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Database: PDB
Entry: 3P5J
LinkDB: 3P5J
Original site: 3P5J 
HEADER    HYDROLASE/REPLICATION                   08-OCT-10   3P5J              
TITLE     THE STRUCTURE OF THE HUMAN RNASE H2 COMPLEX DEFINES KEY INTERACTION   
TITLE    2 INTERFACES RELEVANT TO ENZYME FUNCTION AND HUMAN DISEASE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBONUCLEASE H2 SUBUNIT A;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RNASE H2 SUBUNIT A, RIBONUCLEASE HI LARGE SUBUNIT, RNASE HI 
COMPND   5 LARGE SUBUNIT, RIBONUCLEASE HI SUBUNIT A;                            
COMPND   6 EC: 3.1.26.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RIBONUCLEASE H2 SUBUNIT B;                                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: RNASE H2 SUBUNIT B, DELETED IN LYMPHOCYTIC LEUKEMIA 8       
COMPND  12 HOMOLOG, RIBONUCLEASE HI SUBUNIT B;                                  
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: RIBONUCLEASE H2 SUBUNIT C;                                 
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: RNASE H2 SUBUNIT C, RIBONUCLEASE HI SUBUNIT C;              
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RNASEH2A, RNASEHI;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: RNASEH2B, DLEU8;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: MOUSE;                                              
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 GENE: RNASEH2C, AYP1;                                                
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RNASE H2 FOLD, TRIPLE BETA-BARREL, NUCLEASE THAT CLEAVES RNA/DNA      
KEYWDS   2 HYBRIDS, PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) AND RNA/DNA       
KEYWDS   3 HYBRIDS, NUCLEUS, HYDROLASE-REPLICATION COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BUBECK,S.C.GRAHAM,E.Y.JONES                                         
REVDAT   3   12-OCT-11 3P5J    1       REMARK VERSN                             
REVDAT   2   13-APR-11 3P5J    1       JRNL                                     
REVDAT   1   17-NOV-10 3P5J    0                                                
JRNL        AUTH   M.A.REIJNS,D.BUBECK,L.C.GIBSON,S.C.GRAHAM,G.S.BAILLIE,       
JRNL        AUTH 2 E.Y.JONES,A.P.JACKSON                                        
JRNL        TITL   THE STRUCTURE OF THE HUMAN RNASE H2 COMPLEX DEFINES KEY      
JRNL        TITL 2 INTERACTION INTERFACES RELEVANT TO ENZYME FUNCTION AND HUMAN 
JRNL        TITL 3 DISEASE.                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 286 10530 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21177854                                                     
JRNL        DOI    10.1074/JBC.M110.177394                                      
REMARK   0                                                                      
REMARK   0 THIS ENTRY 3P5J REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL     
REMARK   0 STRUCTURAL DATA R3KIOSF DETERMINED BY AUTHORS OF THE PDB ENTRY       
REMARK   0 3KIO: N.SHABAN,D.HARVEY,F.W.PERRINO,T.HOLLIS.                        
