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Database: PDB
Entry: 1KKB
LinkDB: 1KKB
Original site: 1KKB 
HEADER    LIGASE                                  06-DEC-01   1KKB              
TITLE     COMPLEX OF ESCHERICHIA COLI ADENYLOSUCCINATE SYNTHETASE WITH IMP AND  
TITLE    2 HADACIDIN                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENYLOSUCCINATE SYNTHETASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.4.4;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;                           
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: PUR A H1238                                
KEYWDS    LIGASE, GTP-HYDROLYSING ENZYMES, PURINE NUCLEOTIDE, BIOSYNTHESIS,     
KEYWDS   2 INDUCED FIT                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.HOU,W.WANG,H.J.FROMM,R.B.HONZATKO                                   
REVDAT   5   11-OCT-17 1KKB    1       REMARK                                   
REVDAT   4   13-JUL-11 1KKB    1       VERSN                                    
REVDAT   3   27-OCT-10 1KKB    1       FORMUL HET    HETATM HETNAM              
REVDAT   2   24-FEB-09 1KKB    1       VERSN                                    
REVDAT   1   20-MAR-02 1KKB    0                                                
JRNL        AUTH   Z.HOU,W.WANG,H.J.FROMM,R.B.HONZATKO                          
JRNL        TITL   IMP ALONE ORGANIZES THE ACTIVE SITE OF ADENYLOSUCCINATE      
JRNL        TITL 2 SYNTHETASE FROM ESCHERICHIA COLI.                            
JRNL        REF    J.BIOL.CHEM.                  V. 277  5970 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11741996                                                     
JRNL        DOI    10.1074/JBC.M109561200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 10.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13332                          
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 SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1333                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3321                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 303                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.820                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.650                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000015043.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : GRAPHITE MONOCHROMATOR             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : X-GEN                              
REMARK 200  DATA SCALING SOFTWARE          : X-GEN                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22708                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12200                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HEPES, IMP, HADACIDIN,         
REMARK 280  MAGNESIUM ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.78000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.89000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       52.89000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      105.78000            
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 300 REMARK: THE ASYMMETRY UNIT IS ONE SUBUNIT. THE FUNCTIONAL            
REMARK 300 SYNTHETASE IS A DIMER                                                
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      105.78000            
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     0                                                      
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    GLN A  10     -113.28   -107.28                                   
REMARK 500    GLN A  34     -179.00   -172.88                                   
REMARK 500    HIS A  53      -65.70   -121.95                                   
REMARK 500    SER A  57       12.93    -65.86                                   
REMARK 500    LYS A 124       30.71    -79.90                                   
REMARK 500    MET A 191       -4.04    -58.41                                   
REMARK 500    GLN A 224     -144.19     59.87                                   
REMARK 500    ASP A 231      -69.01    -94.82                                   
REMARK 500    PHE A 278       84.01   -165.46                                   
