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Database: PDB
Entry: 4IGK
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HEADER    TRANSCRIPTION                           17-DEC-12   4IGK              
TITLE     STRUCTURE OF HUMAN BRCA1 BRCT IN COMPLEX WITH ATRIP PEPTIDE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: BRCT DOMAIN, UNP RESIDUES 1646-1859;                       
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ATRIP PEPTIDE;                                             
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 237-243;                                      
COMPND  12 SYNONYM: ATM AND RAD3-RELATED-INTERACTING PROTEIN;                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRCA1, RNF53;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    CELL CYCLE, DISEASE MUTATION, DNA DAMAGE, DNA REPAIR, FATTY ACID      
KEYWDS   2 BIOSYNTHESIS, LIGASE, LIPID SYNTHESIS, METAL-BINDING, NUCLEUS,       
KEYWDS   3 PHOSPHOPROTEIN, TUMOR SUPPRESSOR, UBL CONJUGATION PATHWAY, ZINC-     
KEYWDS   4 FINGER, BRCT DOMAIN, DNA DAMAGE RESPONSE, PHOSPHO PEPTIDE            
KEYWDS   5 INTERACTIONS, DNA-BINDING, PHOSPHO PEPTIDE BINDING, TRANSCRIPTION    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LIU,J.A.A.LADIAS                                                    
REVDAT   2   25-DEC-13 4IGK    1       JRNL                                     
REVDAT   1   30-OCT-13 4IGK    0                                                
JRNL        AUTH   X.LIU,J.A.LADIAS                                             
JRNL        TITL   STRUCTURAL BASIS FOR THE BRCA1 BRCT INTERACTION WITH THE     
JRNL        TITL 2 PROTEINS ATRIP AND BAAT1.                                    
JRNL        REF    BIOCHEMISTRY                  V.  52  7618 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24073851                                                     
JRNL        DOI    10.1021/BI400714V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 41617                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2204                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3060                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.2250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3442                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 429                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.87000                                              
REMARK   3    B22 (A**2) : -0.82000                                             
REMARK   3    B33 (A**2) : -0.53000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.49000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.631         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3573 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3392 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4843 ; 1.982 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7790 ; 0.974 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   435 ; 6.465 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   158 ;34.408 ;23.481       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   590 ;12.805 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.730 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   535 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3985 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   849 ; 0.001 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1649        A  1749                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9218  -1.2906   7.4321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0787 T22:   0.0582                                     
REMARK   3      T33:   0.0411 T12:   0.0002                                     
REMARK   3      T13:  -0.0049 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2402 L22:   2.6007                                     
REMARK   3      L33:   0.6988 L12:   0.0285                                     
REMARK   3      L13:  -0.2290 L23:   0.2004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0551 S12:  -0.1496 S13:   0.1649                       
REMARK   3      S21:   0.1785 S22:   0.0419 S23:   0.1793                       
REMARK   3      S31:  -0.0326 S32:   0.0627 S33:   0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1750        A  1815                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8314 -20.1968  -7.6079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1102 T22:   0.0434                                     
REMARK   3      T33:   0.1453 T12:  -0.0057                                     
REMARK   3      T13:  -0.0661 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3466 L22:   3.8259                                     
REMARK   3      L33:   0.8796 L12:   0.4129                                     
REMARK   3      L13:   0.1224 L23:  -0.3035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0877 S12:   0.1240 S13:  -0.1582                       
REMARK   3      S21:  -0.4352 S22:   0.1595 S23:   0.6125                       
REMARK   3      S31:   0.0204 S32:  -0.0431 S33:  -0.0718                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1819        A  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6091 -29.7327  -3.6346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0952 T22:   0.0543                                     
REMARK   3      T33:   0.2118 T12:  -0.0054                                     
REMARK   3      T13:  -0.0018 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7611 L22:   6.6831                                     
REMARK   3      L33:   0.7723 L12:   1.3718                                     
REMARK   3      L13:   0.3099 L23:  -0.2021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0483 S12:   0.0237 S13:  -0.1790                       
REMARK   3      S21:  -0.2286 S22:   0.1806 S23:   0.4560                       
REMARK   3      S31:   0.0602 S32:   0.0027 S33:  -0.1323                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4IGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076724.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : FAST MONOCHROMATIC ROTARY BEAM     
REMARK 200                                   SHUTTERS                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43950                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.17800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1Y98                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 M AMMONIUM ACETATE,     
REMARK 280  8% GLYCEROL, 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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                                                                      
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: 1250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 1270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2118  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2184  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2194  LIES ON A SPECIAL POSITION.                          