REMARK   0                                                                      
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 3KIO                                                        
REMARK   0  AUTH   N.M.SHABAN,S.HARVEY,F.W.PERRINO,T.HOLLIS                     
REMARK   0  TITL   THE STRUCTURE OF THE MAMMALIAN RNASE H2 COMPLEX PROVIDES     
REMARK   0  TITL 2 INSIGHT INTO RNA.NA HYBRID PROCESSING TO PREVENT IMMUNE      
REMARK   0  TITL 3 DYSFUNCTION.                                                 
REMARK   0  REF    J.BIOL.CHEM.                  V. 285  3617 2010              
REMARK   0  REFN                   ISSN 0021-9258                               
REMARK   0  PMID   19923215                                                     
REMARK   0  DOI    10.1074/JBC.M109.059048                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 17777                          
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)  : 0.213                          
REMARK   3   R VALUE            (WORKING SET)  : 0.210                          
REMARK   3   FREE R VALUE                      : 0.272                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.200                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 925                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.08                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2812                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2326                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2649                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2290                   
REMARK   3   BIN FREE R VALUE                        : 0.2934                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.80                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 163                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4016                                    
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) : 62.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.06710                                             
REMARK   3    B22 (A**2) : -4.47470                                             
REMARK   3    B33 (A**2) : -8.59230                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.41                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.897                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.835                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4116   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5614   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1269   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 68     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 630    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4116   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 548    ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4644   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.28                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.09                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.53                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A   10    A  299                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   73.2007    9.6824   22.1632           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1858 T22:   -0.2376                                    
REMARK   3     T33:   -0.3040 T12:   -0.0251                                    
REMARK   3     T13:   -0.0022 T23:   -0.0287                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1145 L22:    1.2523                                    
REMARK   3     L33:    2.3424 L12:   -0.2948                                    
REMARK   3     L13:    0.7102 L23:   -0.5222                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0432 S12:   -0.0372 S13:   -0.1281                     
REMARK   3     S21:    0.0149 S22:    0.0176 S23:   -0.0206                     
REMARK   3     S31:   -0.0651 S32:    0.1222 S33:    0.0257                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   B   11    B  231                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   22.3709   -7.1893    3.4824           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3040 T22:   -0.2907                                    
REMARK   3     T33:    0.3040 T12:   -0.0503                                    
REMARK   3     T13:   -0.0420 T23:   -0.0841                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.9326 L22:    0.0013                                    
REMARK   3     L33:    0.4014 L12:    2.5634                                    
REMARK   3     L13:   -0.1113 L23:   -0.3888                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0230 S12:    0.1306 S13:   -0.1646                     
REMARK   3     S21:   -0.1336 S22:    0.0269 S23:    0.5442                     
REMARK   3     S31:    0.0586 S32:   -0.3411 S33:   -0.0040                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   C   14    C  162                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   45.4622   -2.7782    4.2073           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0704 T22:   -0.2576                                    
REMARK   3     T33:   -0.1683 T12:   -0.0255                                    
REMARK   3     T13:   -0.0155 T23:   -0.0167                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5519 L22:    3.6213                                    
REMARK   3     L33:    1.5601 L12:    0.2111                                    
