GenomeNet

Database: PDB
Entry: 1IM9
LinkDB: 1IM9
Original site: 1IM9 
HEADER    IMMUNE SYSTEM                           10-MAY-01   1IM9              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN NATURAL KILLER CELL                    
TITLE    2 INHIBITORY RECEPTOR KIR2DL1 BOUND TO ITS MHC LIGAND HLA-CW4          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, CW-4               
COMPND   3 CW*0401 ALPHA CHAIN;                                                 
COMPND   4 CHAIN: A, E;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BETA-2 MICROGLOBULIN;                                      
COMPND   8 CHAIN: B, F;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: HLA-CW4-SPECIFIC PEPTIDE;                                  
COMPND  12 CHAIN: C, G;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL1;             
COMPND  16 CHAIN: D;                                                            
COMPND  17 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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PLM-1;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;                            
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PLM-1;                                    
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 OTHER_DETAILS: THIS SEQUENCE HAS BEEN OBTAINED BY POOL               
SOURCE  22 SEQUENCING OF THE PEPTIDES BOUND TO HLA-CW4 NATURALLY.;              
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;                            
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  31 EXPRESSION_SYSTEM_PLASMID: PLM-1                                     
KEYWDS    PROTEIN-PROTEIN COMPLEX, IMMUNOGLOBULIN DOMAIN,                       
KEYWDS   2 ANTIPARALLEL BETA SHEET, ALPHA HELIX, IMMUNE SYSTEM                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.R.FAN,E.O.LONG,D.C.WILEY                                            
REVDAT   3   24-FEB-09 1IM9    1       VERSN                                    
REVDAT   2   01-APR-03 1IM9    1       JRNL                                     
REVDAT   1   30-MAY-01 1IM9    0                                                
JRNL        AUTH   Q.R.FAN,E.O.LONG,D.C.WILEY                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN NATURAL KILLER CELL           
JRNL        TITL 2 INHIBITORY RECEPTOR KIR2DL1-HLA-CW4 COMPLEX.                 
JRNL        REF    NAT.IMMUNOL.                  V.   2   452 2001              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   11323700                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1559783.810                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 41881                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4229                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5579                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE                    : 0.4070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 612                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7858                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 238                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.06000                                              
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : -1.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 15.60000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.45                            
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) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.29                                                 
REMARK   3   BSOL        : 12.53                                                
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 1IM9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013408.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS - B4                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41881                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.19100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: PDB ENTRY 1QQD      PDB ENTRY 1NKR                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, MAGNESIUM CHLORIDE,             
REMARK 280  ETHYLENE GLYCOL, N-(2-ACETAMINDO)IMINODIACETIC ACID , PH 6.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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      106.81550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.93350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.81550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.93350            