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     THR A  1816                                                      
REMARK 465     GLU A  1817                                                      
REMARK 465     ASP A  1818                                                      
REMARK 465     THR B  1816                                                      
REMARK 465     GLU B  1817                                                      
REMARK 465     ASP B  1818                                                      
REMARK 465     ALA D     4                                                      
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     GLU A1660    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1682    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1793    CG   CD   CE   NZ                                   
REMARK 470     GLU A1794    CG   CD   OE1  OE2                                  
REMARK 470     THR A1799    CB   OG1  CG2                                       
REMARK 470     VAL A1804    CB   CG1  CG2                                       
REMARK 470     ASN A1819    CB   CG   OD1  ND2                                  
REMARK 470     ALA A1823    CB                                                  
REMARK 470     GLN A1826    CG   CD   OE1  NE2                                  
REMARK 470     GLU B1682    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1793    CG   CD   CE   NZ                                   
REMARK 470     GLU B1794    CG   CD   OE1  OE2                                  
REMARK 470     VAL B1804    CG1  CG2                                            
REMARK 470     ASN B1819    CB   CG   OD1  ND2                                  
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   OE2  GLU A  1698     O    HOH A  2129              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU B1836   CD    GLU B1836   OE1     0.095                       
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    ARG A1751   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A1751   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A1762   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A1762   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG A1762   NE  -  CZ  -  NH2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    LYS B1750   CD  -  CE  -  NZ  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ARG B1751   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A1745       36.77   -143.78                                   
REMARK 500    MET A1775       97.83   -165.72                                   
REMARK 500    PHE A1798     -103.73    -63.47                                   
REMARK 500    THR A1799      143.58     83.06                                   
REMARK 500    LEU A1800      -94.49   -151.09                                   
REMARK 500    THR A1802     -102.28     14.95                                   
REMARK 500    VAL A1804      -95.01   -102.34                                   
REMARK 500    ASN B1745       42.68   -142.28                                   
REMARK 500    ARG B1758       64.87   -156.83                                   
REMARK 500    MET B1775       99.95   -165.26                                   
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    THR A1802        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP B1813        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2092        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH A2112        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A2124        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A2149        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH A2151        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A2156        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A2158        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A2159        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A2165        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A2184        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH B2037        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH B2049        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B2065        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH B2173        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH B2189        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH B2201        DISTANCE =  7.75 ANGSTROMS                       
REMARK 525    HOH C 112        DISTANCE =  6.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1902                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1902                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IFI   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH BAAT PEPTIDE                            
DBREF  4IGK A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4IGK B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4IGK C    4    10  UNP    Q8WXE1   ATRIP_HUMAN    237    243             
DBREF  4IGK D    4    10  UNP    Q8WXE1   ATRIP_HUMAN    237    243             
SEQRES   1 A  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 A  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 A  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 A  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 A  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 A  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 A  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 A  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 A  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 A  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 A  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 A  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 A  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 A  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 A  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 A  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 A  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 B  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 B  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 B  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 B  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 B  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 B  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 B  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 B  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 B  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 B  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 B  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 B  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 B  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 B  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 B  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 B  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 B  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 C    7  ALA CYS SEP PRO GLN PHE GLY                                  