REMARK 500    THR A 280       20.41    -68.26                                   
REMARK 500    GLU A 285      -36.09    -39.83                                   
REMARK 500    LEU A 360      -91.76   -111.70                                   
REMARK 500    LYS A 366      -86.33    -22.13                                   
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 HDA A 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP A 440                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CIB   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI WITH IMP, GDP,   
REMARK 900 HADACIDIN, NITRATE, AND MG2+                                         
REMARK 900 RELATED ID: 1KJX   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI WITH IMP         
DBREF  1KKB A    0   431  UNP    P12283   PURA_ECOLI       1    432             
SEQRES   1 A  432  MET GLY ASN ASN VAL VAL VAL LEU GLY THR GLN TRP GLY          
SEQRES   2 A  432  ASP GLU GLY LYS GLY LYS ILE VAL ASP LEU LEU THR GLU          
SEQRES   3 A  432  ARG ALA LYS TYR VAL VAL ARG TYR GLN GLY GLY HIS ASN          
SEQRES   4 A  432  ALA GLY HIS THR LEU VAL ILE ASN GLY GLU LYS THR VAL          
SEQRES   5 A  432  LEU HIS LEU ILE PRO SER GLY ILE LEU ARG GLU ASN VAL          
SEQRES   6 A  432  THR SER ILE ILE GLY ASN GLY VAL VAL LEU SER PRO ALA          
SEQRES   7 A  432  ALA LEU MET LYS GLU MET LYS GLU LEU GLU ASP ARG GLY          
SEQRES   8 A  432  ILE PRO VAL ARG GLU ARG LEU LEU LEU SER GLU ALA CYS          
SEQRES   9 A  432  PRO LEU ILE LEU ASP TYR HIS VAL ALA LEU ASP ASN ALA          
SEQRES  10 A  432  ARG GLU LYS ALA ARG GLY ALA LYS ALA ILE GLY THR THR          
SEQRES  11 A  432  GLY ARG GLY ILE GLY PRO ALA TYR GLU ASP LYS VAL ALA          
SEQRES  12 A  432  ARG ARG GLY LEU ARG VAL GLY ASP LEU PHE ASP LYS GLU          
SEQRES  13 A  432  THR PHE ALA GLU LYS LEU LYS GLU VAL MET GLU TYR HIS          
SEQRES  14 A  432  ASN PHE GLN LEU VAL ASN TYR TYR LYS ALA GLU ALA VAL          
SEQRES  15 A  432  ASP TYR GLN LYS VAL LEU ASP ASP THR MET ALA VAL ALA          
SEQRES  16 A  432  ASP ILE LEU THR SER MET VAL VAL ASP VAL SER ASP LEU          
SEQRES  17 A  432  LEU ASP GLN ALA ARG GLN ARG GLY ASP PHE VAL MET PHE          
SEQRES  18 A  432  GLU GLY ALA GLN GLY THR LEU LEU ASP ILE ASP HIS GLY          
SEQRES  19 A  432  THR TYR PRO TYR VAL THR SER SER ASN THR THR ALA GLY          
SEQRES  20 A  432  GLY VAL ALA THR GLY SER GLY LEU GLY PRO ARG TYR VAL          
SEQRES  21 A  432  ASP TYR VAL LEU GLY ILE LEU LYS ALA TYR SER THR ARG          
SEQRES  22 A  432  VAL GLY ALA GLY PRO PHE PRO THR GLU LEU PHE ASP GLU          
SEQRES  23 A  432  THR GLY GLU PHE LEU CYS LYS GLN GLY ASN GLU PHE GLY          
SEQRES  24 A  432  ALA THR THR GLY ARG ARG ARG ARG THR GLY TRP LEU ASP          
SEQRES  25 A  432  THR VAL ALA VAL ARG ARG ALA VAL GLN LEU ASN SER LEU          
SEQRES  26 A  432  SER GLY PHE CYS LEU THR LYS LEU ASP VAL LEU ASP GLY          
SEQRES  27 A  432  LEU LYS GLU VAL LYS LEU CYS VAL ALA TYR ARG MET PRO          
SEQRES  28 A  432  ASP GLY ARG GLU VAL THR THR THR PRO LEU ALA ALA ASP          
SEQRES  29 A  432  ASP TRP LYS GLY VAL GLU PRO ILE TYR GLU THR MET PRO          
SEQRES  30 A  432  GLY TRP SER GLU SER THR PHE GLY VAL LYS ASP ARG SER          
SEQRES  31 A  432  GLY LEU PRO GLN ALA ALA LEU ASN TYR ILE LYS ARG ILE          
SEQRES  32 A  432  GLU GLU LEU THR GLY VAL PRO ILE ASP ILE ILE SER THR          
SEQRES  33 A  432  GLY PRO ASP ARG THR GLU THR MET ILE LEU ARG ASP PRO          
SEQRES  34 A  432  PHE ASP ALA                                                  
HET    HDA  A 437       8                                                       
HET    IMP  A 440      23                                                       
HETNAM     HDA HADACIDIN                                                        
HETNAM     IMP INOSINIC ACID                                                    
FORMUL   2  HDA    C3 H5 N O4                                                   
FORMUL   3  IMP    C10 H13 N4 O8 P                                              
FORMUL   4  HOH   *303(H2 O)                                                    
HELIX    1   1 GLY A   15  THR A   24  1                                  10    
HELIX    2   2 GLU A   25  ALA A   27  5                                   3    