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: HEPTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET D     0                                                      
REMARK 465     HIS D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     GLY D   201                                                      
REMARK 465     ASN D   202                                                      
REMARK 465     PRO D   203                                                      
REMARK 465     SER D   204                                                      
REMARK 465     ASN D   205                                                      
REMARK 465     SER D   206                                                      
REMARK 465     TRP D   207                                                      
REMARK 465     PRO D   208                                                      
REMARK 465     SER D   209                                                      
REMARK 465     PRO D   210                                                      
REMARK 465     THR D   211                                                      
REMARK 465     GLU D   212                                                      
REMARK 465     PRO D   213                                                      
REMARK 465     SER D   214                                                      
REMARK 465     SER D   215                                                      
REMARK 465     LYS D   216                                                      
REMARK 465     THR D   217                                                      
REMARK 465     GLY D   218                                                      
REMARK 465     ASN D   219                                                      
REMARK 465     PRO D   220                                                      
REMARK 465     ARG D   221                                                      
REMARK 465     HIS D   222                                                      
REMARK 465     LEU D   223                                                      
REMARK 465     HIS D   224                                                      
REMARK 465     MET E     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B  58    CB   CG   CD   CE   NZ                              
REMARK 470     LYS F  58    CB   CG   CD   CE   NZ                              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET B  99   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    THR D 200   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
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    ASP A  29     -136.34     61.35                                   
REMARK 500    ASP A  30       31.03    -94.45                                   
REMARK 500    SER A  38       -7.76    -54.69                                   
REMARK 500    ALA A  41      -76.18    -35.75                                   
REMARK 500    TRP A  51       13.76    -63.93                                   
REMARK 500    GLN A  54        1.03    -65.69                                   
REMARK 500    PRO A 105       -5.41    -49.39                                   
REMARK 500    LEU A 109      106.35    -55.43                                   
REMARK 500    ARG A 111      145.20   -173.40                                   
REMARK 500    ASN A 114       86.25   -168.30                                   
REMARK 500    TYR A 123      -51.31   -125.22                                   
REMARK 500    ASP A 129        1.90    -68.80                                   
REMARK 500    ALA A 158      -72.36    -50.55                                   
REMARK 500    LYS A 176      -47.88    -15.22                                   
REMARK 500    SER A 195     -154.03   -148.97                                   
REMARK 500    PRO A 210     -174.02    -61.94                                   
REMARK 500    ASP A 227       17.52   -141.06                                   
REMARK 500    PRO A 267      -72.89    -57.99                                   
REMARK 500    ASN B  21     -159.86   -166.65                                   
REMARK 500    HIS B  31      132.39   -172.31                                   
REMARK 500    SER B  52      176.59    -58.21                                   
REMARK 500    TRP B  60       -0.64     78.64                                   
REMARK 500    THR B  73      -14.91   -140.84                                   
REMARK 500    GLU B  74      -26.36     93.27                                   
