GLU TYR ILE ALA THR VAL CYS GLY SER          
SEQRES   8 E  252  PHE ARG ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL          
SEQRES   9 E  252  LEU LEU THR HIS PRO ASN PHE THR SER GLU SER SER LYS          
SEQRES  10 E  252  GLN PRO LYS LEU LEU HIS ARG VAL VAL GLU GLN LEU GLN          
SEQRES  11 E  252  LYS VAL ARG PHE ILE THR ASP THR LEU SER LYS GLY GLU          
SEQRES  12 E  252  THR LYS PHE MET GLY VAL CYS GLN LEU PRO SER GLU ASN          
SEQRES  13 E  252  ASP GLU ASN GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG          
SEQRES  14 E  252  LEU ILE PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR          
SEQRES  15 E  252  PHE THR GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA          
SEQRES  16 E  252  HIS ALA LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR          
SEQRES  17 E  252  ILE ARG PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO          
SEQRES  18 E  252  LEU PRO VAL ASP SER GLU GLN ASP ILE PHE ASP TYR ILE          
SEQRES  19 E  252  GLN TRP ARG TYR ARG GLU PRO LYS ASP ARG SER GLU HIS          
SEQRES  20 E  252  HIS HIS HIS HIS HIS                                          
HELIX    1   1 CYS B   20  LEU B   25  5                                   6    
HELIX    2   2 SER B   95  SER B  101  1                                   7    
HELIX    3   3 GLY B  112  LEU B  116  5                                   5    
HELIX    4   4 VAL B  117  LYS B  123  1                                   7    
HELIX    5   5 SER C   95  GLY C  102  1                                   8    
HELIX    6   6 GLY C  112  LEU C  116  5                                   5    
HELIX    7   7 ASP D   92  THR D  101  1                                  10    
HELIX    8   8 GLY D  107  GLU D  117  1                                  11    
HELIX    9   9 THR D  121  ARG D  126  1                                   6    
HELIX   10  10 LYS D  127  LEU D  132  5                                   6    
HELIX   11  11 ASN D  133  TYR D  142  1                                  10    
HELIX   12  12 TYR D  142  LYS D  148  1                                   7    
HELIX   13  13 ARG D  152  ASP D  170  1                                  19    
HELIX   14  14 CYS D  178  ARG D  183  1                                   6    
HELIX   15  15 GLN D  207  VAL D  221  1                                  15    
HELIX   16  16 PRO D  261  ASP D  263  5                                   3    
HELIX   17  17 GLN D  264  GLY D  274  1                                  11    
HELIX   18  18 SER D  275  LYS D  289  1                                  15    
HELIX   19  19 SER D  315  GLN D  324  1                                  10    
HELIX   20  20 GLU D  329  ARG D  333  5                                   5    
HELIX   21  21 THR E   93  ARG E  102  1                                  10    
HELIX   22  22 GLY E  107  GLU E  117  1                                  11    
HELIX   23  23 THR E  121  ASN E  128  1                                   8    
HELIX   24  24 GLU E  129  LEU E  132  5                                   4    
HELIX   25  25 ASN E  133  TYR E  142  1                                  10    
HELIX   26  26 ARG E  152  ASP E  170  1                                  19    
HELIX   27  27 GLY E  179  GLY E  184  5                                   6    
HELIX   28  28 GLN E  207  VAL E  221  1                                  15    
HELIX   29  29 PRO E  261  ASP E  263  5                                   3    
HELIX   30  30 GLN E  264  GLY E  274  1                                  11    
