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Database: PDB
Entry: 1WDY
LinkDB: 1WDY
Original site: 1WDY 
HEADER    HYDROLASE                               19-MAY-04   1WDY              
TITLE     CRYSTAL STRUCTURE OF RIBONUCLEASE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-5A-DEPENDENT RIBONUCLEASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-305;                                           
COMPND   5 SYNONYM: 2-5A-DEPENDENT RNASE, RIBONUCLEASE L, RNASE L,              
COMPND   6 RIBONUCLEASE 4;                                                      
COMPND   7 EC: 3.1.26.-;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, NUCLEASE, RNA-BINDING                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.TANAKA,M.NAKANISHI,Y.KUSAKABE,Y.GOTO,Y.KITADE,K.T.NAKAMURA          
REVDAT   3   24-FEB-09 1WDY    1       VERSN                                    
REVDAT   2   09-NOV-04 1WDY    1       JRNL                                     
REVDAT   1   05-OCT-04 1WDY    0                                                
JRNL        AUTH   N.TANAKA,M.NAKANISHI,Y.KUSAKABE,Y.GOTO,Y.KITADE,             
JRNL        AUTH 2 K.T.NAKAMURA                                                 
JRNL        TITL   STRUCTURAL BASIS FOR RECOGNITION OF 2',5'-LINKED             
JRNL        TITL 2 OLIGOADENYLATES BY HUMAN RIBONUCLEASE L                      
JRNL        REF    EMBO J.                       V.  23  3929 2004              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15385955                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600420                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 34084                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1791                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2482                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 123                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2185                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 220                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : -0.59000                                             
REMARK   3    B33 (A**2) : 0.81000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.118         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.114         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.316         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2283 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2109 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3085 ; 1.119 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4916 ; 0.770 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   284 ; 4.997 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   361 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2499 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   402 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   523 ; 0.239 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2472 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1397 ; 0.079 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   164 ; 0.144 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     6 ; 0.110 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.288 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.121 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1406 ; 0.669 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2233 ; 1.295 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   877 ; 1.825 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   852 ; 3.084 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WDY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023475.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-04                          
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35922                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM ACETATE, GLYCEROL,       
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       31.60150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.31700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.41700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.31700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.60150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.41700            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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    GLU A 237      -80.94    -45.85                                   
REMARK 500    ARG A 238       49.85    -82.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25A A 1001                