REMARK 500    ARG B  97      -77.22    -62.38                                   
REMARK 500    PRO D   8     -167.40    -77.28                                   
REMARK 500    GLU D  21      -16.14     80.24                                   
REMARK 500    GLU D  22     -160.18    -72.03                                   
REMARK 500    TRP D  29      148.27   -174.26                                   
REMARK 500    ASP D  57       54.01     83.82                                   
REMARK 500    ASP D  72       -3.46    -56.69                                   
REMARK 500    THR D  84      -26.43     59.95                                   
REMARK 500    HIS D  85       -9.14     70.50                                   
REMARK 500    ALA D 120      151.61    -45.48                                   
REMARK 500    ASN D 157       54.67   -116.77                                   
REMARK 500    THR D 170      -87.80   -108.59                                   
REMARK 500    PRO D 194      153.64    -45.10                                   
REMARK 500    PRO E  20      151.40    -48.52                                   
REMARK 500    ASP E  29     -121.75     64.47                                   
REMARK 500    TRP E  51        3.53    -61.02                                   
REMARK 500    ASN E 114       83.93   -170.02                                   
REMARK 500    TYR E 123      -54.57   -121.43                                   
REMARK 500    ALA E 140       -7.46    -58.88                                   
REMARK 500    ALA E 150       13.74   -143.56                                   
REMARK 500    THR E 178      -41.37   -147.13                                   
REMARK 500    SER E 195     -171.19    177.85                                   
REMARK 500    PRO E 210     -179.26    -66.75                                   
REMARK 500    HIS F  31      130.01    178.60                                   
REMARK 500    PRO F  32      172.83    -58.20                                   
REMARK 500    GLU F  47      -70.95    -91.83                                   
REMARK 500    THR F  68      136.03    177.99                                   
REMARK 500    GLU F  74      -29.21     98.19                                   
REMARK 500    PRO F  90      139.13    -39.94                                   
REMARK 500    ASP G   4       80.26    -69.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NKR   RELATED DB: PDB                                   
REMARK 900 1NKR CONTAINS THE STRUCTURE OF THE FREE NATURAL KILLER CELL          
REMARK 900 RECEPTOR KIR2DL1                                                     
REMARK 900 RELATED ID: 1QQD   RELATED DB: PDB                                   
REMARK 900 1QQD CONTAINS THE STRUCTURE OF HLA-CW4                               
DBREF  1IM9 A    1   275  UNP    P30504   1C04_HUMAN      25    299             
DBREF  1IM9 B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  1IM9 D    1   224  UNP    P43626   KI2L1_HUMAN     22    245             
DBREF  1IM9 E    1   275  UNP    P30504   1C04_HUMAN      25    299             
DBREF  1IM9 F    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  1IM9 C    1     9  PDB    1IM9     1IM9             1      9             
DBREF  1IM9 G    1     9  PDB    1IM9     1IM9             1      9             
SEQADV 1IM9 MET A    0  UNP  P30504              CLONING ARTIFACT               
SEQADV 1IM9 MET E    0  UNP  P30504              CLONING ARTIFACT               
SEQADV 1IM9 MET B    0  UNP  P61769              CLONING ARTIFACT               
SEQADV 1IM9 MET F    0  UNP  P61769              CLONING ARTIFACT               
SEQADV 1IM9 MET D    0  UNP  P43626              CLONING ARTIFACT               
SEQRES   1 A  276  MET GLY SER HIS SER MET ARG TYR PHE SER THR SER VAL          
SEQRES   2 A  276  SER TRP PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL          
SEQRES   3 A  276  GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER          
SEQRES   4 A  276  ASP ALA ALA SER PRO ARG GLY GLU PRO ARG GLU PRO TRP          
SEQRES   5 A  276  VAL GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR          
SEQRES   6 A  276  GLN LYS TYR LYS ARG GLN ALA GLN ALA ASP ARG VAL ASN          
SEQRES   7 A  276  LEU ARG LYS LEU ARG GLY TYR TYR ASN GLN SER GLU ASP          
SEQRES   8 A  276  GLY SER HIS THR LEU GLN ARG MET PHE GLY CYS ASP LEU          
SEQRES   9 A  276  GLY PRO ASP GLY ARG LEU LEU ARG GLY TYR ASN GLN PHE          
SEQRES  10 A  276  ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP          
SEQRES  11 A  276  LEU ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE          