REMARK   3     L13:    0.9306 L23:    0.8695                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1005 S12:    0.2979 S13:   -0.4617                     
REMARK   3     S21:   -0.1266 S22:   -0.0983 S23:    0.5442                     
REMARK   3     S31:    0.1970 S32:   -0.1822 S33:   -0.0021                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS IS A RE-REFINEMENT OF THE MURINE     
REMARK   3  RNASE H2 COORDINATES PREVIOUSLY DEPOSITED BY SHABAN ET AL., 2010    
REMARK   3  (PDB ID 3KIO)                                                       
REMARK   4                                                                      
REMARK   4 3P5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061982.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 3KIO.                     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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      139.64500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      139.64500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       20.21000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     ASP A    67                                                      
REMARK 465     SER A    68                                                      
REMARK 465     LYS A    69                                                      
REMARK 465     GLU A   258A                                                     
REMARK 465     ALA A   258B                                                     
REMARK 465     GLU A   258C                                                     
REMARK 465     GLU A   258D                                                     
REMARK 465     ASP A   258E                                                     
REMARK 465     PRO A   258F                                                     
REMARK 465     GLU A   258G                                                     
REMARK 465     ARG A   258H                                                     
REMARK 465     PRO A   258I                                                     
REMARK 465     GLY A   258J                                                     
REMARK 465     LYS A   258K                                                     
REMARK 465     ILE A   258L                                                     
REMARK 465     THR A   258M                                                     
REMARK 465     SER A   258N                                                     
REMARK 465     TYR A   258O                                                     
REMARK 465     PHE A   258P                                                     
REMARK 465     SER A   258Q                                                     
REMARK 465     GLN A   258R                                                     
REMARK 465     GLY A   258S                                                     
REMARK 465     PRO A   258T                                                     
REMARK 465     GLN A   258U                                                     
REMARK 465     THR A   258V                                                     
REMARK 465     CYS A   258W                                                     
REMARK 465     ARG A   258X                                                     
REMARK 465     PRO A   258Y                                                     
REMARK 465     GLN A   258Z                                                     
REMARK 465     ALA A   259A                                                     
REMARK 465     MET B   -23                                                      
REMARK 465     GLY B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLN B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     ASN B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     LYS B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     TYR B   110                                                      
REMARK 465     GLN B   111                                                      
REMARK 465     PRO B   112                                                      
REMARK 465     LEU B   113                                                      
REMARK 465     ASP B   114                                                      
REMARK 465     GLN B   115                                                      
REMARK 465     VAL B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     VAL B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     ASP B   120                                                      
REMARK 465     THR B   121                                                      
REMARK 465     PHE B   122                                                      
REMARK 465     GLU B   144                                                      
REMARK 465     LYS B   145                                                      
REMARK 465     GLU B   146                                                      
REMARK 465     VAL B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     SER B   149                                                      
REMARK 465     LYS B   150                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     GLY B   183                                                      
REMARK 465     ALA B   184                                                      
REMARK 465     ARG B   185                                                      
REMARK 465     VAL B   186                                                      
REMARK 465     GLN B   187                                                      
REMARK 465     SER B   188                                                      