DBREF  1WDY A   21   305  UNP    Q05823   RN5A_HUMAN      21    305             
SEQADV 1WDY LEU A   97  UNP  Q05823    ILE    97 ENGINEERED                     
SEQRES   1 A  285  ALA ALA VAL GLU ASP ASN HIS LEU LEU ILE LYS ALA VAL          
SEQRES   2 A  285  GLN ASN GLU ASP VAL ASP LEU VAL GLN GLN LEU LEU GLU          
SEQRES   3 A  285  GLY GLY ALA ASN VAL ASN PHE GLN GLU GLU GLU GLY GLY          
SEQRES   4 A  285  TRP THR PRO LEU HIS ASN ALA VAL GLN MET SER ARG GLU          
SEQRES   5 A  285  ASP ILE VAL GLU LEU LEU LEU ARG HIS GLY ALA ASP PRO          
SEQRES   6 A  285  VAL LEU ARG LYS LYS ASN GLY ALA THR PRO PHE LEU LEU          
SEQRES   7 A  285  ALA ALA ILE ALA GLY SER VAL LYS LEU LEU LYS LEU PHE          
SEQRES   8 A  285  LEU SER LYS GLY ALA ASP VAL ASN GLU CYS ASP PHE TYR          
SEQRES   9 A  285  GLY PHE THR ALA PHE MET GLU ALA ALA VAL TYR GLY LYS          
SEQRES  10 A  285  VAL LYS ALA LEU LYS PHE LEU TYR LYS ARG GLY ALA ASN          
SEQRES  11 A  285  VAL ASN LEU ARG ARG LYS THR LYS GLU ASP GLN GLU ARG          
SEQRES  12 A  285  LEU ARG LYS GLY GLY ALA THR ALA LEU MET ASP ALA ALA          
SEQRES  13 A  285  GLU LYS GLY HIS VAL GLU VAL LEU LYS ILE LEU LEU ASP          
SEQRES  14 A  285  GLU MET GLY ALA ASP VAL ASN ALA CYS ASP ASN MET GLY          
SEQRES  15 A  285  ARG ASN ALA LEU ILE HIS ALA LEU LEU SER SER ASP ASP          
SEQRES  16 A  285  SER ASP VAL GLU ALA ILE THR HIS LEU LEU LEU ASP HIS          
SEQRES  17 A  285  GLY ALA ASP VAL ASN VAL ARG GLY GLU ARG GLY LYS THR          
SEQRES  18 A  285  PRO LEU ILE LEU ALA VAL GLU LYS LYS HIS LEU GLY LEU          
SEQRES  19 A  285  VAL GLN ARG LEU LEU GLU GLN GLU HIS ILE GLU ILE ASN          
SEQRES  20 A  285  ASP THR ASP SER ASP GLY LYS THR ALA LEU LEU LEU ALA          
SEQRES  21 A  285  VAL GLU LEU LYS LEU LYS LYS ILE ALA GLU LEU LEU CYS          
SEQRES  22 A  285  LYS ARG GLY ALA SER THR ASP CYS GLY ASP LEU VAL              
HET    25A  A1001      67                                                       
HETNAM     25A 5'-O-MONOPHOSPHORYLADENYLYL(2'->5')ADENYLYL(2'->5')              
HETNAM   2 25A  ADENOSINE                                                       
FORMUL   2  25A    C30 H38 N15 O19 P3                                           
FORMUL   3  HOH   *220(H2 O)                                                    
HELIX    1   1 ALA A   21  ASN A   35  1                                  15    
HELIX    2   2 ASP A   37  GLY A   47  1                                  11    
HELIX    3   3 THR A   61  MET A   69  1                                   9    
HELIX    4   4 ARG A   71  HIS A   81  1                                  11    
HELIX    5   5 THR A   94  GLY A  103  1                                  10    
HELIX    6   6 SER A  104  LYS A  114  1                                  11    
HELIX    7   7 THR A  127  TYR A  135  1                                   9    
HELIX    8   8 LYS A  137  ARG A  147  1                                  11    
HELIX    9   9 LYS A  158  LEU A  164  1                                   7    
HELIX   10  10 THR A  170  GLY A  179  1                                  10    
HELIX   11  11 HIS A  180  GLU A  190  1                                  11    
HELIX   12  12 ASN A  204  SER A  212  1                                   9    
HELIX   13  13 ASP A  217  HIS A  228  1                                  12    
HELIX   14  14 THR A  241  LYS A  249  1                                   9    
HELIX   15  15 HIS A  251  GLN A  261  1                                  11    
HELIX   16  16 THR A  275  LEU A  283  1                                   9    
HELIX   17  17 LEU A  285  GLY A  296  1                                  12    
SSBOND   1 CYS A  293    CYS A  301                          1555   1555  2.07  
SITE     1 AC1 25 GLU A  55  GLY A  58  TRP A  60  ASN A  65                    
SITE     2 AC1 25 GLN A  68  LYS A  89  ASP A 122  TYR A 124                    
SITE     3 AC1 25 PHE A 126  GLU A 131  TYR A 135  ARG A 155                    
SITE     4 AC1 25 HOH A1004  HOH A1005  HOH A1017  HOH A1022                    
SITE     5 AC1 25 HOH A1036  HOH A1051  HOH A1059  HOH A1088                    
SITE     6 AC1 25 HOH A1098  HOH A1109  HOH A1115  HOH A1143                    
SITE     7 AC1 25 HOH A1159                                                     
CRYST1   63.203   72.834   82.634  90.00  90.00  90.00 P 21 21 21    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      0.015822  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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