SEQRES  12 A  276  THR GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN          
SEQRES  13 A  276  ARG ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU          
SEQRES  14 A  276  ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG          
SEQRES  15 A  276  ALA GLU HIS PRO LYS THR HIS VAL THR HIS HIS PRO VAL          
SEQRES  16 A  276  SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY          
SEQRES  17 A  276  PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN TRP ASP          
SEQRES  18 A  276  GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR          
SEQRES  19 A  276  ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA          
SEQRES  20 A  276  VAL VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS          
SEQRES  21 A  276  HIS VAL GLN HIS GLU GLY LEU PRO GLU PRO LEU THR LEU          
SEQRES  22 A  276  ARG TRP LYS                                                  
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 C    9  GLN TYR ASP ASP ALA VAL TYR LYS LEU                          
SEQRES   1 D  225  MET HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA          
SEQRES   2 D  225  HIS PRO GLY PRO LEU VAL LYS SER GLU GLU THR VAL ILE          
SEQRES   3 D  225  LEU GLN CYS TRP SER ASP VAL MET PHE GLU HIS PHE LEU          
SEQRES   4 D  225  LEU HIS ARG GLU GLY MET PHE ASN ASP THR LEU ARG LEU          
SEQRES   5 D  225  ILE GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE          
SEQRES   6 D  225  SER ILE SER ARG MET THR GLN ASP LEU ALA GLY THR TYR          
SEQRES   7 D  225  ARG CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN VAL          
SEQRES   8 D  225  SER ALA PRO SER ASP PRO LEU ASP ILE VAL ILE ILE GLY          
SEQRES   9 D  225  LEU TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO          
SEQRES  10 D  225  THR VAL LEU ALA GLY GLU ASN VAL THR LEU SER CYS SER          
SEQRES  11 D  225  SER ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU          
SEQRES  12 D  225  GLY GLU ALA HIS GLU ARG ARG LEU PRO ALA GLY PRO LYS          
SEQRES  13 D  225  VAL ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO          
SEQRES  14 D  225  ALA THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE          
SEQRES  15 D  225  HIS ASP SER PRO TYR GLU TRP SER LYS SER SER ASP PRO          
SEQRES  16 D  225  LEU LEU VAL SER VAL THR GLY ASN PRO SER ASN SER TRP          
SEQRES  17 D  225  PRO SER PRO THR GLU PRO SER SER LYS THR GLY ASN PRO          
SEQRES  18 D  225  ARG HIS LEU HIS                                              
SEQRES   1 E  276  MET GLY SER HIS SER MET ARG TYR PHE SER THR SER VAL          
SEQRES   2 E  276  SER TRP PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL          
SEQRES   3 E  276  GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER          
SEQRES   4 E  276  ASP ALA ALA SER PRO ARG GLY GLU PRO ARG GLU PRO TRP          
SEQRES   5 E  276  VAL GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR          
SEQRES   6 E  276  GLN LYS TYR LYS ARG GLN ALA GLN ALA ASP ARG VAL ASN          
SEQRES   7 E  276  LEU ARG LYS LEU ARG GLY TYR TYR ASN GLN SER GLU ASP          
SEQRES   8 E  276  GLY SER HIS THR LEU GLN ARG MET PHE GLY CYS ASP LEU          
SEQRES   9 E  276  GLY PRO ASP GLY ARG LEU LEU ARG GLY TYR ASN GLN PHE          
SEQRES  10 E  276  ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP          
SEQRES  11 E  276  LEU ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE          
SEQRES  12 E  276  THR GLN ARG LYS TRP GLU ALA ALA ARG GLU ALA GLU GLN          
SEQRES  13 E  276  ARG ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU          
SEQRES  14 E  276  ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG          
SEQRES  15 E  276  ALA GLU HIS PRO LYS THR HIS VAL THR HIS HIS PRO VAL          
SEQRES  16 E  276  SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY          
SEQRES  17 E  276  PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN TRP ASP          
SEQRES  18 E  276  GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR          
SEQRES  19 E  276  ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA          
SEQRES  20 E  276  VAL VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS          
SEQRES  21 E  276  HIS VAL GLN HIS GLU GLY LEU PRO GLU PRO LEU THR LEU          
SEQRES  22 E  276  ARG TRP LYS                                                  
