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Database: PDB
Entry: 1S2X
LinkDB: 1S2X
Original site: 1S2X 
HEADER    UNKNOWN FUNCTION                        12-JAN-04   1S2X              
TITLE     CRYSTAL STRUCTURE OF CAG-Z FROM HELICOBACTER PYLORI                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAG-Z;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_TAXID: 210;                                                 
SOURCE   4 GENE: CAGZ;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3                                 
KEYWDS    CAG-Z, HELICOBACTER PYLORI, CAG PATHOGENICITY ISLAND, TYPE            
KEYWDS   2 IV SECRETION SYSTEM, UNKNOWN FUNCTION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.CENDRON,A.SEYDEL,A.ANGELINI,R.BATTISTUTTA,G.ZANOTTI                 
REVDAT   3   24-FEB-09 1S2X    1       VERSN                                    
REVDAT   2   10-AUG-04 1S2X    1       TITLE                                    
REVDAT   1   27-JUL-04 1S2X    0                                                
JRNL        AUTH   L.CENDRON,A.SEYDEL,A.ANGELINI,R.BATTISTUTTA,                 
JRNL        AUTH 2 G.ZANOTTI                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF CAGZ, A PROTEIN FROM THE                
JRNL        TITL 2 HELICOBACTER PYLORI PATHOGENICITY ISLAND THAT                
JRNL        TITL 3 ENCODES FOR A TYPE IV SECRETION SYSTEM                       
JRNL        REF    J.MOL.BIOL.                   V. 340   881 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15223328                                                     
JRNL        DOI    10.1016/J.JMB.2004.05.016                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.245                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.229                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.263                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1381                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 17961                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.229                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 13176                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1463                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 95                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1556.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 6267                    
REMARK   3   NUMBER OF RESTRAINTS                     : 5971                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.006                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.020                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.022                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.026                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.031                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.030                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.085                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE        
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56         
REMARK   4                                                                      
REMARK   4 1S2X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021299.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-03                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9202                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, HEPES, PH         
REMARK 280  7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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       15.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.80000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.32500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.80000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       22.32500            
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 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     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ASN A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     ARG A    -1                                                      
REMARK 465     THR A   180                                                      
REMARK 465     TYR A   181                                                      
REMARK 465     LEU A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     LEU A   185                                                      
REMARK 465     GLU A   186                                                      
REMARK 465     ARG A   187                                                      
REMARK 465     ALA A   188                                                      
REMARK 465     LYS A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     ILE A   191                                                      
REMARK 465     THR A   192                                                      
REMARK 465     GLN A   193                                                      
REMARK 465     LEU A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     ASN A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     GLU A   199                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A    41     O    HOH A  1065              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   6      158.19    -49.37                                   