SEQRES   1 D    7  ALA CYS SEP PRO GLN PHE GLY                                  
MODRES 4IGK SEP C    6  SER  PHOSPHOSERINE                                      
MODRES 4IGK SEP D    6  SER  PHOSPHOSERINE                                      
HET    SEP  C   6      10                                                       
HET    SEP  D   6      10                                                       
HET    GOL  A1901       6                                                       
HET    GOL  A1902       6                                                       
HET    GOL  B1901       6                                                       
HET    GOL  B1902       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  HOH   *429(H2 O)                                                    
HELIX    1   1 THR A 1658  HIS A 1672  1                                  15    
HELIX    2   2 THR A 1700  GLY A 1709  1                                  10    
HELIX    3   3 TYR A 1716  ARG A 1726  1                                  11    
HELIX    4   4 ASN A 1730  GLU A 1735  5                                   6    
HELIX    5   5 GLN A 1747  SER A 1755  1                                   9    
HELIX    6   6 PRO A 1776  CYS A 1787  1                                  12    
HELIX    7   7 GLU A 1794  PHE A 1798  5                                   5    
HELIX    8   8 GLN A 1811  TRP A 1815  5                                   5    
HELIX    9   9 ASN A 1819  HIS A 1822  5                                   4    
HELIX   10  10 ALA A 1823  CYS A 1828  1                                   6    
HELIX   11  11 ARG A 1835  TYR A 1845  1                                  11    
HELIX   12  12 LEU A 1850  LEU A 1854  5                                   5    
HELIX   13  13 THR B 1658  HIS B 1673  1                                  16    
HELIX   14  14 THR B 1700  GLY B 1709  1                                  10    
HELIX   15  15 TYR B 1716  GLU B 1725  1                                  10    
HELIX   16  16 ASN B 1730  GLU B 1735  5                                   6    
HELIX   17  17 GLN B 1747  GLU B 1754  1                                   8    
HELIX   18  18 PRO B 1776  CYS B 1787  1                                  12    
HELIX   19  19 GLU B 1794  PHE B 1798  5                                   5    
HELIX   20  20 GLN B 1811  TRP B 1815  5                                   5    
HELIX   21  21 ASN B 1819  MET B 1827  5                                   9    
HELIX   22  22 ARG B 1835  TYR B 1845  1                                  11    
HELIX   23  23 LEU B 1850  LEU B 1854  5                                   5    
SHEET    1   A 4 THR A1675  LEU A1676  0                                        
SHEET    2   A 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3   A 4 HIS A1686  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    4   A 4 TRP A1712  SER A1715  1  O  TRP A1712   N  VAL A1687           
SHEET    1   B 2 VAL A1696  CYS A1697  0                                        
SHEET    2   B 2 GLY A1738  ASP A1739  1  O  GLY A1738   N  CYS A1697           
SHEET    1   C 4 SER A1790  VAL A1792  0                                        
SHEET    2   C 4 GLU A1765  CYS A1768  1  N  ILE A1766   O  SER A1790           
SHEET    3   C 4 PRO A1806  VAL A1810  1  O  VAL A1809   N  CYS A1767           
SHEET    4   C 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1808           
SHEET    1   D 4 THR B1675  LEU B1676  0                                        
SHEET    2   D 4 SER B1651  SER B1655  1  N  MET B1652   O  THR B1675           
SHEET    3   D 4 HIS B1686  MET B1689  1  O  VAL B1688   N  VAL B1653           
SHEET    4   D 4 TRP B1712  SER B1715  1  O  TRP B1712   N  VAL B1687           
SHEET    1   E 2 VAL B1696  CYS B1697  0                                        
SHEET    2   E 2 GLY B1738  ASP B1739  1  O  GLY B1738   N  CYS B1697           
SHEET    1   F 4 SER B1790  VAL B1791  0                                        
SHEET    2   F 4 LEU B1764  CYS B1768  1  N  LEU B1764   O  SER B1790           
SHEET    3   F 4 HIS B1805  VAL B1810  1  O  VAL B1809   N  CYS B1767           
SHEET    4   F 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SSBOND   1 CYS C    5    CYS D    5                          1555   1556  2.88  
LINK         C   CYS C   5                 N   SEP C   6     1555   1555  1.32  
LINK         C   SEP C   6                 N   PRO C   7     1555   1555  1.30  
LINK         C   CYS D   5                 N   SEP D   6     1555   1555  1.34  
LINK         C   SEP D   6                 N   PRO D   7     1555   1555  1.34  
CISPEP   1 THR A 1799    LEU A 1800          0        14.00                     
CISPEP   2 VAL A 1804    HIS A 1805          0        -6.26                     
SITE     1 AC1  8 VAL A1654  SER A1655  GLY A1656  LEU A1657                    
SITE     2 AC1  8 ASN A1678  HOH A2009  GLU B1660  SEP C   6                    
SITE     1 AC2  6 GLY A1710  LYS A1711  TRP A1712  ARG A1753                    
SITE     2 AC2  6 HOH A2052  HOH A2053                                          
SITE     1 AC3  9 VAL B1654  SER B1655  GLY B1656  LEU B1657                    
SITE     2 AC3  9 ASN B1678  HOH B2048  HOH B2050  HOH B2139                    
SITE     3 AC3  9 SEP D   6                                                     
SITE     1 AC4  6 GLY B1710  LYS B1711  TRP B1712  ARG B1753                    
SITE     2 AC4  6 HOH B2054  HOH B2178                                          
CRYST1   65.666   50.309   73.977  90.00 116.03  90.00 P 1 2 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      0.015229  0.000000  0.007437        0.00000                         
SCALE2      0.000000  0.019877  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015044        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.998429 -0.002344 -0.055991       47.18395    1                    
MTRIX2   2 -0.002478  0.999994  0.002324        0.33283    1                    
MTRIX3   2  0.055986  0.002459 -0.998429      -34.21409    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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