SEQRES   1 F  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 F  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 F  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 F  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 F  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 F  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 F  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 F  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 G    9  GLN TYR ASP ASP ALA VAL TYR LYS LEU                          
FORMUL   8  HOH   *238(H2 O)                                                    
HELIX    1   1 GLU A   49  GLU A   53  5                                   5    
HELIX    2   2 GLY A   56  TYR A   85  1                                  30    
HELIX    3   3 ASP A  137  ALA A  150  1                                  14    
HELIX    4   4 ARG A  151  GLY A  162  1                                  12    
HELIX    5   5 GLY A  162  GLY A  175  1                                  14    
HELIX    6   6 GLY A  175  GLN A  180  1                                   6    
HELIX    7   7 GLU A  253  GLN A  255  5                                   3    
HELIX    8   8 THR D   70  ALA D   74  5                                   5    
HELIX    9   9 GLU E   49  GLU E   53  5                                   5    
HELIX   10  10 GLY E   56  TYR E   85  1                                  30    
HELIX   11  11 THR E  138  ALA E  149  1                                  12    
HELIX   12  12 ARG E  151  GLY E  162  1                                  12    
HELIX   13  13 GLY E  162  LYS E  176  1                                  15    
HELIX   14  14 GLY E  175  GLN E  180  1                                   6    
HELIX   15  15 GLU E  253  GLN E  255  5                                   3    
SHEET    1   A 8 GLU A  46  PRO A  47  0                                        
SHEET    2   A 8 THR A  31  ASP A  37 -1  O  ARG A  35   N  GLU A  46           
SHEET    3   A 8 ARG A  21  VAL A  28 -1  O  ALA A  24   N  PHE A  36           
SHEET    4   A 8 HIS A   3  VAL A  12 -1  O  ARG A   6   N  TYR A  27           
SHEET    5   A 8 THR A  94  LEU A 103 -1  O  LEU A  95   N  SER A  11           
SHEET    6   A 8 LEU A 109  TYR A 118 -1  N  LEU A 110   O  ASP A 102           
SHEET    7   A 8 LYS A 121  LEU A 126 -1  O  LYS A 121   N  TYR A 118           
SHEET    8   A 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1   B 4 LYS A 186  PRO A 193  0                                        
SHEET    2   B 4 GLU A 198  PHE A 208 -1  N  THR A 200   O  HIS A 192           
SHEET    3   B 4 PHE A 241  PRO A 250 -1  N  PHE A 241   O  PHE A 208           
SHEET    4   B 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    5   B 4 ARG A 234  PRO A 235  0                                        
SHEET    6   B 4 PHE A 241  PRO A 250 -1  N  GLN A 242   O  ARG A 234           
SHEET    1   C 4 GLU A 222  ASP A 223  0                                        
SHEET    2   C 4 THR A 214  TRP A 219 -1  N  TRP A 219   O  GLU A 222           
SHEET    3   C 4 TYR A 257  GLN A 262 -1  O  THR A 258   N  GLN A 218           
SHEET    4   C 4 LEU A 270  LEU A 272 -1  N  LEU A 270   O  VAL A 261           
SHEET    1   D 4 LYS B   6  SER B  11  0                                        
SHEET    2   D 4 ASN B  21  PHE B  30 -1  N  ASN B  24   O  TYR B  10           
SHEET    3   D 4 PHE B  62  PHE B  70 -1  N  PHE B  62   O  PHE B  30           
SHEET    4   D 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    5   D 4 SER B  55  PHE B  56  0                                        
SHEET    6   D 4 PHE B  62  PHE B  70 -1  N  TYR B  63   O  SER B  55           
SHEET    1   E 4 GLU B  44  ARG B  45  0                                        
SHEET    2   E 4 GLU B  36  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   E 4 TYR B  78  ASN B  83 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   E 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1   F 4 SER D   9  HIS D  13  0                                        
SHEET    2   F 4 VAL D  24  SER D  30 -1  N  ILE D  25   O  HIS D  13           
SHEET    3   F 4 SER D  60  ILE D  66 -1  O  SER D  60   N  SER D  30           
SHEET    4   F 4 GLU D  54  HIS D  55 -1  N  GLU D  54   O  LYS D  61           
SHEET    1   G 5 LEU D  17  LYS D  19  0                                        
SHEET    2   G 5 LEU D  97  ILE D 102  1  O  VAL D 100   N  VAL D  18           
SHEET    3   G 5 GLY D  75  SER D  82 -1  O  GLY D  75   N  ILE D  99           
SHEET    4   G 5 HIS D  36  GLU D  42 -1  O  HIS D  36   N  SER D  82           
SHEET    5   G 5 ASP D  47  ILE D  52 -1  O  ASP D  47   N  ARG D  41           