REMARK 465     SER B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     TYR B   191                                                      
REMARK 465     PHE B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     GLN B   196                                                      
REMARK 465     VAL B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     ASP B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     GLU B   202                                                      
REMARK 465     PRO B   232                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     PRO B   235                                                      
REMARK 465     ALA B   236                                                      
REMARK 465     SER B   237                                                      
REMARK 465     LEU B   238                                                      
REMARK 465     THR B   239                                                      
REMARK 465     ASN B   240                                                      
REMARK 465     PRO B   241                                                      
REMARK 465     PRO B   242                                                      
REMARK 465     SER B   243                                                      
REMARK 465     LYS B   244                                                      
REMARK 465     LYS B   245                                                      
REMARK 465     LEU B   246                                                      
REMARK 465     LYS B   247                                                      
REMARK 465     LEU B   248                                                      
REMARK 465     SER B   249                                                      
REMARK 465     ASP B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     PRO B   252                                                      
REMARK 465     VAL B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     ASP B   258                                                      
REMARK 465     TYR B   259                                                      
REMARK 465     THR B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     PHE B   262                                                      
REMARK 465     ASN B   263                                                      
REMARK 465     THR B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     ASP B   266                                                      
REMARK 465     LEU B   267                                                      
REMARK 465     LYS B   268                                                      
REMARK 465     THR B   269                                                      
REMARK 465     GLY B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     LYS B   272                                                      
REMARK 465     ASN B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     LYS B   275                                                      
REMARK 465     MET B   276                                                      
REMARK 465     THR B   277                                                      
REMARK 465     ALA B   278                                                      
REMARK 465     ALA B   279                                                      
REMARK 465     GLN B   280                                                      
REMARK 465     LYS B   281                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     LEU B   283                                                      
REMARK 465     ALA B   284                                                      
REMARK 465     LYS B   285                                                      
REMARK 465     VAL B   286                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     SER B   289                                                      
REMARK 465     GLY B   290                                                      
REMARK 465     MET B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     ILE B   294                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     ALA B   296                                                      
REMARK 465     PHE B   297                                                      
REMARK 465     PHE B   298                                                      
REMARK 465     GLY B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     ASN B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     LYS B   304                                                      
REMARK 465     THR B   305                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     ILE B   308                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     LYS C    11                                                      
REMARK 465     GLN C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     GLU C    87                                                      
REMARK 465     GLU C    88                                                      
REMARK 465     LYS C    89                                                      
REMARK 465     GLY C    90                                                      
REMARK 465     GLU C    91                                                      
REMARK 465     GLY C    92                                                      
REMARK 465     LEU C    93                                                      
REMARK 465     ILE C    94                                                      
REMARK 465     GLY C    95                                                      
