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Database: PDB
Entry: 1UFU
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Original site: 1UFU 
HEADER    IMMUNE SYSTEM                           10-JUN-03   1UFU              
TITLE     CRYSTAL STRUCTURE OF LIGAND BINDING DOMAIN OF IMMUNOGLOBULIN-LIKE     
TITLE    2 TRANSCRIPT 2 (ILT2; LIR-1)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMMUNOGLOBULIN-LIKE TRANSCRIPT 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (DOMAIN1 AND 2);                     
COMPND   5 SYNONYM: ILT2;                                                       
COMPND   6 ENGINEERED: 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 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: PGMT7                                     
KEYWDS    IMMUNOGLOBULIN-LIKE FOLDS, IMMUNE SYSTEM                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SHIROISHI,K.AMANO,L.RASUBALA,K.TSUMOTO,I.KUMAGAI,D.KOHDA,K.MAENAKA  
REVDAT   3   25-OCT-23 1UFU    1       REMARK                                   
REVDAT   2   24-FEB-09 1UFU    1       VERSN                                    
REVDAT   1   10-AUG-04 1UFU    0                                                
JRNL        AUTH   M.SHIROISHI,K.AMANO,L.RASUBALA,K.TSUMOTO,I.KUMAGAI,D.KOHDA,  
JRNL        AUTH 2 K.MAENAKA                                                    
JRNL        TITL   KINETIC AND THERMODYNAMIC PROPERTIES OF THE INTERACTION      
JRNL        TITL 2 BETWEEN IMMUNOGLOBULIN LIKE TRANSCRIPT (ILT) AND MHC CLASS I 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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)   (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 3607                           
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) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 339                             
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 68                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.042                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1355                                    
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) : 41.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.40                          
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) : 0.41                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.42                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.57                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.020                           
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1UFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000005781.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4406                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 12.20                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1G0X                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM FORMATE, 0.08M NA-ACETATE,   
REMARK 280  PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
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       18.11000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.20000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.11000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.20000            
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    29                                                      
REMARK 465     GLN A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     GLU A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     HIS A   141                                                      
REMARK 465     PRO A   142                                                      
REMARK 465     GLN A   143                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     PRO A   149                                                      
REMARK 465     HIS A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     SER A   165                                                      
REMARK 465     PRO A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     ARG A   169                                                      
REMARK 465     VAL A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     GLY A   198                                                      
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    LEU A   3      -85.63   -179.93                                   
REMARK 500    GLN A  33      -36.77   -145.90                                   
REMARK 500    LYS A  41      -29.10     47.41                                   
REMARK 500    TYR A  99     -117.05   -131.38                                   
REMARK 500    SER A 181       56.50   -158.71                                   
REMARK 500    SER A 186     -162.11    -76.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1G0X   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE FROM THE DIFFERENT FORM OF CRYSTAL (P21212) OF THE     
REMARK 900 SAME PROTEIN.                                                        
DBREF  1UFU A    2   198  UNP    Q8NHL6   LIRB1_HUMAN     25    221             
SEQRES   1 A  197  HIS LEU PRO LYS PRO THR LEU TRP ALA GLU PRO GLY SER          
SEQRES   2 A  197  VAL ILE THR GLN GLY SER PRO VAL THR LEU ARG CYS GLN          
SEQRES   3 A  197  GLY GLY GLN GLU THR GLN GLU TYR ARG LEU TYR ARG GLU          
SEQRES   4 A  197  LYS LYS THR ALA PRO TRP ILE THR ARG ILE PRO GLN GLU          
SEQRES   5 A  197  LEU VAL LYS LYS GLY GLN PHE PRO ILE PRO SER ILE THR          
SEQRES   6 A  197  TRP GLU HIS ALA GLY ARG TYR ARG CYS TYR TYR GLY SER          
SEQRES   7 A  197  ASP THR ALA GLY ARG SER GLU SER SER ASP PRO LEU GLU          
SEQRES   8 A  197  LEU VAL VAL THR GLY ALA TYR ILE LYS PRO THR LEU SER          
SEQRES   9 A  197  ALA GLN PRO SER PRO VAL VAL ASN SER GLY GLY ASN VAL          
SEQRES  10 A  197  THR LEU GLN CYS ASP SER GLN VAL ALA PHE ASP GLY PHE          
SEQRES  11 A  197  ILE LEU CYS LYS GLU GLY GLU ASP GLU HIS PRO GLN CYS          
SEQRES  12 A  197  LEU ASN SER GLN PRO HIS ALA ARG GLY SER SER ARG ALA          
SEQRES  13 A  197  ILE PHE SER VAL GLY PRO VAL SER PRO SER ARG ARG TRP          
SEQRES  14 A  197  TRP TYR ARG CYS TYR ALA TYR ASP SER ASN SER PRO TYR          
SEQRES  15 A  197  GLU TRP SER LEU PRO SER ASP LEU LEU GLU LEU LEU VAL          
SEQRES  16 A  197  LEU GLY                                                      
HELIX    1   1 ALA A   44  ILE A   50  5                                   7    
HELIX    2   2 PRO A   51  LYS A   56  1                                   6    
SHEET    1   A 3 THR A   7  GLU A  11  0                                        
SHEET    2   A 3 VAL A  22  GLN A  27 -1  O  ARG A  25   N  TRP A   9           
SHEET    3   A 3 GLN A  59  ILE A  62 -1  O  ILE A  62   N  VAL A  22           
SHEET    1   B 4 VAL A  15  THR A  17  0                                        
SHEET    2   B 4 LEU A  91  THR A  96  1  O  VAL A  94   N  ILE A  16           
SHEET    3   B 4 GLY A  71  SER A  79 -1  N  TYR A  73   O  LEU A  91           
SHEET    4   B 4 GLY A  83  ARG A  84 -1  O  GLY A  83   N  SER A  79           
SHEET    1   C 4 TYR A  35  ARG A  39  0                                        
SHEET    2   C 4 GLY A  71  SER A  79 -1  O  TYR A  76   N  ARG A  36           
SHEET    3   C 4 LEU A  91  THR A  96 -1  O  LEU A  91   N  TYR A  73           
SHEET    4   C 4 GLU A 184  TRP A 185  1  O  TRP A 185   N  VAL A  95           
SHEET    1   D 3 THR A 103  GLN A 107  0                                        
SHEET    2   D 3 VAL A 118  ASP A 123 -1  O  THR A 119   N  GLN A 107           
SHEET    3   D 3 ARG A 156  VAL A 161 -1  O  PHE A 159   N  LEU A 120           
SHEET    1   E 4 LEU A 145  ASN A 146  0                                        
SHEET    2   E 4 PHE A 131  CYS A 134 -1  N  LEU A 133   O  LEU A 145           
SHEET    3   E 4 TRP A 171  ALA A 176 -1  O  ARG A 173   N  CYS A 134           
SHEET    4   E 4 LEU A 192  GLU A 193 -1  O  LEU A 192   N  TYR A 172           
SSBOND   1 CYS A   26    CYS A   75                          1555   1555  2.06  
SSBOND   2 CYS A  122    CYS A  174                          1555   1555  2.03  
SSBOND   3 CYS A  134    CYS A  144                          1555   1555  2.03  
CISPEP   1 GLU A   11    PRO A   12          0         2.36                     
CISPEP   2 GLN A  107    PRO A  108          0         1.68                     
CRYST1   36.220  104.400   53.460  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      0.027609  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009579  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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