SHEET    1   H 4 SER D 109  GLN D 113  0                                        
SHEET    2   H 4 ASN D 123  SER D 130 -1  N  THR D 125   O  GLN D 113           
SHEET    3   H 4 PHE D 160  PRO D 168 -1  N  PHE D 160   O  SER D 130           
SHEET    4   H 4 GLY D 153  PRO D 154 -1  O  GLY D 153   N  GLN D 161           
SHEET    1   I 5 THR D 117  VAL D 118  0                                        
SHEET    2   I 5 LEU D 195  VAL D 199  1  O  SER D 198   N  VAL D 118           
SHEET    3   I 5 GLY D 173  PHE D 181 -1  O  GLY D 173   N  VAL D 197           
SHEET    4   I 5 MET D 136  ARG D 141 -1  O  MET D 136   N  SER D 180           
SHEET    5   I 5 ARG D 148  PRO D 151 -1  O  ARG D 148   N  LEU D 139           
SHEET    6   I 5 GLY D 173  PHE D 181  0                                        
SHEET    7   I 5 SER D 184  TRP D 188 -1  N  SER D 184   O  PHE D 181           
SHEET    1   J 7 GLU E  46  PRO E  47  0                                        
SHEET    2   J 7 THR E  31  ASP E  37 -1  O  ARG E  35   N  GLU E  46           
SHEET    3   J 7 ARG E  21  VAL E  28 -1  N  ALA E  24   O  PHE E  36           
SHEET    4   J 7 HIS E   3  VAL E  12 -1  O  ARG E   6   N  TYR E  27           
SHEET    5   J 7 THR E  94  LEU E 103 -1  O  LEU E  95   N  SER E  11           
SHEET    6   J 7 LEU E 109  TYR E 118 -1  N  LEU E 110   O  ASP E 102           
SHEET    7   J 7 LYS E 121  ALA E 125 -1  O  LYS E 121   N  TYR E 118           
SHEET    1   K 4 LYS E 186  PRO E 193  0                                        
SHEET    2   K 4 GLU E 198  PHE E 208 -1  N  THR E 200   O  HIS E 192           
SHEET    3   K 4 PHE E 241  PRO E 250 -1  N  PHE E 241   O  PHE E 208           
SHEET    4   K 4 THR E 228  LEU E 230 -1  N  GLU E 229   O  ALA E 246           
SHEET    5   K 4 ARG E 234  PRO E 235  0                                        
SHEET    6   K 4 PHE E 241  PRO E 250 -1  O  GLN E 242   N  ARG E 234           
SHEET    1   L 4 GLU E 222  ASP E 223  0                                        
SHEET    2   L 4 THR E 214  TRP E 219 -1  N  TRP E 219   O  GLU E 222           
SHEET    3   L 4 TYR E 257  GLN E 262 -1  O  THR E 258   N  GLN E 218           
SHEET    4   L 4 LEU E 270  LEU E 272 -1  N  LEU E 270   O  VAL E 261           
SHEET    1   M 4 LYS F   6  SER F  11  0                                        
SHEET    2   M 4 ASN F  21  PHE F  30 -1  N  ASN F  24   O  TYR F  10           
SHEET    3   M 4 PHE F  62  TYR F  67 -1  N  PHE F  62   O  PHE F  30           
SHEET    4   M 4 GLU F  50  HIS F  51 -1  O  GLU F  50   N  TYR F  67           
SHEET    5   M 4 SER F  55  PHE F  56  0                                        
SHEET    6   M 4 PHE F  62  TYR F  67 -1  N  TYR F  63   O  SER F  55           
SHEET    7   M 4 ASN F  21  PHE F  30  0                                        
SHEET    8   M 4 GLU F  69  PHE F  70 -1  O  PHE F  70   N  ASN F  21           
SHEET    1   N 4 GLU F  44  ARG F  45  0                                        
SHEET    2   N 4 GLU F  36  LYS F  41 -1  N  LYS F  41   O  GLU F  44           
SHEET    3   N 4 TYR F  78  ASN F  83 -1  O  ALA F  79   N  LEU F  40           
SHEET    4   N 4 LYS F  91  LYS F  94 -1  N  LYS F  91   O  VAL F  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.04  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.03  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS D   28    CYS D   79                          1555   1555  2.04  
SSBOND   5 CYS D  128    CYS D  177                          1555   1555  2.04  
SSBOND   6 CYS E  101    CYS E  164                          1555   1555  2.05  
SSBOND   7 CYS E  203    CYS E  259                          1555   1555  2.03  
SSBOND   8 CYS F   25    CYS F   80                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0        -3.14                     
CISPEP   2 HIS B   31    PRO B   32          0        -0.51                     
CISPEP   3 HIS D   13    PRO D   14          0         0.12                     
CISPEP   4 GLN D  113    PRO D  114          0         0.08                     
CISPEP   5 TYR E  209    PRO E  210          0         3.93                     
CISPEP   6 HIS F   31    PRO F   32          0         0.86                     
CRYST1  213.631   75.867  125.746  90.00 120.96  90.00 C 1 2 1       8          
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      0.004681  0.000000  0.002808        0.00000                         
SCALE2      0.000000  0.013181  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009274        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system