REMARK 465     LYS C    96                                                      
REMARK 465     LEU C    97                                                      
REMARK 465     ASN C    98                                                      
REMARK 465     PHE C    99                                                      
REMARK 465     SER C   100                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     ASP C   102                                                      
REMARK 465     ALA C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     ASP C   105                                                      
REMARK 465     LYS C   106                                                      
REMARK 465     ALA C   107                                                      
REMARK 465     ASP C   108                                                      
REMARK 465     GLU C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     GLN C   111                                                      
REMARK 465     GLU C   112                                                      
REMARK 465     PRO C   113                                                      
REMARK 465     LEU C   114                                                      
REMARK 465     GLU C   115                                                      
REMARK 465     ARG C   116                                                      
REMARK 465     ASP C   117                                                      
REMARK 465     PHE C   118                                                      
REMARK 465     ASP C   119                                                      
REMARK 465     VAL C   163                                                      
REMARK 465     PRO C   164                                                      
REMARK 465     GLU C   165                                                      
REMARK 465     ASP C   166                                                      
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     ASN A  10    CG   OD1  ND2                                       
REMARK 470     THR A  11    OG1  CG2                                            
REMARK 470     LYS A  26    CG   CD   CE   NZ                                   
REMARK 470     ASP A  59    CG   OD1  OD2                                       
REMARK 470     GLU A  61    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  63    CG   CD1  CD2                                       
REMARK 470     LEU A  71    CG   CD1  CD2                                       
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  74    CG   OD1  ND2                                       
REMARK 470     GLU A  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  82    CG   CD   CE   NZ                                   
REMARK 470     ASP A  88    CG   OD1  OD2                                       
REMARK 470     SER A 258    OG                                                  
REMARK 470     GLN A 289    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     SER A 297    OG                                                  
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     SER B  27    OG                                                  
REMARK 470     SER B  34    OG                                                  
REMARK 470     LEU B  35    CG   CD1  CD2                                       
REMARK 470     LEU B  36    CG   CD1  CD2                                       
REMARK 470     VAL B  38    CG1  CG2                                            
REMARK 470     LYS B  39    CG   CD   CE   NZ                                   
REMARK 470     LEU B  40    CG   CD1  CD2                                       
REMARK 470     SER B  45    OG                                                  
REMARK 470     GLU B  47    CG   CD   OE1  OE2                                  
REMARK 470     CYS B  56    SG                                                  
REMARK 470     LEU B  57    CG   CD1  CD2                                       
REMARK 470     GLN B  58    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  59    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  60    CG   CD1  CD2                                       
REMARK 470     LYS B  67    CG   CD   CE   NZ                                   
REMARK 470     LYS B  69    CG   CD   CE   NZ                                   
REMARK 470     LEU B  96    CG   CD1  CD2                                       
REMARK 470     LEU B  97    CG   CD1  CD2                                       
REMARK 470     LEU B 101    CG   CD1  CD2                                       
REMARK 470     LEU B 102    CG   CD1  CD2                                       
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     LYS B 106    CG   CD   CE   NZ                                   
REMARK 470     LEU B 127    CG   CD1  CD2                                       
REMARK 470     LEU B 128    CG   CD1  CD2                                       
REMARK 470     LEU B 129    CG   CD1  CD2                                       
REMARK 470     GLU B 133    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 134    CG   CD1  CD2                                       
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     SER B 137    OG                                                  
REMARK 470     ARG B 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 142    OG1  CG2                                            
REMARK 470     GLU B 143    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 151    CG   CD   CE   NZ                                   