HELIX   31  31 SER E  275  LYS E  289  1                                  15    
HELIX   32  32 SER E  315  ILE E  323  1                                   9    
HELIX   33  33 GLU E  329  ARG E  333  5                                   5    
SHEET    1   A 5 LEU B   6  CYS B  12  0                                        
SHEET    2   A 5 THR B  42  GLU B  53 -1  O  VAL B  46   N  VAL B  10           
SHEET    3   A 5 TRP B 125  SER B 133 -1  O  ASP B 126   N  LEU B  49           
SHEET    4   A 5 PHE B  67  GLY B  73 -1  N  LEU B  71   O  LYS B 129           
SHEET    5   A 5 GLU B  85  SER B  92 -1  O  SER B  91   N  VAL B  68           
SHEET    1   B 4 TRP B  33  ARG B  34  0                                        
SHEET    2   B 4 GLY B 143  HIS B 150 -1  O  LEU B 144   N  TRP B  33           
SHEET    3   B 4 SER B  57  ASP B  63 -1  N  ASP B  59   O  ARG B 148           
SHEET    4   B 4 VAL B 108  PHE B 111 -1  O  PHE B 111   N  VAL B  58           
SHEET    1   C 5 HIS C   8  CYS C  12  0                                        
SHEET    2   C 5 THR C  42  GLN C  48 -1  O  GLN C  48   N  HIS C   8           
SHEET    3   C 5 ARG C 127  SER C 133 -1  O  ILE C 130   N  VAL C  45           
SHEET    4   C 5 PHE C  67  GLY C  73 -1  N  GLU C  69   O  VAL C 131           
SHEET    5   C 5 GLU C  85  SER C  92 -1  O  SER C  91   N  VAL C  68           
SHEET    1   D 4 TRP C  33  ARG C  34  0                                        
SHEET    2   D 4 GLY C 143  PHE C 149 -1  O  LEU C 144   N  TRP C  33           
SHEET    3   D 4 VAL C  58  ASN C  62 -1  N  ASP C  59   O  ARG C 148           
SHEET    4   D 4 VAL C 108  PHE C 111 -1  O  ARG C 109   N  ILE C  60           
SHEET    1   E 2 ILE D 150  PRO D 151  0                                        
SHEET    2   E 2 SER D 187  SER D 188 -1  O  SER D 188   N  ILE D 150           
SHEET    1   F 5 ILE D 174  VAL D 177  0                                        
SHEET    2   F 5 MET D 191  THR D 196 -1  O  LEU D 194   N  THR D 176           
SHEET    3   F 5 ARG D 253  LEU D 259  1  O  ARG D 258   N  LEU D 195           
SHEET    4   F 5 LYS D 234  CYS D 239 -1  N  PHE D 235   O  ILE D 257           
SHEET    5   F 5 ILE D 224  LYS D 230 -1  N  ASP D 226   O  VAL D 238           
SHEET    1   G 2 PHE D 291  ILE D 293  0                                        
SHEET    2   G 2 ILE D 298  PRO D 300 -1  O  ARG D 299   N  THR D 292           
SHEET    1   H 2 ILE E 150  PRO E 151  0                                        
SHEET    2   H 2 SER E 187  SER E 188 -1  O  SER E 188   N  ILE E 150           
SHEET    1   I 5 ILE E 174  VAL E 177  0                                        
SHEET    2   I 5 MET E 191  THR E 196 -1  O  LEU E 194   N  THR E 176           
SHEET    3   I 5 HIS E 252  LEU E 259  1  O  ASP E 256   N  MET E 191           
SHEET    4   I 5 LYS E 234  GLN E 240 -1  N  CYS E 239   O  ARG E 253           
SHEET    5   I 5 ILE E 224  LYS E 230 -1  N  ASP E 226   O  VAL E 238           
SHEET    1   J 2 PHE E 291  ASN E 294  0                                        
SHEET    2   J 2 THR E 297  PRO E 300 -1  O  ARG E 299   N  THR E 292           
CISPEP   1 GLU E  244    ASN E  245          0        -1.56                     
CRYST1  140.770   44.050  152.770  90.00 107.21  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007104  0.000000  0.002201        0.00000                         
SCALE2      0.000000  0.022701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006853        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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