REMARK 500    LYS A 177      104.31    -39.24                                   
REMARK 500    ASN A 178      165.43    -39.68                                   
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 IPA A 201                 
DBREF  1S2X A    1   199  UNP    Q9JMX9   Q9JMX9_HELPY     1    199             
SEQADV 1S2X GLY A   -6  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X SER A   -5  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X PRO A   -4  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X ASN A   -3  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X SER A   -2  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X ARG A   -1  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X VAL A    0  UNP  Q9JMX9              CLONING ARTIFACT               
SEQADV 1S2X ASP A    1  UNP  Q9JMX9    MET     1 ENGINEERED                     
SEQADV 1S2X MSE A   21  UNP  Q9JMX9    MET    21 MODIFIED RESIDUE               
SEQADV 1S2X MSE A   59  UNP  Q9JMX9    MET    59 MODIFIED RESIDUE               
SEQADV 1S2X MSE A  144  UNP  Q9JMX9    MET   144 MODIFIED RESIDUE               
SEQADV 1S2X MSE A  145  UNP  Q9JMX9    MET   145 MODIFIED RESIDUE               
SEQRES   1 A  206  GLY SER PRO ASN SER ARG VAL ASP GLU LEU GLY PHE ASN          
SEQRES   2 A  206  GLU ALA GLU ARG GLN LYS ILE LEU ASP SER ASN SER SER          
SEQRES   3 A  206  LEU MSE ARG ASN ALA ASN GLU VAL ARG ASP LYS PHE ILE          
SEQRES   4 A  206  GLN ASN TYR ALA THR SER LEU LYS ASP SER ASN ASP PRO          
SEQRES   5 A  206  GLN ASP PHE LEU ARG ARG VAL GLN GLU LEU ARG ILE ASN          
SEQRES   6 A  206  MSE GLN LYS ASN PHE ILE SER PHE ASP ALA TYR TYR ASN          
SEQRES   7 A  206  TYR LEU ASN ASN LEU VAL LEU ALA SER TYR ASN ARG CYS          
SEQRES   8 A  206  LYS GLN GLU LYS THR PHE ALA GLU SER THR ILE LYS ASN          
SEQRES   9 A  206  GLU LEU THR LEU GLY GLU PHE VAL ALA GLU ILE SER ASP          
SEQRES  10 A  206  ASN PHE ASN ASN PHE THR CYS ASP GLU VAL ALA ARG ILE          
SEQRES  11 A  206  SER ASP LEU VAL ALA SER TYR LEU PRO ARG GLU TYR LEU          
SEQRES  12 A  206  PRO PRO PHE ILE ASP GLY ASN MSE MSE GLY VAL ALA PHE          
SEQRES  13 A  206  GLN ILE LEU GLY ILE ASP ASP PHE GLY LYS LYS LEU ASN          
SEQRES  14 A  206  GLU ILE VAL GLN ASP ILE GLY THR LYS TYR ILE ILE LEU          
SEQRES  15 A  206  SER LYS ASN LYS THR TYR LEU THR SER LEU GLU ARG ALA          
SEQRES  16 A  206  LYS LEU ILE THR GLN LEU LYS LEU ASN LEU GLU                  
MODRES 1S2X MSE A   21  MET  SELENOMETHIONINE                                   
MODRES 1S2X MSE A   59  MET  SELENOMETHIONINE                                   
MODRES 1S2X MSE A  144  MET  SELENOMETHIONINE                                   
MODRES 1S2X MSE A  145  MET  SELENOMETHIONINE                                   
HET    MSE  A  21       8                                                       
HET    MSE  A  59       8                                                       
HET    MSE  A 144       8                                                       
HET    MSE  A 145       8                                                       
HET    IPA  A 201       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2  IPA    C3 H8 O                                                      
FORMUL   3  HOH   *91(H2 O)                                                     
HELIX    1   1 ASN A    6  ASN A   17  1                                  12    
HELIX    2   2 ASN A   23  ALA A   36  1                                  14    
HELIX    3   3 THR A   37  SER A   42  5                                   6    
HELIX    4   4 ASP A   44  ASN A   62  1                                  19    
HELIX    5   5 PHE A   66  ILE A   95  1                                  30    
HELIX    6   6 ASN A   97  SER A  129  1                                  33    
HELIX    7   7 TYR A  130  LEU A  131  5                                   2    
HELIX    8   8 PRO A  132  LEU A  136  5                                   5    
HELIX    9   9 ASP A  141  LEU A  152  1                                  12    
HELIX   10  10 GLY A  153  LYS A  177  1                                  25    
LINK         C   LEU A  20                 N   MSE A  21     1555   1555  1.33  
LINK         C   MSE A  21                 N   ARG A  22     1555   1555  1.33  
LINK         C   ASN A  58                 N   MSE A  59     1555   1555  1.33  
LINK         C   MSE A  59                 N   GLN A  60     1555   1555  1.33  
LINK         C   ASN A 143                 N   MSE A 144     1555   1555  1.32  
LINK         C   MSE A 144                 N   MSE A 145     1555   1555  1.34  
LINK         C   MSE A 145                 N   GLY A 146     1555   1555  1.33  
SITE     1 AC1  1 SER A 124                                                     
CRYST1   31.550   44.650  159.600  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      0.031696  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006266        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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