REMARK 470     LYS B 154    CG   CD   CE   NZ                                   
REMARK 470     TYR B 155    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 157    OG                                                  
REMARK 470     GLU B 158    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 161    CG   CD1  CD2                                       
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     LEU B 164    CG   CD1  CD2                                       
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     VAL B 172    CG1  CG2                                            
REMARK 470     LEU B 175    CG   CD1  CD2                                       
REMARK 470     LYS B 176    CG   CD   CE   NZ                                   
REMARK 470     ASN B 178    CG   OD1  ND2                                       
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     VAL B 180    CG1  CG2                                            
REMARK 470     ASN B 181    CG   OD1  ND2                                       
REMARK 470     GLU B 203    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 204    CG   OD1  OD2                                       
REMARK 470     VAL B 206    CG1  CG2                                            
REMARK 470     ARG B 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 216    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     GLU B 220    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 221    CG   CD1  CD2                                       
REMARK 470     SER B 222    OG                                                  
REMARK 470     ASP B 223    CG   OD1  OD2                                       
REMARK 470     ASP B 224    CG   OD1  OD2                                       
REMARK 470     LEU B 225    CG   CD1  CD2                                       
REMARK 470     SER B 226    OG                                                  
REMARK 470     LYS B 227    CG   CD   CE   NZ                                   
REMARK 470     LEU B 229    CG   CD1  CD2                                       
REMARK 470     LYS B 230    CG   CD   CE   NZ                                   
REMARK 470     LEU B 231    CG   CD1  CD2                                       
REMARK 470     HIS C  15    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 121    CG   CD1  CD2                                       
REMARK 470     ILE C 122    CG1  CG2  CD1                                       
REMARK 470     THR C 138    OG1  CG2                                            
REMARK 470     ASP C 143    CG   OD1  OD2                                       
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    THR A  11     -116.28     63.33                                   
REMARK 500    PHE A  89      -25.75   -142.94                                   
REMARK 500    TYR A 112       88.11   -159.79                                   
REMARK 500    ASN A 135       54.54    -69.61                                   
REMARK 500    MET A 146       87.50      0.02                                   
REMARK 500    GLU A 148      -80.05    -41.63                                   
REMARK 500    PHE A 158       70.16   -112.11                                   
REMARK 500    GLN A 201       24.21    -76.93                                   
REMARK 500    ASP A 206       70.83   -101.18                                   
REMARK 500    PHE A 234      -29.71    -38.94                                   
REMARK 500    GLU B  21      -34.45    -38.87                                   
REMARK 500    LEU B  23      -32.11    -39.90                                   
REMARK 500    GLN B  58       64.73     60.42                                   
REMARK 500    HIS B  70       78.34     62.24                                   
REMARK 500    ASN B  76     -125.73     57.78                                   
REMARK 500    GLN B  77       56.60   -101.60                                   
REMARK 500    ARG B 130       95.28    -58.31                                   
REMARK 500    ARG B 139       42.13    -78.26                                   
REMARK 500    THR B 142     -105.45    -89.62                                   
REMARK 500    ASN B 179       65.01     60.75                                   
REMARK 500    PHE B 228      -57.64     78.78                                   
REMARK 500    LYS B 230      -34.81     59.93                                   
REMARK 500    ARG C  17      164.79    -49.70                                   
REMARK 500    LEU C  37      -17.66    -45.66                                   
REMARK 500    PHE C  48      -76.53    -66.96                                   
REMARK 500    GLU C  71      140.16   -170.38                                   
REMARK 500    GLU C 137      -33.86     49.02                                   
REMARK 500    ASP C 143       54.68    -94.86                                   
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    ASP A 188        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE B  63        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU C  16        23.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU C  37        23.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P56   RELATED DB: PDB                                   
REMARK 900 HUMAN RNASE H2                                                       
REMARK 900 RELATED ID: 3KIO   RELATED DB: PDB                                   
REMARK 900 MURINE RNASE H2. THIS ENTRY 3P5J REFLECTS AN ALTERNATIVE             
REMARK 900 MODELING OF X-RAY DATA R3KIOSF                                       