HELIX    3   3 SER A   75  ASP A   88  1                                  14    
HELIX    4   4 PRO A   92  ARG A   96  1                                   5    
HELIX    5   5 LEU A  107  ARG A  121  1                                  15    
HELIX    6   6 GLY A  122  ALA A  125  5                                   4    
HELIX    7   7 GLY A  132  ALA A  142  1                                  11    
HELIX    8   8 ARG A  147  PHE A  152  5                                   6    
HELIX    9   9 ASP A  153  TYR A  175  1                                  23    
HELIX   10  10 ASP A  182  MET A  191  1                                  10    
HELIX   11  11 VAL A  193  MET A  200  1                                   8    
HELIX   12  12 ASP A  203  GLY A  215  1                                  13    
HELIX   13  13 GLY A  225  ASP A  229  5                                   5    
HELIX   14  14 ALA A  245  GLY A  251  1                                   7    
HELIX   15  15 GLY A  255  VAL A  259  5                                   5    
HELIX   16  16 ASP A  284  GLY A  294  1                                  11    
HELIX   17  17 THR A  312  SER A  323  1                                  12    
HELIX   18  18 LYS A  331  ASP A  336  5                                   6    
HELIX   19  19 ALA A  361  LYS A  366  5                                   6    
HELIX   20  20 ASP A  387  LEU A  391  5                                   5    
HELIX   21  21 PRO A  392  GLY A  407  1                                  16    
SHEET    1   A10 VAL A 201  VAL A 202  0                                        
SHEET    2   A10 LEU A  97  SER A 100  1  N  LEU A  99   O  VAL A 202           
SHEET    3   A10 THR A  65  ILE A  68  1  N  SER A  66   O  LEU A  98           
SHEET    4   A10 TYR A  29  ARG A  32  1  N  VAL A  30   O  ILE A  67           
SHEET    5   A10 VAL A 218  GLU A 221  1  O  GLU A 221   N  VAL A  31           
SHEET    6   A10 ASN A   3  GLY A   8  1  N  VAL A   6   O  PHE A 220           
SHEET    7   A10 TYR A 261  LYS A 267  1  O  LEU A 263   N  VAL A   5           
SHEET    8   A10 GLY A 326  THR A 330  1  O  GLY A 326   N  GLY A 264           
SHEET    9   A10 ILE A 410  SER A 414  1  O  SER A 414   N  LEU A 329           
SHEET   10   A10 THR A 422  ILE A 424 -1  O  MET A 423   N  ILE A 413           
SHEET    1   B 2 HIS A  41  ILE A  45  0                                        
SHEET    2   B 2 GLU A  48  LEU A  52 -1  O  THR A  50   N  LEU A  43           
SHEET    1   C 2 SER A 270  ARG A 272  0                                        
SHEET    2   C 2 ARG A 306  GLY A 308 -1  O  ARG A 306   N  ARG A 272           
SHEET    1   D 3 GLU A 369  PRO A 376  0                                        
SHEET    2   D 3 GLU A 340  ARG A 348 -1  N  ARG A 348   O  GLU A 369           
SHEET    3   D 3 LEU A 310  ASP A 311  1  N  LEU A 310   O  CYS A 344           
SHEET    1   E 3 GLU A 369  PRO A 376  0                                        
SHEET    2   E 3 GLU A 340  ARG A 348 -1  N  ARG A 348   O  GLU A 369           
SHEET    3   E 3 GLU A 354  VAL A 355 -1  O  VAL A 355   N  TYR A 347           
CISPEP   1 TYR A  235    PRO A  236          0        -0.14                     
SITE     1 AC1 10 ASP A  13  GLY A  40  THR A 129  GLY A 298                    
SITE     2 AC1 10 ALA A 299  THR A 300  THR A 301  ARG A 303                    
SITE     3 AC1 10 ARG A 305  IMP A 440                                          
SITE     1 AC2 19 TRP A  11  ASP A  13  ASN A  38  ALA A  39                    
SITE     2 AC2 19 ILE A 126  GLY A 127  THR A 128  THR A 129                    
SITE     3 AC2 19 ARG A 143  GLN A 224  VAL A 238  THR A 239                    
SITE     4 AC2 19 VAL A 273  GLY A 274  ARG A 303  HDA A 437                    
SITE     5 AC2 19 HOH A 559  HOH A 560  HOH A 569                               
CRYST1   80.120   80.120  158.670  90.00  90.00 120.00 P 32 2 1      6          
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      0.012481  0.007206  0.000000        0.00000                         
SCALE2      0.000000  0.014412  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006302        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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