DBREF  3P5J A    1   299  UNP    Q9CWY8   RNH2A_MOUSE      1    301             
DBREF  3P5J B    1   308  UNP    Q80ZV0   RNH2B_MOUSE      1    308             
DBREF  3P5J C    1   166  UNP    Q9CQ18   RNH2C_MOUSE      1    166             
SEQADV 3P5J MET B  -23  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J GLY B  -22  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J SER B  -21  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J SER B  -20  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -19  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -18  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -17  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -16  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -15  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J HIS B  -14  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J SER B  -13  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J GLN B  -12  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J ASP B  -11  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J PRO B  -10  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J ASN B   -9  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J SER B   -8  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J LEU B   -7  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J GLU B   -6  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J VAL B   -5  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J LEU B   -4  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J PHE B   -3  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J GLN B   -2  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J GLY B   -1  UNP  Q80ZV0              EXPRESSION TAG                 
SEQADV 3P5J PRO B    0  UNP  Q80ZV0              EXPRESSION TAG                 
SEQRES   1 A  301  MET ASP LEU SER GLU LEU GLU ARG ASP ASN THR GLY ARG          
SEQRES   2 A  301  CYS ARG LEU SER SER PRO VAL PRO ALA VAL CYS LEU LYS          
SEQRES   3 A  301  GLU PRO CYS VAL LEU GLY VAL ASP GLU ALA GLY ARG GLY          
SEQRES   4 A  301  PRO VAL LEU GLY PRO MET VAL TYR ALA ILE CYS TYR CYS          
SEQRES   5 A  301  PRO LEU SER ARG LEU ALA ASP LEU GLU ALA LEU LYS VAL          
SEQRES   6 A  301  ALA ASP SER LYS THR LEU THR GLU ASN GLU ARG GLU ARG          
SEQRES   7 A  301  LEU PHE ALA LYS MET GLU GLU ASP GLY ASP PHE VAL GLY          
SEQRES   8 A  301  TRP ALA LEU ASP VAL LEU SER PRO ASN LEU ILE SER THR          
SEQRES   9 A  301  SER MET LEU GLY ARG VAL LYS TYR ASN LEU ASN SER LEU          
SEQRES  10 A  301  SER HIS ASP THR ALA ALA GLY LEU ILE GLN TYR ALA LEU          
SEQRES  11 A  301  ASP GLN ASN VAL ASN VAL THR GLN VAL PHE VAL ASP THR          
SEQRES  12 A  301  VAL GLY MET PRO GLU THR TYR GLN ALA ARG LEU GLN GLN          
SEQRES  13 A  301  HIS PHE PRO GLY ILE GLU VAL THR VAL LYS ALA LYS ALA          
SEQRES  14 A  301  ASP SER LEU PHE PRO VAL VAL SER ALA ALA SER ILE PHE          
SEQRES  15 A  301  ALA LYS VAL ALA ARG ASP LYS ALA VAL LYS ASN TRP GLN          
SEQRES  16 A  301  PHE VAL GLU ASN LEU GLN ASP LEU ASP SER ASP TYR GLY          
SEQRES  17 A  301  SER GLY TYR PRO ASN ASP PRO LYS THR LYS ALA TRP LEU          
SEQRES  18 A  301  ARG LYS HIS VAL ASP PRO VAL PHE GLY PHE PRO GLN PHE          
SEQRES  19 A  301  VAL ARG PHE SER TRP SER THR ALA GLN ALA ILE LEU GLU          
SEQRES  20 A  301  LYS GLU ALA GLU ASP VAL ILE TRP GLU ASP SER GLU ALA          
SEQRES  21 A  301  GLU GLU ASP PRO GLU ARG PRO GLY LYS ILE THR SER TYR          
SEQRES  22 A  301  PHE SER GLN GLY PRO GLN THR CYS ARG PRO GLN ALA PRO          
SEQRES  23 A  301  HIS ARG TYR PHE GLN GLU ARG GLY LEU GLU ALA ALA SER          
SEQRES  24 A  301  SER LEU                                                      
SEQRES   1 B  332  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  332  PRO ASN SER LEU GLU VAL LEU PHE GLN GLY PRO MET ALA          
SEQRES   3 B  332  GLY GLY ARG ASP ARG GLY ASP LEU ALA ALA ARG GLN LEU          
SEQRES   4 B  332  VAL PHE LEU LEU PRO GLU HIS LEU LYS ASP ALA SER LYS          
SEQRES   5 B  332  LYS LYS LYS LYS SER SER LEU LEU PHE VAL LYS LEU ALA          
SEQRES   6 B  332  ASN PRO HIS SER GLY GLU GLY ALA THR TYR LEU ILE ASP          
SEQRES   7 B  332  MET CYS LEU GLN GLN LEU PHE GLU ILE LYS VAL PHE LYS          
SEQRES   8 B  332  GLU LYS HIS HIS SER TRP PHE ILE ASN GLN SER VAL GLN          
SEQRES   9 B  332  SER GLY GLY LEU LEU HIS PHE ALA THR PRO MET ASP PRO          
SEQRES  10 B  332  LEU PHE LEU LEU LEU HIS TYR LEU LEU LYS ALA GLY LYS          
SEQRES  11 B  332  GLU GLY LYS TYR GLN PRO LEU ASP GLN VAL VAL VAL ASP          
SEQRES  12 B  332  ASP THR PHE PRO ASP CYS THR LEU LEU LEU ARG PHE PRO          
SEQRES  13 B  332  GLU LEU GLU LYS SER LEU ARG HIS VAL THR GLU GLU LYS          
SEQRES  14 B  332  GLU VAL ASN SER LYS LYS TYR TYR LYS TYR SER SER GLU          
SEQRES  15 B  332  LYS THR LEU LYS TRP LEU GLU LYS LYS VAL ASN GLN THR          
SEQRES  16 B  332  VAL VAL ALA LEU LYS ALA ASN ASN VAL ASN VAL GLY ALA          
SEQRES  17 B  332  ARG VAL GLN SER SER ALA TYR PHE SER GLY GLY GLN VAL          
SEQRES  18 B  332  SER ARG ASP LYS GLU GLU ASP TYR VAL ARG TYR ALA HIS          
SEQRES  19 B  332  GLY LEU ILE SER ASP TYR ILE PRO LYS GLU LEU SER ASP          
SEQRES  20 B  332  ASP LEU SER LYS PHE LEU LYS LEU PRO GLU PRO PRO ALA          
SEQRES  21 B  332  SER LEU THR ASN PRO PRO SER LYS LYS LEU LYS LEU SER          
SEQRES  22 B  332  ASP GLU PRO VAL GLU ALA LYS GLU ASP TYR THR LYS PHE          
SEQRES  23 B  332  ASN THR LYS ASP LEU LYS THR GLY LYS LYS ASN SER LYS          
SEQRES  24 B  332  MET THR ALA ALA GLN LYS ALA LEU ALA LYS VAL ASP LYS          
SEQRES  25 B  332  SER GLY MET LYS SER ILE ASP ALA PHE PHE GLY ALA LYS          
SEQRES  26 B  332  ASN LYS LYS THR GLY LYS ILE                                  
SEQRES   1 C  166  MET LYS ASN PRO GLU GLU ALA ALA ASP GLY LYS GLN ARG          
SEQRES   2 C  166  ILE HIS LEU ARG PRO GLY SER LEU ARG GLY ALA ALA PRO          
SEQRES   3 C  166  ALA LYS LEU HIS LEU LEU PRO CYS ASP VAL LEU VAL SER          
SEQRES   4 C  166  ARG PRO ALA PRO VAL ASP ARG PHE PHE THR PRO ALA VAL          
SEQRES   5 C  166  ARG HIS ASP ALA ASP GLY LEU GLN ALA SER PHE ARG GLY          
SEQRES   6 C  166  ARG GLY LEU ARG GLY GLU GLU VAL ALA VAL PRO PRO GLY          
SEQRES   7 C  166  PHE ALA GLY PHE VAL MET VAL THR GLU GLU LYS GLY GLU          
SEQRES   8 C  166  GLY LEU ILE GLY LYS LEU ASN PHE SER GLY ASP ALA GLU          
SEQRES   9 C  166  ASP LYS ALA ASP GLU ALA GLN GLU PRO LEU GLU ARG ASP          
SEQRES  10 C  166  PHE ASP ARG LEU ILE GLY ALA THR GLY SER PHE SER HIS          
SEQRES  11 C  166  PHE THR LEU TRP GLY LEU GLU THR VAL PRO GLY PRO ASP          
SEQRES  12 C  166  ALA LYS VAL HIS ARG ALA LEU GLY TRP PRO SER LEU ALA          
SEQRES  13 C  166  ALA ALA ILE HIS ALA GLN VAL PRO GLU ASP                      
HELIX    1   1 ALA A   22  GLU A   27  1                                   6    
HELIX    2   2 ARG A   56  ALA A   62  1                                   7    
HELIX    3   3 THR A   72  ASP A   86  1                                  15    
HELIX    4   4 SER A   98  LEU A  107  1                                  10    
HELIX    5   5 ASN A  113  GLN A  132  1                                  20    
HELIX    6   6 PRO A  147  PHE A  158  1                                  12    
HELIX    7   7 LYS A  168  PHE A  173  1                                   6    
HELIX    8   8 PHE A  173  GLN A  201  1                                  29    
HELIX    9   9 ASP A  214  LYS A  223  1                                  10    
HELIX   10  10 TRP A  239  ALA A  250  1                                  12    
HELIX   11  11 PRO A  284  GLY A  292  1                                   9    
HELIX   12  12 HIS B   22  ASP B   25  5                                   4    
HELIX   13  13 ASP B   92  LEU B   98  1                                   7    
HELIX   14  14 HIS B   99  LEU B  101  5                                   3    
HELIX   15  15 ASP B  124  ARG B  130  1                                   7    
HELIX   16  16 GLU B  133  ARG B  139  1                                   7    
HELIX   17  17 SER B  156  ASN B  178  1                                  23    
HELIX   18  18 ASP B  204  ASP B  215  1                                  12    
HELIX   19  19 TYR B  216  LEU B  221  5                                   6    
HELIX   20  20 ARG C   17  GLY C   23  1                                   7    
HELIX   21  21 PRO C   43  PHE C   48  1                                   6    
HELIX   22  22 THR C   49  VAL C   52  5                                   4    
HELIX   23  23 ALA C  144  LEU C  150  1                                   7    
HELIX   24  24 GLY C  151  HIS C  160  1                                  10    
SHEET    1   A 6 ARG A  13  SER A  17  0                                        
SHEET    2   A 6 GLY A  91  LEU A  97 -1  O  LEU A  94   N  LEU A  16           
SHEET    3   A 6 MET A  45  PRO A  53 -1  N  MET A  45   O  LEU A  97           
SHEET    4   A 6 CYS A  29  ALA A  36 -1  N  GLY A  32   O  CYS A  50           
SHEET    5   A 6 VAL A 136  ASP A 142  1  O  THR A 137   N  CYS A  29           
SHEET    6   A 6 GLU A 162  LYS A 166  1  O  THR A 164   N  VAL A 139           
SHEET    1   B 2 VAL A 253  ILE A 254  0                                        
SHEET    2   B 2 ASP C  35  VAL C  36 -1  O  ASP C  35   N  ILE A 254           
SHEET    1   C 4 LEU A 293  ALA A 295  0                                        
SHEET    2   C 4 GLN B  59  PHE B  66 -1  O  VAL B  65   N  GLU A 294           
SHEET    3   C 4 ALA B  49  ASP B  54 -1  N  ASP B  54   O  GLN B  59           
SHEET    4   C 4 LEU B  35  LEU B  40 -1  N  LEU B  36   O  ILE B  53           
SHEET    1   D 7 LEU A 293  ALA A 295  0                                        
SHEET    2   D 7 GLN B  59  PHE B  66 -1  O  VAL B  65   N  GLU A 294           
SHEET    3   D 7 LEU B  85  PRO B  90 -1  O  LEU B  85   N  PHE B  66           
SHEET    4   D 7 LEU B  15  PRO B  20  1  N  VAL B  16   O  HIS B  86           
SHEET    5   D 7 PHE C  79  VAL C  85 -1  O  ALA C  80   N  LEU B  19           
SHEET    6   D 7 GLY C 123  PHE C 128 -1  O  PHE C 128   N  GLY C  81           
SHEET    7   D 7 ALA C  25  PRO C  26  1  N  ALA C  25   O  SER C 127           
SHEET    1   E 8 ARG C  40  PRO C  41  0                                        
SHEET    2   E 8 SER B  78  SER B  81 -1  N  VAL B  79   O  ARG C  40           
SHEET    3   E 8 SER B  72  ILE B  75 -1  N  TRP B  73   O  GLN B  80           
SHEET    4   E 8 LEU C  29  LEU C  32 -1  O  HIS C  30   N  PHE B  74           
SHEET    5   E 8 HIS C 130  LEU C 136  1  O  THR C 132   N  LEU C  31           
SHEET    6   E 8 ARG C  66  ALA C  74 -1  N  GLU C  71   O  LEU C 133           
SHEET    7   E 8 LEU C  59  PHE C  63 -1  N  LEU C  59   O  GLY C  70           
SHEET    8   E 8 ARG C  53  HIS C  54 -1  N  ARG C  53   O  GLN C  60           
CRYST1  279.290   40.420   67.820  90.00  90.00  90.00 P 21 21 2     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      0.003581  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.024740  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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